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Conserved domains on  [gi|1785364863|ref|XP_004913939|]
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brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2 [Xenopus tropicalis]

Protein Classification

brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2( domain architecture ID 10166438)

brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2 (BAIAP2L2) is a phosphoinositide-binding protein that induces the formation of planar or gently curved membrane structures

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
I-BAR_IMD_BAIAP2L2 cd07644
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
6-220 7.32e-138

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. This group is composed of uncharacterized proteins known as BAIAP2L2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2). They contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


:

Pssm-ID: 153328  Cd Length: 215  Bit Score: 395.06  E-value: 7.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863   6 DSIYASTIGTYKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTA 85
Cdd:cd07644     1 DLLYRSTISIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIAKIGEQALQSLTSQSLGEILIQMSETQRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  86 SAGLNIVFQTLHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQRDRNLREMKENVNMLHNDM 165
Cdd:cd07644    81 SADLEVVFQTFHVDLLQHMDKNTKLDMQFIEDSRRVYELEYRHRAANLEKCMSELWRMERQRDRNVREMKENVNRLRQSM 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785364863 166 LAFVKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKEQI 220
Cdd:cd07644   161 QAFLKESQRAAELEEKRRYRFLAEKHYLLNNTFLQFQSRARGMLQTRVPSWKEQP 215
SH3_BAIAP2L2 cd11914
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; ...
312-370 1.91e-35

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212847 [Multi-domain]  Cd Length: 59  Bit Score: 125.70  E-value: 1.91e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364863 312 RRVQAIVDHNTGGNRTLLQFKKADIITVLVPEARNGWLYGKLEGLSMNGWFPEAYVKSM 370
Cdd:cd11914     1 RRVRAIVSHPAGSNPTLLRFNRGDIITVLVPEARNGWLYGKLEGSSRQGWFPEAYVKAL 59
 
Name Accession Description Interval E-value
I-BAR_IMD_BAIAP2L2 cd07644
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
6-220 7.32e-138

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. This group is composed of uncharacterized proteins known as BAIAP2L2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2). They contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153328  Cd Length: 215  Bit Score: 395.06  E-value: 7.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863   6 DSIYASTIGTYKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTA 85
Cdd:cd07644     1 DLLYRSTISIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIAKIGEQALQSLTSQSLGEILIQMSETQRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  86 SAGLNIVFQTLHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQRDRNLREMKENVNMLHNDM 165
Cdd:cd07644    81 SADLEVVFQTFHVDLLQHMDKNTKLDMQFIEDSRRVYELEYRHRAANLEKCMSELWRMERQRDRNVREMKENVNRLRQSM 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785364863 166 LAFVKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKEQI 220
Cdd:cd07644   161 QAFLKESQRAAELEEKRRYRFLAEKHYLLNNTFLQFQSRARGMLQTRVPSWKEQP 215
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
16-223 2.82e-73

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 230.53  E-value: 2.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  16 YKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTASAGLNIVFQT 95
Cdd:pfam08397   1 YKTIMEQFNPALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRGSRELGSALTQMCMRHRSIESKLEQFVQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  96 LHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQRDR-------NLREMKENVNMLHNDMLAF 168
Cdd:pfam08397  81 FHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKgkgdqqpQLDEALQDVNDKYLLLEET 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785364863 169 VKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKEQIDAS 223
Cdd:pfam08397 161 VSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEAITHLQNIVLLWKELTSEP 215
SH3_BAIAP2L2 cd11914
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; ...
312-370 1.91e-35

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212847 [Multi-domain]  Cd Length: 59  Bit Score: 125.70  E-value: 1.91e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364863 312 RRVQAIVDHNTGGNRTLLQFKKADIITVLVPEARNGWLYGKLEGLSMNGWFPEAYVKSM 370
Cdd:cd11914     1 RRVRAIVSHPAGSNPTLLRFNRGDIITVLVPEARNGWLYGKLEGSSRQGWFPEAYVKAL 59
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
312-368 8.49e-06

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 42.91  E-value: 8.49e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785364863  312 RRVQAIVDHnTGGNRTLLQFKKADIITVLvPEARNGWLYGKLEGLSMnGWFPEAYVK 368
Cdd:smart00326   3 PQVRALYDY-TAQDPDELSFKKGDIITVL-EKSDDGWWKGRLGRGKE-GLFPSNYVE 56
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
313-368 7.74e-05

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 40.27  E-value: 7.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785364863 313 RVQAIVDHNtGGNRTLLQFKKADIITVLvPEARNGWLYGKLEGlsMNGWFPEAYVK 368
Cdd:pfam07653   1 YGRVIFDYV-GTDKNGLTLKKGDVVKVL-GKDNDGWWEGETGG--RVGLVPSTAVE 52
 
Name Accession Description Interval E-value
I-BAR_IMD_BAIAP2L2 cd07644
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
6-220 7.32e-138

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. This group is composed of uncharacterized proteins known as BAIAP2L2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2). They contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153328  Cd Length: 215  Bit Score: 395.06  E-value: 7.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863   6 DSIYASTIGTYKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTA 85
Cdd:cd07644     1 DLLYRSTISIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIAKIGEQALQSLTSQSLGEILIQMSETQRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  86 SAGLNIVFQTLHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQRDRNLREMKENVNMLHNDM 165
Cdd:cd07644    81 SADLEVVFQTFHVDLLQHMDKNTKLDMQFIEDSRRVYELEYRHRAANLEKCMSELWRMERQRDRNVREMKENVNRLRQSM 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785364863 166 LAFVKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKEQI 220
Cdd:cd07644   161 QAFLKESQRAAELEEKRRYRFLAEKHYLLNNTFLQFQSRARGMLQTRVPSWKEQP 215
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
16-223 2.82e-73

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 230.53  E-value: 2.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  16 YKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTASAGLNIVFQT 95
Cdd:pfam08397   1 YKTIMEQFNPALENFIYKGNNYLSALRTTVEAAEAYFDAFQKVGEMATNSRGSRELGSALTQMCMRHRSIESKLEQFVQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  96 LHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQRDR-------NLREMKENVNMLHNDMLAF 168
Cdd:pfam08397  81 FHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSELLKLQKKADKgkgdqqpQLDEALQDVNDKYLLLEET 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785364863 169 VKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKEQIDAS 223
Cdd:pfam08397 161 VSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEAITHLQNIVLLWKELTSEP 215
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
6-220 2.97e-67

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 214.92  E-value: 2.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863   6 DSIYASTIGTYKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTA 85
Cdd:cd07605     1 EELNRLTENIYKNIKEQFNPVLRNLIKAGKKYQKALQALSQAAKVFFDALAKIGELASQSRGSQELGEALKQIVDTHKSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  86 SAGLNIVFQTLHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQ--------RDRNLREMKEN 157
Cdd:cd07605    81 EASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSELKKLQKKsqksgtgkYQEKLDQALEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785364863 158 VNMLHNDMLAFVKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKEQI 220
Cdd:cd07605   161 LNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYHAKAMTLLSTRLPLWQELC 223
I-BAR_IMD_BAIAP2L1 cd07645
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific ...
6-218 2.25e-37

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. BAIAP2L1 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1) is also known as IRTKS (Insulin Receptor Tyrosine Kinase Substrate). It is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. It contains an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The IMD domain of BAIAP2L1 binds and bundles actin filaments, and binds the small GTPase Rac.


Pssm-ID: 153329  Cd Length: 226  Bit Score: 136.59  E-value: 2.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863   6 DSIYASTIGTYKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTA 85
Cdd:cd07645     1 DEVNKLTESTYKNVMEQFNPGLRNLINLGKNYEKAVNAMVLAGKAYYDGVAKIGEIAAVSPVSKELGHVLMEISDVHKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  86 SAGLNIVFQTLHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMER--QRDRNLR--EMKEN---- 157
Cdd:cd07645    81 NDSLEENFKKFHREIIAELERKTDLDVKYMTATLKRYQTEHKNKLDSLEKSQADLKKIRRksQGRRNASkyEHKENeyle 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785364863 158 -VNMLHNDMLAFVKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKE 218
Cdd:cd07645   161 tVTSRQSDIQKFIADGCREALLEEKRRFCFLVDKHCSFSNHIHYFHQQAAELLNSKLPVWQE 222
SH3_BAIAP2L2 cd11914
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; ...
312-370 1.91e-35

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 2; BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The related proteins, BAIAP2L1 and IRSp53, function as regulators of membrane dynamics and the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212847 [Multi-domain]  Cd Length: 59  Bit Score: 125.70  E-value: 1.91e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785364863 312 RRVQAIVDHNTGGNRTLLQFKKADIITVLVPEARNGWLYGKLEGLSMNGWFPEAYVKSM 370
Cdd:cd11914     1 RRVRAIVSHPAGSNPTLLRFNRGDIITVLVPEARNGWLYGKLEGSSRQGWFPEAYVKAL 59
I-BAR_IMD_IRSp53 cd07646
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor ...
6-218 7.75e-35

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor tyrosine kinase Substrate p53; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. IRSp53 (Insulin Receptor tyrosine kinase Substrate p53) is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. Its IMD domain binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153330  Cd Length: 232  Bit Score: 130.05  E-value: 7.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863   6 DSIYASTIGTYKKILGQFNPALENLVYLGNNYLRALNALSEVAETYYNAIKKIGEQALQNVTCQGLGQLLIQMAEHCRTA 85
Cdd:cd07646     3 EEVNRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALASVTFAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785364863  86 SAGLNIVFQTLHGDIVQQMDKNTKLDMQFITDSQNRYEIEYRHRSANLEKCMSEAWKMERQ-------RDRNLREMK--E 156
Cdd:cd07646    83 QNQLEEMLKSFHNELLTQLEQKVELDSRYLTAALKKYQTEHRSKGESLEKCQAELKKLRKKsqgsknpQKYSDKELQyiE 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785364863 157 NVNMLHNDMLAFVKESQRAAELEEKRRYRFLAEKHWLLCSSFLQYHSRAQGLLQARVPPWKE 218
Cdd:cd07646   163 AISNKQGELENYVSDGYKTALTEERRRYCFLVEKQCAVAKNSIAYHSKGKELLTQKLPSWQQ 224
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
312-369 9.14e-20

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 82.76  E-value: 9.14e-20
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gi 1785364863 312 RRVQAIVDHnTGGNRTLLQFKKADIITVLVPEARNGWLYGKLEGLSMNGWFPEAYVKS 369
Cdd:cd11779     1 PRVKALYPH-AAGGETQLSFEEGDVITLLGPEPRDGWHYGENERSGRRGWFPIAYTEP 57
SH3_Irsp53 cd11915
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known ...
313-370 7.22e-19

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53; IRSp53 is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 can also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRSp53 has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212848  Cd Length: 59  Bit Score: 80.06  E-value: 7.22e-19
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gi 1785364863 313 RVQAIVDHNTGGNRTLLQFKKADIITVLVPEARNGWLYGKLEGLSMNGWFPEAYVKSM 370
Cdd:cd11915     2 RVQAIFSHAAGDNSTLLSFKEGDYITLLVPEARDGWHYGECEKTKMRGWFPFSYTRVL 59
SH3_BAIAP2L1 cd11913
Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, ...
312-369 1.90e-17

Src Homology 3 domain of Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-Like 1, also called Insulin Receptor Tyrosine Kinase Substrate (IRTKS); BAIAP2L1 or IRTKS is widely expressed, serves as a substrate for the insulin receptor, and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. BAIAP2L1 expression leads to the formation of short actin bundles, distinct from filopodia-like protrusions induced by the expression of the related protein IRSp53. IRTKS mediates the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. It contains an N-terminal IMD or Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. The SH3 domain of IRTKS has been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212846  Cd Length: 58  Bit Score: 76.11  E-value: 1.90e-17
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gi 1785364863 312 RRVQAIVDHNTGGNRTLLQFKKADIITVLVPEARNGWLYGKLEGLSMNGWFPEAYVKS 369
Cdd:cd11913     1 QKVKTIFPHTAGNNKTLLSFAQGDVITLLIPEEKDGWLYGEHDTTKARGWFPSSYTRP 58
SH3_Intersectin_2 cd11837
Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor ...
329-368 3.35e-07

Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212771 [Multi-domain]  Cd Length: 53  Bit Score: 46.98  E-value: 3.35e-07
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gi 1785364863 329 LQFKKADIITVLvpEARNGWLYGKLEGLSmNGWFPEAYVK 368
Cdd:cd11837    16 LSFAKGDIITVL--EQQEMWWFGELEGGE-EGWFPKSYVK 52
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
325-367 4.50e-07

Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212817 [Multi-domain]  Cd Length: 56  Bit Score: 46.55  E-value: 4.50e-07
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gi 1785364863 325 NRTLLQFKKADIITvLVPEARN---GWLYGKLEGLSmnGWFPEAYV 367
Cdd:cd11884    12 DQTLLSFHKGDVIK-LLPKEGPldpGWLFGTLDGRS--GAFPKEYV 54
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
313-366 3.87e-06

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 43.99  E-value: 3.87e-06
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gi 1785364863 313 RVQAIVDHnTGGNRTLLQFKKADIITVLvPEARNGWLYGKLEGLSMnGWFPEAY 366
Cdd:cd00174     1 YARALYDY-EAQDDDELSFKKGDIITVL-EKDDDGWWEGELNGGRE-GLFPANY 51
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
314-368 4.81e-06

Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212810 [Multi-domain]  Cd Length: 53  Bit Score: 43.84  E-value: 4.81e-06
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gi 1785364863 314 VQAIVDHnTGGNRTLLQFKKADIITVlVPEARNGWLYGKLEGlsMNGWFPEAYVK 368
Cdd:cd11877     2 VRAKFNF-EGTNEDELSFDKGDIITV-TQVVEGGWWEGTLNG--KTGWFPSNYVK 52
SH3_Intersectin2_2 cd11990
Second Src homology 3 domain (or SH3B) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
329-368 7.62e-06

Second Src homology 3 domain (or SH3B) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212923 [Multi-domain]  Cd Length: 52  Bit Score: 43.11  E-value: 7.62e-06
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gi 1785364863 329 LQFKKADIITVLvpEARNGWLYGKLEGlsMNGWFPEAYVK 368
Cdd:cd11990    16 LNFSKNDIITVL--EQQENWWFGEVHG--GRGWFPKSYVK 51
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
312-368 8.49e-06

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 42.91  E-value: 8.49e-06
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gi 1785364863  312 RRVQAIVDHnTGGNRTLLQFKKADIITVLvPEARNGWLYGKLEGLSMnGWFPEAYVK 368
Cdd:smart00326   3 PQVRALYDY-TAQDPDELSFKKGDIITVL-EKSDDGWWKGRLGRGKE-GLFPSNYVE 56
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
329-367 1.14e-05

First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212770 [Multi-domain]  Cd Length: 55  Bit Score: 42.73  E-value: 1.14e-05
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gi 1785364863 329 LQFKKADIITV-LVPEARNGWLYGKLEGLSmnGWFPEAYV 367
Cdd:cd11836    16 ISFQPGDIIQVdESQVAEPGWLAGELKGKT--GWFPANYV 53
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
313-368 7.74e-05

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 40.27  E-value: 7.74e-05
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gi 1785364863 313 RVQAIVDHNtGGNRTLLQFKKADIITVLvPEARNGWLYGKLEGlsMNGWFPEAYVK 368
Cdd:pfam07653   1 YGRVIFDYV-GTDKNGLTLKKGDVVKVL-GKDNDGWWEGETGG--RVGLVPSTAVE 52
SH3_Intersectin1_2 cd11989
Second Src homology 3 domain (or SH3B) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
329-368 9.43e-05

Second Src homology 3 domain (or SH3B) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212922 [Multi-domain]  Cd Length: 52  Bit Score: 40.08  E-value: 9.43e-05
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gi 1785364863 329 LQFKKADIITVLvpEARNGWLYGKLEGlsMNGWFPEAYVK 368
Cdd:cd11989    16 LNFNKNDVITVL--EQQDMWWFGEVQG--QKGWFPKSYVK 51
SH3_VAV1_2 cd11976
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ...
325-368 4.73e-04

C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The C-terminal SH3 domain of Vav1 interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212909 [Multi-domain]  Cd Length: 54  Bit Score: 38.00  E-value: 4.73e-04
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gi 1785364863 325 NRTLLQFKKADIITVLVPEARNGWLYGKLEGLSmnGWFPEAYVK 368
Cdd:cd11976    12 DRSELSLKEGDIIKILNKKGQQGWWRGEIYGRV--GWFPANYVE 53
SH3_GAS7 cd11829
Src homology 3 domain of Growth Arrest Specific protein 7; GAS7 is mainly expressed in the ...
329-367 5.69e-04

Src homology 3 domain of Growth Arrest Specific protein 7; GAS7 is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212763 [Multi-domain]  Cd Length: 52  Bit Score: 37.88  E-value: 5.69e-04
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gi 1785364863 329 LQFKKADIITVL-VPEarNGWLYGKLEGlsMNGWFPEAYV 367
Cdd:cd11829    17 LSFEAGELIRVLqAPD--GGWWEGEKDG--LRGWFPASYV 52
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
312-370 7.94e-04

C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212867 [Multi-domain]  Cd Length: 59  Bit Score: 37.67  E-value: 7.94e-04
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gi 1785364863 312 RRVQAIVDHNtGGNRTLLQFKKADIItVLVPEARNGWLYGKLEGLSMNGWFPEAYVKSM 370
Cdd:cd11934     3 KRYRAVYDYN-AADEDEVSFQDGDTI-VNVQQIDDGWMYGTVERTGDTGMLPANYVEAI 59
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
314-366 1.22e-03

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 36.88  E-value: 1.22e-03
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gi 1785364863 314 VQAIVDHNTGgNRTLLQFKKADIITVLVPEArNGWLYGKLEGLSMN---GWFPEAY 366
Cdd:cd11883     2 VVALYDFTPK-SKNQLSFKAGDIIYVLNKDP-SGWWDGVIISSSGKvkrGWFPSNY 55
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
329-368 1.72e-03

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212815 [Multi-domain]  Cd Length: 54  Bit Score: 36.50  E-value: 1.72e-03
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gi 1785364863 329 LQFKKADIITVLVPEARNGWLYGKLEGLSmnGWFPEAYVK 368
Cdd:cd11882    16 LSFEPGQIITNVQPSDEPGWLEGTLNGRT--GLIPENYVE 53
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
314-366 1.98e-03

Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212712 [Multi-domain]  Cd Length: 51  Bit Score: 36.32  E-value: 1.98e-03
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gi 1785364863 314 VQAIVDHNTGGNRTLlQFKKADIITVLVPEARNGWLYGKLEGLsmNGWFPEAY 366
Cdd:cd11778     2 VEALYDYEAQGDDEI-SIRVGDRIAVIRGDDGSGWTYGEINGV--KGLFPTSY 51
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
313-368 2.14e-03

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 36.54  E-value: 2.14e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785364863 313 RVQAIVDHnTGGNRTLLQFKKADIITVlVP-----EARNGWLYGKLEGLSMNGWFPEAYVK 368
Cdd:cd11790     4 KVRATHDY-TAEDTDELTFEKGDVILV-IPfddpeEQDEGWLMGVKESTGCRGVFPENFTE 62
SH3_SGSM3 cd11813
Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called ...
329-368 2.38e-03

Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called Merlin-associated protein (MAP), RUN and SH3 domain-containing protein (RUSC3), RUN and TBC1 domain-containing protein 3 (RUTBC3), Rab GTPase-activating protein 5 (RabGAP5), or Rab GAP-like protein (RabGAPLP). It is expressed ubiquitously and functions as a regulator of small G protein RAP- and RAB-mediated neuronal signaling. It is involved in modulating NGF-mediated neurite outgrowth and differentiation. It also interacts with the tumor suppressor merlin and may play a role in the merlin-associated suppression of cell growth. SGSM3 contains TBC, SH3, and RUN domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212747  Cd Length: 53  Bit Score: 35.94  E-value: 2.38e-03
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gi 1785364863 329 LQFKKADIITVLVPEARNGWLyGKLEGLsmNGWFPEAYVK 368
Cdd:cd11813    16 LGFRKNDIITIISQKDEHCWV-GELNGL--RGWFPAKFVE 52
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
329-368 3.75e-03

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 35.44  E-value: 3.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1785364863 329 LQFKKADIITVLVPEArNGWLYGKLEGLSMNGWFPEAYVK 368
Cdd:cd11858    16 LSLKKDDIVYIVQKED-NGWWLAKKLDESKEGWVPAAYLE 54
SH3_VAV_2 cd11830
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ...
325-368 3.99e-03

C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212764 [Multi-domain]  Cd Length: 54  Bit Score: 35.68  E-value: 3.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1785364863 325 NRTLLQFKKADIITVLVPEARNGWLYGKLEGLSmnGWFPEAYVK 368
Cdd:cd11830    12 DMRELSLKEGDVVKIYNKKGQQGWWRGEINGRI--GWFPSTYVE 53
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
314-368 7.22e-03

Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212762 [Multi-domain]  Cd Length: 53  Bit Score: 34.66  E-value: 7.22e-03
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                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785364863 314 VQAIVDHNTGGNRTLlQFKKADIITVLVPEARNgWLYGKLEglSMNGWFPEAYVK 368
Cdd:cd11828     2 AEALWDHVTMDPEEL-GFKAGDVIEVLDMSDKD-WWWGSIR--DEEGWFPASFVR 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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