NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148225136|ref|NP_001084045|]
View 

catenin beta-1 [Xenopus laevis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CTNNAbd_CTNNB1 cd21724
alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, ...
78-151 1.73e-45

alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, it forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues, and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes. CTNNB1 is involved in the regulation of cell adhesion as a component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. This model corresponds to a small region at the C-terminus of CTNNB1, which is responsible for alpha-catenin binding.


:

Pssm-ID: 439241  Cd Length: 74  Bit Score: 156.96  E-value: 1.73e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148225136  78 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 151
Cdd:cd21724    1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
350-390 2.03e-06

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


:

Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 45.11  E-value: 2.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 148225136   350 CSSNKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 390
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
585-622 3.55e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


:

Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 41.29  E-value: 3.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148225136  585 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELA 622
Cdd:pfam00514   3 ENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
230-262 7.92e-05

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


:

Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 40.49  E-value: 7.92e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 148225136   230 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 262
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
216-661 1.31e-04

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.86  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  216 GTLHNLSHHREGLL-AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFL 294
Cdd:PLN03200  169 GALRNLCGSTDGFWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  295 -AITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSnkpAIVeAGGMQALGLHLTDS 373
Cdd:PLN03200  249 rAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGEL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  374 SQ--RLVQNCLWTLRNLSDAATKQEGMEG---------LLGTLVQLLGSDDINVV---TCAA-------GILSNLTCNNY 432
Cdd:PLN03200  325 SEspRSPAPIADTLGALAYALMVFDSSAEstrafdptvIEQILVKLLKPRDTKLVqerIIEAlaslygnAYLSRKLNHAE 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  433 KNKMMVC----QVGGI-EALVRTVL----------RA-GDREDI--------------TEPAICALRHLTSRHQEAEMAQ 482
Cdd:PLN03200  405 AKKVLVGlitmATADVqEELIRALSslccgkgglwEAlGGREGVqllisllglsseqqQEYAVALLAILTDEVDESKWAI 484
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  483 NAVRlhyGLPVVVKLLHPPSHwpliKA---TVGLIRNlaLCpaNH-----APLREQGAIPRLVQLLVRAHQDTQR----- 549
Cdd:PLN03200  485 TAAG---GIPPLVQLLETGSQ----KAkedSATVLWN--LC--CHsedirACVESAGAVPALLWLLKNGGPKGQEiaakt 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  550 -----RTSMGGTQQQfVEGVRMEEIVEGCTGAL----HILARDIHNRIVIRGL---NTIPLFVQLLYSPIENIQRVAAGV 617
Cdd:PLN03200  554 ltklvRTADAATISQ-LTALLLGDLPESKVHVLdvlgHVLSVASLEDLVREGSaanDALRTLIQLLSSSKEETQEKAASV 632
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 148225136  618 LCEL-AQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAA---AVLFR 661
Cdd:PLN03200  633 LADIfSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSAralAALSR 680
 
Name Accession Description Interval E-value
CTNNAbd_CTNNB1 cd21724
alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, ...
78-151 1.73e-45

alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, it forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues, and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes. CTNNB1 is involved in the regulation of cell adhesion as a component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. This model corresponds to a small region at the C-terminus of CTNNB1, which is responsible for alpha-catenin binding.


Pssm-ID: 439241  Cd Length: 74  Bit Score: 156.96  E-value: 1.73e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148225136  78 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 151
Cdd:cd21724    1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
350-390 2.03e-06

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 45.11  E-value: 2.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 148225136   350 CSSNKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 390
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
353-390 1.30e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.83  E-value: 1.30e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148225136  353 NKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 390
Cdd:pfam00514   4 NKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
585-622 3.55e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 41.29  E-value: 3.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148225136  585 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELA 622
Cdd:pfam00514   3 ENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
230-262 7.92e-05

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 40.49  E-value: 7.92e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 148225136   230 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 262
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
216-661 1.31e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.86  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  216 GTLHNLSHHREGLL-AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFL 294
Cdd:PLN03200  169 GALRNLCGSTDGFWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  295 -AITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSnkpAIVeAGGMQALGLHLTDS 373
Cdd:PLN03200  249 rAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGEL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  374 SQ--RLVQNCLWTLRNLSDAATKQEGMEG---------LLGTLVQLLGSDDINVV---TCAA-------GILSNLTCNNY 432
Cdd:PLN03200  325 SEspRSPAPIADTLGALAYALMVFDSSAEstrafdptvIEQILVKLLKPRDTKLVqerIIEAlaslygnAYLSRKLNHAE 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  433 KNKMMVC----QVGGI-EALVRTVL----------RA-GDREDI--------------TEPAICALRHLTSRHQEAEMAQ 482
Cdd:PLN03200  405 AKKVLVGlitmATADVqEELIRALSslccgkgglwEAlGGREGVqllisllglsseqqQEYAVALLAILTDEVDESKWAI 484
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  483 NAVRlhyGLPVVVKLLHPPSHwpliKA---TVGLIRNlaLCpaNH-----APLREQGAIPRLVQLLVRAHQDTQR----- 549
Cdd:PLN03200  485 TAAG---GIPPLVQLLETGSQ----KAkedSATVLWN--LC--CHsedirACVESAGAVPALLWLLKNGGPKGQEiaakt 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  550 -----RTSMGGTQQQfVEGVRMEEIVEGCTGAL----HILARDIHNRIVIRGL---NTIPLFVQLLYSPIENIQRVAAGV 617
Cdd:PLN03200  554 ltklvRTADAATISQ-LTALLLGDLPESKVHVLdvlgHVLSVASLEDLVREGSaanDALRTLIQLLSSSKEETQEKAASV 632
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 148225136  618 LCEL-AQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAA---AVLFR 661
Cdd:PLN03200  633 LADIfSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSAralAALSR 680
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
230-262 2.06e-04

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 39.36  E-value: 2.06e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 148225136  230 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 262
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
585-623 8.82e-04

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 37.41  E-value: 8.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 148225136   585 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQ 623
Cdd:smart00185   3 ENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
431-473 1.40e-03

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 37.05  E-value: 1.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148225136  431 NYKNKMMVCQVGGIEALVRtVLRAGDrEDITEPAICALRHLTS 473
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVR-LLSSPD-EEVQEEAAWALSNLAA 41
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
431-473 4.99e-03

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 35.48  E-value: 4.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 148225136   431 NYKNKMMVCQVGGIEALVRTVLRagDREDITEPAICALRHLTS 473
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKS--EDEEVVKEAAWALSNLSS 41
 
Name Accession Description Interval E-value
CTNNAbd_CTNNB1 cd21724
alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, ...
78-151 1.73e-45

alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, it forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues, and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes. CTNNB1 is involved in the regulation of cell adhesion as a component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. This model corresponds to a small region at the C-terminus of CTNNB1, which is responsible for alpha-catenin binding.


Pssm-ID: 439241  Cd Length: 74  Bit Score: 156.96  E-value: 1.73e-45
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148225136  78 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 151
Cdd:cd21724    1 QVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74
CTNNAbd_dArm cd21726
alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity ...
77-151 2.75e-41

alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity protein (dArm) and similar proteins; dArm is a Drosophila catenin that plays a role during central nervous system development. It can associate with alpha-catenin. The neural isoform of dArm may associate with CadN and participate in the transmission of developmental information. Its cytoplasmic isoform accumulates through Wingless (Wg) signaling; arm function in Wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis. This model corresponds to a small region at the C-terminus of dArm, which shows high sequence similarity with alpha-catenin binding domain of catenin beta-1 (CTNNB1).


Pssm-ID: 439243  Cd Length: 75  Bit Score: 145.25  E-value: 2.75e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148225136  77 DQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 151
Cdd:cd21726    1 EQVDEMNQQLNQTRSQRVRAAMFPETLEEGVQIPSTQFDPQQPTAVQRLAEPSQMLKHAVVNLINYQDDADLATR 75
CTNNAbd_CTNNB1-like cd21719
alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and ...
82-151 5.91e-39

alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and similar proteins; This family includes alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG), as well as Drosophila melanogaster armadillo segment polarity protein (dArm). CTNNB1, also called beta-catenin, is a key downstream component of the canonical Wnt signaling pathway. It is involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. It acts as a negative regulator of centrosome cohesion. It is involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. It blocks anoikis of malignant kidney and intestinal epithelial cells, and promotes their anchorage-independent growth by down-regulating DAPK2. It disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. CTNNG, also called junction plakoglobin (JUP), or desmoplakin III, or desmoplakin-3 (DP3), is a common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. CTNNG acts as a substrate for VE-PTP and is required to stimulate VE-cadherin function in endothelial cells. It can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. dArm, which shows high sequence similarity with CTNNB1, is a Drosophila catenin that plays a role during central nervous system development. It can associate with alpha-catenin. Its neural isoform may associate with CadN and participate in the transmission of developmental information. Its cytoplasmic isoform accumulates through Wingless (Wg) signaling; arm function in Wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis. This model corresponds to a small region at the C-termini of dArm, CTNNB1 and CTNNG; in CTNNB1, this region is responsible for alpha-catenin binding.


Pssm-ID: 439240  Cd Length: 70  Bit Score: 138.19  E-value: 5.91e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  82 IDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 151
Cdd:cd21719    1 LNDQLTQTRAQRVRAAMFPETLDEGEEIPSTQFDPGRSTNVQRLAEPSQLLKTAVVNLINYQDDADLATR 70
CTNNAbd_CTNNG cd21725
alpha-catenin binding domain found in catenin gamma (CTNNG) and similar proteins; CTNNG, also ...
82-151 1.89e-30

alpha-catenin binding domain found in catenin gamma (CTNNG) and similar proteins; CTNNG, also called junction plakoglobin (JUP), or desmoplakin III, or desmoplakin-3 (DP3), is a common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. CTNNG acts as a substrate for VE-PTP and is required to stimulate VE-cadherin function in endothelial cells. It can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. This model corresponds to a small region at the C-terminus of CTNNG, which shows high sequence similarity with alpha-catenin binding domain of catenin beta-1 (CTNNB1).


Pssm-ID: 439242  Cd Length: 70  Bit Score: 114.20  E-value: 1.89e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  82 IDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 151
Cdd:cd21725    1 MESQLTMTRAQRVRAAMFPETVEEGSYLLSTQIEPSQQTNVQKLAEPSQMLKSAIVHLINYQDDAELATR 70
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
350-390 2.03e-06

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 45.11  E-value: 2.03e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 148225136   350 CSSNKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 390
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
353-390 1.30e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 42.83  E-value: 1.30e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148225136  353 NKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSD 390
Cdd:pfam00514   4 NKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
585-622 3.55e-05

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 41.29  E-value: 3.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148225136  585 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELA 622
Cdd:pfam00514   3 ENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
230-262 7.92e-05

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 40.49  E-value: 7.92e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 148225136   230 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 262
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
216-661 1.31e-04

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 45.86  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  216 GTLHNLSHHREGLL-AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFL 294
Cdd:PLN03200  169 GALRNLCGSTDGFWsATLEAGGVDILVKLLSSGNSDAQANAASLLARLMMAFESSISKVLDAGAVKQLLKLLGQGNEVSV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  295 -AITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSnkpAIVeAGGMQALGLHLTDS 373
Cdd:PLN03200  249 rAEAAGALEALSSQSKEAKQAIADAGGIPALINATVAPSKEFMQGEFAQALQENAMGAL---ANI-CGGMSALILYLGEL 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  374 SQ--RLVQNCLWTLRNLSDAATKQEGMEG---------LLGTLVQLLGSDDINVV---TCAA-------GILSNLTCNNY 432
Cdd:PLN03200  325 SEspRSPAPIADTLGALAYALMVFDSSAEstrafdptvIEQILVKLLKPRDTKLVqerIIEAlaslygnAYLSRKLNHAE 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  433 KNKMMVC----QVGGI-EALVRTVL----------RA-GDREDI--------------TEPAICALRHLTSRHQEAEMAQ 482
Cdd:PLN03200  405 AKKVLVGlitmATADVqEELIRALSslccgkgglwEAlGGREGVqllisllglsseqqQEYAVALLAILTDEVDESKWAI 484
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  483 NAVRlhyGLPVVVKLLHPPSHwpliKA---TVGLIRNlaLCpaNH-----APLREQGAIPRLVQLLVRAHQDTQR----- 549
Cdd:PLN03200  485 TAAG---GIPPLVQLLETGSQ----KAkedSATVLWN--LC--CHsedirACVESAGAVPALLWLLKNGGPKGQEiaakt 553
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225136  550 -----RTSMGGTQQQfVEGVRMEEIVEGCTGAL----HILARDIHNRIVIRGL---NTIPLFVQLLYSPIENIQRVAAGV 617
Cdd:PLN03200  554 ltklvRTADAATISQ-LTALLLGDLPESKVHVLdvlgHVLSVASLEDLVREGSaanDALRTLIQLLSSSKEETQEKAASV 632
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 148225136  618 LCEL-AQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAA---AVLFR 661
Cdd:PLN03200  633 LADIfSSRQDLCESLATDEIINPCIKLLTNNTEAVATQSAralAALSR 680
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
230-262 2.06e-04

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 39.36  E-value: 2.06e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 148225136  230 AIFKSGGIPALVKMLGSPVDSVLFYAITTLHNL 262
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
585-623 8.82e-04

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 37.41  E-value: 8.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 148225136   585 HNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQ 623
Cdd:smart00185   3 ENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
431-473 1.40e-03

Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form super-helix of helices that is proposed to mediate interaction of beta-catenin with its ligands. CAUTION: This family does not contain all known armadillo repeats.


Pssm-ID: 425727 [Multi-domain]  Cd Length: 41  Bit Score: 37.05  E-value: 1.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148225136  431 NYKNKMMVCQVGGIEALVRtVLRAGDrEDITEPAICALRHLTS 473
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVR-LLSSPD-EEVQEEAAWALSNLAA 41
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
431-473 4.99e-03

Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form superhelix of helices that is proposed to mediate interaction of beta-catenin with its ligands. Involved in transducing the Wingless/Wnt signal. In plakoglobin arm repeats bind alpha-catenin and N-cadherin.


Pssm-ID: 214547 [Multi-domain]  Cd Length: 41  Bit Score: 35.48  E-value: 4.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 148225136   431 NYKNKMMVCQVGGIEALVRTVLRagDREDITEPAICALRHLTS 473
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKS--EDEEVVKEAAWALSNLSS 41
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH