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Conserved domains on  [gi|1034599580|ref|XP_016880079|]
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junction plakoglobin isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CTNNAbd_CTNNB1-like super family cl45904
alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and ...
 73-142 2.20e-29

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.


The actual alignment was detected with superfamily member cd21725:

Pssm-ID: 459249  Cd Length: 70  Bit Score: 111.12  E-value: 2.20e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034599580  73 EYQMSTTARAKRVREAMCPGVSGEDSSLLlATQVEG-QATNLQRLAEPSQLLKSAIVHLINYQDDAELATR 142
Cdd:cd21725     1 MESQLTMTRAQRVRAAMFPETVEEGSYLL-STQIEPsQQTNVQKLAEPSQMLKSAIVHLINYQDDAELATR 70
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 341-381 1.76e-07

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: 47.81  E-value: 1.76e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034599580  341 CPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSD 381
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
PLN03200 super family cl33659
cellulose synthase-interactive protein; Provisional
 328-658 1.47e-05

cellulose synthase-interactive protein; Provisional


The actual alignment was detected with superfamily member PLN03200:

Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 48.95  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  328 LWttsrVLKVL-SVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNC------------LWTLRNLSDVaTKQEGLESVLK 394
Cdd:PLN03200   978 LW----LLSVIaSHDAKSKLAIMEAGGIEVLTEKLASYTSNRQAEFedsesiwisallLAILFQDRDV-VRAPATMRAIP 1052

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  395 ILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSG-VEALIHAILRAgdKDDItePAVCALRHLTS--RHPEAEM 471
Cdd:PLN03200  1053 SLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGaVGGLISLLGCA--ESDI--SNLVALSEEFSlvRNPDQVA 1128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  472 AQNSVRLN---YG------IPAIVKLL----NQPNQWPLvkaTIGLIRNLAL-CPANHAPLQEAAVIPRLVQLLVKAHQD 537
Cdd:PLN03200  1129 LERLFRVEdirVGatarkaIPLLVDLLkpipDRPGAPPL---ALGLLTQLAEgSDVNKLAMAEAGALDALTKYLSLGPQD 1205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  538 AQrhvaagtqqpytdgvrmEEIVegcTGALHILARDPmnrmEIFR----LNTIPLFVQLLYSSVENIQRVAAGVLCELAQ 613
Cdd:PLN03200  1206 ST-----------------EEAA---SELLRILFSSP----ELRRhesaFGAVNQLVAVLRLGSRSARYSAARALQELFS 1261

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034599580  614 DKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNP 658
Cdd:PLN03200  1262 AEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPS 1306
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 221-253 2.92e-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: 41.67  E-value: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034599580 221 AIFKSGGIPALVRMLSSPVESVLFYAITTLHNL 253
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39
 
Name Accession Description Interval E-value
CTNNAbd_CTNNG cd21725
alpha-catenin binding domain found in catenin gamma (CTNNG) and similar proteins; CTNNG, also ...
 73-142 2.20e-29

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: 111.12  E-value: 2.20e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034599580  73 EYQMSTTARAKRVREAMCPGVSGEDSSLLlATQVEG-QATNLQRLAEPSQLLKSAIVHLINYQDDAELATR 142
Cdd:cd21725     1 MESQLTMTRAQRVRAAMFPETVEEGSYLL-STQIEPsQQTNVQKLAEPSQMLKSAIVHLINYQDDAELATR 70
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 341-381 1.76e-07

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: 47.81  E-value: 1.76e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034599580  341 CPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSD 381
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 341-381 2.02e-07

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: 47.83  E-value: 2.02e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034599580 341 CPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSD 381
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 328-658 1.47e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 48.95  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  328 LWttsrVLKVL-SVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNC------------LWTLRNLSDVaTKQEGLESVLK 394
Cdd:PLN03200   978 LW----LLSVIaSHDAKSKLAIMEAGGIEVLTEKLASYTSNRQAEFedsesiwisallLAILFQDRDV-VRAPATMRAIP 1052

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  395 ILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSG-VEALIHAILRAgdKDDItePAVCALRHLTS--RHPEAEM 471
Cdd:PLN03200  1053 SLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGaVGGLISLLGCA--ESDI--SNLVALSEEFSlvRNPDQVA 1128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  472 AQNSVRLN---YG------IPAIVKLL----NQPNQWPLvkaTIGLIRNLAL-CPANHAPLQEAAVIPRLVQLLVKAHQD 537
Cdd:PLN03200  1129 LERLFRVEdirVGatarkaIPLLVDLLkpipDRPGAPPL---ALGLLTQLAEgSDVNKLAMAEAGALDALTKYLSLGPQD 1205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  538 AQrhvaagtqqpytdgvrmEEIVegcTGALHILARDPmnrmEIFR----LNTIPLFVQLLYSSVENIQRVAAGVLCELAQ 613
Cdd:PLN03200  1206 ST-----------------EEAA---SELLRILFSSP----ELRRhesaFGAVNQLVAVLRLGSRSARYSAARALQELFS 1261

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034599580  614 DKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNP 658
Cdd:PLN03200  1262 AEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPS 1306
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 221-253 2.92e-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: 41.67  E-value: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034599580 221 AIFKSGGIPALVRMLSSPVESVLFYAITTLHNL 253
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 573-612 3.45e-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: 3.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034599580 573 DPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELA 612
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 221-253 6.21e-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: 40.88  E-value: 6.21e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034599580  221 AIFKSGGIPALVRMLSSPVESVLFYAITTLHNL 253
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 573-613 5.09e-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: 38.18  E-value: 5.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034599580  573 DPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQ 613
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
 120-524 3.75e-03

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 40.68  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 120 SQLLKSAIV---HLinYQDDAELATRALPELTKLLNDEDPVVVTKAAMivnqlskkeasrralmgspqLVAAVVRTMQNT 196
Cdd:pfam01602 128 PYVRKKAALailKL--YRKSPDLVRDFVPELKELLSDKDPGVQSAAVA--------------------LLYEICKNDRLY 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 197 SDLdtarcttsiLHNLSHHREGLLAIFKSGGIPALVRMLSS-----PVESVLFyaITTLHNLL-------LYqEGAKMAV 264
Cdd:pfam01602 186 LKL---------LPLLFRRLCNLLGVLNPWLQVKILRLLTRlapldPLLPKEL--LEDLLNLLqnsnnavLY-ETANTIV 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 265 RLADGLQKMVPLLNK---------NNPKFLAITTdcLQLLAYgnQESKLIilanggpQALVQIMRNYSYEKLLWTTSRVL 335
Cdd:pfam01602 254 HLAPAPELIVLAVNAlgrllsspdENLRYVALRN--LNKIVM--KEPKAV-------QHLDLIIFCLKTDDDISIRLRAL 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 336 KVLS--VCPSNKPAIveaggMQALGKHLTSNS-PRLVQNCLWTLRNLSD-VATKQeglESVLKILVNQLSVDDVNVLTCA 411
Cdd:pfam01602 323 DLLYalVNESNVKEI-----VKELLKYVHEIAdPDFKIELVRAIGRLAEkFPTDA---EWYLDVLLDLLSLAGSYVVDEI 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 412 TGTLSNLTCNNSKNK-----TLV--TQNSGVEALIHAIL----RAGDKDDITEPAVCALRHLTSRHpeaeMAQNSVRLNY 480
Cdd:pfam01602 395 VEVIRDIIQNVPELReyileHLCelLEDIESPEALAAALwilgEYGELIPNGSSPPDLLRSILEVF----VLESAKVRAA 470

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1034599580 481 GIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVI 524
Cdd:pfam01602 471 ALTALAKLGLTSPEETTQNLIIQLLLTLATQDSLDLEVRDRAVE 514
 
Name Accession Description Interval E-value
CTNNAbd_CTNNG cd21725
alpha-catenin binding domain found in catenin gamma (CTNNG) and similar proteins; CTNNG, also ...
 73-142 2.20e-29

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: 111.12  E-value: 2.20e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034599580  73 EYQMSTTARAKRVREAMCPGVSGEDSSLLlATQVEG-QATNLQRLAEPSQLLKSAIVHLINYQDDAELATR 142
Cdd:cd21725     1 MESQLTMTRAQRVRAAMFPETVEEGSYLL-STQIEPsQQTNVQKLAEPSQMLKSAIVHLINYQDDAELATR 70
CTNNAbd_CTNNB1-like cd21719
alpha-catenin binding domain found in catenin beta-1 (CTNNB1), catenin gamma (CTNNG) and ...
 75-142 1.75e-24

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: 96.97  E-value: 1.75e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034599580  75 QMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATR 142
Cdd:cd21719     3 DQLTQTRAQRVRAAMFPETLDEGEEIPSTQFDPGRSTNVQRLAEPSQLLKTAVVNLINYQDDADLATR 70
CTNNAbd_dArm cd21726
alpha-catenin binding domain found in Drosophila melanogaster armadillo segment polarity ...
 71-142 2.15e-16

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: 74.37  E-value: 2.15e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599580  71 DLEYQMSTTaRAKRVREAMCPGvSGEDSSLLLATQVE-GQATNLQRLAEPSQLLKSAIVHLINYQDDAELATR 142
Cdd:cd21726     5 EMNQQLNQT-RSQRVRAAMFPE-TLEEGVQIPSTQFDpQQPTAVQRLAEPSQMLKHAVVNLINYQDDADLATR 75
CTNNAbd_CTNNB1 cd21724
alpha-catenin binding domain found in catenin beta-1 (CTNNB1) and similar proteins; CTNNB1, ...
 70-142 2.94e-15

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: 71.06  E-value: 2.94e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034599580  70 GDLEYQMSTTaRAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATR 142
Cdd:cd21724     3 ADIDGQYAMT-RAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATR 74
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 341-381 1.76e-07

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: 47.81  E-value: 1.76e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034599580  341 CPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSD 381
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 341-381 2.02e-07

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: 47.83  E-value: 2.02e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034599580 341 CPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSD 381
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLAA 41
PLN03200 PLN03200
cellulose synthase-interactive protein; Provisional
 328-658 1.47e-05

cellulose synthase-interactive protein; Provisional


Pssm-ID: 215629 [Multi-domain]  Cd Length: 2102  Bit Score: 48.95  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  328 LWttsrVLKVL-SVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNC------------LWTLRNLSDVaTKQEGLESVLK 394
Cdd:PLN03200   978 LW----LLSVIaSHDAKSKLAIMEAGGIEVLTEKLASYTSNRQAEFedsesiwisallLAILFQDRDV-VRAPATMRAIP 1052

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  395 ILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSG-VEALIHAILRAgdKDDItePAVCALRHLTS--RHPEAEM 471
Cdd:PLN03200  1053 SLANLLKSEETIDRYFAAQALASLVCNGSRGTLLAVANSGaVGGLISLLGCA--ESDI--SNLVALSEEFSlvRNPDQVA 1128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  472 AQNSVRLN---YG------IPAIVKLL----NQPNQWPLvkaTIGLIRNLAL-CPANHAPLQEAAVIPRLVQLLVKAHQD 537
Cdd:PLN03200  1129 LERLFRVEdirVGatarkaIPLLVDLLkpipDRPGAPPL---ALGLLTQLAEgSDVNKLAMAEAGALDALTKYLSLGPQD 1205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580  538 AQrhvaagtqqpytdgvrmEEIVegcTGALHILARDPmnrmEIFR----LNTIPLFVQLLYSSVENIQRVAAGVLCELAQ 613
Cdd:PLN03200  1206 ST-----------------EEAA---SELLRILFSSP----ELRRhesaFGAVNQLVAVLRLGSRSARYSAARALQELFS 1261

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034599580  614 DKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNP 658
Cdd:PLN03200  1262 AEHIRDSELARQAVQPLVEMLNTGSESEQHAAIGALIKLSSGNPS 1306
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 221-253 2.92e-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: 41.67  E-value: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034599580 221 AIFKSGGIPALVRMLSSPVESVLFYAITTLHNL 253
Cdd:pfam00514   7 AVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNL 39
Arm pfam00514
Armadillo/beta-catenin-like repeat; Approx. 40 amino acid repeat. Tandem repeats form ...
 573-612 3.45e-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: 3.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034599580 573 DPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELA 612
Cdd:pfam00514   1 SPENKQAVIEAGAVPPLVRLLSSPDEEVQEEAAWALSNLA 40
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 221-253 6.21e-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: 40.88  E-value: 6.21e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034599580  221 AIFKSGGIPALVRMLSSPVESVLFYAITTLHNL 253
Cdd:smart00185   7 AVVDAGGLPALVELLKSEDEEVVKEAAWALSNL 39
ARM smart00185
Armadillo/beta-catenin-like repeats; Approx. 40 amino acid repeat. Tandem repeats form ...
 573-613 5.09e-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: 38.18  E-value: 5.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034599580  573 DPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQ 613
Cdd:smart00185   1 DDENKQAVVDAGGLPALVELLKSEDEEVVKEAAWALSNLSS 41
Adaptin_N pfam01602
Adaptin N terminal region; This family consists of the N terminal region of various alpha, ...
 120-524 3.75e-03

Adaptin N terminal region; This family consists of the N terminal region of various alpha, beta and gamma subunits of the AP-1, AP-2 and AP-3 adaptor protein complexes. The adaptor protein (AP) complexes are involved in the formation of clathrin-coated pits and vesicles. The N-terminal region of the various adaptor proteins (APs) is constant by comparison to the C-terminal which is variable within members of the AP-2 family; and it has been proposed that this constant region interacts with another uniform component of the coated vesicles.


Pssm-ID: 396262 [Multi-domain]  Cd Length: 523  Bit Score: 40.68  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 120 SQLLKSAIV---HLinYQDDAELATRALPELTKLLNDEDPVVVTKAAMivnqlskkeasrralmgspqLVAAVVRTMQNT 196
Cdd:pfam01602 128 PYVRKKAALailKL--YRKSPDLVRDFVPELKELLSDKDPGVQSAAVA--------------------LLYEICKNDRLY 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 197 SDLdtarcttsiLHNLSHHREGLLAIFKSGGIPALVRMLSS-----PVESVLFyaITTLHNLL-------LYqEGAKMAV 264
Cdd:pfam01602 186 LKL---------LPLLFRRLCNLLGVLNPWLQVKILRLLTRlapldPLLPKEL--LEDLLNLLqnsnnavLY-ETANTIV 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 265 RLADGLQKMVPLLNK---------NNPKFLAITTdcLQLLAYgnQESKLIilanggpQALVQIMRNYSYEKLLWTTSRVL 335
Cdd:pfam01602 254 HLAPAPELIVLAVNAlgrllsspdENLRYVALRN--LNKIVM--KEPKAV-------QHLDLIIFCLKTDDDISIRLRAL 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 336 KVLS--VCPSNKPAIveaggMQALGKHLTSNS-PRLVQNCLWTLRNLSD-VATKQeglESVLKILVNQLSVDDVNVLTCA 411
Cdd:pfam01602 323 DLLYalVNESNVKEI-----VKELLKYVHEIAdPDFKIELVRAIGRLAEkFPTDA---EWYLDVLLDLLSLAGSYVVDEI 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034599580 412 TGTLSNLTCNNSKNK-----TLV--TQNSGVEALIHAIL----RAGDKDDITEPAVCALRHLTSRHpeaeMAQNSVRLNY 480
Cdd:pfam01602 395 VEVIRDIIQNVPELReyileHLCelLEDIESPEALAAALwilgEYGELIPNGSSPPDLLRSILEVF----VLESAKVRAA 470

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1034599580 481 GIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVI 524
Cdd:pfam01602 471 ALTALAKLGLTSPEETTQNLIIQLLLTLATQDSLDLEVRDRAVE 514
 
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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