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Protein Page:
CTNNG (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CTNNG 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. Acts as a substrate for VE-PTP and is required by it to stimulate VE- cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton. Homodimer. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1 and gamma- catenin/JUP, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Interacts with MUC1. Interacts with CAV1. Interacts with PTPRJ. Interacts with DSC2. Belongs to the beta-catenin family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Cytoskeletal
Chromosomal Location of Human Ortholog: 17q21
Cellular Component: actin cytoskeleton; apicolateral plasma membrane; catenin complex; cell-cell adherens junction; cytoplasm; cytoskeleton; cytosol; desmosome; fascia adherens; focal adhesion; hemidesmosome; intercellular junction; intermediate filament; internal side of plasma membrane; lateral plasma membrane; nucleus; plasma membrane; Z disc; zonula adherens
Molecular Function: alpha-catenin binding; cadherin binding; cell adhesion molecule binding; protein binding; protein homodimerization activity; protein kinase binding; protein phosphatase binding; signal transducer activity; structural constituent of cell wall; structural molecule activity; transcription coactivator activity
Biological Process: cell migration; cell-cell adhesion; cytoskeletal anchoring; detection of mechanical stimulus; positive regulation of protein import into nucleus; positive regulation of transcription factor activity; protein heterooligomerization; regulation of cell proliferation; signal transduction; skin development
Disease: Arrhythmogenic Right Ventricular Dysplasia, Familial, 12; Naxos Disease
Reference #:  P14923 (UniProtKB)
Gene Symbols: JUP
Molecular weight: 81,745 Da
Basal Isoelectric point: 5.75  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CTNNG

Protein Structure Not Found.
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Sites Implicated In
transcription, induced: Y133‑p, Y550‑p, Y644‑p
molecular association, regulation: Y133‑p, Y550‑p, Y644‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 T14‑gl MEQPIKVtEWQQtyt
0 1 T19‑p KVtEWQQtytyDsGI
0 126 Y20‑p VtEWQQtytyDsGIH
0 9 T21‑p tEWQQtytyDsGIHS
0 55 Y22‑p EWQQtytyDsGIHSG
0 1 S24‑p QQtytyDsGIHSGAN
0 1 K40‑ub CVPSVSSkGIMEEDE
0 13 Y53‑p DEACGRQytLKKttt
0 28 T54‑p EACGRQytLKKttty
0 1 K56 CGRQytLKKtttytQ
0 1 K57 GRQytLKKtttytQG
0 3 T58‑p RQytLKKtttytQGV
0 3 T59‑p QytLKKtttytQGVP
0 3 T60‑p ytLKKtttytQGVPP
0 9 Y61‑p tLKKtttytQGVPPs
0 3 T62‑p LKKtttytQGVPPsQ
0 10 S68‑p ytQGVPPsQGDLEyQ
0 116 Y74‑p PsQGDLEyQMsTTAR
0 2 S77‑p GDLEyQMsTTARAKR
0 1 S94‑p EAMCPGVsGEDSsLL
0 2 S99‑p GVsGEDSsLLLATQV
0 2 S120‑p LQRLAEPsQLLksAI
0 3 K124‑ub AEPsQLLksAIVHLI
0 1 S125‑p EPsQLLksAIVHLIN
1 2 Y133‑p AIVHLINyQDDAELA
0 1 T141‑p QDDAELAtRALPELT
0 1 K149‑ub RALPELTkLLNDEDP
0 1 T160‑p DEDPVVVtkAAMIVN
0 2 K161‑ub EDPVVVtkAAMIVNQ
0 1 S170‑p AMIVNQLsKKEASRR
0 1 K171 MIVNQLsKKEASRRA
0 21 S182‑p SRRALMGsPQLVAAV
0 7 T196‑p VVRTMQNtsDLDTAR
0 1 S197‑p VRTMQNtsDLDTARC
0 1 T205 DLDTARCTTSILHNL
0 3 K224‑ub EGLLAIFkSGGIPAL
0 1 K326‑ac MRNYSYEkLLWTTSR
0 1 K345‑ub LSVCPSNkPAIVEAG
0 1 K385‑ub NLSDVATkQEGLESV
0 1 T430‑p SKNKTLVtQNSGVEA
0 2 K448‑ub AILRAGDkDDITEPA
0 1 T463‑p VCALRHLtSRHPEAE
0 106 Y480‑p QNSVRLNyGIPAIVK
0 8 K499‑ub PNQWPLVkATIGLIR
1 138 Y550‑p AAGTQQPytDGVRME
0 2 T551‑p AGTQQPytDGVRMEE
0 1 S596‑p FVQLLYSsVENIQRV
1 29 Y644‑p RNEGTATyAAAVLFR
0 159 Y660‑p SEDKNPDyRKRVsVE
1 24 S665‑p PDyRKRVsVELtNsL
0 1 T669‑p KRVsVELtNsLFKHD
0 3 S671‑p VsVELtNsLFKHDPA
0 1 Y693 MIPINEPYGDDMDAT
0 4 Y701‑p GDDMDATyRPMYSSD
0 5 Y724‑p HMDMDGDyPIDtysD
0 3 T728‑p DGDyPIDtysDGLRP
0 4 Y729‑p GDyPIDtysDGLRPP
0 1 S730‑p DyPIDtysDGLRPPY
  mouse

 
T14 IEQPIKVTEWQQTYT
T19 KVTEWQQTYTYDSGI
Y20 VTEWQQTYTYDSGIH
T21 TEWQQTYTYDSGIHS
Y22 EWQQTYTYDSGIHSG
S24 QQTYTYDSGIHSGVN
K40 CVPSVSSKGIMDEDD
Y53‑p DDACGRQytLkkTTT
T54‑p DACGRQytLkkTTTY
K56‑ac CGRQytLkkTTTYTQ
K57‑ub GRQytLkkTTTYTQG
T58 RQytLkkTTTYTQGV
T59 QytLkkTTTYTQGVP
T60 ytLkkTTTYTQGVPQ
Y61 tLkkTTTYTQGVPQN
T62 LkkTTTYTQGVPQNQ
N68 YTQGVPQNQGDLEYQ
Y74 QNQGDLEYQMsTTAR
S77‑p GDLEYQMsTTARAKR
S94 EAMCPGVSGEDSSLL
S99 GVSGEDSSLLLATQV
S120‑p LQRLAEPsQLLkSAI
K124‑ub AEPsQLLkSAIVHLI
S125 EPsQLLkSAIVHLIN
Y133 AIVHLINYQDDAELA
T141 QDDAELATRALPELT
K149 RALPELTKLLNDEDP
T160 DEDPVVVTKAAMIVN
K161 EDPVVVTKAAMIVNQ
S170 AMIVNQLSkKEASRR
K171‑ub MIVNQLSkKEASRRA
S182‑p SRRALMGsPQLVAAV
T196 VVRTMQNTSDLDTAR
S197 VRTMQNTSDLDTARC
T205‑p DLDTARCtTSILHNL
K224‑ub EGLLAIFkSGGIPAL
K326 MRNYSYEKLLWTTSR
K345 LSVCPSNKPAIVEAG
K385 NLSDVATKQEGLESV
T430 SKNKTLVTQNSGVEA
K448‑ub AILRAGDkDDITEPA
T463 VCALRHLTSRHPEAE
Y480‑p QNSVRLNyGIPAIVK
K499 PNQWPLVKATIGLIR
Y550 AAGTQQPYTDGVRME
T551 AGTQQPYTDGVRMEE
S596 FVQLLYSSVENIQRV
Y644 RNEGTATYAAAVLFR
Y660 SEDKNPDYRKRVsVE
S665‑p PDYRKRVsVELTNsL
T669 KRVsVELTNsLFKHD
S671‑p VsVELTNsLFKHDPA
Y693 MIPINEPYADDMDAT
Y701 ADDMDATYRPMYSSD
Y724 HMDLDGDYPMDTYSD
T728 DGDYPMDTYSDGLRP
Y729 GDYPMDTYSDGLRPP
S730 DYPMDTYSDGLRPPY
  rat

 
T14 IEQPIKVTEWQQTYT
T19 KVTEWQQTYTYDSGI
Y20 VTEWQQTYTYDSGIH
T21 TEWQQTYTYDSGIHS
Y22 EWQQTYTYDSGIHSG
S24 QQTYTYDSGIHSGVN
K40 CVPSVSSKGLLDEDD
Y53 DDTCGRQYTLKKTTT
T54 DTCGRQYTLKKTTTY
K56 CGRQYTLKKTTTYTQ
K57 GRQYTLKKTTTYTQG
T58 RQYTLKKTTTYTQGV
T59 QYTLKKTTTYTQGVP
T60 YTLKKTTTYTQGVPQ
Y61 TLKKTTTYTQGVPQS
T62 LKKTTTYTQGVPQSQ
S68 YTQGVPQSQGDLEYQ
Y74 QSQGDLEYQMSTTAR
S77 GDLEYQMSTTARAKR
S94 EAMCPGVSGEDSSLL
S99 GVSGEDSSLLLATQV
S120 LQRLAEPSQLLKSAI
K124 AEPSQLLKSAIVHLI
S125 EPSQLLKSAIVHLIN
Y133 AIVHLINYQDDAELA
T141 QDDAELATRALPELT
K149 RALPELTKLLNDEDP
T160 DEDPVVVTKAAMIVN
K161 EDPVVVTKAAMIVNQ
S170 AMIVNQLSKKEASRR
K171 MIVNQLSKKEASRRA
S182‑p SRRALMGsPQLVAAV
T196 VVRTMQNTSDLDTAR
S197 VRTMQNTSDLDTARC
T205 DLDTARCTTSILHNL
K224 EGLLAIFKSGGIPAL
K326 MRNYSYEKLLWTTSR
K345 LSVCPSNKPAIVEAG
K385 NLSDVATKQEGLENV
T430 SKNKTLVTQNSGVEA
K448 AILRAGDKDDITEPA
T463 VCALRHLTSRHPEAE
Y480 QNSVRLNYGIPAIVK
K499 PNQWPLVKATIGLIR
Y550 AAGTQQPYTDGVRME
T551 AGTQQPYTDGVRMEE
S596 FVQLLYSSVENIQRV
Y644‑p RNEGTATyAAAVLFR
Y660‑p SEDKNPDyRKRVsVE
S665‑p PDyRKRVsVELTNSL
T669 KRVsVELTNSLFKHD
S671 VsVELTNSLFKHDPA
Y693‑p MIPINEPyADDMDAT
Y701‑p ADDMDATyRPMYSSD
Y724 HMDMDGDYPMDTYSD
T728 DGDYPMDTYSDGLRP
Y729 GDYPMDTYSDGLRPP
S730 DYPMDTYSDGLRPPY
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