Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Adenomatous polyposis coli protein  

UniProtKB / Swiss-Prot ID :  APC_HUMAN

Gene Name (Synonyms) : 
APC, DP2.5  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell junction, adherens junction. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle membrane. Cytoplasm. Cell membrane. Note=Associated with the microtubule network at the growing distal tip of microtubules. Accumulates in  

Protein Function :  Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. 

Protein Sequence MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLE...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHCCHHHHHHHHCCHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHCCCCHHHHH...
Protein Variant
LocationDescription
99R -> W (in FAP; could be a rarepolymorphism).
171S -> I (in FAP). VAR_005032
414R -> C (in FAP). VAR_005033
722S -> G (in FAP). VAR_009614
784S -> T (in FAP). VAR_005034
817G -> C (in gastric cancer). VAR_005035
870P -> S (in dbSNP:rs33974176). VAR_053976
880I -> T (in colorectal carcinoma andgastric cancer; from a patient with
890V -> I (in colorectal carcinoma; from apatient with MMRCS).
906S -> Y (in colorectal tumor). VAR_005037
911E -> G (in FAP and colorectal tumor). VAR_005038
942N -> D (in gastric cancer). VAR_005039
1027Y -> C (in colorectal tumor). VAR_005040
1057E -> G (in non-FAP; unknown pathologicalsignificance).
1118N -> D. VAR_005041
1120G -> E (in gastric cancer;dbSNP:rs28933379).
1171R -> C. VAR_008992
1171R -> H (in gastric cancer). VAR_005043
1176P -> L (in FAP). VAR_005044
1184A -> P (in FAP). VAR_009616
1197F -> S (in gastric cancer). VAR_005045
1254I -> F (in a colorectal cancer sample;somatic mutation).
1259I -> T (in gastric cancer). VAR_005046
1292T -> M. VAR_005047
1296A -> V (in MDB; sporadic). VAR_017653
1304I -> V. VAR_005048
1307I -> K (in 6% of Ashkenazi Jews;associated with slightly increased risk
1312G -> E (in gastric cancer). VAR_005050
1313T -> A (in FAP and colorectal tumor). VAR_005051
1317E -> Q (may contribute to colorectaltumor development; dbSNP:rs1801166).
1326V -> A (in gastric cancer). VAR_005052
1348R -> W (in FAP). VAR_005053
1395S -> C (in hepatoblastoma). VAR_065133
1422D -> H (in colorectal tumor). VAR_005054
1472V -> I (in MDB; sporadic). VAR_017654
1495S -> G (in MDB; sporadic). VAR_017655
1496T -> S (in dbSNP:rs2229996). VAR_020141
1508A -> V (in colorectal carcinoma from apatient with MMRCS).
1822V -> D (in dbSNP:rs459552). VAR_008993
1882R -> T (in dbSNP:rs34157245). VAR_053977
1973S -> T (in dbSNP:rs4987109). VAR_020142
2499V -> L (in dbSNP:rs33941929). VAR_053978
2502G -> S (in dbSNP:rs2229995). VAR_005055
2621S -> C (in FAP). VAR_005056
2738I -> T. VAR_008994
2839L -> F (in FAP). VAR_005057
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
316PhosphotyrosineVEMVYSLLS
HHHHHHHHH
7.71HPRD
Link-
722PhosphoserineIAMGSAAAL
HHHHHHHHH
11.14HPRD
Link-
744PhosphoserineANIMSPGSS
HHEECCCCC
23.47HPRD
Link-
744PhosphoserineANIMSPGSS
HHEECCCCC
23.47Phosphositeplus
Link-
780PhosphoserineIDNLSPKAS
HHHHCCCCC
30.52HPRD
Link-
780PhosphoserineIDNLSPKAS
HHHHCCCCC
30.52PhosphoELM
Link-
780PhosphoserineIDNLSPKAS
HHHHCCCCC
30.52Phosphositeplus
Link-
780PhosphoserineIDNLSPKAS
HHHHCCCCC
30.52SysPTM
Link-
780Phosphoserine.IDNLSPKAS
HHHHCCCCC
30.52UniProtKB
Link-
863PhosphotyrosineGLGNYHPAT
CCCCCCCCC
13.84HPRD
Link-
863PhosphotyrosineGLGNYHPAT
CCCCCCCCC
13.84Phosphositeplus
Link-
867PhosphothreonineYHPATENPG
CCCCCCCCC
40.52HPRD
Link-
883PhosphothreonineQISTTAAQI
EEEHHHHHH
17.13HPRD
Link-
895PhosphoserineMEEVSAIHT
HHHHHHHHH
25.45HPRD
Link-
895PhosphoserineMEEVSAIHT
HHHHHHHHH
25.45Phosphositeplus
Link-
899PhosphothreonineSAIHTSQED
HHHHHHHHC
26.45HPRD
Link-
899PhosphothreonineSAIHTSQED
HHHHHHHHC
26.45Phosphositeplus
Link-
951PhosphotyrosineCSMPYAKLE
CCCHHHHHH
14.02Phosphositeplus
Link-
987PhosphoserineIESYSEDDE
CCCCCCCCC
43.77HPRD
Link-
987Phosphoserine.IESYSEDDE
CCCCCCCCC
43.77UniProtKB
Link-
1032PhosphoserineSLKYSDEQL
HHHCCHHHH
32.84Phosphositeplus
Link-
1038PhosphoserineEQLNSGRQS
HHHHCCCCC
43.90Phosphositeplus
Link-
1042PhosphoserineSGRQSPSQN
CCCCCCCHH
25.76HPRD
Link-
1042PhosphoserineSGRQSPSQN
CCCCCCCHH
25.76PhosphoELM
Link-
1042PhosphoserineSGRQSPSQN
CCCCCCCHH
25.76Phosphositeplus
Link-
1042PhosphoserineSGRQSPSQN
CCCCCCCHH
25.76SysPTM
Link-
1042Phosphoserine.SGRQSPSQN
CCCCCCCHH
25.76UniProtKB
Link-
1044PhosphoserineRQSPSQNER
CCCCCHHHH
51.38HPRD
Link-
1078PhosphotyrosineTYPVYTEST
CCCCCCCCC
10.57Phosphositeplus
Link-
1279PhosphoserineSSLSSLSSA
CCCCCCCCC
37.25Phosphositeplus
Link-
1279Phosphoserine (CK1_group;CK1_epsilon)SSLSSLSSA
CCCCCCCCC
37.25PhosphoELM
Link-
1279Phosphoserine (CSNK1E)SSLSSLSSA
CCCCCCCCC
37.25HPRD
Link-
1360PhosphoserineSGAKSPSKS
CCCCCCCCC
33.59HPRD
Link-
1360PhosphoserineSGAKSPSKS
CCCCCCCCC
33.59PhosphoELM
Link-
1360PhosphoserineSGAKSPSKS
CCCCCCCCC
33.59Phosphositeplus
Link-
1360PhosphoserineSGAKSPSKS
CCCCCCCCC
33.59SysPTM
Link-
1360Phosphoserine.SGAKSPSKS
CCCCCCCCC
33.59UniProtKB
Link-
1371PhosphoserineQTPKSPPEH
CCCCCCCCC
47.06HPRD
Link-
1371PhosphoserineQTPKSPPEH
CCCCCCCCC
47.06Phosphositeplus
Link-
1392PhosphoserineTSVSSLDSF
CCCCCCCCC
33.76Phosphositeplus
Link-
1392Phosphoserine (CK1_group;CK1_epsilon)TSVSSLDSF
CCCCCCCCC
33.76PhosphoELM
Link-
1392Phosphoserine (CSNK1E)TSVSSLDSF
CCCCCCCCC
33.76HPRD
Link-
1438PhosphothreonineSRSKTPPPP
CCCCCCCCC
42.13HPRD
Link-
1438PhosphothreonineSRSKTPPPP
CCCCCCCCC
42.13PhosphoELM
Link-
1438PhosphothreonineSRSKTPPPP
CCCCCCCCC
42.13Phosphositeplus
Link-
1438Phosphothreonine.SRSKTPPPP
CCCCCCCCC
42.13UniProtKB
Link-
1501PhosphoserinePDGFSCSSS
CCCCCCCCC
20.72Phosphositeplus
Link-
1501Phosphoserine (GSK3B)PDGFSCSSS
CCCCCCCCC
20.72HPRD
Link-
1503PhosphoserineGFSCSSSLS
CCCCCCCCC
23.05Phosphositeplus
Link-
1503Phosphoserine (GSK3B)GFSCSSSLS
CCCCCCCCC
23.05HPRD
Link-
1504PhosphoserineFSCSSSLSA
CCCCCCCCC
39.36Phosphositeplus
Link-
1504Phosphoserine (CSNK1E)FSCSSSLSA
CCCCCCCCC
39.36HPRD
Link-
1505PhosphoserineSCSSSLSAL
CCCCCCCCC
15.28Phosphositeplus
Link-
1505Phosphoserine (CSNK1E)SCSSSLSAL
CCCCCCCCC
15.28HPRD
Link-
1507PhosphoserineSSSLSALSL
CCCCCCCCH
29.16Phosphositeplus
Link-
1507Phosphoserine (CSNK1E)SSSLSALSL
CCCCCCCCH
29.16HPRD
Link-
1510PhosphoserineLSALSLDEP
CCCCCHHCC
33.23Phosphositeplus
Link-
1510Phosphoserine (CSNK1E)LSALSLDEP
CCCCCHHCC
33.23HPRD
Link-
1854PhosphotyrosineEGTPYCFSR
CCCEEEECC
13.13Phosphositeplus
Link-
1861PhosphoserineSRNDSLSSL
CCCCCCCCC
33.43HPRD
Link-
1861PhosphoserineSRNDSLSSL
CCCCCCCCC
33.43PhosphoELM
Link-
1861PhosphoserineSRNDSLSSL
CCCCCCCCC
33.43Phosphositeplus
Link-
1861PhosphoserineSRNDSLSSL
CCCCCCCCC
33.43SysPTM
Link-
1861PhosphoserineSRNDSLSSL
CCCCCCCCC
33.43SysPTM
Link-
1861Phosphoserine.SRNDSLSSL
CCCCCCCCC
33.43UniProtKB
Link-
1863PhosphoserineNDSLSSLDF
CCCCCCCCC
32.57HPRD
Link-
1863PhosphoserineNDSLSSLDF
CCCCCCCCC
32.57PhosphoELM
Link-
1863PhosphoserineNDSLSSLDF
CCCCCCCCC
32.57Phosphositeplus
Link-
1863PhosphoserineNDSLSSLDF
CCCCCCCCC
32.57SysPTM
Link-
1863PhosphoserineNDSLSSLDF
CCCCCCCCC
32.57SysPTM
Link-
1863Phosphoserine.NDSLSSLDF
CCCCCCCCC
32.57UniProtKB
Link-
1864PhosphoserineDSLSSLDFD
CCCCCCCCC
36.93HPRD
Link-
1864PhosphoserineDSLSSLDFD
CCCCCCCCC
36.93PhosphoELM
Link-
1864PhosphoserineDSLSSLDFD
CCCCCCCCC
36.93Phosphositeplus
Link-
1864PhosphoserineDSLSSLDFD
CCCCCCCCC
36.93SysPTM
Link-
1864PhosphoserineDSLSSLDFD
CCCCCCCCC
36.93SysPTM
Link-
1864Phosphoserine.DSLSSLDFD
CCCCCCCCC
36.93UniProtKB
Link-
1995PhosphoserineEPPDSQGEP
CCCCCCCCC
45.95SysPTM
Link-
2034PhosphoserineLSIDSEDDL
CCCCCCCCC
41.05PhosphoELM
Link-
2034PhosphoserineLSIDSEDDL
CCCCCCCCC
41.05Phosphositeplus
Link-
2054PhosphoserineKKKPSRLKG
CCCCCCCCC
60.16Phosphositeplus
Link-
2054Phosphoserine (PKA_group)KKKPSRLKG
CCCCCCCCC
60.16PhosphoELM
Link-
2054Phosphoserine (PRKACA)KKKPSRLKG
CCCCCCCCC
60.16HPRD
Link-
2088PhosphoserineQRPDSEHGL
HCCHHHCCC
33.89HPRD
Link-
2088PhosphoserineQRPDSEHGL
HCCHHHCCC
33.89PhosphoELM
Link-
2088PhosphoserineQRPDSEHGL
HCCHHHCCC
33.89Phosphositeplus
Link-
2088PhosphoserineQRPDSEHGL
HCCHHHCCC
33.89SysPTM
Link-
2088Phosphoserine.QRPDSEHGL
HCCHHHCCC
33.89UniProtKB
Link-
2093PhosphoserineEHGLSPDSE
HCCCCCCCC
31.11HPRD
Link-
2093PhosphoserineEHGLSPDSE
HCCCCCCCC
31.11PhosphoELM
Link-
2093PhosphoserineEHGLSPDSE
HCCCCCCCC
31.11Phosphositeplus
Link-
2093PhosphoserineEHGLSPDSE
HCCCCCCCC
31.11SysPTM
Link-
2093PhosphoserineEHGLSPDSE
HCCCCCCCC
31.11SysPTM
Link-
2093Phosphoserine.EHGLSPDSE
HCCCCCCCC
31.11UniProtKB
Link-
2096PhosphoserineLSPDSENFD
CCCCCCCCC
37.51HPRD
Link-
2096PhosphoserineLSPDSENFD
CCCCCCCCC
37.51PhosphoELM
Link-
2096PhosphoserineLSPDSENFD
CCCCCCCCC
37.51Phosphositeplus
Link-
2096Phosphoserine.LSPDSENFD
CCCCCCCCC
37.51UniProtKB
Link-
2125PhosphoserineAACLSRQAS
CCCCCCCCC
23.41PhosphoELM
Link-
2125PhosphoserineAACLSRQAS
CCCCCCCCC
23.41Phosphositeplus
Link-
2125Phosphoserine.AACLSRQAS
CCCCCCCCC
23.41UniProtKB
Link-
2129PhosphoserineSRQASSDSD
CCCCCCCCC
26.75HPRD
Link-
2129PhosphoserineSRQASSDSD
CCCCCCCCC
26.75PhosphoELM
Link-
2129PhosphoserineSRQASSDSD
CCCCCCCCC
26.75Phosphositeplus
Link-
2130PhosphoserineRQASSDSDS
CCCCCCCCC
44.12HPRD
Link-
2130PhosphoserineRQASSDSDS
CCCCCCCCC
44.12PhosphoELM
Link-
2143PhosphoserineKSGISLGSP
CCCCCCCCC
30.15HPRD
Link-
2143PhosphoserineKSGISLGSP
CCCCCCCCC
30.15PhosphoELM
Link-
2143PhosphoserineKSGISLGSP
CCCCCCCCC
30.15SysPTM
Link-
2143Phosphoserine.KSGISLGSP
CCCCCCCCC
30.15UniProtKB
Link-
2146PhosphoserineISLGSPFHL
CCCCCCCCC
29.68Phosphositeplus
Link-
2151PhosphothreoninePFHLTPDQE
CCCCCCCCC
19.09HPRD
Link-
2151PhosphothreoninePFHLTPDQE
CCCCCCCCC
19.09PhosphoELM
Link-
2151PhosphothreoninePFHLTPDQE
CCCCCCCCC
19.09Phosphositeplus
Link-
2151PhosphothreoninePFHLTPDQE
CCCCCCCCC
19.09SysPTM
Link-
2151Phosphothreonine.PFHLTPDQE
CCCCCCCCC
19.09UniProtKB
Link-
2239PhosphoserineGVRNSSSST
CCCCCCCCC
22.49HPRD
Link-
2241PhosphoserineRNSSSSTSP
CCCCCCCCC
37.14HPRD
Link-
2260PhosphoserinePASKSPSEG
CCCCCCCCC
31.03HPRD
Link-
2260PhosphoserinePASKSPSEG
CCCCCCCCC
31.03PhosphoELM
Link-
2260PhosphoserinePASKSPSEG
CCCCCCCCC
31.03Phosphositeplus
Link-
2260PhosphoserinePASKSPSEG
CCCCCCCCC
31.03SysPTM
Link-
2260Phosphoserine.PASKSPSEG
CCCCCCCCC
31.03UniProtKB
Link-
2262PhosphoserineSKSPSEGQT
CCCCCCCCC
62.54Phosphositeplus
Link-
2266PhosphothreonineSEGQTATTS
CCCCCCCCC
36.51HPRD
Link-
2266Phosphothreonine.SEGQTATTS
CCCCCCCCC
36.51UniProtKB
Link-
2270PhosphoserineTATTSPRGA
CCCCCCCCC
14.30HPRD
Link-
2270PhosphoserineTATTSPRGA
CCCCCCCCC
14.30PhosphoELM
Link-
2270PhosphoserineTATTSPRGA
CCCCCCCCC
14.30Phosphositeplus
Link-
2270PhosphoserineTATTSPRGA
CCCCCCCCC
14.30SysPTM
Link-
2270Phosphoserine.TATTSPRGA
CCCCCCCCC
14.30UniProtKB
Link-
2283PhosphoserineKSELSPVAR
CCCCCCCCC
17.18HPRD
Link-
2283PhosphoserineKSELSPVAR
CCCCCCCCC
17.18PhosphoELM
Link-
2283PhosphoserineKSELSPVAR
CCCCCCCCC
17.18Phosphositeplus
Link-
2283PhosphoserineKSELSPVAR
CCCCCCCCC
17.18SysPTM
Link-
2283PhosphoserineKSELSPVAR
CCCCCCCCC
17.18SysPTM
Link-
2283Phosphoserine.KSELSPVAR
CCCCCCCCC
17.18UniProtKB
Link-
2330PhosphoserineRNSISPGRN
CCCCCCCCC
22.56Phosphositeplus
Link-
2337PhosphoserineRNGISPPNK
CCCCCCCCC
35.39Phosphositeplus
Link-
2368PhosphoserineMSYTSPGRQ
CCCCCCCCC
19.68SysPTM
Link-
2398PhosphoserineSESASKGLN
CCCCCCCCC
36.21HPRD
Link-
2398PhosphoserineSESASKGLN
CCCCCCCCC
36.21PhosphoELM
Link-
2398PhosphoserineSESASKGLN
CCCCCCCCC
36.21SysPTM
Link-
2398Phosphoserine.SESASKGLN
CCCCCCCCC
36.21UniProtKB
Link-
2432PhosphoserineESDRSERPV
CCCCCCCCC
42.84SysPTM
Link-
2441PhosphoserineLVRQSTFIK
CCCCCCCCC
18.08Phosphositeplus
Link-
2442PhosphothreonineVRQSTFIKE
CCCCCCCCC
22.50Phosphositeplus
Link-
2449PhosphoserineKEAPSPTLR
CCCCCCCCC
37.25Phosphositeplus
Link-
2451PhosphothreonineAPSPTLRRK
CCCCCCCCC
36.92Phosphositeplus
Link-
2461PhosphoserineEESASFESL
CCCCCCCCC
38.53HPRD
Link-
2464PhosphoserineASFESLSPS
CCCCCCCCC
31.94HPRD
Link-
2464PhosphoserineASFESLSPS
CCCCCCCCC
31.94PhosphoELM
Link-
2464PhosphoserineASFESLSPS
CCCCCCCCC
31.94Phosphositeplus
Link-
2464PhosphoserineASFESLSPS
CCCCCCCCC
31.94SysPTM
Link-
2464Phosphoserine.ASFESLSPS
CCCCCCCCC
31.94UniProtKB
Link-
2469PhosphoserineLSPSSRPAS
CCCCCCCCC
45.74HPRD
Link-
2469PhosphoserineLSPSSRPAS
CCCCCCCCC
45.74PhosphoELM
Link-
2469Phosphoserine.LSPSSRPAS
CCCCCCCCC
45.74UniProtKB
Link-
2473PhosphoserineSRPASPTRS
CCCCCCCCC
29.50HPRD
Link-
2473PhosphoserineSRPASPTRS
CCCCCCCCC
29.50PhosphoELM
Link-
2473PhosphoserineSRPASPTRS
CCCCCCCCC
29.50Phosphositeplus
Link-
2473PhosphoserineSRPASPTRS
CCCCCCCCC
29.50SysPTM
Link-
2473Phosphoserine.SRPASPTRS
CCCCCCCCC
29.50UniProtKB
Link-
2531PhosphoserineDIARSHSES
CCCCCCCCC
23.49HPRD
Link-
2533PhosphoserineARSHSESPS
CCCCCCCCC
40.80HPRD
Link-
2533PhosphoserineARSHSESPS
CCCCCCCCC
40.80PhosphoELM
Link-
2533PhosphoserineARSHSESPS
CCCCCCCCC
40.80Phosphositeplus
Link-
2533Phosphoserine.ARSHSESPS
CCCCCCCCC
40.80UniProtKB
Link-
2535PhosphoserineSHSESPSRL
CCCCCCCCC
31.06HPRD
Link-
2535PhosphoserineSHSESPSRL
CCCCCCCCC
31.06PhosphoELM
Link-
2535PhosphoserineSHSESPSRL
CCCCCCCCC
31.06Phosphositeplus
Link-
2535PhosphoserineSHSESPSRL
CCCCCCCCC
31.06SysPTM
Link-
2535Phosphoserine.SHSESPSRL
CCCCCCCCC
31.06UniProtKB
Link-
2537PhosphoserineSESPSRLPI
CCCCCCCCC
56.58HPRD
Link-
2570PhosphoserineRTGSSSSIL
CCCCCCCCC
29.47SysPTM
Link-
2621PhosphoserineENEFSPTNS
CCCCCCCCC
25.33HPRD
Link-
2645PhosphotyrosineKTLIYQMAP
CCCCCCCCC
8.71Phosphositeplus
Link-
2671PhosphoserineNNPRSGRSP
CCCCCCCCC
39.55HPRD
Link-
2671PhosphoserineNNPRSGRSP
CCCCCCCCC
39.55PhosphoELM
Link-
2671PhosphoserineNNPRSGRSP
CCCCCCCCC
39.55Phosphositeplus
Link-
2671Phosphoserine.NNPRSGRSP
CCCCCCCCC
39.55UniProtKB
Link-
2674PhosphoserineRSGRSPTGN
CCCCCCCCC
30.27HPRD
Link-
2674PhosphoserineRSGRSPTGN
CCCCCCCCC
30.27PhosphoELM
Link-
2674PhosphoserineRSGRSPTGN
CCCCCCCCC
30.27Phosphositeplus
Link-
2674PhosphoserineRSGRSPTGN
CCCCCCCCC
30.27SysPTM
Link-
2674Phosphoserine.RSGRSPTGN
CCCCCCCCC
30.27UniProtKB
Link-
2676PhosphothreonineGRSPTGNTP
CCCCCCCCC
44.29HPRD
Link-
2676PhosphothreonineGRSPTGNTP
CCCCCCCCC
44.29PhosphoELM
Link-
2676PhosphothreonineGRSPTGNTP
CCCCCCCCC
44.29Phosphositeplus
Link-
2676Phosphothreonine.GRSPTGNTP
CCCCCCCCC
44.29UniProtKB
Link-
2679PhosphothreoninePTGNTPPVI
CCCCCCCCC
30.25HPRD
Link-
2679PhosphothreoninePTGNTPPVI
CCCCCCCCC
30.25PhosphoELM
Link-
2679PhosphothreoninePTGNTPPVI
CCCCCCCCC
30.25Phosphositeplus
Link-
2679PhosphothreoninePTGNTPPVI
CCCCCCCCC
30.25SysPTM
Link-
2679Phosphothreonine.PTGNTPPVI
CCCCCCCCC
30.25UniProtKB
Link-
2764PhosphoserineTPFSSSSSS
CCCCCCCCC
34.32Phosphositeplus
Link-
2768PhosphoserineSSSSSKHSS
CCCCCCCCC
36.01Phosphositeplus
Link-
2772PhosphoserineSKHSSPSGT
CCCCCCCCC
23.86Phosphositeplus
Link-
2789PhosphoserineNYNPSPRKS
CCCCCCCCC
33.43HPRD
Link-
2789PhosphoserineNYNPSPRKS
CCCCCCCCC
33.43PhosphoELM
Link-
2789PhosphoserineNYNPSPRKS
CCCCCCCCC
33.43Phosphositeplus
Link-
2789PhosphoserineNYNPSPRKS
CCCCCCCCC
33.43SysPTM
Link-
2789Phosphoserine.NYNPSPRKS
CCCCCCCCC
33.43UniProtKB
Link-
2793PhosphoserineSPRKSSADS
CCCCCCCCC
31.85Phosphositeplus
Link-
2799PhosphoserineADSTSARPS
CCCCCCCCC
26.66HPRD
Link-
2835PhosphoserinePKRHSGSYL
CCCCCCCEE
33.20HPRD
Link-
2835PhosphoserinePKRHSGSYL
CCCCCCCEE
33.20PhosphoELM
Link-
2835PhosphoserinePKRHSGSYL
CCCCCCCEE
33.20Phosphositeplus
Link-
2835Phosphoserine.PKRHSGSYL
CCCCCCCEE
33.20UniProtKB
Link-
2837PhosphoserineRHSGSYLVT
CCCCCEEEC
20.50HPRD
Link-
2837PhosphoserineRHSGSYLVT
CCCCCEEEC
20.50PhosphoELM
Link-
2837PhosphoserineRHSGSYLVT
CCCCCEEEC
20.50Phosphositeplus
Link-
2837Phosphoserine.RHSGSYLVT
CCCCCEEEC
20.50UniProtKB
Link-
2838PhosphotyrosineHSGSYLVTS
CCCCEEECC
14.55HPRD
Link-
2838PhosphotyrosineHSGSYLVTS
CCCCEEECC
14.55PhosphoELM
Link-
2838PhosphotyrosineHSGSYLVTS
CCCCEEECC
14.55Phosphositeplus
Link-
2838Phosphotyrosine.HSGSYLVTS
CCCCEEECC
14.55UniProtKB
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PLAK_HUMANphysical interactionMINT-17657MINT7890674
CTNB1_HUMANphysical interactionMINT-4508229MINT17318191
CTNB1_HUMANphysical interactionMINT-14763MINT7890674
CTNB1_HUMANphysical interactionMINT-16885MINT9482734
1433Z_HUMANphysical interactionMINT-3296068MINT15161933
MARE1_HUMANphysical interactionMINT-13708MINT7606712
KC1E_HUMANphosphorylationEBI-1187596
intact17218255
K1C9_HUMANphysical interactionEBI-727740
intact16212417
K2C1_HUMANphysical interactionEBI-727740
intact16212417
IGHA1_HUMANphysical interactionEBI-727740
intact16212417
CTNB1_HUMANphysical interaction
physical interaction
direct interaction
EBI-763296
EBI-1039979
EBI-10
intact16212417
15327768
15327769
TIF1B_HUMANphysical interactionEBI-763296
intact16212417
CAZA2_HUMANphysical interactionEBI-763296
intact16212417
MCM5_HUMANphysical interactionEBI-763296
intact16212417
DDB1_HUMANphysical interactionEBI-763296
intact16212417
SC23A_HUMANphysical interactionEBI-763296
intact16212417
CNBP1_HUMANphysical interactionEBI-1039979
intact15327768
CTNB1_HUMANin vitro
in vivo
HPRD:01439HPRD12000790
9482734
7890674
PLAK_HUMANin vitroHPRD:01439HPRD11707392
11348595
11136974
9298899
APC_HUMANin vitroHPRD:01439HPRD10926498
CTBP1_HUMANin vitro
in vivo
HPRD:01439HPRD15525529
IQGA1_HUMANin vitro
in vivo
HPRD:01439HPRD15572129
GSK3B_HUMANin vitroHPRD:01439HPRD8638126
GSK3A_HUMANENSP00000257430STRING
SKP1_HUMANENSP00000257430STRING
MLH1_HUMANENSP00000257430STRING
AXN1_HUMANENSP00000257430STRING
IQGA1_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
PHIP_HUMANENSP00000257430STRING
BUB1B_HUMANENSP00000257430STRING
BUB1_HUMANENSP00000257430STRING
AXN2_HUMANENSP00000257430STRING
CDC20_HUMANENSP00000257430STRING
DVL3_HUMANENSP00000257430STRING
CUL1_HUMANENSP00000257430STRING
CTNB1_HUMANENSP00000257430STRING
SIAH1_HUMANENSP00000257430STRING
SIAH1_HUMANENSP00000257430STRING
KC1E_HUMANENSP00000257430STRING
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Disease Reference
Kegg disease
H00017 Esophageal cancer
H00018 Gastric cancer
H00044 Cancer of the anal canal
H00047 Gallbladder cancer
H01025 Familial adenomatous polyposis
OMIM disease
175100Familial adenomatous polyposis (FAP)
135290Hereditary desmoid disease (HDD)
155255Medulloblastoma (MDB)
276300Mismatch repair cancer syndrome (MMRCS)
613659Gastric cancer (GASC)
114550Hepatocellular carcinoma (HCC)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861; SER-1863; SER-1864AND SER-2398, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2283, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2125; SER-2671;SER-2674; THR-2676; SER-2789; SER-2835; SER-2837 AND TYR-2838, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1042; SER-1360;SER-1861; SER-1863; SER-1864; SER-2088; SER-2093; SER-2096; SER-2143;THR-2151; SER-2260; SER-2270; SER-2283; SER-2464; SER-2469; SER-2473;SER-2533; SER-2535; SER-2671; SER-2674; THR-2679 AND SER-2789, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987; THR-1438; SER-2260;THR-2266 AND SER-2270, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures