SCRIB_HUMAN - dbPTM
SCRIB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCRIB_HUMAN
UniProt AC Q14160
Protein Name Protein scribble homolog
Gene Name SCRIB
Organism Homo sapiens (Human).
Sequence Length 1630
Subcellular Localization Cell membrane
Peripheral membrane protein. Cell junction, adherens junction. Cell projection, lamellipodium. Cytoplasm. Targeting to cell-cell junctions which is CDH1-dependent is required for the pro-apoptotic activity. Localizes to neuronal post-
Protein Description Scaffold protein involved in different aspects of polarized cells differentiation regulating epithelial and neuronal morphogenesis. Most probably functions in the establishment of apico-basal cell polarity. May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium. May also function in cell migration and adhesion and hence regulate cell invasion through MAPK signaling. May play a role in exocytosis and in the targeting synaptic vesicles to synapses. Functions as an activator of Rac GTPase activity..
Protein Sequence MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEVEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEASTDAALEVSPGVIANPFAAGIGHRNSLESISSIDRELSPEGPGKEKELPGQTLHWGPEATEAAGRGLQPLKLDYRALAAVPSAGSVQRVPSGAAGGKMAESPCSPSGQQPPSPPSPDELPANVKQAYRAFAAVPTSHPPEDAPAQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALDGETLGEEEQEDEQPPWASPSPTSRQSPASPPPLGGGAPVRTAKAERRHQERLRVQSPEPPAPERALSPAELRALEAEKRALWRAARMKSLEQDALRAQMVLSRSQEGRGTRGPLERLAEAPSPAPTPSPTPVEDLGPQTSTSPGRLSPDFAEELRSLEPSPSPGPQEEDGEVALVLLGRPSPGAVGPEDVALCSSRRPVRPGRRGLGPVPS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
4S-palmitoylation----MLKCIPLWRCN
----CCCCEEHHHCC		6.4027380321
10S-palmitoylationKCIPLWRCNRHVESV
CCEEHHHCCCCCHHC		3.3827380321
19UbiquitinationRHVESVDKRHCSLQA
CCCHHCCCCCCCCCC		41.72-
23PhosphorylationSVDKRHCSLQAVPEE
HCCCCCCCCCCCCHH		19.8623927012
32PhosphorylationQAVPEEIYRYSRSLE
CCCCHHHHHHCCCHH		13.5323927012
34PhosphorylationVPEEIYRYSRSLEEL
CCHHHHHHCCCHHHH		7.4623927012
34 (in isoform 2)Ubiquitination-7.4621890473
35PhosphorylationPEEIYRYSRSLEELL
CHHHHHHCCCHHHHH		13.3430266825
37PhosphorylationEIYRYSRSLEELLLD
HHHHHCCCHHHHHCC		33.9019664994
53UbiquitinationNQLRELPKPFFRLLN
HHHHCCCHHHHHHHH		68.0621890473
53 (in isoform 1)Ubiquitination-68.0621890473
53 (in isoform 3)Ubiquitination-68.0621890473
63UbiquitinationFRLLNLRKLGLSDNE
HHHHHHHHCCCCHHH		50.50-
63 (in isoform 1)Ubiquitination-50.5021890473
63 (in isoform 3)Ubiquitination-50.5021890473
67PhosphorylationNLRKLGLSDNEIQRL
HHHHCCCCHHHHHHC		36.2727732954
83 (in isoform 2)Ubiquitination-37.91-
102UbiquitinationPEIPESIKFCKALEI
CCCCHHHHHHHHHHE		54.72-
105UbiquitinationPESIKFCKALEIADF
CHHHHHHHHHHEECC		60.17-
105 (in isoform 3)Ubiquitination-60.17-
113PhosphorylationALEIADFSGNPLSRL
HHHEECCCCCCHHHC		37.9024732914
118PhosphorylationDFSGNPLSRLPDGFT
CCCCCCHHHCCCHHH		32.7824732914
125PhosphorylationSRLPDGFTQLRSLAH
HHCCCHHHHHHHHHH		32.0224732914
135 (in isoform 2)Ubiquitination-7.6621890473
164UbiquitinationELRENLLKSLPASLS
HHHHHHHHHCCHHHH		53.7821890473
164 (in isoform 1)Ubiquitination-53.7821890473
164 (in isoform 3)Ubiquitination-53.7821890473
165PhosphorylationLRENLLKSLPASLSF
HHHHHHHHCCHHHHH		39.2828348404
185 (in isoform 2)Ubiquitination-47.70-
232 (in isoform 2)Ubiquitination-10.13-
237 (in isoform 2)Ubiquitination-36.9521890473
266UbiquitinationPDGIGQLKQLSILKV
CCCCHHHHEEEEEEE		41.1121890473
266 (in isoform 1)Ubiquitination-41.1121890473
266 (in isoform 3)Ubiquitination-41.1121890473
269PhosphorylationIGQLKQLSILKVDQN
CHHHHEEEEEEECHH		24.3124719451
272UbiquitinationLKQLSILKVDQNRLC
HHEEEEEEECHHHHH		41.9421890473
272 (in isoform 1)Ubiquitination-41.9421890473
272 (in isoform 3)Ubiquitination-41.9421890473
284 (in isoform 2)Ubiquitination-11.1621890473
313UbiquitinationRSLGKLTKLTNLNVD
HHHHHHHHHHCCCCC		64.8421906983
313 (in isoform 1)Ubiquitination-64.8421890473
313 (in isoform 3)Ubiquitination-64.8421890473
372PhosphorylationVAGNRLQSLPFALTH
CCCCCHHHHCHHHHH		42.4720873877
378PhosphorylationQSLPFALTHLNLKAL
HHHCHHHHHCCHHHH		22.3820873877
386 (in isoform 2)Ubiquitination-9.82-
400PhosphorylationQPMLRFQTEDDARTG
CCCEEEECCCCCCCC		38.3722985185
432PhosphorylationEDAGQQGSLSETWSD
HHCCCCCCCCCCCCC		25.1228348404
438 (in isoform 2)Ubiquitination-31.1721890473
446PhosphorylationDAPPSRVSVIQFLEA
CCCCCCEEEEEEEEC		16.6426657352
467UbiquitinationAEEAAAEKRGLQRRA
HHHHHHHHHCCCCCC		47.2222053931
467 (in isoform 1)Ubiquitination-47.2221890473
467 (in isoform 3)Ubiquitination-47.2221890473
475O-linked_GlycosylationRGLQRRATPHPSELK
HCCCCCCCCCHHHHH		21.9630379171
475PhosphorylationRGLQRRATPHPSELK
HCCCCCCCCCHHHHH		21.9623401153
479PhosphorylationRRATPHPSELKVMKR
CCCCCCHHHHHHHHH		53.1530266825
487PhosphorylationELKVMKRSIEGRRSE
HHHHHHHHHCCCCCC		21.3428102081
493PhosphorylationRSIEGRRSEACPCQP
HHHCCCCCCCCCCCC		28.3423927012
502PhosphorylationACPCQPDSGSPLPAE
CCCCCCCCCCCCCHH		48.1029255136
504PhosphorylationPCQPDSGSPLPAEEE
CCCCCCCCCCCHHHH		27.5019664994
512UbiquitinationPLPAEEEKRLSAESG
CCCHHHHHHHHHHCC		63.02-
515PhosphorylationAEEEKRLSAESGLSE
HHHHHHHHHHCCCCC		33.7425849741
518PhosphorylationEKRLSAESGLSEDSR
HHHHHHHCCCCCCCC		44.7623312004
521PhosphorylationLSAESGLSEDSRPSA
HHHHCCCCCCCCCCC		42.7722210691
524PhosphorylationESGLSEDSRPSASTV
HCCCCCCCCCCCCCC		41.8822210691
527PhosphorylationLSEDSRPSASTVSEA
CCCCCCCCCCCCCCC		33.4724275569
564PhosphorylationEEDAEEDYQEPTVHF
CCCHHHHHCCCCEEC		20.3220736484
607PhosphorylationQRLIRKDTPHYKKHF
HEEEECCCCHHHHHC		18.2626657352
610PhosphorylationIRKDTPHYKKHFKIS
EECCCCHHHHHCCCC		23.96-
668PhosphorylationEEEEEEGSPQEEEVE
HHHHHCCCCCHHHHH		27.0420068231
688PhosphorylationRAEEEEASTEEEDKE
HHHHHHHCCHHHHHC		39.3630266825
689PhosphorylationAEEEEASTEEEDKEG
HHHHHHCCHHHHHCC		55.2330266825
700PhosphorylationDKEGAVVSAPSVKGV
HHCCCEEECCCCCCC		28.0629255136
703PhosphorylationGAVVSAPSVKGVSFD
CCEEECCCCCCCCHH		35.8629255136
705UbiquitinationVVSAPSVKGVSFDQA
EEECCCCCCCCHHHH		58.91-
708PhosphorylationAPSVKGVSFDQANNL
CCCCCCCCHHHHCCE		31.6030266825
728PhosphorylationRIEEEELTLTILRQT
CCCCHHHEEEHHHHC		25.74-
730PhosphorylationEEEELTLTILRQTGG
CCHHHEEEHHHHCCC		16.84-
735PhosphorylationTLTILRQTGGLGISI
EEEHHHHCCCCCEEE		27.1220068231
741PhosphorylationQTGGLGISIAGGKGS
HCCCCCEEECCCCCC		12.4620068231
748PhosphorylationSIAGGKGSTPYKGDD
EECCCCCCCCCCCCC		29.6930266825
749PhosphorylationIAGGKGSTPYKGDDE
ECCCCCCCCCCCCCC		39.0330266825
751PhosphorylationGGKGSTPYKGDDEGI
CCCCCCCCCCCCCCE		27.9121712546
752UbiquitinationGKGSTPYKGDDEGIF
CCCCCCCCCCCCCEE		58.00-
761PhosphorylationDDEGIFISRVSEEGP
CCCCEEEEEECCCCH		18.8430266825
764O-linked_GlycosylationGIFISRVSEEGPAAR
CEEEEEECCCCHHHH		28.9030379171
764PhosphorylationGIFISRVSEEGPAAR
CEEEEEECCCCHHHH		28.9030266825
824PhosphorylationVEPENAVTITPLRPE
CCCCCCEEECCCCCC		19.4021945579
826PhosphorylationPENAVTITPLRPEDD
CCCCEEECCCCCCCC		13.6029255136
834PhosphorylationPLRPEDDYSPRERRG
CCCCCCCCCCCCCCC		32.6623927012
835PhosphorylationLRPEDDYSPRERRGG
CCCCCCCCCCCCCCC		25.1929255136
853PhosphorylationLPLLPPESPGPLRQR
CCCCCCCCCCCCHHH		40.7119664994
868PhosphorylationHVACLARSERGLGFS
HHHHHHHCCCCCCEE		26.4923312004
875PhosphorylationSERGLGFSIAGGKGS
CCCCCCEEECCCCCC		15.1023911959
880AcetylationGFSIAGGKGSTPYRA
CEEECCCCCCCCCCC		49.0926051181
880UbiquitinationGFSIAGGKGSTPYRA
CEEECCCCCCCCCCC		49.09-
880 (in isoform 3)Ubiquitination-49.09-
882PhosphorylationSIAGGKGSTPYRAGD
EECCCCCCCCCCCCC		29.6922199227
883PhosphorylationIAGGKGSTPYRAGDA
ECCCCCCCCCCCCCC		32.7630576142
885PhosphorylationGGKGSTPYRAGDAGI
CCCCCCCCCCCCCEE		17.1223090842
886MethylationGKGSTPYRAGDAGIF
CCCCCCCCCCCCEEE		33.04115493419
908PhosphorylationGAAHRAGTLQVGDRV
CCCCCCCCCEECCEE		17.0328857561
917PhosphorylationQVGDRVLSINGVDVT
EECCEEEEECCEECC		15.9127050516
933PhosphorylationARHDHAVSLLTAASP
CCHHHHHHHHHHCCH		20.6024732914
936PhosphorylationDHAVSLLTAASPTIA
HHHHHHHHHCCHHHH		26.0224732914
939PhosphorylationVSLLTAASPTIALLL
HHHHHHCCHHHHHHH		21.8029255136
941PhosphorylationLLTAASPTIALLLER
HHHHCCHHHHHHHHH		19.1829255136
957PhosphorylationAGGPLPPSPLPHSSP
CCCCCCCCCCCCCCC		36.8128348404
962PhosphorylationPPSPLPHSSPPTAAV
CCCCCCCCCCCCEEE		42.4728348404
963PhosphorylationPSPLPHSSPPTAAVA
CCCCCCCCCCCEEEE		31.6829496963
966PhosphorylationLPHSSPPTAAVATTS
CCCCCCCCEEEEEEE		30.5429496963
990PhosphorylationGLPSLAPSLLAAALE
CCCCHHHHHHHHHHH		30.3329496963
1000PhosphorylationAAALEGPYPVEEIRL
HHHHHCCCCHHEEEC		30.6620736484
1017PhosphorylationAGGPLGLSIVGGSDH
CCCCCCEEEECCCCC		17.27-
1022PhosphorylationGLSIVGGSDHSSHPF
CEEEECCCCCCCCCC		26.6529759185
1040UbiquitinationEPGVFISKVLPRGLA
CCCEEEECCCCCCHH		42.87-
1050PhosphorylationPRGLAARSGLRVGDR
CCCHHHHCCCCCCCE		37.14-
1105UbiquitinationLRELCIQKAPGERLG
HHHHHEEECCCCCCC		36.32-
1105 (in isoform 3)Ubiquitination-36.32-
1109 (in isoform 2)Ubiquitination-43.6121890473
1114PhosphorylationPGERLGISIRGGARG
CCCCCCEEECCCCCC		12.3924670416
1116MethylationERLGISIRGGARGHA
CCCCEEECCCCCCCC		30.6080702107
1120MethylationISIRGGARGHAGNPR
EEECCCCCCCCCCCC		40.48115493411
1130PhosphorylationAGNPRDPTDEGIFIS
CCCCCCCCCCCEEEE		51.4723403867
1137PhosphorylationTDEGIFISKVSPTGA
CCCCEEEEEECCCCC		19.0930266825
1138UbiquitinationDEGIFISKVSPTGAA
CCCEEEEEECCCCCC		41.752190698
1138 (in isoform 1)Ubiquitination-41.7521890473
1138 (in isoform 3)Ubiquitination-41.7521890473
1140O-linked_GlycosylationGIFISKVSPTGAAGR
CEEEEEECCCCCCCC		22.0830379171
1140PhosphorylationGIFISKVSPTGAAGR
CEEEEEECCCCCCCC		22.0830266825
1142PhosphorylationFISKVSPTGAAGRDG
EEEEECCCCCCCCCC		31.7630266825
1174 (in isoform 2)Phosphorylation-3.4218669648
1203PhosphorylationTDAALEVSPGVIANP
CCCCCCCCCCCCCCC		13.4226074081
1220PhosphorylationAGIGHRNSLESISSI
CCCCCCCCHHHHHHC		33.2119664994
1223PhosphorylationGHRNSLESISSIDRE
CCCCCHHHHHHCCCC		32.8229255136
1225PhosphorylationRNSLESISSIDRELS
CCCHHHHHHCCCCCC		30.4429255136
1226PhosphorylationNSLESISSIDRELSP
CCHHHHHHCCCCCCC		27.1719664994
1232PhosphorylationSSIDRELSPEGPGKE
HHCCCCCCCCCCCCC		19.0229255136
1240UbiquitinationPEGPGKEKELPGQTL
CCCCCCCCCCCCCCE		68.95-
1259MethylationEATEAAGRGLQPLKL
HHHHHCCCCCCCCCC		37.6182955073
1265UbiquitinationGRGLQPLKLDYRALA
CCCCCCCCCCHHHHC		46.09-
1268PhosphorylationLQPLKLDYRALAAVP
CCCCCCCHHHHCCCC		14.2825106551
1276PhosphorylationRALAAVPSAGSVQRV
HHHCCCCCCCCCEEC		38.3723401153
1279PhosphorylationAAVPSAGSVQRVPSG
CCCCCCCCCEECCCC		18.1330266825
1285PhosphorylationGSVQRVPSGAAGGKM
CCCEECCCCCCCCCC		37.9027273156
1295PhosphorylationAGGKMAESPCSPSGQ
CCCCCCCCCCCCCCC		22.9730266825
1298PhosphorylationKMAESPCSPSGQQPP
CCCCCCCCCCCCCCC		26.0330266825
1300PhosphorylationAESPCSPSGQQPPSP
CCCCCCCCCCCCCCC		32.7030266825
1306PhosphorylationPSGQQPPSPPSPDEL
CCCCCCCCCCCCCCC		57.0129255136
1309PhosphorylationQQPPSPPSPDELPAN
CCCCCCCCCCCCCCC		48.6529255136
1329PhosphorylationRAFAAVPTSHPPEDA
HHHHCCCCCCCCCCC		32.8229255136
1330PhosphorylationAFAAVPTSHPPEDAP
HHHCCCCCCCCCCCC		28.1129255136
1342PhosphorylationDAPAQPPTPGPAASP
CCCCCCCCCCCCCCH		47.7829255136
1348PhosphorylationPTPGPAASPEQLSFR
CCCCCCCCHHHCCHH		30.9529255136
1353PhosphorylationAASPEQLSFRERQKY
CCCHHHCCHHHHHHE		23.1929255136
1360PhosphorylationSFRERQKYFELEVRV
CHHHHHHEEEEEEEC		8.2425159151
1378PhosphorylationEGPPKRVSLVGADDL
CCCCCEEEEECHHHH		22.7529255136
1422PhosphorylationRLALDGETLGEEEQE
HHHHCCCCCCCCCCC		45.6623403867
1437PhosphorylationDEQPPWASPSPTSRQ
CCCCCCCCCCCCCCC		23.2630266825
1439PhosphorylationQPPWASPSPTSRQSP
CCCCCCCCCCCCCCC		38.0130266825
1441PhosphorylationPWASPSPTSRQSPAS
CCCCCCCCCCCCCCC		40.6630266825
1442PhosphorylationWASPSPTSRQSPASP
CCCCCCCCCCCCCCC		31.5430266825
1445PhosphorylationPSPTSRQSPASPPPL
CCCCCCCCCCCCCCC		22.7129255136
1448PhosphorylationTSRQSPASPPPLGGG
CCCCCCCCCCCCCCC		41.1329255136
1460PhosphorylationGGGAPVRTAKAERRH
CCCCCCCCHHHHHHH		32.5126074081
1475PhosphorylationQERLRVQSPEPPAPE
HHHHHCCCCCCCCCH		28.5119664994
1486PhosphorylationPAPERALSPAELRAL
CCCHHCCCHHHHHHH		22.5329255136
1500 (in isoform 2)Phosphorylation-3.5518669648
1507MethylationLWRAARMKSLEQDAL
HHHHHHCHHHHHHHH		46.46115977601
1508PhosphorylationWRAARMKSLEQDALR
HHHHHCHHHHHHHHH		28.0029255136
1521PhosphorylationLRAQMVLSRSQEGRG
HHHHHHHHHCCCCCC		20.6222617229
1523PhosphorylationAQMVLSRSQEGRGTR
HHHHHHHCCCCCCCC		29.2529214152
1527MethylationLSRSQEGRGTRGPLE
HHHCCCCCCCCCHHH		42.4283435543
1529PhosphorylationRSQEGRGTRGPLERL
HCCCCCCCCCHHHHH		30.9628348404
1541PhosphorylationERLAEAPSPAPTPSP
HHHHCCCCCCCCCCC		40.5229255136
1541 (in isoform 3)Phosphorylation-40.5222617229
1545PhosphorylationEAPSPAPTPSPTPVE
CCCCCCCCCCCCCHH		38.2129255136
1545 (in isoform 3)Phosphorylation-38.2128450419
1547PhosphorylationPSPAPTPSPTPVEDL
CCCCCCCCCCCHHHC		43.8329255136
1547 (in isoform 3)Phosphorylation-43.8328387310
1549PhosphorylationPAPTPSPTPVEDLGP
CCCCCCCCCHHHCCC		44.2829255136
1549 (in isoform 3)Phosphorylation-44.2828450419
1558PhosphorylationVEDLGPQTSTSPGRL
HHHCCCCCCCCCCCC		36.7929255136
1558 (in isoform 3)Phosphorylation-36.7926657352
1559PhosphorylationEDLGPQTSTSPGRLS
HHCCCCCCCCCCCCC		22.9529255136
1559 (in isoform 3)Phosphorylation-22.9528387310
1560PhosphorylationDLGPQTSTSPGRLSP
HCCCCCCCCCCCCCH		42.1829255136
1560 (in isoform 3)Phosphorylation-42.1828450419
1561PhosphorylationLGPQTSTSPGRLSPD
CCCCCCCCCCCCCHH		25.7323927012
1561 (in isoform 3)Phosphorylation-25.7328450419
1566PhosphorylationSTSPGRLSPDFAEEL
CCCCCCCCHHHHHHH		22.5129255136
1568 (in isoform 3)Phosphorylation-52.6028450419
1575PhosphorylationDFAEELRSLEPSPSP
HHHHHHHHCCCCCCC		50.1128102081
1579PhosphorylationELRSLEPSPSPGPQE
HHHHCCCCCCCCCCC		28.7428102081
1581PhosphorylationRSLEPSPSPGPQEED
HHCCCCCCCCCCCCC		46.9919664994
1587 (in isoform 3)Phosphorylation-67.10-
1591PhosphorylationPQEEDGEVALVLLGR
CCCCCCCEEEEEECC		6.4515345747
1591 (in isoform 3)Phosphorylation-6.4515345747
1600PhosphorylationLVLLGRPSPGAVGPE
EEEECCCCCCCCCHH		34.3128387310
1600 (in isoform 3)Phosphorylation-34.3129507054
1604PhosphorylationGRPSPGAVGPEDVAL
CCCCCCCCCHHHHHH		19.0627251275
1604 (in isoform 3)Phosphorylation-19.0629507054
1606PhosphorylationPSPGAVGPEDVALCS
CCCCCCCHHHHHHCC		28.1919664994
1613PhosphorylationPEDVALCSSRRPVRP
HHHHHHCCCCCCCCC		27.9426503892
1614PhosphorylationEDVALCSSRRPVRPG
HHHHHCCCCCCCCCC		31.1726503892
1625PhosphorylationVRPGRRGLGPVPS--
CCCCCCCCCCCCC--		7.1327251275
1630PhosphorylationRGLGPVPS-------
CCCCCCCC-------		53.7620860994
1638Phosphorylation---------------
---------------		-
1655Phosphorylation--------------------------------
--------------------------------		-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1378SPhosphorylationKinaseROCK1Q13464
PSP
1508SPhosphorylationKinaseROCK1Q13464
PSP
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:11027293
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCRIB_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SCRIB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC_HUMANAPCphysical
16611247
UBE3A_HUMANUBE3Aphysical
11027293
ARHG7_HUMANARHGEF7physical
24550280
GCYA2_HUMANGUCY1A2physical
24550280
PKP4_HUMANPKP4physical
24550280
MK12_HUMANMAPK12physical
24550280
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
182940Neural tube defects (NTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCRIB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-826; SER-853; SER-875;SER-1220; THR-1342; SER-1348; SER-1475; SER-1547 AND SER-1566, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1348; SER-1448 ANDSER-1561, AND MASS 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-504; SER-853; SER-1298;SER-1300; SER-1306; SER-1309; SER-1437; SER-1448; SER-1475; SER-1486AND SER-1566, AND MASS 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 THR-826; SER-835; SER-853;SER-939; SER-1223; SER-1225; SER-1232; SER-1306; SER-1309; THR-1342;SER-1348; SER-1378; SER-1437; SER-1439; SER-1475; SER-1486; SER-1508;SER-1547 AND SER-1566, AND MASS SPECTROMETRY.
"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-35; SER-504; THR-749;TYR-834; SER-835; SER-853; SER-1475; SER-1561 AND SER-1566, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1448, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232 AND SER-1475, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939 AND THR-941, ANDMASS 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-1486, AND MASSSPECTROMETRY.
"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-487; SER-853; SER-1225;SER-1226; SER-1306; SER-1309; SER-1348; SER-1378 AND SER-1448, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1140; SER-1220;SER-1309; SER-1348; SER-1448; SER-1475; SER-1486 AND SER-1566, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1360, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1360, AND MASSSPECTROMETRY.

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