STK10_HUMAN - dbPTM
STK10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STK10_HUMAN
UniProt AC O94804
Protein Name Serine/threonine-protein kinase 10
Gene Name STK10
Organism Homo sapiens (Human).
Sequence Length 968
Subcellular Localization Cell membrane
Peripheral membrane protein .
Protein Description Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo..
Protein Sequence MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNEVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYHDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHSKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLEHPFVSSITSNKALRELVAEAKAEVMEEIEDGRDEGEEEDAVDAASTLENHTQNSSEVSPPSLNADKPLEESPSTPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVAPGNENGLAVPVPLRKSRPVSMDARIQVAQEKQVAEQGGDLSPAANRSQKASQSRPNSSALETLGGEKLANGSLEPPAQAAPGPSKRDSDCSSLCTSESMDYGTNLSTDLSLNKEMGSLSIKDPKLYKKTLKRTRKFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSNKHELQLEQMHKRFEQEINAKKKFFDTELENLERQQKQQVEKMEQDHAVRRREEARRIRLEQDRDYTRFQEQLKLMKKEVKNEVEKLPRQQRKESMKQKMEEHTQKKQLLDRDFVAKQKEDLELAMKRLTTDNRREICDKERECLMKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKVRQQQEKARLPKIQRSEGKTRMAMYKKSLHINGGGSAAEQREKIKQFSQQEEKRQKSERLQQQQKHENQMRDMLAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQNLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAECPNPSTPSKAAKFFPYSSADAS
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
11MethylationANFRRILRLSTFEKR
HHHHHHHHHHHHHHH		24.99115482217
13PhosphorylationFRRILRLSTFEKRKS
HHHHHHHHHHHHHHH		25.3129255136
14PhosphorylationRRILRLSTFEKRKSR
HHHHHHHHHHHHHHH		40.1729255136
20PhosphorylationSTFEKRKSREYEHVR
HHHHHHHHHHHHHHH		34.0823401153
23PhosphorylationEKRKSREYEHVRRDL
HHHHHHHHHHHHCCC		15.3830266825
51UbiquitinationDGAFGKVYKAKNKET
CCCCCEEEEECCCCC		14.5522817900
56UbiquitinationKVYKAKNKETGALAA
EEEEECCCCCCCCHH		56.8229967540
65UbiquitinationTGALAAAKVIETKSE
CCCCHHHEEECCCCH		38.7329967540
73UbiquitinationVIETKSEEELEDYIV
EECCCCHHHHHHHEE		74.9922817900
76UbiquitinationTKSEEELEDYIVEIE
CCCHHHHHHHEEEEE		52.6422817900
151UbiquitinationALNFLHSKRIIHRDL
HHHHHHHCCEECCCC		36.55-
159UbiquitinationRIIHRDLKAGNVLMT
CEECCCCCCCCEEEE		59.5422817900
166PhosphorylationKAGNVLMTLEGDIRL
CCCCEEEEEECCEEH		19.93-
179PhosphorylationRLADFGVSAKNLKTL
EHHHCCCCHHHHHHH		33.6327067055
181UbiquitinationADFGVSAKNLKTLQK
HHCCCCHHHHHHHHH		56.1322817900
184UbiquitinationGVSAKNLKTLQKRDS
CCCHHHHHHHHHCCC		57.4922817900
185PhosphorylationVSAKNLKTLQKRDSF
CCHHHHHHHHHCCCC		37.2723401153
191PhosphorylationKTLQKRDSFIGTPYW
HHHHHCCCCCCCCCC		23.8523401153
195PhosphorylationKRDSFIGTPYWMAPE
HCCCCCCCCCCCCCE		14.3720058876
197PhosphorylationDSFIGTPYWMAPEVV
CCCCCCCCCCCCEEE		13.9820058876
208PhosphorylationPEVVMCETMKDTPYD
CEEEEECCCCCCCCC		25.2923401153
212PhosphorylationMCETMKDTPYDYKAD
EECCCCCCCCCCHHH		20.4529978859
214PhosphorylationETMKDTPYDYKADIW
CCCCCCCCCCHHHHH		33.7222210691
248AcetylationNPMRVLLKIAKSDPP
CHHHHHHHHHCCCCC		36.1425953088
248MalonylationNPMRVLLKIAKSDPP
CHHHHHHHHHCCCCC		36.1426320211
252PhosphorylationVLLKIAKSDPPTLLT
HHHHHHCCCCCCEEC		46.4529083192
256PhosphorylationIAKSDPPTLLTPSKW
HHCCCCCCEECCCCC		39.5329083192
259PhosphorylationSDPPTLLTPSKWSVE
CCCCCEECCCCCCEE		28.7325159151
261PhosphorylationPPTLLTPSKWSVEFR
CCCEECCCCCCEEHH		41.3329083192
262UbiquitinationPTLLTPSKWSVEFRD
CCEECCCCCCEEHHH		44.7029967540
264PhosphorylationLLTPSKWSVEFRDFL
EECCCCCCEEHHHHH		18.5927067055
277UbiquitinationFLKIALDKNPETRPS
HHHHHHCCCCCCCCC		75.2229967540
295PhosphorylationLLEHPFVSSITSNKA
HHHCCCHHHHCCCHH		19.1923312004
296PhosphorylationLEHPFVSSITSNKAL
HHCCCHHHHCCCHHH		25.2823312004
298PhosphorylationHPFVSSITSNKALRE
CCCHHHHCCCHHHHH		28.3523312004
299PhosphorylationPFVSSITSNKALREL
CCHHHHCCCHHHHHH		34.3623312004
301UbiquitinationVSSITSNKALRELVA
HHHHCCCHHHHHHHH		48.8729967540
361PhosphorylationADKPLEESPSTPLAP
CCCCCCCCCCCCCCC		18.1225627689
363PhosphorylationKPLEESPSTPLAPSQ
CCCCCCCCCCCCCCC		52.5225627689
364PhosphorylationPLEESPSTPLAPSQS
CCCCCCCCCCCCCCC		26.2125627689
369PhosphorylationPSTPLAPSQSQDSVN
CCCCCCCCCCCCCCC		36.5426074081
371PhosphorylationTPLAPSQSQDSVNEP
CCCCCCCCCCCCCCC		40.0525849741
374PhosphorylationAPSQSQDSVNEPCSQ
CCCCCCCCCCCCCCC		21.1429507054
387PhosphorylationSQPSGDRSLQTTSPP
CCCCCCCCCCCCCCC		29.5722115753
390PhosphorylationSGDRSLQTTSPPVVA
CCCCCCCCCCCCEEC		34.2425159151
391PhosphorylationGDRSLQTTSPPVVAP
CCCCCCCCCCCEECC		26.6925159151
392PhosphorylationDRSLQTTSPPVVAPG
CCCCCCCCCCEECCC		30.5125159151
413PhosphorylationVPVPLRKSRPVSMDA
CCCCCCCCCCCCHHH		35.0723403867
417PhosphorylationLRKSRPVSMDARIQV
CCCCCCCCHHHHHHH		17.3923401153
438PhosphorylationAEQGGDLSPAANRSQ
HHCCCCCCHHHHHHH		19.7519664994
444PhosphorylationLSPAANRSQKASQSR
CCHHHHHHHHHHHCC		35.5228450419
446UbiquitinationPAANRSQKASQSRPN
HHHHHHHHHHHCCCC		51.7829967540
448PhosphorylationANRSQKASQSRPNSS
HHHHHHHHHCCCCCH		35.4123927012
450PhosphorylationRSQKASQSRPNSSAL
HHHHHHHCCCCCHHH		47.4019664994
454PhosphorylationASQSRPNSSALETLG
HHHCCCCCHHHHHHC		21.4819664994
455PhosphorylationSQSRPNSSALETLGG
HHCCCCCHHHHHHCC		43.4419664994
459PhosphorylationPNSSALETLGGEKLA
CCCHHHHHHCCCCCC		31.3923927012
469PhosphorylationGEKLANGSLEPPAQA
CCCCCCCCCCCCCCC		29.3925850435
481PhosphorylationAQAAPGPSKRDSDCS
CCCCCCCCCCCCCCH		46.3626074081
485PhosphorylationPGPSKRDSDCSSLCT
CCCCCCCCCCHHHCC		44.5430576142
488PhosphorylationSKRDSDCSSLCTSES
CCCCCCCHHHCCCCC		31.1926074081
489PhosphorylationKRDSDCSSLCTSESM
CCCCCCHHHCCCCCC		33.5225159151
492PhosphorylationSDCSSLCTSESMDYG
CCCHHHCCCCCCCCC		40.6026074081
493PhosphorylationDCSSLCTSESMDYGT
CCHHHCCCCCCCCCC		27.0326074081
495PhosphorylationSSLCTSESMDYGTNL
HHHCCCCCCCCCCCC		19.4028270605
500PhosphorylationSESMDYGTNLSTDLS
CCCCCCCCCCCCCCC		27.1030576142
503PhosphorylationMDYGTNLSTDLSLNK
CCCCCCCCCCCCCCH		23.1930576142
504PhosphorylationDYGTNLSTDLSLNKE
CCCCCCCCCCCCCHH		44.0930576142
507PhosphorylationTNLSTDLSLNKEMGS
CCCCCCCCCCHHCCC		32.4822210691
514PhosphorylationSLNKEMGSLSIKDPK
CCCHHCCCCCCCCHH		20.0323401153
516PhosphorylationNKEMGSLSIKDPKLY
CHHCCCCCCCCHHHH		29.3230266825
530PhosphorylationYKKTLKRTRKFVVDG
HHHHHHHHHCEEECC		36.30-
544PhosphorylationGVEVSITTSKIISED
CEEEEEEHHHCCCCC		26.7630576142
545PhosphorylationVEVSITTSKIISEDE
EEEEEEHHHCCCCCH		17.1330576142
549PhosphorylationITTSKIISEDEKKDE
EEHHHCCCCCHHHHH		42.3330576142
6052-HydroxyisobutyrylationFEQEINAKKKFFDTE
HHHHHHHHHHHHHHH		52.59-
621UbiquitinationENLERQQKQQVEKME
HHHHHHHHHHHHHHH		34.07-
665MalonylationKLMKKEVKNEVEKLP
HHHHHHHHHHHHHCH		48.7826320211
679PhosphorylationPRQQRKESMKQKMEE
HHHHHHHHHHHHHHH		34.02-
688PhosphorylationKQKMEEHTQKKQLLD
HHHHHHHHHHHHHHC		45.42-
690AcetylationKMEEHTQKKQLLDRD
HHHHHHHHHHHHCHH		43.5830590125
701UbiquitinationLDRDFVAKQKEDLEL
HCHHHHHHHHHHHHH		57.5133845483
714UbiquitinationELAMKRLTTDNRREI
HHHHHHHCCCCHHHH		35.8223000965
715UbiquitinationLAMKRLTTDNRREIC
HHHHHHCCCCHHHHH		35.5523000965
746SulfoxidationREAALWEMEEHQLQE
HHHHHHHHHHHHHHH		5.0430846556
759UbiquitinationQERHQLVKQQLKDQY
HHHHHHHHHHHHHHH		40.7029967540
766PhosphorylationKQQLKDQYFLQRHEL
HHHHHHHHHHHHHHH		19.1828102081
787PhosphorylationEREQMQRYNQRMIEQ
HHHHHHHHHHHHHHH		9.9624245541
796UbiquitinationQRMIEQLKVRQQQEK
HHHHHHHHHHHHHHH		34.7629967540
822UbiquitinationKTRMAMYKKSLHING
CCCEEEEEECCCCCC		23.8523000965
823UbiquitinationTRMAMYKKSLHINGG
CCEEEEEECCCCCCC		40.5423000965
824PhosphorylationRMAMYKKSLHINGGG
CEEEEEECCCCCCCC		22.4922777824
832PhosphorylationLHINGGGSAAEQREK
CCCCCCCCHHHHHHH		27.8124719451
841UbiquitinationAEQREKIKQFSQQEE
HHHHHHHHHHHHHHH		57.2529967540
844PhosphorylationREKIKQFSQQEEKRQ
HHHHHHHHHHHHHHH		28.5820068231
849UbiquitinationQFSQQEEKRQKSERL
HHHHHHHHHHHHHHH		60.42-
942PhosphorylationQEMFFKLSEEAECPN
HHHHHHHHHCCCCCC		33.7023403867
951PhosphorylationEAECPNPSTPSKAAK
CCCCCCCCCCCHHHH		60.6429255136
952PhosphorylationAECPNPSTPSKAAKF
CCCCCCCCCCHHHHC		32.6016175573
954PhosphorylationCPNPSTPSKAAKFFP
CCCCCCCCHHHHCCC		34.7130266825
962PhosphorylationKAAKFFPYSSADAS-
HHHHCCCCCCCCCC-		15.3129978859
963PhosphorylationAAKFFPYSSADAS--
HHHCCCCCCCCCC--		21.2026074081
964PhosphorylationAKFFPYSSADAS---
HHCCCCCCCCCC---		25.0726074081
968PhosphorylationPYSSADAS-------
CCCCCCCC-------		41.1025159151
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

Oops, there are no upstream regulatory protein records of STK10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STK10_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 STK10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIFC1_HUMANKIFC1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
273300Testicular germ cell tumor (TGCT)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STK10_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 SER-438 AND SER-450, 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-13; SER-20; THR-185;SER-191; THR-391; SER-438; SER-444; SER-448; SER-450; SER-454;SER-514; SER-549; SER-951 AND THR-952, 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-438; SER-450; SER-454;SER-455; SER-951 AND THR-952, 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 SER-13; THR-185; SER-191;SER-438; SER-454 AND THR-952, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-14; SER-20;THR-185; SER-191; SER-392; SER-438 AND THR-952, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"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-438, AND MASSSPECTROMETRY.
"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-438, AND MASSSPECTROMETRY.

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