STA5B_HUMAN - dbPTM
STA5B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STA5B_HUMAN
UniProt AC P51692
Protein Name Signal transducer and activator of transcription 5B
Gene Name STAT5B
Organism Homo sapiens (Human).
Sequence Length 787
Subcellular Localization Cytoplasm . Nucleus . Translocated into the nucleus in response to phosphorylation..
Protein Description Carries out a dual signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation..
Protein Sequence MAVWIQAQQLQGEALHQMQALYGQHFPIEVRHYLSQWIESQAWDSVDLDNPQENIKATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNGSSPAGSLADAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFGPLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNDYSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRSDRRGAESVTEEKFTILFESQFSVGGNELVFQVKTLSLPVVVIVHGSQDNNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGRNYTFWQWFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCESATAKAVDGYVKPQIKQVVPEFVNASADAGGGSATYMDQAPSPAVCPQAHYNMYPQNPDSVLDTDGDFDLEDTMDVARRVEELLGRPMDSQWIPHAQS
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
56SumoylationDNPQENIKATQLLEG
CCHHHHHHHHHHHHH		57.89-
69UbiquitinationEGLVQELQKKAEHQV
HHHHHHHHHHHHHHC		44.4422505724
70UbiquitinationGLVQELQKKAEHQVG
HHHHHHHHHHHHHCC		67.5829967540
71UbiquitinationLVQELQKKAEHQVGE
HHHHHHHHHHHHCCC		46.1529967540
84AcetylationGEDGFLLKIKLGHYA
CCCCEEEEEHHHHHH		39.68-
84UbiquitinationGEDGFLLKIKLGHYA
CCCCEEEEEHHHHHH		39.68-
86UbiquitinationDGFLLKIKLGHYATQ
CCEEEEEHHHHHHHH		46.9929967540
90PhosphorylationLKIKLGHYATQLQNT
EEEHHHHHHHHHHHH		15.0020090780
92PhosphorylationIKLGHYATQLQNTYD
EHHHHHHHHHHHHHH		23.73-
98PhosphorylationATQLQNTYDRCPMEL
HHHHHHHHHCCHHHH		14.6716497976
113UbiquitinationVRCIRHILYNEQRLV
HHHHHHHHHCHHHHH		2.8422053931
114PhosphorylationRCIRHILYNEQRLVR
HHHHHHHHCHHHHHH		18.9520090780
127PhosphorylationVREANNGSSPAGSLA
HHHHCCCCCCCCHHH		34.9623401153
128PhosphorylationREANNGSSPAGSLAD
HHHCCCCCCCCHHHH		21.8421955146
132PhosphorylationNGSSPAGSLADAMSQ
CCCCCCCHHHHHHHH		23.6121712546
138PhosphorylationGSLADAMSQKHLQIN
CHHHHHHHHHHHHHC		37.4923403867
140UbiquitinationLADAMSQKHLQINQT
HHHHHHHHHHHHCHH		38.69-
163UbiquitinationQDTENELKKLQQTQE
CCCHHHHHHHHHHHH		45.3022505724
164UbiquitinationDTENELKKLQQTQEY
CCHHHHHHHHHHHHE		65.24-
168PhosphorylationELKKLQQTQEYFIIQ
HHHHHHHHHHEEEEE		15.4824043423
171PhosphorylationKLQQTQEYFIIQYQE
HHHHHHHEEEEEEHH		7.1124043423
176PhosphorylationQEYFIIQYQESLRIQ
HHEEEEEEHHHHHHH		12.1124043423
179PhosphorylationFIIQYQESLRIQAQF
EEEEEHHHHHHHHHH		13.8624043423
193PhosphorylationFGPLAQLSPQERLSR
HCCHHHCCHHHHHCH		16.6829255136
207UbiquitinationRETALQQKQVSLEAW
HHHHHHHHHHHHHHH		39.4422053931
232UbiquitinationYRVELAEKHQKTLQL
HHHHHHHHHHHHHHH		45.8129967540
235UbiquitinationELAEKHQKTLQLLRK
HHHHHHHHHHHHHHH		51.4229967540
242UbiquitinationKTLQLLRKQQTIILD
HHHHHHHHCCEEEEC		46.8829967540
245PhosphorylationQLLRKQQTIILDDEL
HHHHHCCEEEECHHH		13.90-
256UbiquitinationDDELIQWKRRQQLAG
CHHHHHHHHHHHHCC		22.7129967540
256SumoylationDDELIQWKRRQQLAG
CHHHHHHHHHHHHCC		22.71-
336SumoylationTSTFIIEKQPPQVLK
HCEEEEECCCCCCCC		58.66-
343UbiquitinationKQPPQVLKTQTKFAA
CCCCCCCCCCCCCHH		39.4729967540
359UbiquitinationVRLLVGGKLNVHMNP
HHHHHCCEEEECCCC		30.8429967540
370UbiquitinationHMNPPQVKATIISEQ
CCCCHHHHEEECCHH		34.2729967540
372PhosphorylationNPPQVKATIISEQQA
CCHHHHEEECCHHHH		17.0822817900
375PhosphorylationQVKATIISEQQAKSL
HHHEEECCHHHHHHH		26.0422817900
380UbiquitinationIISEQQAKSLLKNEN
ECCHHHHHHHHHCCC		36.9829967540
381PhosphorylationISEQQAKSLLKNENT
CCHHHHHHHHHCCCC		41.7824719451
384SumoylationQQAKSLLKNENTRND
HHHHHHHHCCCCCCC		68.46-
384UbiquitinationQQAKSLLKNENTRND
HHHHHHHHCCCCCCC		68.4629967540
384AcetylationQQAKSLLKNENTRND
HHHHHHHHCCCCCCC		68.467365059
384SumoylationQQAKSLLKNENTRND
HHHHHHHHCCCCCCC		68.46-
392PhosphorylationNENTRNDYSGEILNN
CCCCCCCCCCHHHHC		23.3220090780
433UbiquitinationRSDRRGAESVTEEKF
HHCCCCCCCCCHHHE		48.8721890473
516UbiquitinationEALNMKFKAEVQSNR
HHHCCHHHHHHHHCC		37.8129967540
516SumoylationEALNMKFKAEVQSNR
HHHCCHHHHHHHHCC		37.81-
516SumoylationEALNMKFKAEVQSNR
HHHCCHHHHHHHHCC		37.81-
527UbiquitinationQSNRGLTKENLVFLA
HHCCCCCHHHHHHHH		50.0421890473
583UbiquitinationGVMEVLKKHLKPHWN
HHHHHHHHHCCCCCC		50.4329967540
586UbiquitinationEVLKKHLKPHWNDGA
HHHHHHCCCCCCCCC		34.2629967540
607UbiquitinationKQQAHDLLINKPDGT
HHHHHHEEEECCCCE		5.1622505724
655PhosphorylationTRDFSIRSLADRLGD
CCCCCHHHHHHHHCC		26.6620068231
665PhosphorylationDRLGDLNYLIYVFPD
HHHCCCCEEEEECCC		11.1920068231
668PhosphorylationGDLNYLIYVFPDRPK
CCCCEEEEECCCCCC		8.0820068231
675SumoylationYVFPDRPKDEVYSKY
EECCCCCCCCCHHCC		68.37-
675UbiquitinationYVFPDRPKDEVYSKY
EECCCCCCCCCHHCC		68.37-
679PhosphorylationDRPKDEVYSKYYTPV
CCCCCCCHHCCCCCC		9.4412621061
681UbiquitinationPKDEVYSKYYTPVPC
CCCCCHHCCCCCCCC		25.2929967540
681AcetylationPKDEVYSKYYTPVPC
CCCCCHHCCCCCCCC		25.29124968639
682PhosphorylationKDEVYSKYYTPVPCE
CCCCHHCCCCCCCCC		13.4625159151
683PhosphorylationDEVYSKYYTPVPCES
CCCHHCCCCCCCCCC		14.3325159151
684PhosphorylationEVYSKYYTPVPCESA
CCHHCCCCCCCCCCC		18.0823186163
690PhosphorylationYTPVPCESATAKAVD
CCCCCCCCCCCHHCC		37.3228555341
692PhosphorylationPVPCESATAKAVDGY
CCCCCCCCCHHCCCC		37.66-
694UbiquitinationPCESATAKAVDGYVK
CCCCCCCHHCCCCCC		44.5929967540
694AcetylationPCESATAKAVDGYVK
CCCCCCCHHCCCCCC		44.59124968643
699PhosphorylationTAKAVDGYVKPQIKQ
CCHHCCCCCCHHHHH		10.8022322096
701UbiquitinationKAVDGYVKPQIKQVV
HHCCCCCCHHHHHHH		23.7929967540
701SumoylationKAVDGYVKPQIKQVV
HHCCCCCCHHHHHHH		23.79-
701AcetylationKAVDGYVKPQIKQVV
HHCCCCCCHHHHHHH		23.7919608861
701SumoylationKAVDGYVKPQIKQVV
HHCCCCCCHHHHHHH		23.7919608861
705AcetylationGYVKPQIKQVVPEFV
CCCCHHHHHHHHHHH		31.62124968641
705SumoylationGYVKPQIKQVVPEFV
CCCCHHHHHHHHHHH		31.62-
725PhosphorylationAGGGSATYMDQAPSP
CCCCCCCCCCCCCCC		9.8316772534
731PhosphorylationTYMDQAPSPAVCPQA
CCCCCCCCCCCCCCC		28.6222442148
740PhosphorylationAVCPQAHYNMYPQNP
CCCCCCCCCCCCCCC		12.4918550772
743PhosphorylationPQAHYNMYPQNPDSV
CCCCCCCCCCCCCCC		9.6818550772
749PhosphorylationMYPQNPDSVLDTDGD
CCCCCCCCCCCCCCC		26.3226074081
787PhosphorylationQWIPHAQS-------
CCCCCCCC-------		42.8625159151
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
679YPhosphorylationKinaseSRCP12931
GPS
679YPhosphorylationKinaseSRC64-PhosphoELM
699YPhosphorylationKinaseEGFRP00533
GPS
699YPhosphorylationKinaseHCKP08631
Uniprot
699YPhosphorylationKinaseMERTKQ12866
GPS
699YPhosphorylationKinaseBRKQ13882
PSP
699YPhosphorylationKinaseSRCP12931
PSP
699YPhosphorylationKinaseAXLP30530
PSP
699YPhosphorylationKinaseJAK-FAMILY-GPS
699YPhosphorylationKinaseJAK-Uniprot
725YPhosphorylationKinaseEGFRP00533
PhosphoELM
731SPhosphorylationKinasePIM1P11309
PSP
731SPhosphorylationKinasePIM2Q9P1W9
PSP
731SPhosphorylationKinasePIM3Q86V86
PSP
740YPhosphorylationKinaseEGFRP00533
PhosphoELM
743YPhosphorylationKinaseEGFRP00533
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STA5B_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 STA5B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JAK2_HUMANJAK2physical
9575217
JAK1_HUMANJAK1physical
9047382
GCR_HUMANNR3C1physical
8878484
CD3Z_HUMANCD247physical
9880255
FGFR2_HUMANFGFR2physical
21464042
PRGR_HUMANPGRphysical
21464042
STA5B_HUMANSTAT5Bphysical
20962278
PRLR_HUMANPRLRphysical
20962278
A4_HUMANAPPphysical
21832049
TFG_HUMANTFGphysical
21988832
SYAC_HUMANAARSphysical
22863883
ANKY2_HUMANANKMY2physical
22863883
NIF3L_HUMANNIF3L1physical
22863883
RPR1A_HUMANRPRD1Aphysical
22863883
TM1L1_HUMANTOM1L1physical
22863883
MCMBP_HUMANMCMBPphysical
26344197
ODP2_HUMANDLATphysical
26496610
DLDH_HUMANDLDphysical
26496610
ZEP1_HUMANHIVEP1physical
26496610
ODPA_HUMANPDHA1physical
26496610
ODPB_HUMANPDHBphysical
26496610
ODPX_HUMANPDHXphysical
26496610
MVP_HUMANMVPphysical
26496610
KANL3_HUMANKANSL3physical
26496610
ASF1B_HUMANASF1Bphysical
26496610
PUS7L_HUMANPUS7Lphysical
26496610
GHR_HUMANGHRphysical
25241761
CTLA4_HUMANCTLA4physical
25241761
STAT3_HUMANSTAT3physical
25241761
STA5B_HUMANSTAT5Bphysical
22729867
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
245590Growth hormone insensitivity with immunodeficiency (GHII)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01254Dasatinib
Regulatory Network of STA5B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-701, AND MASS SPECTROMETRY.
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-128 AND SER-193, 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-193, AND MASSSPECTROMETRY.
"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-128 AND SER-193, 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-193, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-699, AND MASSSPECTROMETRY.
"Signal transducer and activator of transcription 5b: a new target ofbreast tumor kinase/protein tyrosine kinase 6.";
Weaver A.M., Silva C.M.;
Breast Cancer Res. 9:R79-R79(2007).
Cited for: PHOSPHORYLATION AT TYR-699 BY PTK6.
"The Src family kinase Hck couples BCR/ABL to STAT5 activation inmyeloid leukemia cells.";
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A.,Wilson M., Smithgall T.E., Skorski T.;
EMBO J. 21:5766-5774(2002).
Cited for: PHOSPHORYLATION AT TYR-699, AND MUTAGENESIS OF TYR-699.

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