STA5A_HUMAN - dbPTM
STA5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STA5A_HUMAN
UniProt AC P42229
Protein Name Signal transducer and activator of transcription 5A
Gene Name STAT5A
Organism Homo sapiens (Human).
Sequence Length 794
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. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation..
Protein Sequence MAGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPQDRAQATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQKTYDRCPLELVRCIRHILYNEQRLVREANNCSSPAGILVDAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFAQLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNECSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGSNELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGWNYTFWQWFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPERNLWNLKPFTTRDFSIRSLADRLGDLSYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVNASADAGGSSATYMDQAPSPAVCPQAPYNMYPQNPDHVLDQDGEFDLDETMDVARHVEELLRRPMDSLDSRLSPPAGLFTSARGSLS
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
22PhosphorylationLRQMQVLYGQHFPIE
HHHHHHHHCCCCCHH		18.84-
70UbiquitinationGLVQELQKKAEHQVG
HHHHHHHHHHHHHCC		67.58-
71UbiquitinationLVQELQKKAEHQVGE
HHHHHHHHHHHHCCC		46.15-
84AcetylationGEDGFLLKIKLGHYA
CCCCEEEEEHHHHHH		39.6820167786
84UbiquitinationGEDGFLLKIKLGHYA
CCCCEEEEEHHHHHH		39.68-
86UbiquitinationDGFLLKIKLGHYATQ
CCEEEEEHHHHHHHH		46.99-
90PhosphorylationLKIKLGHYATQLQKT
EEEHHHHHHHHHHHH		15.0016464493
92PhosphorylationIKLGHYATQLQKTYD
EHHHHHHHHHHHHHC		23.73-
92O-linked_GlycosylationIKLGHYATQLQKTYD
EHHHHHHHHHHHHHC		23.7328074064
114PhosphorylationRCIRHILYNEQRLVR
HHHHHHHHCHHHHHH		18.9520090780
127PhosphorylationVREANNCSSPAGILV
HHHHHCCCCCCHHHH		41.2923401153
128PhosphorylationREANNCSSPAGILVD
HHHHCCCCCCHHHHH		22.4423401153
163UbiquitinationQDTENELKKLQQTQE
CCCHHHHHHHHHHHH		45.30-
164UbiquitinationDTENELKKLQQTQEY
CCHHHHHHHHHHHHE		65.24-
168PhosphorylationELKKLQQTQEYFIIQ
HHHHHHHHHHEEHHH		15.4824043423
171PhosphorylationKLQQTQEYFIIQYQE
HHHHHHHEEHHHHHH		7.1124043423
176PhosphorylationQEYFIIQYQESLRIQ
HHEEHHHHHHHHHHH		12.1124043423
179PhosphorylationFIIQYQESLRIQAQF
EHHHHHHHHHHHHHH		13.8624043423
193PhosphorylationFAQLAQLSPQERLSR
HHHHHCCCHHHHHCH		16.6823401153
199PhosphorylationLSPQERLSRETALQQ
CCHHHHHCHHHHHHH		34.0027174698
207UbiquitinationRETALQQKQVSLEAW
HHHHHHHHHHHHHHH		39.4421890473
232UbiquitinationYRVELAEKHQKTLQL
HHHHHHHHHHHHHHH		45.81-
235UbiquitinationELAEKHQKTLQLLRK
HHHHHHHHHHHHHHH		51.42-
242UbiquitinationKTLQLLRKQQTIILD
HHHHHHHHCCEEEEC		46.88-
245PhosphorylationQLLRKQQTIILDDEL
HHHHHCCEEEECHHH		13.90-
256UbiquitinationDDELIQWKRRQQLAG
CHHHHHHHHHHHHCC		22.71-
256SumoylationDDELIQWKRRQQLAG
CHHHHHHHHHHHHCC		22.71-
336SumoylationTSTFIIEKQPPQVLK
HCEEEHCCCCCCCCC		58.66-
343UbiquitinationKQPPQVLKTQTKFAA
CCCCCCCCCCCCCHH		39.47-
347AcetylationQVLKTQTKFAATVRL
CCCCCCCCCHHHHHH		24.1625953088
359UbiquitinationVRLLVGGKLNVHMNP
HHHHHCCEEEECCCC		30.84-
370UbiquitinationHMNPPQVKATIISEQ
CCCCHHHHEEECCHH		34.27-
372PhosphorylationNPPQVKATIISEQQA
CCHHHHEEECCHHHH		17.0822817900
375PhosphorylationQVKATIISEQQAKSL
HHHEEECCHHHHHHH		26.0422817900
380UbiquitinationIISEQQAKSLLKNEN
ECCHHHHHHHHCCCC		36.98-
381PhosphorylationISEQQAKSLLKNENT
CCHHHHHHHHCCCCC		41.7824719451
384SumoylationQQAKSLLKNENTRNE
HHHHHHHCCCCCCCC		68.46-
384UbiquitinationQQAKSLLKNENTRNE
HHHHHHHCCCCCCCC		68.46-
384AcetylationQQAKSLLKNENTRNE
HHHHHHHCCCCCCCC		68.467365045
384SumoylationQQAKSLLKNENTRNE
HHHHHHHCCCCCCCC		68.46-
516UbiquitinationEALNMKFKAEVQSNR
HHHCCHHHHHHHHCC		37.81-
516SumoylationEALNMKFKAEVQSNR
HHHCCHHHHHHHHCC		37.81-
516SumoylationEALNMKFKAEVQSNR
HHHCCHHHHHHHHCC		37.81-
527UbiquitinationQSNRGLTKENLVFLA
HHCCCCCHHHHHHHH		50.0421890473
527UbiquitinationQSNRGLTKENLVFLA
HHCCCCCHHHHHHHH		50.0421890473
586UbiquitinationEVLKKHHKPHWNDGA
HHHHHHCCCCCCCCC		37.99-
644UbiquitinationERNLWNLKPFTTRDF
CCCCCCCCCCCCCCC		34.57-
647PhosphorylationLWNLKPFTTRDFSIR
CCCCCCCCCCCCHHH		29.46-
648PhosphorylationWNLKPFTTRDFSIRS
CCCCCCCCCCCHHHH		28.72-
655PhosphorylationTRDFSIRSLADRLGD
CCCCHHHHHHHHHCC		26.6622817900
668PhosphorylationGDLSYLIYVFPDRPK
CCCEEEEEECCCCCC		8.08-
675UbiquitinationYVFPDRPKDEVFSKY
EECCCCCCCHHHHHC		68.37-
681UbiquitinationPKDEVFSKYYTPVLA
CCCHHHHHCCHHHHH		30.71-
682PhosphorylationKDEVFSKYYTPVLAK
CCHHHHHCCHHHHHH		16.0425159151
683PhosphorylationDEVFSKYYTPVLAKA
CHHHHHCCHHHHHHH		14.3322817900
689UbiquitinationYYTPVLAKAVDGYVK
CCHHHHHHHHCCCCC		44.79-
694PhosphorylationLAKAVDGYVKPQIKQ
HHHHHCCCCCHHHHH		10.8021918175
696UbiquitinationKAVDGYVKPQIKQVV
HHHCCCCCHHHHHHH		23.79-
696SumoylationKAVDGYVKPQIKQVV
HHHCCCCCHHHHHHH		23.79-
696AcetylationKAVDGYVKPQIKQVV
HHHCCCCCHHHHHHH		23.7923954790
696SumoylationKAVDGYVKPQIKQVV
HHHCCCCCHHHHHHH		23.79-
700AcetylationGYVKPQIKQVVPEFV
CCCCHHHHHHHHHHH		31.62300368799
700SumoylationGYVKPQIKQVVPEFV
CCCCHHHHHHHHHHH		31.62-
720PhosphorylationAGGSSATYMDQAPSP
CCCCCCCCCCCCCCC		9.83-
726PhosphorylationTYMDQAPSPAVCPQA
CCCCCCCCCCCCCCC		28.6221716071
774PhosphorylationLLRRPMDSLDSRLSP
HHHCCHHHCCCCCCC		28.0223898821
777PhosphorylationRPMDSLDSRLSPPAG
CCHHHCCCCCCCCCC		40.1823401153
780PhosphorylationDSLDSRLSPPAGLFT
HHCCCCCCCCCCCCC		27.9423401153
787PhosphorylationSPPAGLFTSARGSLS
CCCCCCCCCCCCCCC		26.9023403867
788PhosphorylationPPAGLFTSARGSLS-
CCCCCCCCCCCCCC-		14.5023403867
792PhosphorylationLFTSARGSLS-----
CCCCCCCCCC-----		21.6424670416
794PhosphorylationTSARGSLS-------
CCCCCCCC-------		39.6123917254
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
694YPhosphorylationKinaseHCKP08631
PSP
694YPhosphorylationKinaseJAK1P23458
PSP
694YPhosphorylationKinaseJAK2O60674
Uniprot
694YPhosphorylationKinaseJAK3P52333
PSP
694YPhosphorylationKinaseSYKP43405
PSP
694YPhosphorylationKinaseLCKP06239
PSP
694YPhosphorylationKinaseLYNP07948
PhosphoELM
694YPhosphorylationKinaseLYNP25911
PSP
694YPhosphorylationKinaseMERTKQ12866
GPS
694YPhosphorylationKinaseSRCP12931
PSP
694YPhosphorylationKinaseAXLP30530
PSP
694YPhosphorylationKinaseSRC64-PhosphoELM
780SPhosphorylationKinaseMAPK1P28482
GPS
780SPhosphorylationKinaseMAPK3P27361
GPS
-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 STA5A_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 STA5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRDC1_HUMANPRTFDC1physical
16189514
JAK2_HUMANJAK2physical
9575217
ESR1_HUMANESR1physical
11682624
ESR2_HUMANESR2physical
11682624
EGFR_HUMANEGFRphysical
10358079
JAK1_HUMANJAK1physical
9047382
MK01_HUMANMAPK1physical
10194762
PTN11_HUMANPTPN11physical
12060651
CD3Z_HUMANCD247physical
9880255
NCOA1_HUMANNCOA1physical
12954634
HDAC1_HUMANHDAC1physical
12574125
FGFR2_HUMANFGFR2physical
21464042
PRGR_HUMANPGRphysical
21464042
GBB2_HUMANGNB2physical
21900206
MYB_HUMANMYBphysical
19036881
BTK_HUMANBTKphysical
11413148
CBL_HUMANCBLphysical
23533197
STA5A_HUMANSTAT5Aphysical
21988832
UD2B4_HUMANUGT2B4physical
21988832
TXD11_HUMANTXNDC11physical
21988832
ZN596_HUMANZNF596physical
21988832
HTF4_HUMANTCF12physical
25416956
PPARG_HUMANPPARGphysical
23223023
PPARG_HUMANPPARGphysical
18927468
NLK_HUMANNLKphysical
24394665
NARF_HUMANNARFphysical
24394665
OLIG1_HUMANOLIG1physical
25814554
CBL_HUMANCBLphysical
25814554
ADDG_HUMANADD3physical
26496610
ODP2_HUMANDLATphysical
26496610
ODPA_HUMANPDHA1physical
26496610
ODPB_HUMANPDHBphysical
26496610
ICAM5_HUMANICAM5physical
26496610
ODPX_HUMANPDHXphysical
26496610
GDF15_HUMANGDF15physical
26496610
SYFM_HUMANFARS2physical
26496610
RNF13_HUMANRNF13physical
26496610
R3HD2_HUMANR3HDM2physical
26496610
ERMP1_HUMANERMP1physical
26496610
ILKAP_HUMANILKAPphysical
26496610
SPICE_HUMANSPICE1physical
26496610
GHR_HUMANGHRphysical
25241761
CTLA4_HUMANCTLA4physical
25241761
MK01_HUMANMAPK1physical
25241761
STA5B_HUMANSTAT5Bphysical
28514442
PDK2_HUMANPDK2physical
28514442
PDK3_HUMANPDK3physical
28514442
KLHL7_HUMANKLHL7physical
28514442
ODPA_HUMANPDHA1physical
28514442
ODPB_HUMANPDHBphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STA5A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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 THR-372 AND SER-375, 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-694, 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-694, 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 TYR-694, AND MASSSPECTROMETRY.
"STAT5a activation mediates the epithelial to mesenchymal transitioninduced by oncogenic RhoA.";
Benitah S.A., Valeron P.F., Rui H., Lacal J.C.;
Mol. Biol. Cell 14:40-53(2003).
Cited for: PHOSPHORYLATION AT TYR-694 BY JAK2.

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