STAP2_HUMAN - dbPTM
STAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAP2_HUMAN
UniProt AC Q9UGK3
Protein Name Signal-transducing adaptor protein 2
Gene Name STAP2
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization Cytoplasm .
Protein Description Substrate of protein kinase PTK6. May play a regulatory role in the acute-phase response in systemic inflammation and may modulate STAT3 activity..
Protein Sequence MASALRPPRVPKPKGVLPSHYYESFLEKKGPCDRDYKKFWAGLQGLTIYFYNSNRDFQHVEKLNLGAFEKLTDEIPWGSSRDPGTHFSLILRDQEIKFKVETLECREMWKGFILTVVELRVPTDLTLLPGHLYMMSEVLAKEEARRALETPSCFLKVSRLEAQLLLERYPECGNLLLRPSGDGADGVSVTTRQMHNGTHVVRHYKVKREGPKYVIDVEQPFSCTSLDAVVNYFVSHTKKALVPFLLDEDYEKVLGYVEADKENGENVWVAPSAPGPGPAPCTGGPKPLSPASSQDKLPPLPPLPNQEENYVTPIGDGPAVDYENQDVASSSWPVILKPKKLPKPPAKLPKPPVGPKPEPKVFNGGLGRKLPVSSAQPLFPTAGLADMTAELQKKLEKRRALEH
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
21PhosphorylationKGVLPSHYYESFLEK
CCCCCHHHHHHHHHH
17.1728152594
22PhosphorylationGVLPSHYYESFLEKK
CCCCHHHHHHHHHHH
10.3212540842
24PhosphorylationLPSHYYESFLEKKGP
CCHHHHHHHHHHHCC
21.0028857561
72PhosphorylationLGAFEKLTDEIPWGS
CCHHHHHCCCCCCCC
42.5330266825
79PhosphorylationTDEIPWGSSRDPGTH
CCCCCCCCCCCCCCC
20.5230266825
80PhosphorylationDEIPWGSSRDPGTHF
CCCCCCCCCCCCCCE
36.4430266825
191PhosphorylationADGVSVTTRQMHNGT
CCCEEEEEEEEECCE
19.42-
204PhosphorylationGTHVVRHYKVKREGP
CEEEEEEEEECCCCC
13.60-
250PhosphorylationPFLLDEDYEKVLGYV
HHHCCCCHHHHHCCE
18.6617368569
256PhosphorylationDYEKVLGYVEADKEN
CHHHHHCCEEECCCC
7.3126074081
272PhosphorylationENVWVAPSAPGPGPA
CEEEECCCCCCCCCC
37.0422199227
282PhosphorylationGPGPAPCTGGPKPLS
CCCCCCCCCCCCCCC
44.0822199227
289PhosphorylationTGGPKPLSPASSQDK
CCCCCCCCCCCCCCC
27.2625849741
292PhosphorylationPKPLSPASSQDKLPP
CCCCCCCCCCCCCCC
31.7322199227
293PhosphorylationKPLSPASSQDKLPPL
CCCCCCCCCCCCCCC
44.5025849741
310PhosphorylationLPNQEENYVTPIGDG
CCCCCCCCCCCCCCC
14.6912540842
322PhosphorylationGDGPAVDYENQDVAS
CCCCCCCCCCCCCCC
15.3512540842
329PhosphorylationYENQDVASSSWPVIL
CCCCCCCCCCCCEEE
25.4227642862
337UbiquitinationSSWPVILKPKKLPKP
CCCCEEECCCCCCCC
43.60-
388PhosphorylationTAGLADMTAELQKKL
CCCHHHHHHHHHHHH
19.96-

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
22YPhosphorylationKinaseJAK2O60674
PSP
22YPhosphorylationKinaseSRCP12931
Uniprot
250YPhosphorylationKinaseJAK2O60674
PSP
250YPhosphorylationKinaseBRKQ13882
PSP
250YPhosphorylationKinaseSRCP12931
PSP
310YPhosphorylationKinaseJAK2O60674
PSP
322YPhosphorylationKinaseJAK2O60674
PSP
322YPhosphorylationKinaseSRCP12931
Uniprot
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:19401194

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAP2_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 STAP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTK6_HUMANPTK6physical
10980601
CBL_HUMANCBLphysical
19401194
FAK1_HUMANPTK2physical
17675501
CSF1R_HUMANCSF1Rphysical
17512498
MYD88_HUMANMYD88physical
16365431
IKKB_HUMANIKBKBphysical
16365431
IKKA_HUMANCHUKphysical
16365431

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 STAP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation.";
Ikeda O., Miyasaka Y., Sekine Y., Mizushima A., Muromoto R., Nanbo A.,Yoshimura A., Matsuda T.;
Biochem. Biophys. Res. Commun. 384:71-75(2009).
Cited for: PHOSPHORYLATION AT TYR-250 BY PTK6, AND INTERACTION WITH PTK6.
"STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation inacute-phase response through its YXXQ motif.";
Minoguchi M., Minoguchi S., Aki D., Joo A., Yamamoto T., Yumioka T.,Matsuda T., Yoshimura A.;
J. Biol. Chem. 278:11182-11189(2003).
Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-22; TYR-250; TYR-310 ANDTYR-322, AND MUTAGENESIS OF TYR-22; TYR-250; TYR-310 AND TYR-322.

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