STYK1_HUMAN - dbPTM
STYK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STYK1_HUMAN
UniProt AC Q6J9G0
Protein Name Tyrosine-protein kinase STYK1
Gene Name STYK1
Organism Homo sapiens (Human).
Sequence Length 422
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description Probable tyrosine protein-kinase, which has strong transforming capabilities on a variety of cell lines. When overexpressed, it can also induce tumor cell invasion as well as metastasis in distant organs. May act by activating both MAP kinase and phosphatidylinositol 3'-kinases (PI3K) pathways (By similarity)..
Protein Sequence MGMTRMLLECSLSDKLCVIQEKQYEVIIVPTLLVTIFLILLGVILWLFIREQRTQQQRSGPQGIAPVPPPRDLSWEAGHGGNVALPLKETSVENFLGATTPALAKLQVPREQLSEVLEQICSGSCGPIFRANMNTGDPSKPKSVILKALKEPAGLHEVQDFLGRIQFHQYLGKHKNLVQLEGCCTEKLPLYMVLEDVAQGDLLSFLWTCRRDVMTMDGLLYDLTEKQVYHIGKQVLLALEFLQEKHLFHGDVAARNILMQSDLTAKLCGLGLAYEVYTRGAISSTQTIPLKWLAPERLLLRPASIRADVWSFGILLYEMVTLGAPPYPEVPPTSILEHLQRRKIMKRPSSCTHTMYSIMKSCWRWREADRPSPRELRLRLEAAIKTADDEAVLQVPELVVPELYAAVAGIRVESLFYNYSML
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
4Phosphorylation----MGMTRMLLECS
----CCCHHHHHHCC
13.7529116813
13PhosphorylationMLLECSLSDKLCVIQ
HHHHCCCCCCEEEEE
19.1929116813
15UbiquitinationLECSLSDKLCVIQEK
HHCCCCCCEEEEECC
40.1727667366
59PhosphorylationQRTQQQRSGPQGIAP
HHHHHHHCCCCCCCC
50.95-
74PhosphorylationVPPPRDLSWEAGHGG
CCCCCCCCCCCCCCC
27.4526657352
88UbiquitinationGNVALPLKETSVENF
CCCEEECCCCCHHHH
57.94-
90PhosphorylationVALPLKETSVENFLG
CEEECCCCCHHHHHC
36.1620886841
91PhosphorylationALPLKETSVENFLGA
EEECCCCCHHHHHCC
28.6420886841
105UbiquitinationATTPALAKLQVPREQ
CCCHHHHHCCCCHHH
40.0622817900
147UbiquitinationKPKSVILKALKEPAG
CCHHHHHHHHCCCCC
40.3227667366
191PhosphorylationCTEKLPLYMVLEDVA
CCCCCCCEEEEEHHH
5.35-
215PhosphorylationTCRRDVMTMDGLLYD
HHCCCCEECCCCEEE
16.3824732914
221PhosphorylationMTMDGLLYDLTEKQV
EECCCCEEECCHHHH
17.6024732914
224PhosphorylationDGLLYDLTEKQVYHI
CCCEEECCHHHHHHH
37.9324732914
274PhosphorylationLCGLGLAYEVYTRGA
HHCCCCEEEEECCCC
15.8029083192
277PhosphorylationLGLAYEVYTRGAISS
CCCEEEEECCCCCCC
4.4529083192
278PhosphorylationGLAYEVYTRGAISST
CCEEEEECCCCCCCC
28.0029083192
283PhosphorylationVYTRGAISSTQTIPL
EECCCCCCCCCCCCC
27.1429116813
284PhosphorylationYTRGAISSTQTIPLK
ECCCCCCCCCCCCCC
20.5829116813
285PhosphorylationTRGAISSTQTIPLKW
CCCCCCCCCCCCCCH
23.9629116813
287PhosphorylationGAISSTQTIPLKWLA
CCCCCCCCCCCCHHC
25.3424719451
304PhosphorylationRLLLRPASIRADVWS
HHCCCCHHHHHHHHH
18.4529396449
350PhosphorylationKIMKRPSSCTHTMYS
CCCCCCCCCHHHHHH
26.2219845377
352PhosphorylationMKRPSSCTHTMYSIM
CCCCCCCHHHHHHHH
23.4819845377
356PhosphorylationSSCTHTMYSIMKSCW
CCCHHHHHHHHHHHH
9.0119845377
372PhosphorylationWREADRPSPRELRLR
HHHCCCCCHHHHHHH
37.1717081983

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 STYK1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STYK1_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 STYK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of STYK1_HUMAN !!

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 STYK1_HUMAN

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Related Literatures of Post-Translational Modification

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