ST7_HUMAN - dbPTM
ST7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ST7_HUMAN
UniProt AC Q9NRC1
Protein Name Suppressor of tumorigenicity 7 protein
Gene Name ST7
Organism Homo sapiens (Human).
Sequence Length 585
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description May act as a tumor suppressor..
Protein Sequence MAEAATGFLEQLKSCIVWSWTYLWTVWFFIVLFLVYILRVPLKINDNLSTVSMFLNTLTPKFYVALTGTSSLISGLILIFEWWYFRKYGTSFIEQVSVSHLRPLLGGVDNNSSNNSNSSNGDSDSNRQSVSECKVWRNPLNLFRGAEYNRYTWVTGREPLTYYDMNLSAQDHQTFFTCDSDHLRPADAIMQKAWRERNPQARISAAHEALEINEIRSRVEVPLIASSTIWEIKLLPKCATAYILLAEEEATTIAEAEKLFKQALKAGDGCYRRSQQLQHHGSQYEAQHRRDTNVLVYIKRRLAMCARRLGRTREAVKMMRDLMKEFPLLSMFNIHENLLEALLELQAYADVQAVLAKYDDISLPKSATICYTAALLKARAVSDKFSPEAASRRGLSTAEMNAVEAIHRAVEFNPHVPKYLLEMKSLILPPEHILKRGDSEAIAYAFFHLAHWKRVEGALNLLHCTWEGTFRMIPYPLEKGHLFYPYPICTETADRELLPSFHEVSVYPKKELPFFILFTAGLCSFTAMLALLTHQFPELMGVFAKAMIDIFCSAEFRDWNCKSIFMRVEDELEIPPAPQSQHFQN
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
25PhosphorylationWSWTYLWTVWFFIVL
HHHHHHHHHHHHHHH		12.7926074081
36PhosphorylationFIVLFLVYILRVPLK
HHHHHHHHHHHCCCC		9.0826074081
47N-linked_GlycosylationVPLKINDNLSTVSMF
CCCCCCCCHHHHHHH		31.25UniProtKB CARBOHYD
49PhosphorylationLKINDNLSTVSMFLN
CCCCCCHHHHHHHHH		32.7722210691
50PhosphorylationKINDNLSTVSMFLNT
CCCCCHHHHHHHHHH		21.5522210691
52PhosphorylationNDNLSTVSMFLNTLT
CCCHHHHHHHHHHCC		12.1422210691
57PhosphorylationTVSMFLNTLTPKFYV
HHHHHHHHCCCCEEE		33.8723663014
67PhosphorylationPKFYVALTGTSSLIS
CCEEEEHHCCHHHHH		28.7722210691
69PhosphorylationFYVALTGTSSLISGL
EEEEHHCCHHHHHHH		15.2022210691
88PhosphorylationEWWYFRKYGTSFIEQ
HHHHHHHHCCCHHEE		22.7527732954
90PhosphorylationWYFRKYGTSFIEQVS
HHHHHHCCCHHEEEE		19.8527732954
91PhosphorylationYFRKYGTSFIEQVSV
HHHHHCCCHHEEEEH		21.6227732954
97PhosphorylationTSFIEQVSVSHLRPL
CCHHEEEEHHHHHHC		20.0027732954
99PhosphorylationFIEQVSVSHLRPLLG
HHEEEEHHHHHHCCC		14.8624719451
261UbiquitinationAEAEKLFKQALKAGD
HHHHHHHHHHHHHCC		45.13-
265UbiquitinationKLFKQALKAGDGCYR
HHHHHHHHHCCCCHH		54.03-
304 (in isoform 6)Ubiquitination-1.8621890473
311 (in isoform 6)Ubiquitination-34.8921890473
331 (in isoform 5)Ubiquitination-2.7721890473
338 (in isoform 5)Ubiquitination-4.1021890473
345 (in isoform 6)Ubiquitination-3.4021890473
347 (in isoform 3)Ubiquitination-17.6921890473
354 (in isoform 7)Ubiquitination-2.7421890473
354 (in isoform 3)Ubiquitination-2.7421890473
354 (in isoform 2)Ubiquitination-2.7421890473
358PhosphorylationVQAVLAKYDDISLPK
HHHHHHHCCCCCCCC		17.15-
361 (in isoform 7)Ubiquitination-4.1021890473
361 (in isoform 2)Ubiquitination-4.1021890473
362PhosphorylationLAKYDDISLPKSATI
HHHCCCCCCCCCHHH		45.6824719451
372 (in isoform 5)Ubiquitination-10.8821890473
377UbiquitinationCYTAALLKARAVSDK
HHHHHHHHHHHCCCC		36.3521890473
377 (in isoform 4)Ubiquitination-36.3521890473
377 (in isoform 1)Ubiquitination-36.3521890473
382PhosphorylationLLKARAVSDKFSPEA
HHHHHHCCCCCCHHH		33.8123186163
384 (in isoform 1)Ubiquitination-39.9921890473
384 (in isoform 4)Ubiquitination-39.9921890473
384UbiquitinationKARAVSDKFSPEAAS
HHHHCCCCCCHHHHH		39.9921890473
386PhosphorylationRAVSDKFSPEAASRR
HHCCCCCCHHHHHHC		27.8010889047
388 (in isoform 3)Ubiquitination-56.5221890473
391PhosphorylationKFSPEAASRRGLSTA
CCCHHHHHHCCCCHH		29.5619691289
395 (in isoform 2)Ubiquitination-3.7921890473
395 (in isoform 7)Ubiquitination-3.7921890473
396PhosphorylationAASRRGLSTAEMNAV
HHHHCCCCHHHHHHH		28.53-
397PhosphorylationASRRGLSTAEMNAVE
HHHCCCCHHHHHHHH		31.51-
418 (in isoform 1)Ubiquitination-47.6521890473
418 (in isoform 4)Ubiquitination-47.6521890473
418UbiquitinationEFNPHVPKYLLEMKS
HHCCCCCHHHHHHHH		47.6521890473
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
-KUbiquitinationE3 ubiquitin ligaseDCAF4Q8WV16
PMID:30945288
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ST7_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 ST7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ST7_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 ST7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-386, AND MASSSPECTROMETRY.

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