ST65G_HUMAN - dbPTM
ST65G_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ST65G_HUMAN
UniProt AC O94864
Protein Name STAGA complex 65 subunit gamma
Gene Name SUPT7L
Organism Homo sapiens (Human).
Sequence Length 414
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MNLQRYWGEIPISSSQTNRSSFDLLPREFRLVEVHDPPLHQPSANKPKPPTMLDIPSEPCSLTIHTIQLIQHNRRLRNLIATAQAQNQQQTEGVKTEESEPLPSCPGSPPLPDDLLPLDCKNPNAPFQIRHSDPESDFYRGKGEPVTELSWHSCRQLLYQAVATILAHAGFDCANESVLETLTDVAHEYCLKFTKLLRFAVDREARLGQTPFPDVMEQVFHEVGIGSVLSLQKFWQHRIKDYHSYMLQISKQLSEEYERIVNPEKATEDAKPVKIKEEPVSDITFPVSEELEADLASGDQSLPMGVLGAQSERFPSNLEVEASPQASSAEVNASPLWNLAHVKMEPQESEEGNVSGHGVLGSDVFEEPMSGMSEAGIPQSPDDSDSSYGSHSTDSLMGSSPVFNQRCKKRMRKI
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
6Phosphorylation--MNLQRYWGEIPIS
--CCCCCCCEECCCC		12.5725072903
7Ubiquitination-MNLQRYWGEIPISS
-CCCCCCCEECCCCC		10.51-
13PhosphorylationYWGEIPISSSQTNRS
CCEECCCCCCCCCCC		20.7027174698
14PhosphorylationWGEIPISSSQTNRSS
CEECCCCCCCCCCCC		27.4727174698
15PhosphorylationGEIPISSSQTNRSSF
EECCCCCCCCCCCCC		33.9427174698
15 (in isoform 4)Phosphorylation-33.9429083192
17PhosphorylationIPISSSQTNRSSFDL
CCCCCCCCCCCCCCC		34.2527174698
18 (in isoform 4)Phosphorylation-33.9129083192
20PhosphorylationSSSQTNRSSFDLLPR
CCCCCCCCCCCCCCC		37.1124043423
21PhosphorylationSSQTNRSSFDLLPRE
CCCCCCCCCCCCCCE		21.3922985185
60UbiquitinationLDIPSEPCSLTIHTI
CCCCCCCCCEEHHHH		4.5827667366
82PhosphorylationRLRNLIATAQAQNQQ
HHHHHHHHHHHHHHH		16.5927174698
91PhosphorylationQAQNQQQTEGVKTEE
HHHHHHHCCCCCCCC		30.3027174698
95SumoylationQQQTEGVKTEESEPL
HHHCCCCCCCCCCCC		62.16-
96PhosphorylationQQTEGVKTEESEPLP
HHCCCCCCCCCCCCC		42.4520873877
99PhosphorylationEGVKTEESEPLPSCP
CCCCCCCCCCCCCCC		37.9820873877
104PhosphorylationEESEPLPSCPGSPPL
CCCCCCCCCCCCCCC		40.4025159151
106PhosphorylationSEPLPSCPGSPPLPD
CCCCCCCCCCCCCCC		51.1132142685
108PhosphorylationPLPSCPGSPPLPDDL
CCCCCCCCCCCCCCC		14.4230278072
116UbiquitinationPPLPDDLLPLDCKNP
CCCCCCCCCCCCCCC		5.2129967540
130UbiquitinationPNAPFQIRHSDPESD
CCCCCEEECCCCCCC		16.6929967540
132PhosphorylationAPFQIRHSDPESDFY
CCCEEECCCCCCCCC		45.0425159151
136UbiquitinationIRHSDPESDFYRGKG
EECCCCCCCCCCCCC		38.1127667366
139UbiquitinationSDPESDFYRGKGEPV
CCCCCCCCCCCCCCC		24.3629967540
142UbiquitinationESDFYRGKGEPVTEL
CCCCCCCCCCCCCHH		51.61-
188PhosphorylationTLTDVAHEYCLKFTK
HHHHHHHHHHHHHHH		28.3632142685
193PhosphorylationAHEYCLKFTKLLRFA
HHHHHHHHHHHHHHH		4.7432142685
193UbiquitinationAHEYCLKFTKLLRFA
HHHHHHHHHHHHHHH		4.7427667366
195UbiquitinationEYCLKFTKLLRFAVD
HHHHHHHHHHHHHHC		48.9727667366
230PhosphorylationVGIGSVLSLQKFWQH
HCCHHHHHHHHHHHH		26.9724719451
242PhosphorylationWQHRIKDYHSYMLQI
HHHHCHHHHHHHHHH		6.4029116813
249UbiquitinationYHSYMLQISKQLSEE
HHHHHHHHHHHHHHH		4.9729967540
251UbiquitinationSYMLQISKQLSEEYE
HHHHHHHHHHHHHHH		57.8129967540
263UbiquitinationEYERIVNPEKATEDA
HHHHHCCHHHCCCCC		33.3029967540
265UbiquitinationERIVNPEKATEDAKP
HHHCCHHHCCCCCCC		62.9629967540
269UbiquitinationNPEKATEDAKPVKIK
CHHHCCCCCCCCCCC		56.3827667366
271SumoylationEKATEDAKPVKIKEE
HHCCCCCCCCCCCEE		63.77-
271UbiquitinationEKATEDAKPVKIKEE
HHCCCCCCCCCCCEE		63.7727667366
271SumoylationEKATEDAKPVKIKEE
HHCCCCCCCCCCCEE		63.7728112733
272UbiquitinationKATEDAKPVKIKEEP
HCCCCCCCCCCCEEE		34.0629967540
274UbiquitinationTEDAKPVKIKEEPVS
CCCCCCCCCCEEECC		57.5029967540
276SumoylationDAKPVKIKEEPVSDI
CCCCCCCCEEECCCC		50.75-
316PhosphorylationAQSERFPSNLEVEAS
CCCCCCCCCCEEEEC		51.8728176443
321PhosphorylationFPSNLEVEASPQASS
CCCCCEEEECCCCCC		33.7732142685
323PhosphorylationSNLEVEASPQASSAE
CCCEEEECCCCCCCC		12.2125159151
326PhosphorylationEVEASPQASSAEVNA
EEEECCCCCCCCCCC		14.6132142685
327PhosphorylationVEASPQASSAEVNAS
EEECCCCCCCCCCCC		25.4928176443
328PhosphorylationEASPQASSAEVNASP
EECCCCCCCCCCCCC		31.3126657352
334PhosphorylationSSAEVNASPLWNLAH
CCCCCCCCCCCCCEE		18.4725159151
349PhosphorylationVKMEPQESEEGNVSG
EECCCCCCCCCCCCC		35.3826074081
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 ST65G_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ST65G_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 ST65G_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN_HUMANPTNphysical
16169070
SRTD1_HUMANSERTAD1physical
17141982
SRTD2_HUMANSERTAD2physical
17141982
CDCA4_HUMANCDCA4physical
17141982
MED16_HUMANMED16physical
17967894
MED17_HUMANMED17physical
17967894
TAF9_HUMANTAF9physical
17967894
SUPT3_HUMANSUPT3Hphysical
17967894
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 ST65G_HUMAN

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Related Literatures of Post-Translational Modification
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-323 AND SER-334, 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-316 AND SER-334, ANDMASS SPECTROMETRY.

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