GRAM4_HUMAN - dbPTM
GRAM4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRAM4_HUMAN
UniProt AC Q6IC98
Protein Name GRAM domain-containing protein 4
Gene Name GRAMD4
Organism Homo sapiens (Human).
Sequence Length 578
Subcellular Localization Mitochondrion membrane
Multi-pass membrane protein . Colocalizes with COX4I1.
Protein Description Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53..
Protein Sequence MLRRLDKIRFRGHKRDDFLDLAESPNASDTECSDEIPLKVPRTSPRDSEELRDPAGPGTLIMATGVQDFNRTEFDRLNEIKGHLEIALLEKHFLQEELRKLREETNAEMLRQELDRERQRRMELEQKVQEVLKARTEEQMAQQPPKGQAQASNGAERRSQGLSSRLQKWFYERFGEYVEDFRFQPEENTVETEEPLSARRLTENMRRLKRGAKPVTNFVKNLSALSDWYSVYTSAIAFTVYMNAVWHGWAIPLFLFLAILRLSLNYLIARGWRIQWSIVPEVSEPVEPPKEDLTVSEKFQLVLDVAQKAQNLFGKMADILEKIKNLFMWVQPEITQKLYVALWAAFLASCFFPYRLVGLAVGLYAGIKFFLIDFIFKRCPRLRAKYDTPYIIWRSLPTDPQLKERSSAAVSRRLQTTSSRSYVPSAPAGLGKEEDAGRFHSTKKGNFHEIFNLTENERPLAVCENGWRCCLINRDRKMPTDYIRNGVLYVTENYLCFESSKSGSSKRNKVIKLVDITDIQKYKVLSVLPGSGMGIAVSTPSTQKPLVFGAMVHRDEAFETILSQYIKITSAAASGGDS
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
24PhosphorylationDFLDLAESPNASDTE
CCHHHHCCCCCCCCC		20.1825159151
28PhosphorylationLAESPNASDTECSDE
HHCCCCCCCCCCCCC		52.2725159151
30PhosphorylationESPNASDTECSDEIP
CCCCCCCCCCCCCCC		36.0722617229
33PhosphorylationNASDTECSDEIPLKV
CCCCCCCCCCCCCCC		31.8522617229
127UbiquitinationRRMELEQKVQEVLKA
HHHHHHHHHHHHHHH		36.1930230243
133UbiquitinationQKVQEVLKARTEEQM
HHHHHHHHHHHHHHH		40.7829967540
153UbiquitinationKGQAQASNGAERRSQ
CCCHHHCCHHHHHHH		57.6230230243
159PhosphorylationSNGAERRSQGLSSRL
CCHHHHHHHCHHHHH		34.5217924679
163PhosphorylationERRSQGLSSRLQKWF
HHHHHCHHHHHHHHH		21.9017924679
164PhosphorylationRRSQGLSSRLQKWFY
HHHHCHHHHHHHHHH		41.8917924679
168 (in isoform 1)Ubiquitination-43.8121890473
168UbiquitinationGLSSRLQKWFYERFG
CHHHHHHHHHHHHHH		43.8122817900
177PhosphorylationFYERFGEYVEDFRFQ
HHHHHHHHHHHCCCC		14.9828796482
191UbiquitinationQPEENTVETEEPLSA
CCCCCCCCCCCCHHH		48.7621890473
194UbiquitinationENTVETEEPLSARRL
CCCCCCCCCHHHHHH		59.9921890473
197PhosphorylationVETEEPLSARRLTEN
CCCCCCHHHHHHHHH		30.37-
385UbiquitinationRCPRLRAKYDTPYII
HCHHHHHHCCCCEEE		36.91-
386PhosphorylationCPRLRAKYDTPYIIW
CHHHHHHCCCCEEEE		24.86-
390PhosphorylationRAKYDTPYIIWRSLP
HHHCCCCEEEEECCC		13.7128450419
403UbiquitinationLPTDPQLKERSSAAV
CCCCHHHHHHHHHHH		45.92-
407PhosphorylationPQLKERSSAAVSRRL
HHHHHHHHHHHHHHH		26.86-
411PhosphorylationERSSAAVSRRLQTTS
HHHHHHHHHHHHCCC		13.63-
416PhosphorylationAVSRRLQTTSSRSYV
HHHHHHHCCCCCCCC		32.9828857561
432UbiquitinationSAPAGLGKEEDAGRF
CCCCCCCCHHCCCCC		64.0724816145
441PhosphorylationEDAGRFHSTKKGNFH
HCCCCCEECCCCCCH		38.93-
442PhosphorylationDAGRFHSTKKGNFHE
CCCCCEECCCCCCHH		28.36-
455UbiquitinationHEIFNLTENERPLAV
HHHEECCCCCCCEEE		61.3324816145
458UbiquitinationFNLTENERPLAVCEN
EECCCCCCCEEEECC		43.0124816145
494PhosphorylationVLYVTENYLCFESSK
EEEEECCEEEECCCC		9.90-
512UbiquitinationSKRNKVIKLVDITDI
CCCCCEEEEEECCHH		45.5029967540
521UbiquitinationVDITDIQKYKVLSVL
EECCHHHHEEEEEEC		47.5829967540
523UbiquitinationITDIQKYKVLSVLPG
CCHHHHEEEEEECCC		43.6730230243
574PhosphorylationKITSAAASGGDS---
HHHHHHHCCCCC---		38.2828102081
578PhosphorylationAAASGGDS-------
HHHCCCCC-------		45.4533259812
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 GRAM4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRAM4_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 GRAM4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 GRAM4_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-24 AND SER-28, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-163 ANDSER-164, AND MASS SPECTROMETRY.

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