ZGPAT_HUMAN - dbPTM
ZGPAT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZGPAT_HUMAN
UniProt AC Q8N5A5
Protein Name Zinc finger CCCH-type with G patch domain-containing protein
Gene Name ZGPAT
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Nucleus .
Isoform 4: Nucleus .
Protein Description Transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. Negatively regulates expression of EGFR, a gene involved in cell proliferation, survival and migration. Its ability to repress genes of the EGFR pathway suggest it may act as a tumor suppressor. Able to suppress breast carcinogenesis.; Isoform 4: Antagonizes the transcription repression by isoform 1 by competing for the binding of the NuRD complex. Does not bind DNA..
Protein Sequence MDEESLESALQTYRAQLQQVELALGAGLDSSEQADLRQLQGDLKELIELTEASLVSVRKSSLLAALDEERPGRQEDAEYQAFREAITEAVEAPAAARGSGSETVPKAEAGPESAAGGQEEEEGEDEEELSGTKVSAPYYSSWGTLEYHNAMVVGTEEAEDGSAGVRVLYLYPTHKSLKPCPFFLEGKCRFKENCRFSHGQVVSLDELRPFQDPDLSSLQAGSACLAKHQDGLWHAARITDVDNGYYTVKFDSLLLREAVVEGDGILPPLRTEATESDSDSDGTGDSSYARVVGSDAVDSAQSSALCPSLAVVGSDAVDSGTCSSAFAGWEVHTRGIGSRLLTKMGYEFGKGLGRHAEGRVEPIHAVVLPRGKSLDQCVETLQKQTRVGKAGTNKPPRCRGRGARPGGRPAPRNVFDFLNEKLQGQAPGALEAGAAPAGRRSKDMYHASKSAKRALSLRLFQTEEKIERTQRDIRSIQEALARNAGRHSVASAQLQEKLAGAQRQLGQLRAQEAGLQQEQRKADTHKKMTEF
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
1Acetylation-------MDEESLES
-------CCHHHHHH		15.3322814378
13PhosphorylationLESALQTYRAQLQQV
HHHHHHHHHHHHHHH		7.32-
50PhosphorylationLKELIELTEASLVSV
HHHHHHHHHHHHHHH		19.4029759185
53PhosphorylationLIELTEASLVSVRKS
HHHHHHHHHHHHHHH		24.0729759185
56PhosphorylationLTEASLVSVRKSSLL
HHHHHHHHHHHHHHH		22.8424719451
79PhosphorylationGRQEDAEYQAFREAI
CCHHHHHHHHHHHHH		13.5828796482
99PhosphorylationAPAAARGSGSETVPK
HHHHHCCCCCCCCCH		33.3225159151
101PhosphorylationAAARGSGSETVPKAE
HHHCCCCCCCCCHHH		31.6225159151
103PhosphorylationARGSGSETVPKAEAG
HCCCCCCCCCHHHCC		43.7525627689
141PhosphorylationVSAPYYSSWGTLEYH
ECCCCCCCCCCEEEE		17.2624275569
169PhosphorylationSAGVRVLYLYPTHKS
CCCEEEEEECCCCCC		11.00-
178UbiquitinationYPTHKSLKPCPFFLE
CCCCCCCCCCCEEEC		52.22-
187UbiquitinationCPFFLEGKCRFKENC
CCEEECCEECCCCCC		16.92-
216PhosphorylationPFQDPDLSSLQAGSA
CCCCCCHHHCCCCCH		36.0627174698
217PhosphorylationFQDPDLSSLQAGSAC
CCCCCHHHCCCCCHH		31.6227174698
222PhosphorylationLSSLQAGSACLAKHQ
HHHCCCCCHHHHHCC		20.8727174698
227UbiquitinationAGSACLAKHQDGLWH
CCCHHHHHCCCCCEE		28.93-
252PhosphorylationYYTVKFDSLLLREAV
EEEEEECCEEEEEHH		24.8528555341
271PhosphorylationGILPPLRTEATESDS
CCCCCCCCCCCCCCC		37.3422115753
274 (in isoform 2)Phosphorylation-29.77-
274PhosphorylationPPLRTEATESDSDSD
CCCCCCCCCCCCCCC		29.7726503892
276 (in isoform 2)Phosphorylation-37.75-
276PhosphorylationLRTEATESDSDSDGT
CCCCCCCCCCCCCCC		37.7526503892
278PhosphorylationTEATESDSDSDGTGD
CCCCCCCCCCCCCCC		48.5726503892
278 (in isoform 2)Phosphorylation-48.57-
280 (in isoform 2)Phosphorylation-41.72-
280PhosphorylationATESDSDSDGTGDSS
CCCCCCCCCCCCCCH		41.7226055452
283 (in isoform 2)Phosphorylation-42.69-
283PhosphorylationSDSDSDGTGDSSYAR
CCCCCCCCCCCHHEE		42.6922115753
286PhosphorylationDSDGTGDSSYARVVG
CCCCCCCCHHEEEEC		26.9620068231
287PhosphorylationSDGTGDSSYARVVGS
CCCCCCCHHEEEECC		27.7920068231
288PhosphorylationDGTGDSSYARVVGSD
CCCCCCHHEEEECCC		11.4620068231
338PhosphorylationVHTRGIGSRLLTKMG
EECCCHHHHHHHHHC		20.17-
343UbiquitinationIGSRLLTKMGYEFGK
HHHHHHHHHCHHCCC		30.23-
370MethylationIHAVVLPRGKSLDQC
CEEEEECCCCCHHHH		62.1054560811
372UbiquitinationAVVLPRGKSLDQCVE
EEEECCCCCHHHHHH		49.47-
373PhosphorylationVVLPRGKSLDQCVET
EEECCCCCHHHHHHH		39.7523401153
380PhosphorylationSLDQCVETLQKQTRV
CHHHHHHHHHHHCCC		17.6821406692
383UbiquitinationQCVETLQKQTRVGKA
HHHHHHHHHCCCCCC		57.67-
385PhosphorylationVETLQKQTRVGKAGT
HHHHHHHCCCCCCCC		34.0730622161
392PhosphorylationTRVGKAGTNKPPRCR
CCCCCCCCCCCCCCC		44.9530622161
401MethylationKPPRCRGRGARPGGR
CCCCCCCCCCCCCCC		19.08115387691
404MethylationRCRGRGARPGGRPAP
CCCCCCCCCCCCCCC		32.97115920377
421UbiquitinationVFDFLNEKLQGQAPG
HHHHHHHHHCCCCCC		45.07-
442MethylationAPAGRRSKDMYHASK
CCCCCCCHHHHHHHH		44.71116253193
456PhosphorylationKSAKRALSLRLFQTE
HHHHHHHHHHHHCCH		15.5124719451
488PhosphorylationARNAGRHSVASAQLQ
HHHCCCCCHHHHHHH		20.3028555341
497UbiquitinationASAQLQEKLAGAQRQ
HHHHHHHHHHHHHHH		30.58-
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 ZGPAT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZGPAT_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 ZGPAT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBBP7_HUMANRBBP7physical
24116224
HDAC1_HUMANHDAC1physical
24116224
MTA2_HUMANMTA2physical
24116224
HAT1_HUMANHAT1physical
24116224
ADIP_HUMANSSX2IPphysical
25416956
K1C40_HUMANKRT40physical
25416956
DYDC1_HUMANDYDC1physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
STAC3_HUMANSTAC3physical
25416956
CCD57_HUMANCCDC57physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
PRP4_HUMANPRPF4physical
28514442
LIPP_HUMANPNLIPphysical
28514442
DHX15_HUMANDHX15physical
28514442
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 ZGPAT_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-276; SER-278 ANDSER-280, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-278 ANDSER-280, AND MASS SPECTROMETRY.

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