FOG1_HUMAN - dbPTM
FOG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOG1_HUMAN
UniProt AC Q8IX07
Protein Name Zinc finger protein ZFPM1
Gene Name ZFPM1
Organism Homo sapiens (Human).
Sequence Length 1006
Subcellular Localization Nucleus.
Protein Description Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2 (By similarity)..
Protein Sequence MSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPPPLPPPTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLLLVDEACWLRTLPQALTEAEANTEIHRKDDALWCRVTKPVPAGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQGTGSPAAAATDEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHSCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAGALFLPQYVFGPDAAPPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCFECEITFSNVNNYYVHKRLYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPPAPSPAAPVRTRRRRKLYELHAAGAPPPPPPGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPPPGALGLPAAACPYCPPNGPVRGDLLEHFRLAHGLLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEPQEPPPGPPPSPAAAPEAVPPPPAPPSYSDKGVQTPSKGTPAPLPNGNHRYCRLCNIKFSSLSTFIAHKKYYCSSHAAEHVK
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
15PhosphorylationNPRQIKRSLGDMEAR
CHHHHHHHHHCHHHH		31.5327251275
38PhosphorylationSHMEQKATAPEAPSP
HHCCCCCCCCCCCCC		50.1822199227
44PhosphorylationATAPEAPSPPSADVN
CCCCCCCCCCCCCCC		57.3922115753
47PhosphorylationPEAPSPPSADVNSPP
CCCCCCCCCCCCCCC		40.2522115753
52PhosphorylationPPSADVNSPPPLPPP
CCCCCCCCCCCCCCC		38.3422115753
60PhosphorylationPPPLPPPTSPGGPKE
CCCCCCCCCCCCCCC		54.0126657352
61PhosphorylationPPLPPPTSPGGPKEL
CCCCCCCCCCCCCCC		27.5922199227
78PhosphorylationQEPEPRPTEEEPGSP
CCCCCCCCCCCCCCC		58.2625850435
84PhosphorylationPTEEEPGSPWSGPDE
CCCCCCCCCCCCCCC		33.6322115753
87PhosphorylationEEPGSPWSGPDELEP
CCCCCCCCCCCCCCC		43.7830576142
127PhosphorylationGSVQTRASSPRQAEP
CCCCCCCCCCCCCCC		37.2724247654
128PhosphorylationSVQTRASSPRQAEPS
CCCCCCCCCCCCCCC		24.10-
139PhosphorylationAEPSPALTLLLVDEA
CCCCCHHHHHHHCHH		19.9124247654
177PhosphorylationDALWCRVTKPVPAGG
CEEEEEECCCCCCCC		15.4123312004
187PhosphorylationVPAGGLLSVLLTAEP
CCCCCCEEEEEECCC		18.7623898821
191PhosphorylationGLLSVLLTAEPHSTP
CCEEEEEECCCCCCC		25.4723898821
196PhosphorylationLLTAEPHSTPGHPVK
EEECCCCCCCCCCCC		47.1929255136
197PhosphorylationLTAEPHSTPGHPVKK
EECCCCCCCCCCCCC		30.2023898821
262PhosphorylationNLQAHLLYYCASRQG
HHHHHHHHHHHHCCC		11.67-
266PhosphorylationHLLYYCASRQGTGSP
HHHHHHHHCCCCCCC		22.90-
270PhosphorylationYCASRQGTGSPAAAA
HHHHCCCCCCCCHHC		26.5829396449
272PhosphorylationASRQGTGSPAAAATD
HHCCCCCCCCHHCCC		15.9425849741
278PhosphorylationGSPAAAATDEKPKET
CCCCHHCCCCCCCCC		39.71-
364PhosphorylationSTTRDILYSHLVTNH
CCHHHHHHHHHHHCC		8.3830266825
365PhosphorylationTTRDILYSHLVTNHM
CHHHHHHHHHHHCCC		13.6030266825
369PhosphorylationILYSHLVTNHMVCQP
HHHHHHHHCCCEECC		26.2630266825
378PhosphorylationHMVCQPGSKGEIYSP
CCEECCCCCCCCCCC		44.1430266825
383PhosphorylationPGSKGEIYSPGAGHP
CCCCCCCCCCCCCCC		12.4326657352
384PhosphorylationGSKGEIYSPGAGHPA
CCCCCCCCCCCCCCC		23.6325849741
423PhosphorylationADLGLAPTPSPGLDR
CCCCCCCCCCCCCCH		30.6927135362
425PhosphorylationLGLAPTPSPGLDRKA
CCCCCCCCCCCCHHH		33.7925627689
463SumoylationPAAPRSIKVEAVEEP
CCCCCEEEEEEECCC		34.96-
463SumoylationPAAPRSIKVEAVEEP
CCCCCEEEEEEECCC		34.96-
487PhosphorylationEPGPQAPSRTPSPRS
CCCCCCCCCCCCCCC		52.3722115753
489PhosphorylationGPQAPSRTPSPRSPA
CCCCCCCCCCCCCCC		32.2422115753
491PhosphorylationQAPSRTPSPRSPAPA
CCCCCCCCCCCCCCC		32.1225159151
494PhosphorylationSRTPSPRSPAPARVK
CCCCCCCCCCCCEEE		28.8828985074
501SumoylationSPAPARVKAELSSPT
CCCCCEEEEEECCCC		30.50-
501SumoylationSPAPARVKAELSSPT
CCCCCEEEEEECCCC		30.50-
505PhosphorylationARVKAELSSPTPGSS
CEEEEEECCCCCCCC		26.2720873877
506PhosphorylationRVKAELSSPTPGSSP
EEEEEECCCCCCCCC		45.4720873877
508PhosphorylationKAELSSPTPGSSPVP
EEEECCCCCCCCCCC		42.0820873877
511PhosphorylationLSSPTPGSSPVPGEL
ECCCCCCCCCCCCCC		32.4520873877
512PhosphorylationSSPTPGSSPVPGELG
CCCCCCCCCCCCCCH		35.5120873877
529PhosphorylationGALFLPQYVFGPDAA
CEEECHHHHCCCCCC		8.8726434776
540PhosphorylationPDAAPPASEILAKMS
CCCCCCHHHHHHHHH		30.8320873877
547PhosphorylationSEILAKMSELVHSRL
HHHHHHHHHHHHHHH		27.3724043423
552PhosphorylationKMSELVHSRLQQGAG
HHHHHHHHHHHHCCC		27.4924043423
567PhosphorylationAGAGGAQTGLFPGAP
CCCCCCCCCCCCCCC		35.0124043423
637PhosphorylationAEPDAPRSSPGPGAR
CCCCCCCCCCCCCCC		39.5625849741
638PhosphorylationEPDAPRSSPGPGARE
CCCCCCCCCCCCCCC		34.8522115753
653PhosphorylationEGAGGAATPEDGAGG
CCCCCCCCCCCCCCC		27.0323401153
663PhosphorylationDGAGGRGSEGSQSPG
CCCCCCCCCCCCCCC		37.1128731282
664PhosphorylationGAGGRGSEGSQSPGS
CCCCCCCCCCCCCCC		66.7317525332
666PhosphorylationGGRGSEGSQSPGSSV
CCCCCCCCCCCCCCC		24.3517525332
668PhosphorylationRGSEGSQSPGSSVDD
CCCCCCCCCCCCCCC		32.6917525332
671PhosphorylationEGSQSPGSSVDDAED
CCCCCCCCCCCCCCC		30.4927794612
672PhosphorylationGSQSPGSSVDDAEDD
CCCCCCCCCCCCCCC		35.1726657352
681PhosphorylationDDAEDDPSRTLCEAC
CCCCCCHHHHHHHHC		44.9123312004
693PhosphorylationEACNIRFSRHETYTV
HHCCCEECCCCEEEE		23.9130576142
698PhosphorylationRFSRHETYTVHKRYY
EECCCCEEEEEHHEE		12.0919835603
699PhosphorylationFSRHETYTVHKRYYC
ECCCCEEEEEHHEEH		24.4519835603
704PhosphorylationTYTVHKRYYCASRHD
EEEEEHHEEHHHCCC		14.01-
708PhosphorylationHKRYYCASRHDPPPR
EHHEEHHHCCCCCCC		26.96-
733PhosphorylationPAAPPAPSPAAPVRT
CCCCCCCCCCCCCCH		29.3127732954
747PhosphorylationTRRRRKLYELHAAGA
HHHHHHHHHHHHCCC		21.3423312004
768PhosphorylationGHAPAPESPRPGSGS
CCCCCCCCCCCCCCC		25.7526657352
773PhosphorylationPESPRPGSGSGSGPG
CCCCCCCCCCCCCCC		32.2526657352
775PhosphorylationSPRPGSGSGSGPGLA
CCCCCCCCCCCCCCC		31.3327251275
777PhosphorylationRPGSGSGSGPGLAPA
CCCCCCCCCCCCCCC		43.4428985074
784PhosphorylationSGPGLAPARSPGPAA
CCCCCCCCCCCCCCC		20.9818669648
786PhosphorylationPGLAPARSPGPAADG
CCCCCCCCCCCCCCC		35.9919664994
798PhosphorylationADGPIDLSKKPRRPL
CCCCCCCCCCCCCCC		34.5819362540
894PhosphorylationGPGVEARTPADRGPS
CCCCCCCCCCCCCCC		29.8530266825
901PhosphorylationTPADRGPSPAPAPAA
CCCCCCCCCCCCCCC		36.2023401153
909PhosphorylationPAPAPAASPQPGSRG
CCCCCCCCCCCCCCC		26.6123401153
914PhosphorylationAASPQPGSRGPRDGL
CCCCCCCCCCCCCCC		40.5230266825
935PhosphorylationPPPGPPPSPAAAPEA
CCCCCCCCCCCCCCC		32.7026657352
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 FOG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOG1_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 FOG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GATA1_HUMANGATA1physical
19513100
RB_MOUSERb1physical
19513100
MTA1_HUMANMTA1physical
21047798
RBBP4_HUMANRBBP4physical
21047798
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 FOG1_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-901 AND SER-909, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901 AND SER-909, 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-786, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666 AND SER-668, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-699, 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 TYR-698, AND MASSSPECTROMETRY.

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