GCFC2_HUMAN - dbPTM
GCFC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCFC2_HUMAN
UniProt AC P16383
Protein Name GC-rich sequence DNA-binding factor 2
Gene Name GCFC2
Organism Homo sapiens (Human).
Sequence Length 781
Subcellular Localization Nucleus, nucleoplasm . Nucleus, nucleolus .
Protein Description Factor that represses transcription. It binds to the GC-rich sequences (5'-GCGGGGC-3') present in the epidermal growth factor receptor, beta-actin, and calcium-dependent protease promoters. Involved in pre-mRNA splicing through regulating spliceosome C complex formation. May play a role during late-stage splicing events and turnover of excised inrons..
Protein Sequence MAHRPKRTFRQRAADSSDSDGAEESPAEPGAPRELPVPGSAEEEPPSGGGRAQVAGLPHRVRGPRGRGRVWASSRRATKAAPRADEGSESRTLDVSTDEEDKIHHSSESKDDQGLSSDSSSSLGEKELSSTVKIPDAAFIQAARRKRELARAQDDYISLDVQHTSSISGMKRESEDDPESEPDDHEKRIPFTLRPQTLRQRMAEESISRNEETSEESQEDEKQDTWEQQQMRKAVKIIEERDIDLSCGNGSSKVKKFDTSISFPPVNLEIIKKQLNTRLTLLQETHRSHLREYEKYVQDVKSSKSTIQNLESSSNQALNCKFYKSMKIYVENLIDCLNEKIINIQEIESSMHALLLKQAMTFMKRRQDELKHESTYLQQLSRKDETSTSGNFSVDEKTQWILEEIESRRTKRRQARVLSGNCNHQEGTSSDDELPSAEMIDFQKSQGDILQKQKKVFEEVQDDFCNIQNILLKFQQWREKFPDSYYEAFISLCIPKLLNPLIRVQLIDWNPLKLESTGLKEMPWFKSVEEFMDSSVEDSKKESSSDKKVLSAIINKTIIPRLTDFVEFLWDPLSTSQTTSLITHCRVILEEHSTCENEVSKSRQDLLKSIVSRMKKAVEDDVFIPLYPKSAVENKTSPHSKFQERQFWSGLKLFRNILLWNGLLTDDTLQELGLGKLLNRYLIIALLNATPGPDVVKKCNQVAACLPEKWFENSAMRTSIPQLENFIQFLLQSAHKLSRSEFRDEVEEIILILVKIKALNQAESFIGEHHLDHLKSLIKED
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
16PhosphorylationFRQRAADSSDSDGAE
HHHHHCCCCCCCCCC		31.1723927012
17PhosphorylationRQRAADSSDSDGAEE
HHHHCCCCCCCCCCC		41.5023927012
19PhosphorylationRAADSSDSDGAEESP
HHCCCCCCCCCCCCC		39.6323927012
25PhosphorylationDSDGAEESPAEPGAP
CCCCCCCCCCCCCCC		22.4023927012
40PhosphorylationRELPVPGSAEEEPPS
CCCCCCCCCCCCCCC		26.8329255136
47PhosphorylationSAEEEPPSGGGRAQV
CCCCCCCCCCCCCCC		61.8723663014
51MethylationEPPSGGGRAQVAGLP
CCCCCCCCCCCCCCC		25.73115918341
73PhosphorylationGRGRVWASSRRATKA
CCCCHHHCCCCCCCC		14.5224719451
79MethylationASSRRATKAAPRADE
HCCCCCCCCCCCCCC		41.38116252127
88PhosphorylationAPRADEGSESRTLDV
CCCCCCCCCCCEECC		30.2828985074
92PhosphorylationDEGSESRTLDVSTDE
CCCCCCCEECCCCCC		36.2723663014
96PhosphorylationESRTLDVSTDEEDKI
CCCEECCCCCCCCCC		29.7929255136
97PhosphorylationSRTLDVSTDEEDKIH
CCEECCCCCCCCCCC		47.4829255136
106PhosphorylationEEDKIHHSSESKDDQ
CCCCCCCCCCCCCCC		22.9523927012
107PhosphorylationEDKIHHSSESKDDQG
CCCCCCCCCCCCCCC		41.3423663014
109PhosphorylationKIHHSSESKDDQGLS
CCCCCCCCCCCCCCC		43.2523663014
116PhosphorylationSKDDQGLSSDSSSSL
CCCCCCCCCCCCCCC		38.6323663014
117PhosphorylationKDDQGLSSDSSSSLG
CCCCCCCCCCCCCCC		46.7025849741
119PhosphorylationDQGLSSDSSSSLGEK
CCCCCCCCCCCCCCC		33.7823663014
120PhosphorylationQGLSSDSSSSLGEKE
CCCCCCCCCCCCCCH		29.0123663014
121PhosphorylationGLSSDSSSSLGEKEL
CCCCCCCCCCCCCHH		33.2723663014
122PhosphorylationLSSDSSSSLGEKELS
CCCCCCCCCCCCHHH		42.2020873877
129PhosphorylationSLGEKELSSTVKIPD
CCCCCHHHCCCCCCH		25.67-
156PhosphorylationLARAQDDYISLDVQH
HHHHCCCEEEEECCC		10.7428796482
158PhosphorylationRAQDDYISLDVQHTS
HHCCCEEEEECCCCC		16.5828796482
164PhosphorylationISLDVQHTSSISGMK
EEEECCCCCCCCCCC		13.6930576142
165PhosphorylationSLDVQHTSSISGMKR
EEECCCCCCCCCCCC		24.4530576142
166PhosphorylationLDVQHTSSISGMKRE
EECCCCCCCCCCCCC		23.1730576142
168PhosphorylationVQHTSSISGMKRESE
CCCCCCCCCCCCCCC		34.4830576142
174PhosphorylationISGMKRESEDDPESE
CCCCCCCCCCCCCCC		50.8129255136
180PhosphorylationESEDDPESEPDDHEK
CCCCCCCCCCCCCHH		60.8729255136
192PhosphorylationHEKRIPFTLRPQTLR
CHHCCCCCCCHHHHH		19.2623312004
197PhosphorylationPFTLRPQTLRQRMAE
CCCCCHHHHHHHHHH		26.9623312004
206PhosphorylationRQRMAEESISRNEET
HHHHHHHHHHCCHHC		19.8529255136
207PhosphorylationQRMAEESISRNEETS
HHHHHHHHHCCHHCC		5.1927251275
207 (in isoform 3)Phosphorylation-5.1929507054
208PhosphorylationRMAEESISRNEETSE
HHHHHHHHCCHHCCH		38.0329255136
213PhosphorylationSISRNEETSEESQED
HHHCCHHCCHHHHHH		34.9522617229
214PhosphorylationISRNEETSEESQEDE
HHCCHHCCHHHHHHH		42.5222617229
217PhosphorylationNEETSEESQEDEKQD
CHHCCHHHHHHHHHH		34.5122617229
225PhosphorylationQEDEKQDTWEQQQMR
HHHHHHHHHHHHHHH		28.5430108239
246PhosphorylationEERDIDLSCGNGSSK
HHCCCCCCCCCCCCC		19.0719664995
251PhosphorylationDLSCGNGSSKVKKFD
CCCCCCCCCCCEECC		30.87-
252PhosphorylationLSCGNGSSKVKKFDT
CCCCCCCCCCEECCC		42.75-
259PhosphorylationSKVKKFDTSISFPPV
CCCEECCCCCCCCCC		30.9618452278
262PhosphorylationKKFDTSISFPPVNLE
EECCCCCCCCCCCHH		31.3118452278
321AcetylationSNQALNCKFYKSMKI
CCHHHCCHHHHHHHH		51.1325953088
321UbiquitinationSNQALNCKFYKSMKI
CCHHHCCHHHHHHHH		51.13-
376PhosphorylationELKHESTYLQQLSRK
HHHCHHHHHHHHHCC		16.2817322306
386PhosphorylationQLSRKDETSTSGNFS
HHHCCCCCCCCCCCC		47.6522210691
387PhosphorylationLSRKDETSTSGNFSV
HHCCCCCCCCCCCCC		20.6622210691
389PhosphorylationRKDETSTSGNFSVDE
CCCCCCCCCCCCCCH		31.3522210691
393PhosphorylationTSTSGNFSVDEKTQW
CCCCCCCCCCHHHHH		32.4322210691
411AcetylationEIESRRTKRRQARVL
HHHHHHHHHHHHHHH		43.7130592889
419PhosphorylationRRQARVLSGNCNHQE
HHHHHHHHCCCCCCC		25.7123927012
428PhosphorylationNCNHQEGTSSDDELP
CCCCCCCCCCCCCCC		25.0625463755
429PhosphorylationCNHQEGTSSDDELPS
CCCCCCCCCCCCCCC		42.5025159151
430PhosphorylationNHQEGTSSDDELPSA
CCCCCCCCCCCCCCH		49.2525159151
436PhosphorylationSSDDELPSAEMIDFQ
CCCCCCCCHHHHHHH		49.8623927012
452UbiquitinationSQGDILQKQKKVFEE
HCHHHHHHHHHHHHH		61.72-
484PhosphorylationWREKFPDSYYEAFIS
HHHHCCHHHHHHHHH		29.8328270605
485PhosphorylationREKFPDSYYEAFISL
HHHCCHHHHHHHHHH		16.8328270605
486PhosphorylationEKFPDSYYEAFISLC
HHCCHHHHHHHHHHH		12.5328270605
491PhosphorylationSYYEAFISLCIPKLL
HHHHHHHHHHHHHHH		15.6728270605
513AcetylationLIDWNPLKLESTGLK
ECCCCCCCCCCCCCC		52.0126051181
513UbiquitinationLIDWNPLKLESTGLK
ECCCCCCCCCCCCCC		52.01-
520UbiquitinationKLESTGLKEMPWFKS
CCCCCCCCCCCCCCC		54.00-
551PhosphorylationSSDKKVLSAIINKTI
CCCHHHHHHHHCCCH		22.0220068231
557PhosphorylationLSAIINKTIIPRLTD
HHHHHCCCHHHHHHH		21.46-
602PhosphorylationCENEVSKSRQDLLKS
CCCHHHHHHHHHHHH		27.8922210691
627PhosphorylationDDVFIPLYPKSAVEN
CCCEEECCCHHHHCC		11.85-
629UbiquitinationVFIPLYPKSAVENKT
CEEECCCHHHHCCCC		37.17-
630PhosphorylationFIPLYPKSAVENKTS
EEECCCHHHHCCCCC		32.8023312004
636PhosphorylationKSAVENKTSPHSKFQ
HHHHCCCCCCCHHHH		60.1028348404
637PhosphorylationSAVENKTSPHSKFQE
HHHCCCCCCCHHHHH		23.4030576142
640PhosphorylationENKTSPHSKFQERQF
CCCCCCCHHHHHHHH		38.2523312004
681PhosphorylationLGKLLNRYLIIALLN
HHHHHHHHHHHHHHH		10.94-
718PhosphorylationFENSAMRTSIPQLEN
HHCCHHHCCCHHHHH		20.2322210691
719PhosphorylationENSAMRTSIPQLENF
HCCHHHCCCHHHHHH		23.1622210691
738PhosphorylationLQSAHKLSRSEFRDE
HHHHHHCCHHHHHHH		38.2726270265
740PhosphorylationSAHKLSRSEFRDEVE
HHHHCCHHHHHHHHH		37.4023828894
775UbiquitinationEHHLDHLKSLIKED-
HHHHHHHHHHHHCC-		39.53-
776PhosphorylationHHLDHLKSLIKED--
HHHHHHHHHHHCC--		41.5124719451
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 GCFC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCFC2_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 GCFC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CR3L2_HUMANCREB3L2physical
21988832
PRP6_HUMANPRPF6physical
26186194
U520_HUMANSNRNP200physical
26186194
PRP8_HUMANPRPF8physical
26186194
DDX23_HUMANDDX23physical
26186194
CSK22_HUMANCSNK2A2physical
26186194
UBR2_HUMANUBR2physical
26186194
CSK21_HUMANCSNK2A1physical
26186194
ECD_HUMANECDphysical
26186194
PRP19_HUMANPRPF19physical
28514442
PRP6_HUMANPRPF6physical
28514442
DDX23_HUMANDDX23physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
U520_HUMANSNRNP200physical
28514442
CSK22_HUMANCSNK2A2physical
28514442
UBR2_HUMANUBR2physical
28514442
PRP8_HUMANPRPF8physical
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 GCFC2_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-16; SER-17; SER-19;THR-213; SER-214; SER-217 AND SER-430, AND MASS 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-40; SER-119; SER-419 ANDSER-430, AND MASS 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-16; SER-17; SER-19;SER-174; SER-180; THR-213; SER-214 AND SER-217, 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-16; SER-17; SER-19;SER-96; THR-97 AND SER-180, AND MASS 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-429 AND SER-430, ANDMASS SPECTROMETRY.

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