GCFC2_MOUSE - dbPTM
GCFC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCFC2_MOUSE
UniProt AC Q8BKT3
Protein Name GC-rich sequence DNA-binding factor 2
Gene Name Gcfc2
Organism Mus musculus (Mouse).
Sequence Length 769
Subcellular Localization Nucleus. 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 (By similarity)..
Protein Sequence MALRPQRTFRRRQVESSDSDSDSDGAKEQSAEEPASAGGRTEGAERPRGARSARGRGRVWASSRRSPGAAPRGDGGAECRTAELSTDEEEGTHTLTGSKGDRSPSSDSSCSLEERDVSPIVEIPDAAFIQAARRKRELARTPGDYISLDVNHSCSTSDCKRSNEEDPESDPDDHEKRILFTPKPQTLRQRMAEETSIRSEESSEESQEDENQDIWEQQQMRKAVRIPAGQNTDLSHSSKSQTLKKFDTSISFPPVNLEIIKKQLNNRLTLLQESHRSHQREYEKYEQDIKSSKTAIQNLESASDHAQNYRFYRGMKSYVENIIDCLNEKIVSIVELESSMYTLLLKRSEALLKRRQDELKCESSYLQQLSRKDETSANGSLAVDEKDQRILEEIEARRMQRRQARELSGSCDHQEGMSSDDELSPAEMTNFHKCQGDILQDCKKVFEDVHDDFCNVQNILLKFQQWREKFPDSYYEAFVGFCLPKLLSPLIRVQLLDWNPLKMDSIGLDKMPWFTAITEFMESSMDDIGKEDGSDKKILAAVINKTVVPRLTDFVETIWDPLSTSQTRSLTVHCRVAFEQFASENEVSKNKQDLLKSIVARMKKSIEDDIFIPLYPKSSEEGKMSPHSKFQERQFWGALKLFRNILLWNGLLPDDTLQDLGLGKLLNRYLIISLTNAVPGPDVVKKCSQIAACLPERWFENSAMRTSIPQLENFIKFLLQSAQKLSSSEFRNEVSEIILILVKVKALTQAESLREERPLEPLPAQSTGV
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
16PhosphorylationFRRRQVESSDSDSDS
CCCCHHCCCCCCCCC		40.36-
17PhosphorylationRRRQVESSDSDSDSD
CCCHHCCCCCCCCCC		27.85-
19PhosphorylationRQVESSDSDSDSDGA
CHHCCCCCCCCCCCC		40.75-
30PhosphorylationSDGAKEQSAEEPASA
CCCCHHHCCCCCHHC		38.4525521595
62PhosphorylationGRGRVWASSRRSPGA
CCCCCEECCCCCCCC		14.5224719451
63PhosphorylationRGRVWASSRRSPGAA
CCCCEECCCCCCCCC		24.7826643407
66PhosphorylationVWASSRRSPGAAPRG
CEECCCCCCCCCCCC		26.9525266776
81PhosphorylationDGGAECRTAELSTDE
CCCCEEEEEECCCCC		35.8225159016
85PhosphorylationECRTAELSTDEEEGT
EEEEEECCCCCCCCE		25.8927087446
86PhosphorylationCRTAELSTDEEEGTH
EEEEECCCCCCCCEE		61.1225521595
92PhosphorylationSTDEEEGTHTLTGSK
CCCCCCCEEECCCCC		18.2426239621
94PhosphorylationDEEEGTHTLTGSKGD
CCCCCEEECCCCCCC		26.3426239621
96PhosphorylationEEGTHTLTGSKGDRS
CCCEEECCCCCCCCC		40.3329550500
98PhosphorylationGTHTLTGSKGDRSPS
CEEECCCCCCCCCCC		28.3829550500
118PhosphorylationSLEERDVSPIVEIPD
CCCCCCCCCCEECCH		17.1326824392
155PhosphorylationLDVNHSCSTSDCKRS
EECCCCCCHHHHCCC		33.6825195567
157PhosphorylationVNHSCSTSDCKRSNE
CCCCCCHHHHCCCCC		25.3925195567
162PhosphorylationSTSDCKRSNEEDPES
CHHHHCCCCCCCCCC		33.8021149613
169PhosphorylationSNEEDPESDPDDHEK
CCCCCCCCCCCCHHH		60.8925521595
181PhosphorylationHEKRILFTPKPQTLR
HHHCCEECCCCHHHH		27.2722817900
196PhosphorylationQRMAEETSIRSEESS
HHHHHHHCCCCHHCC		21.2025338131
199PhosphorylationAEETSIRSEESSEES
HHHHCCCCHHCCHHH		44.0125338131
202PhosphorylationTSIRSEESSEESQED
HCCCCHHCCHHHHHH		38.7125338131
203PhosphorylationSIRSEESSEESQEDE
CCCCHHCCHHHHHHH		48.9725338131
206PhosphorylationSEESSEESQEDENQD
CHHCCHHHHHHHHHH		34.5125338131
408PhosphorylationRRQARELSGSCDHQE
HHHHHHHHCCCCCCC		24.7325159016
410PhosphorylationQARELSGSCDHQEGM
HHHHHHCCCCCCCCC		17.0024759943
418PhosphorylationCDHQEGMSSDDELSP
CCCCCCCCCCCCCCH		41.2825159016
419PhosphorylationDHQEGMSSDDELSPA
CCCCCCCCCCCCCHH		39.9425159016
424PhosphorylationMSSDDELSPAEMTNF
CCCCCCCCHHHHHCH		21.7325195567
429PhosphorylationELSPAEMTNFHKCQG
CCCHHHHHCHHHCCC		26.6625293948
488PhosphorylationFCLPKLLSPLIRVQL
HHHHHHHHHHHHHHH		28.26-
505PhosphorylationWNPLKMDSIGLDKMP
CCCCCCCCCCCCCCC		18.30-
605PhosphorylationIVARMKKSIEDDIFI
HHHHHHHHHCCCCEE		26.20-
615PhosphorylationDDIFIPLYPKSSEEG
CCCEEECCCCCCCCC		11.85-
669PhosphorylationLGKLLNRYLIISLTN
HHHHHHHHHHHHCCC		10.9421454597
673PhosphorylationLNRYLIISLTNAVPG
HHHHHHHHCCCCCCC		23.3421454597
735PhosphorylationSEFRNEVSEIILILV
HHHHHHHHHHHHHHH		19.5221454597
752PhosphorylationKALTQAESLREERPL
HHHHHHHHHHHHCCC		35.4221454597
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCFC2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GCFC2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCFC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.

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