Skip Header

Contribute Send feedback
Read comments (?) or add your own

P16383 (GCFC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GC-rich sequence DNA-binding factor 2
Alternative name(s):
GC-rich sequence DNA-binding factor
Transcription factor 9
Short name=TCF-9
Gene names
Name:GCFC2
Synonyms:C2orf3, GCF, TCF9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Nucleus.

Tissue specificity

Widely expressed in tissues and cell lines.

Sequence similarities

Belongs to the GCF family.

Sequence caution

The sequence AAA35598.1 differs from that shown. Reason: Frameshift at position 147.

The sequence AAA35598.1 differs from that shown. Reason: Contaminating sequence. The N-terminus matches the 2q37.3 region.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandDNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of transcription, DNA-dependent

Non-traceable author statement PubMed 10500253. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P16383-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P16383-2)

The sequence of this isoform differs from the canonical sequence as follows:
     169-207: GMKRESEDDPESEPDDHEKRIPFTLRPQTLRQRMAEESI → V
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 781781GC-rich sequence DNA-binding factor 2
PRO_0000087441

Regions

Coiled coil267 – 31246 Potential
Compositional bias116 – 1227Poly-Ser

Amino acid modifications

Modified residue161Phosphoserine Ref.5 Ref.6 Ref.9
Modified residue171Phosphoserine Ref.5 Ref.6 Ref.9
Modified residue191Phosphoserine Ref.5 Ref.6 Ref.9
Modified residue961Phosphoserine Ref.7 Ref.9
Modified residue971Phosphothreonine Ref.7 Ref.9
Modified residue1291Phosphoserine By similarity
Modified residue1801Phosphoserine By similarity
Modified residue2131Phosphothreonine Ref.5 Ref.6
Modified residue2141Phosphoserine Ref.5 Ref.6
Modified residue2171Phosphoserine Ref.5 Ref.6

Natural variations

Alternative sequence169 – 20739GMKRE…AEESI → V in isoform 2.
VSP_021798
Natural variant321P → A. Ref.2
Corresponds to variant rs7559767 [ dbSNP | Ensembl ].
VAR_051005
Natural variant2491N → S.
Corresponds to variant rs7560262 [ dbSNP | Ensembl ].
VAR_051006
Natural variant3161Q → E.
Corresponds to variant rs6742946 [ dbSNP | Ensembl ].
VAR_051007
Natural variant5941T → A.
Corresponds to variant rs6722682 [ dbSNP | Ensembl ].
VAR_051008
Natural variant7241E → D.
Corresponds to variant rs17690300 [ dbSNP | Ensembl ].
VAR_051009

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 38D34EE4442EB3DF

FASTA78189,385
        10         20         30         40         50         60 
MAHRPKRTFR QRAADSSDSD GAEESPAEPG APRELPVPGS AEEEPPSGGG RAQVAGLPHR 

        70         80         90        100        110        120 
VRGPRGRGRV WASSRRATKA APRADEGSES RTLDVSTDEE DKIHHSSESK DDQGLSSDSS 

       130        140        150        160        170        180 
SSLGEKELSS TVKIPDAAFI QAARRKRELA RAQDDYISLD VQHTSSISGM KRESEDDPES 

       190        200        210        220        230        240 
EPDDHEKRIP FTLRPQTLRQ RMAEESISRN EETSEESQED EKQDTWEQQQ MRKAVKIIEE 

       250        260        270        280        290        300 
RDIDLSCGNG SSKVKKFDTS ISFPPVNLEI IKKQLNTRLT LLQETHRSHL REYEKYVQDV 

       310        320        330        340        350        360 
KSSKSTIQNL ESSSNQALNC KFYKSMKIYV ENLIDCLNEK IINIQEIESS MHALLLKQAM 

       370        380        390        400        410        420 
TFMKRRQDEL KHESTYLQQL SRKDETSTSG NFSVDEKTQW ILEEIESRRT KRRQARVLSG 

       430        440        450        460        470        480 
NCNHQEGTSS DDELPSAEMI DFQKSQGDIL QKQKKVFEEV QDDFCNIQNI LLKFQQWREK 

       490        500        510        520        530        540 
FPDSYYEAFI SLCIPKLLNP LIRVQLIDWN PLKLESTGLK EMPWFKSVEE FMDSSVEDSK 

       550        560        570        580        590        600 
KESSSDKKVL SAIINKTIIP RLTDFVEFLW DPLSTSQTTS LITHCRVILE EHSTCENEVS 

       610        620        630        640        650        660 
KSRQDLLKSI VSRMKKAVED DVFIPLYPKS AVENKTSPHS KFQERQFWSG LKLFRNILLW 

       670        680        690        700        710        720 
NGLLTDDTLQ ELGLGKLLNR YLIIALLNAT PGPDVVKKCN QVAACLPEKW FENSAMRTSI 

       730        740        750        760        770        780 
PQLENFIQFL LQSAHKLSRS EFRDEVEEII LILVKIKALN QAESFIGEHH LDHLKSLIKE 


D 

« Hide

Isoform 2 [UniParc].

Checksum: E0187138CD59CE75
Show »

FASTA74384,847

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a human DNA binding factor that represses transcription."
Kageyama R., Pastan I.
Cell 59:815-825(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-32.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-19; THR-213; SER-214 AND SER-217, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-19; THR-213; SER-214 AND SER-217, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-97, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-19; SER-96 AND THR-97, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29204 mRNA. Translation: AAA35598.1. Sequence problems.
AC005034 Genomic DNA. Translation: AAY14973.1.
BC064559 mRNA. Translation: AAH64559.1.
IPIIPI00418340.
IPI00807475.
PIRA33633.
RefSeqNP_001188263.1. NM_001201334.1.
NP_003194.3. NM_003203.4.
UniGeneHs.303808.
Hs.662279.
Hs.710597.

3D structure databases

ProteinModelPortalP16383.
ModBaseSearch...

Protein-protein interaction databases

IntActP16383. 4 interactions.
MINTMINT-2863474.
STRING9606.ENSP00000318690.

PTM databases

PhosphoSiteP16383.

Polymorphism databases

DMDM118572650.

Proteomic databases

PaxDbP16383.
PRIDEP16383.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321027; ENSP00000318690; ENSG00000005436.
ENST00000409857; ENSP00000386552; ENSG00000005436.
GeneID6936.
KEGGhsa:6936.
UCSCuc002snn.3. human.

Organism-specific databases

CTD6936.
GeneCardsGC02M075880.
HGNCHGNC:1317. GCFC2.
MIM189901. gene.
neXtProtNX_P16383.
PharmGKBPA25892.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294271.
HOGENOMHOG000112699.
HOVERGENHBG101878.
InParanoidP16383.
KOK09061.
OMAQDTWEQQ.
OrthoDBEOG415GDS.
PhylomeDBP16383.

Gene expression databases

ArrayExpressP16383.
BgeeP16383.
CleanExHS_C2orf3.
GenevestigatorP16383.
GermOnlineENSG00000005436. Homo sapiens.

Family and domain databases

InterProIPR012890. GCFC.
IPR022783. GCFC_dom.
[Graphical view]
PANTHERPTHR12214. PTHR12214. 1 hit.
PfamPF07842. GCFC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi6936.
NextBio27141.
SOURCESearch...

Entry information

Entry nameGCFC2_HUMAN
AccessionPrimary (citable) accession number: P16383
Secondary accession number(s): O95032, Q53TY0, Q6P2F2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 28, 2006
Last modified: April 3, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families