SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16383

- GCFC2_HUMAN

UniProt

P16383 - GCFC2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
GC-rich sequence DNA-binding factor 2
Gene
GCFC2, C2orf3, GCF, TCF9
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: UniProtKB
  2. regulation of transcription, DNA-templated Source: UniProtKB
  3. spliceosomal complex assembly Source: UniProtKB
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GCFC2
Synonyms:C2orf3, GCF, TCF9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:1317. GCFC2.

Subcellular locationi

Nucleusnucleoplasm. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. U2-type post-mRNA release spliceosomal complex Source: UniProtKB
  2. nucleolus Source: UniProtKB
  3. nucleoplasm Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25892.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 781781GC-rich sequence DNA-binding factor 2
PRO_0000087441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine3 Publications
Modified residuei17 – 171Phosphoserine3 Publications
Modified residuei19 – 191Phosphoserine3 Publications
Modified residuei96 – 961Phosphoserine2 Publications
Modified residuei97 – 971Phosphothreonine2 Publications
Modified residuei129 – 1291Phosphoserine By similarity
Modified residuei213 – 2131Phosphothreonine2 Publications
Modified residuei214 – 2141Phosphoserine2 Publications
Modified residuei217 – 2171Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16383.
PaxDbiP16383.
PRIDEiP16383.

PTM databases

PhosphoSiteiP16383.

Expressioni

Tissue specificityi

Widely expressed in tissues and cell lines.

Gene expression databases

ArrayExpressiP16383.
BgeeiP16383.
CleanExiHS_C2orf3.
GenevestigatoriP16383.

Interactioni

Subunit structurei

Found in the Intron Large (IL) complex, a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors. Interacts with TFIP11 and DHX15.1 Publication

Protein-protein interaction databases

BioGridi112797. 4 interactions.
IntActiP16383. 8 interactions.
MINTiMINT-2863474.
STRINGi9606.ENSP00000318690.

Structurei

3D structure databases

ProteinModelPortaliP16383.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili267 – 31246 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi116 – 1227Poly-Ser

Sequence similaritiesi

Belongs to the GCF family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG294271.
HOGENOMiHOG000112699.
HOVERGENiHBG101878.
InParanoidiP16383.
KOiK09061.
OMAiQDTWEQQ.
OrthoDBiEOG79KPGP.
PhylomeDBiP16383.
TreeFamiTF315109.

Family and domain databases

InterProiIPR012890. GCFC.
IPR022783. GCFC_dom.
[Graphical view]
PANTHERiPTHR12214. PTHR12214. 1 hit.
PfamiPF07842. GCFC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P16383-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAHRPKRTFR QRAADSSDSD GAEESPAEPG APRELPVPGS AEEEPPSGGG    50
RAQVAGLPHR VRGPRGRGRV WASSRRATKA APRADEGSES RTLDVSTDEE 100
DKIHHSSESK DDQGLSSDSS SSLGEKELSS TVKIPDAAFI QAARRKRELA 150
RAQDDYISLD VQHTSSISGM KRESEDDPES EPDDHEKRIP FTLRPQTLRQ 200
RMAEESISRN EETSEESQED EKQDTWEQQQ MRKAVKIIEE RDIDLSCGNG 250
SSKVKKFDTS ISFPPVNLEI IKKQLNTRLT LLQETHRSHL REYEKYVQDV 300
KSSKSTIQNL ESSSNQALNC KFYKSMKIYV ENLIDCLNEK IINIQEIESS 350
MHALLLKQAM TFMKRRQDEL KHESTYLQQL SRKDETSTSG NFSVDEKTQW 400
ILEEIESRRT KRRQARVLSG NCNHQEGTSS DDELPSAEMI DFQKSQGDIL 450
QKQKKVFEEV QDDFCNIQNI LLKFQQWREK FPDSYYEAFI SLCIPKLLNP 500
LIRVQLIDWN PLKLESTGLK EMPWFKSVEE FMDSSVEDSK KESSSDKKVL 550
SAIINKTIIP RLTDFVEFLW DPLSTSQTTS LITHCRVILE EHSTCENEVS 600
KSRQDLLKSI VSRMKKAVED DVFIPLYPKS AVENKTSPHS KFQERQFWSG 650
LKLFRNILLW NGLLTDDTLQ ELGLGKLLNR YLIIALLNAT PGPDVVKKCN 700
QVAACLPEKW FENSAMRTSI PQLENFIQFL LQSAHKLSRS EFRDEVEEII 750
LILVKIKALN QAESFIGEHH LDHLKSLIKE D 781
Length:781
Mass (Da):89,385
Last modified:November 28, 2006 - v2
Checksum:i38D34EE4442EB3DF
GO
Isoform 2 (identifier: P16383-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-207: GMKRESEDDPESEPDDHEKRIPFTLRPQTLRQRMAEESI → V

Note: No experimental confirmation available.

Show »
Length:743
Mass (Da):84,847
Checksum:iE0187138CD59CE75
GO
Isoform 3 (identifier: P16383-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     207-213: ISRNEET → SMDLPIY
     214-779: Missing.

Show »
Length:215
Mass (Da):23,613
Checksum:iBE28FB823AF92EB5
GO

Sequence cautioni

The sequence AAA35598.1 differs from that shown. Reason: Contaminating sequence. The N-terminus matches the 2q37.3 region.
The sequence AAA35598.1 differs from that shown. Reason: Frameshift at position 147.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321P → A.1 Publication
Corresponds to variant rs7559767 [ dbSNP | Ensembl ].
VAR_051005
Natural varianti249 – 2491N → S.
Corresponds to variant rs7560262 [ dbSNP | Ensembl ].
VAR_051006
Natural varianti316 – 3161Q → E.
Corresponds to variant rs6742946 [ dbSNP | Ensembl ].
VAR_051007
Natural varianti594 – 5941T → A.
Corresponds to variant rs6722682 [ dbSNP | Ensembl ].
VAR_051008
Natural varianti724 – 7241E → D.
Corresponds to variant rs17690300 [ dbSNP | Ensembl ].
VAR_051009

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 20739GMKRE…AEESI → V in isoform 2.
VSP_021798Add
BLAST
Alternative sequencei207 – 2137ISRNEET → SMDLPIY in isoform 3.
VSP_054362
Alternative sequencei214 – 779566Missing in isoform 3.
VSP_054363Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M29204 mRNA. Translation: AAA35598.1. Sequence problems.
EF158467 mRNA. Translation: ABO84856.1.
AC005034 Genomic DNA. Translation: AAY14973.1.
CH471053 Genomic DNA. Translation: EAW99586.1.
BC064559 mRNA. Translation: AAH64559.1.
CCDSiCCDS1961.1. [P16383-1]
CCDS62943.1. [P16383-3]
PIRiA33633.
RefSeqiNP_001188263.1. NM_001201334.1.
NP_001188264.1. NM_001201335.1. [P16383-3]
NP_003194.3. NM_003203.4. [P16383-1]
UniGeneiHs.303808.
Hs.662279.
Hs.710597.

Genome annotation databases

EnsembliENST00000321027; ENSP00000318690; ENSG00000005436. [P16383-1]
ENST00000409857; ENSP00000386552; ENSG00000005436. [P16383-2]
ENST00000470503; ENSP00000474481; ENSG00000005436.
GeneIDi6936.
KEGGihsa:6936.
UCSCiuc002snn.3. human. [P16383-1]
uc002snp.4. human.

Polymorphism databases

DMDMi118572650.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M29204 mRNA. Translation: AAA35598.1 . Sequence problems.
EF158467 mRNA. Translation: ABO84856.1 .
AC005034 Genomic DNA. Translation: AAY14973.1 .
CH471053 Genomic DNA. Translation: EAW99586.1 .
BC064559 mRNA. Translation: AAH64559.1 .
CCDSi CCDS1961.1. [P16383-1 ]
CCDS62943.1. [P16383-3 ]
PIRi A33633.
RefSeqi NP_001188263.1. NM_001201334.1.
NP_001188264.1. NM_001201335.1. [P16383-3 ]
NP_003194.3. NM_003203.4. [P16383-1 ]
UniGenei Hs.303808.
Hs.662279.
Hs.710597.

3D structure databases

ProteinModelPortali P16383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112797. 4 interactions.
IntActi P16383. 8 interactions.
MINTi MINT-2863474.
STRINGi 9606.ENSP00000318690.

PTM databases

PhosphoSitei P16383.

Polymorphism databases

DMDMi 118572650.

Proteomic databases

MaxQBi P16383.
PaxDbi P16383.
PRIDEi P16383.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321027 ; ENSP00000318690 ; ENSG00000005436 . [P16383-1 ]
ENST00000409857 ; ENSP00000386552 ; ENSG00000005436 . [P16383-2 ]
ENST00000470503 ; ENSP00000474481 ; ENSG00000005436 .
GeneIDi 6936.
KEGGi hsa:6936.
UCSCi uc002snn.3. human. [P16383-1 ]
uc002snp.4. human.

Organism-specific databases

CTDi 6936.
GeneCardsi GC02M075880.
HGNCi HGNC:1317. GCFC2.
MIMi 189901. gene.
neXtProti NX_P16383.
PharmGKBi PA25892.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG294271.
HOGENOMi HOG000112699.
HOVERGENi HBG101878.
InParanoidi P16383.
KOi K09061.
OMAi QDTWEQQ.
OrthoDBi EOG79KPGP.
PhylomeDBi P16383.
TreeFami TF315109.

Miscellaneous databases

GeneWikii C2orf3.
GenomeRNAii 6936.
NextBioi 27141.
PROi P16383.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16383.
Bgeei P16383.
CleanExi HS_C2orf3.
Genevestigatori P16383.

Family and domain databases

InterProi IPR012890. GCFC.
IPR022783. GCFC_dom.
[Graphical view ]
PANTHERi PTHR12214. PTHR12214. 1 hit.
Pfami PF07842. GCFC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "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.
    , 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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "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.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-19; THR-213; SER-214 AND SER-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Identification of a novel component C2ORF3 in the lariat-intron complex: lack of C2ORF3 interferes with pre-mRNA splicing via intron turnover pathway."
    Yoshimoto R., Okawa K., Yoshida M., Ohno M., Kataoka N.
    Genes Cells 19:78-87(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE INTRON LARGE COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH TFIP11 AND DHX15.

Entry informationi

Entry nameiGCFC2_HUMAN
AccessioniPrimary (citable) accession number: P16383
Secondary accession number(s): A4UHQ8
, O95032, Q53TY0, Q6P2F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 28, 2006
Last modified: September 3, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi