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Reviewed, UniProtKB/Swiss-Prot Q05048 (CSTF1_HUMAN)

Last modified February 9, 2010. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cleavage stimulation factor 50 kDa subunit
      Short name=CSTF 50 kDa subunit
Alternative name(s):
    CF-1 50 kDa subunit
    CstF-50
Gene names
Name: CSTF1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA.

Subunit structure

Homodimer. The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). Interacts directly with CSTF3. Interacts with BARD1. Ref.5 Ref.6

Subcellular location

Nucleus.

Domain

The WD6 domain is required for interaction with BARD1. WD domains are responsible for interaction with CSTF3.

N-terminus mediates homodimerization.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Contains 6 WD repeats.

Sequence caution

The sequence CAC12718.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from Experiment. Source: Reactome

mRNA cleavage Ref.1

Traceable author statement. Source: ProtInc

mRNA polyadenylation Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentnucleus Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionRNA binding

Traceable author statement. Source: ProtInc

protein binding Ref.5

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Cleavage stimulation factor 50 kDa subunit
PRO_0000050944

Regions

Repeat106 – 14540WD 1
Repeat171 – 21040WD 2
Repeat215 – 25440WD 3
Repeat260 – 30142WD 4
Repeat303 – 34341WD 5
Repeat395 – 43036WD 6
Region14 – 3522Hydrophobic

Amino acid modifications

Modified residue3671Phosphotyrosine Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q05048-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 88A5BE53022AD9E3

FASTA43148,358
        10         20         30         40         50         60 
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN 

        70         80         90        100        110        120 
DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG 

       130        140        150        160        170        180 
QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA 

       190        200        210        220        230        240 
FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT 

       250        260        270        280        290        300 
LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF 

       310        320        330        340        350        360 
EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV 

       370        380        390        400        410        420 
FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR 

       430 
ARFWYRRSTT D 

« Hide

References

« Hide 'large scale' references
[1]"A human polyadenylation factor is a G protein beta-subunit homologue."
Takagaki Y., Manley J.L.
J. Biol. Chem. 267:23471-23474(1992) [PubMed: 1358884] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 101-119 AND 155-170.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[5]"Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50."
Kleiman F.E., Manley J.L.
Science 285:1576-1579(1999) [PubMed: 10477523] [Abstract]
Cited for: INTERACTION WITH BARD1.
[6]"Complex protein interactions within the human polyadenylation machinery identify a novel component."
Takagaki Y., Manley J.L.
Mol. Cell. Biol. 20:1515-1525(2000) [PubMed: 10669729] [Abstract]
Cited for: SUBUNIT.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-367, MASS SPECTROMETRY.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02547 mRNA. Translation: AAA35691.1.
BT007138 mRNA. Translation: AAP35802.1.
AL121914 Genomic DNA. Translation: CAC12718.2. Sequence problems.
BC001011 mRNA. Translation: AAH01011.1.
BC007425 mRNA. Translation: AAH07425.1.
IPIIPI00011528.
PIRA45142.
RefSeqNP_001028693.1.
NP_001028694.1.
NP_001315.1.
UniGeneHs.172865

3D structure databases

SMRQ05048. Positions 44-426.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05048. 3 interactions.
STRINGQ05048.

PTM databases

PhosphoSiteQ05048.

2-D gel databases

REPRODUCTION-2DPAGEIPI00011528.

Proteomic databases

PeptideAtlasQ05048.
PRIDEQ05048.

Genome annotation databases

EnsemblENST00000217109; ENSP00000217109; ENSG00000101138; Homo sapiens. [Genome view]
ENST00000425890; ENSP00000398984; ENSG00000101138; Homo sapiens. [Genome view]
ENST00000451236; ENSP00000415266; ENSG00000101138; Homo sapiens. [Genome view]
GeneID1477.
KEGGhsa:1477.
UCSCuc002xxl.1. human.

Organism-specific databases

CTD1477.
GeneCardsGC20P054401.
H-InvDBHIX0015931.
HGNCHGNC:2483. CSTF1.
HPACAB019270.
MIM600369. gene.
PharmGKBPA26985.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG595084.
HOVERGENQ05048.
InParanoidQ05048.
OMAYINIANG.
OrthoDBEOG979HSF.
PhylomeDBQ05048.

Enzyme and pathway databases

Pathway_Interaction_DBbard1pathway. BARD1 signaling events.
ReactomeREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ05048.
BgeeQ05048.
CleanExHS_CSTF1.
GenevestigatorQ05048.
GermOnlineENSG00000101138. Homo sapiens.

Family and domain databases

InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019782. WD40_repeat_2.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR019781. WD40_repeat_sg.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF00400. WD40. 6 hits.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio6065.
SOURCESearch...

Entry information

Entry nameCSTF1_HUMAN
AccessionPrimary (citable) accession number: Q05048
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 9, 2010
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents