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Q01081 (U2AF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Splicing factor U2AF 35 kDa subunit
Alternative name(s):
U2 auxiliary factor 35 kDa subunit
U2 small nuclear RNA auxiliary factor 1
U2 snRNP auxiliary factor small subunit
Gene names
Name:U2AF1
Synonyms:U2AF35, U2AFBP
ORF Names:FP793
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron. Ref.8

Subunit structure

Interacts (via RS domain) with PHF5A (via N-terminus) By similarity. Identified in the spliceosome C complex. Heterodimer with U2AF2. Interacts with ZRANB2. Ref.9 Ref.10

Subcellular location

Nucleus. Nucleus speckle Ref.2.

Domain

The C-terminal SR-rich domain is required for interactions with SR proteins and the splicing regulators TRA and TRA2, and the N-terminal domain is required for formation of the U2AF1/U2AF2 heterodimer.

Sequence similarities

Belongs to the splicing factor SR family.

Contains 2 C3H1-type zinc fingers.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.1. Source: ProtInc

mRNA splicing, via spliceosome

Inferred by curator Ref.10. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentCajal body

Traceable author statement Ref.1. Source: ProtInc

catalytic step 2 spliceosome

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01081-1)

Also known as: U2AF35a;

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: Q01081-2)

Also known as: U2AF35b;

The sequence of this isoform differs from the canonical sequence as follows:
     47-66: ALLNIYRNPQNSSQSADGLR → LIQNIYRNPQNSAQTADGSH
Note: Interacts with U2AF2 and stimulates U2AF splicing activity in vitro. Less efficient than isoform 1.
Isoform 3 (identifier: Q01081-3)

Also known as: U2AF35c;

The sequence of this isoform differs from the canonical sequence as follows:
     47-66: ALLNIYRNPQNSSQSADGLR → LIQNIYRNPQNSAQTADGSH
     67-75: CAVSDVEMQ → YHCPLEHLP
     76-240: Missing.
Note: Produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 4 (identifier: Q01081-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 240239Splicing factor U2AF 35 kDa subunit
PRO_0000081994

Regions

Domain65 – 14783RRM
Zinc finger12 – 4029C3H1-type 1
Zinc finger149 – 17628C3H1-type 2
Compositional bias178 – 24063Arg/Gly/Ser-rich (RS domain)
Compositional bias210 – 22314Poly-Gly

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue611Phosphoserine Ref.14

Natural variations

Alternative sequence1 – 7373Missing in isoform 4.
VSP_042664
Alternative sequence47 – 6620ALLNI…ADGLR → LIQNIYRNPQNSAQTADGSH in isoform 2 and isoform 3.
VSP_042665
Alternative sequence67 – 759CAVSDVEMQ → YHCPLEHLP in isoform 3.
VSP_042666
Alternative sequence76 – 240165Missing in isoform 3.
VSP_042667

Experimental info

Mutagenesis1341W → A: Decreases affinity for UAF2 by 3 orders of magnitude. Ref.15

Secondary structure

............. 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (U2AF35a) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3DA130DCE0B953F6

FASTA24027,872
        10         20         30         40         50         60 
MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIALLN IYRNPQNSSQ 

        70         80         90        100        110        120 
SADGLRCAVS DVEMQEHYDE FFEEVFTEME EKYGEVEEMN VCDNLGDHLV GNVYVKFRRE 

       130        140        150        160        170        180 
EDAEKAVIDL NNRWFNGQPI HAELSPVTDF REACCRQYEM GECTRGGFCN FMHLKPISRE 

       190        200        210        220        230        240 
LRRELYGRRR KKHRSRSRSR ERRSRSRDRG RGGGGGGGGG GGGRERDRRR SRDRERSGRF 

« Hide

Isoform 2 (U2AF35b) [UniParc].

Checksum: DDBE62F36F0CDF52
Show »

FASTA24027,882
Isoform 3 (U2AF35c) [UniParc].

Checksum: 30BF651C83599A9D
Show »

FASTA758,572
Isoform 4 [UniParc].

Checksum: 3EBB13A8234C736B
Show »

FASTA16719,715

References

« Hide 'large scale' references
[1]"Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit."
Zhang M., Zamore P.D., Carmo-Fonseca M., Lamond A.I., Green M.R.
Proc. Natl. Acad. Sci. U.S.A. 89:8769-8773(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 68-89 AND 126-151.
Tissue: Fetal brain.
[2]"Diversity of vertebrate splicing factor U2AF35: identification of alternatively spliced U2AF1 mRNAs."
Pacheco T.R.D., Gomes N.L., Benes V., Ansorge W., Wollerton M., Smith C.W., Valcarcel J., Carmo-Fonseca M.
J. Biol. Chem. 279:27039-27049(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION.
Tissue: Spleen.
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[4]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Lung.
[7]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]"The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing."
Zuo P., Maniatis T.
Genes Dev. 10:1356-1368(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"ZNF265 -- a novel spliceosomal protein able to induce alternative splicing."
Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., Rasko J.E.J.
J. Cell Biol. 154:25-32(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZRANB2.
[10]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer."
Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.
Cell 106:595-605(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 43-146 IN COMPLEX WITH U2AF2, MUTAGENESIS OF TRP-134.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96982 mRNA. Translation: AAA36619.1.
AJ627978 mRNA. Translation: CAF29556.1.
AF370386 mRNA. Translation: AAQ15222.1.
AP001631 Genomic DNA. No translation available.
AP001748 Genomic DNA. Translation: BAA95534.1.
CH471079 Genomic DNA. Translation: EAX09501.1.
CH471079 Genomic DNA. Translation: EAX09502.1.
CH471079 Genomic DNA. Translation: EAX09504.1.
CH471079 Genomic DNA. Translation: EAX09505.1.
BC001177 mRNA. Translation: AAH01177.1.
BC001923 mRNA. Translation: AAH01923.1.
PIRA46179.
RefSeqNP_001020374.1. NM_001025203.1.
NP_001020375.1. NM_001025204.1.
NP_006749.1. NM_006758.2.
UniGeneHs.365116.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMTX-ray2.20A43-146[»]
ProteinModelPortalQ01081.
SMRQ01081. Positions 43-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113157. 103 interactions.
DIPDIP-1108N.
IntActQ01081. 34 interactions.
MINTMINT-1468226.
STRING9606.ENSP00000291552.

PTM databases

PhosphoSiteQ01081.

Polymorphism databases

DMDM267187.

Proteomic databases

PaxDbQ01081.
PeptideAtlasQ01081.
PRIDEQ01081.

Protocols and materials databases

DNASU7307.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291552; ENSP00000291552; ENSG00000160201. [Q01081-1]
ENST00000380276; ENSP00000369629; ENSG00000160201. [Q01081-2]
ENST00000398137; ENSP00000381205; ENSG00000160201. [Q01081-4]
ENST00000459639; ENSP00000418705; ENSG00000160201. [Q01081-4]
ENST00000464750; ENSP00000420672; ENSG00000160201. [Q01081-3]
GeneID7307.
KEGGhsa:7307.
UCSCuc002zcy.1. human. [Q01081-1]
uc002zda.1. human. [Q01081-2]

Organism-specific databases

CTD7307.
GeneCardsGC21M044513.
HGNCHGNC:12453. U2AF1.
HPAHPA044833.
MIM191317. gene.
neXtProtNX_Q01081.
PharmGKBPA37103.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323920.
HOGENOMHOG000178619.
HOVERGENHBG054605.
KOK12836.
OMATVSDVEM.
OrthoDBEOG70089G.
PhylomeDBQ01081.
TreeFamTF300143.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ01081.
BgeeQ01081.
CleanExHS_U2AF1.
GenevestigatorQ01081.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR009145. U2_small.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERPTHR12620. PTHR12620. 1 hit.
PfamPF00642. zf-CCCH. 2 hits.
[Graphical view]
PRINTSPR01848. U2AUXFACTOR.
SMARTSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSU2AF1. human.
EvolutionaryTraceQ01081.
GeneWikiU2_small_nuclear_RNA_auxiliary_factor_1.
GenomeRNAi7307.
NextBio28572.
PROQ01081.
SOURCESearch...

Entry information

Entry nameU2AF1_HUMAN
AccessionPrimary (citable) accession number: Q01081
Secondary accession number(s): Q701P4, Q71RF1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 162 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM