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Q15696 (U2AFM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
Alternative name(s):
CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2
Renal carcinoma antigen NY-REN-20
U2(RNU2) small nuclear RNA auxiliary factor 1-like 2
U2AF35-related protein
Short name=URP
Gene names
Name:ZRSR2
Synonyms:U2AF1-RS2, U2AF1L2, U2AF1RS2, URP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing. Ref.4 Ref.9

Subunit structure

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts (via RS domain) with SRSF1 and SRSF2. Interacts with U2AF2/U2AF65. Ref.4 Ref.6 Ref.9

Subcellular location

Nucleus Ref.6.

Tissue specificity

Widely expressed. Ref.4

Post-translational modification

Phosphorylated in the RS domain by SRPK1. Ref.4

Sequence similarities

Contains 2 C3H1-type zinc fingers.

Contains 1 RRM (RNA recognition motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
PRO_0000082001

Regions

Domain198 – 304107RRM
Zinc finger166 – 19429C3H1-type 1
Zinc finger306 – 33328C3H1-type 2
Compositional bias46 – 494Poly-Glu
Compositional bias118 – 1236Poly-Glu
Compositional bias414 – 46956Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue3491Phosphoserine Ref.8 Ref.10
Modified residue3841Phosphoserine Ref.7 Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q15696 [UniParc].

Last modified May 1, 1997. Version 2.
Checksum: 1DACC8A6CA4727A6

FASTA48258,045
        10         20         30         40         50         60 
MAAPEKMTFP EKPSHKKYRA ALKKEKRKKR RQELARLRDS GLSQKEEEED TFIEEQQLEE 

        70         80         90        100        110        120 
EKLLERERQR LHEEWLLREQ KAQEEFRIKK EKEEAAKKRQ EEQERKLKEQ WEEQQRKERE 

       130        140        150        160        170        180 
EEEQKRQEKK EKEEALQKML DQAENELENG TTWQNPEPPV DFRVMEKDRA NCPFYSKTGA 

       190        200        210        220        230        240 
CRFGDRCSRK HNFPTSSPTL LIKSMFTTFG MEQCRRDDYD PDASLEYSEE ETYQQFLDFY 

       250        260        270        280        290        300 
EDVLPEFKNV GKVIQFKVSC NLEPHLRGNV YVQYQSEEEC QAALSLFNGR WYAGRQLQCE 

       310        320        330        340        350        360 
FCPVTRWKMA ICGLFEIQQC PRGKHCNFLH VFRNPNNEFW EANRDIYLSP DRTGSSFGKN 

       370        380        390        400        410        420 
SERRERMGHH DDYYSRLRGR RNPSPDHSYK RNGESERKSS RHRGKKSHKR TSKSRERHNS 

       430        440        450        460        470        480 
RSRGRNRDRS RDRSRGRGSR SRSRSRSRRS RRSRSQSSSR SRSRGRRRSG NRDRTVQSPK 


SK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and mapping of human homologues of an imprinted mouse gene U2af1-rs1."
Kitagawa K., Wang X., Hatada I., Yamaoka T., Nojima H., Inazawa J., Abe T., Mitsuya K., Oshimura M., Murata A., Monden M., Mukai T.
Genomics 30:257-263(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
[4]"A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
Tronchere H., Wang J., Fu X.D.
Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH SRSF1; SRSF2; SRPK1 AND U2AF2.
[5]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[6]"The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE U11/U12 SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"The U2AF35-related protein Urp contacts the 3' splice site to promote U12-type intron splicing and the second step of U2-type intron splicing."
Shen H., Zheng X., Luecke S., Green M.R.
Genes Dev. 24:2389-2394(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE U11/U12 SPLICEOSOME COMPLEX, RNA-BINDING.
[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-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49677 mRNA. Translation: BAA08533.1.
AC004106 Genomic DNA. No translation available.
AC096510 Genomic DNA. No translation available.
BC113454 mRNA. Translation: AAI13455.1.
BC113480 mRNA. Translation: AAI13481.1.
CCDSCCDS14172.1.
RefSeqNP_005080.1. NM_005089.3.
UniGeneHs.171909.

3D structure databases

ProteinModelPortalQ15696.
SMRQ15696. Positions 228-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113865. 4 interactions.
IntActQ15696. 2 interactions.
STRING9606.ENSP00000303015.

PTM databases

PhosphoSiteQ15696.

Polymorphism databases

DMDM2833266.

Proteomic databases

MaxQBQ15696.
PaxDbQ15696.
PRIDEQ15696.

Protocols and materials databases

DNASU8233.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307771; ENSP00000303015; ENSG00000169249.
GeneID8233.
KEGGhsa:8233.
UCSCuc004cxg.4. human.

Organism-specific databases

CTD8233.
GeneCardsGC0XP015808.
H-InvDBHIX0017758.
HGNCHGNC:23019. ZRSR2.
HPAHPA047500.
MIM300028. gene.
neXtProtNX_Q15696.
PharmGKBPA162410930.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304335.
HOGENOMHOG000049279.
HOVERGENHBG054605.
InParanoidQ15696.
OMAERMGHHD.
PhylomeDBQ15696.
TreeFamTF324447.

Gene expression databases

ArrayExpressQ15696.
BgeeQ15696.
CleanExHS_ZRSR2.
GenevestigatorQ15696.

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. 1 hit.
[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

ChiTaRSZRSR2. human.
GeneWikiZRSR2.
GenomeRNAi8233.
NextBio30981.
PROQ15696.
SOURCESearch...

Entry information

Entry nameU2AFM_HUMAN
AccessionPrimary (citable) accession number: Q15696
Secondary accession number(s): Q14D69
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 128 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome X

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