Q15696 (U2AFM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	spliceosomal complex assembly Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	U12-type spliceosomal complex Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro pre-mRNA 3'-splice site binding Inferred from direct assay Ref.9. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2		PRO_0000082001
Regions
	Domain	198 – 304	107	RRM
	Zinc finger	166 – 194	29	C3H1-type 1
	Zinc finger	306 – 333	28	C3H1-type 2
	Compositional bias	46 – 49	4	Poly-Glu
	Compositional bias	118 – 123	6	Poly-Glu
	Compositional bias	414 – 469	56	Arg/Ser-rich (RS domain)
Amino acid modifications
	Modified residue	349	1	Phosphoserine Ref.8 Ref.10
	Modified residue	384	1	Phosphoserine Ref.7 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q15696 [UniParc]. Last modified May 1, 1997. Version 2. Checksum: 1DACC8A6CA4727A6	FASTA	482	58,045
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00018954.
RefSeq	NP_005080.1. NM_005089.3.
UniGene	Hs.171909.
3D structure databases
ProteinModelPortal	Q15696.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000303015.
PTM databases
PhosphoSite	Q15696.
Polymorphism databases
DMDM	2833266.
Proteomic databases
PaxDb	Q15696.
PRIDE	Q15696.
Protocols and materials databases
DNASU	8233.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307771; ENSP00000303015; ENSG00000169249.
GeneID	8233.
KEGG	hsa:8233.
UCSC	uc004cxg.4. human.
Organism-specific databases
CTD	8233.
GeneCards	GC0XP015808.
H-InvDB	HIX0017758.
HGNC	HGNC:23019. ZRSR2.
HPA	HPA047500.
MIM	300028. gene.
neXtProt	NX_Q15696.
PharmGKB	PA162410930.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG304335.
HOGENOM	HOG000049279.
HOVERGEN	HBG054605.
InParanoid	Q15696.
OMA	EDAFIEE.
OrthoDB	EOG4CNQRM.
PhylomeDB	Q15696.
Gene expression databases
ArrayExpress	Q15696.
Bgee	Q15696.
CleanEx	HS_ZRSR2.
Genevestigator	Q15696.
GermOnline	ENSG00000169249. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR009145. U2_small. IPR000571. Znf_CCCH. [Graphical view]
PANTHER	PTHR12620. PTHR12620. 1 hit.
Pfam	PF00642. zf-CCCH. 1 hit. [Graphical view]
PRINTS	PR01848. U2AUXFACTOR.
SMART	SM00360. RRM. 1 hit. SM00356. ZnF_C3H1. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. PS50103. ZF_C3H1. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZRSR2. human.
GenomeRNAi	8233.
NextBio	30981.
SOURCE	Search...

Entry information

Entry name

U2AFM_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.