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Protein

U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2

Gene

ZRSR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri166 – 19429C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri306 – 33328C3H1-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: InterPro
  • pre-mRNA 3'-splice site binding Source: UniProtKB

GO - Biological processi

  • mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: HGNC
  • spliceosomal complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:ZRSR2
Synonyms:U2AF1-RS2, U2AF1L2, U2AF1RS2, URP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:23019. ZRSR2.

Subcellular locationi

GO - Cellular componenti

  • U12-type spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162410930.

Polymorphism and mutation databases

BioMutaiZRSR2.
DMDMi2833266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2PRO_0000082001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491Phosphoserine2 Publications
Modified residuei384 – 3841Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated in the RS domain by SRPK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15696.
PaxDbiQ15696.
PRIDEiQ15696.

PTM databases

PhosphoSiteiQ15696.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ15696.
CleanExiHS_ZRSR2.
ExpressionAtlasiQ15696. baseline and differential.
GenevisibleiQ15696. HS.

Organism-specific databases

HPAiHPA047500.

Interactioni

Subunit structurei

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/U2AF65.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLK2P497603EBI-6657923,EBI-750020
SDCBP2Q9H1903EBI-6657923,EBI-742426
SRPK2P783624EBI-6657923,EBI-593303
SSX2IPQ9Y2D83EBI-6657923,EBI-2212028

Protein-protein interaction databases

BioGridi113865. 38 interactions.
IntActiQ15696. 6 interactions.
STRINGi9606.ENSP00000303015.

Structurei

3D structure databases

ProteinModelPortaliQ15696.
SMRiQ15696. Positions 228-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 304107RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi46 – 494Poly-Glu
Compositional biasi118 – 1236Poly-Glu
Compositional biasi414 – 46956Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Contains 2 C3H1-type zinc fingers.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri166 – 19429C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri306 – 33328C3H1-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG304335.
GeneTreeiENSGT00530000063193.
HOGENOMiHOG000049279.
HOVERGENiHBG054605.
InParanoidiQ15696.
OMAiERMGHHD.
PhylomeDBiQ15696.
TreeFamiTF324447.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR009145. U2_small.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERiPTHR12620. PTHR12620. 1 hit.
PfamiPF00642. zf-CCCH. 1 hit.
[Graphical view]
PRINTSiPR01848. U2AUXFACTOR.
SMARTiSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPEKMTFP EKPSHKKYRA ALKKEKRKKR RQELARLRDS GLSQKEEEED
60 70 80 90 100
TFIEEQQLEE EKLLERERQR LHEEWLLREQ KAQEEFRIKK EKEEAAKKRQ
110 120 130 140 150
EEQERKLKEQ WEEQQRKERE EEEQKRQEKK EKEEALQKML DQAENELENG
160 170 180 190 200
TTWQNPEPPV DFRVMEKDRA NCPFYSKTGA CRFGDRCSRK HNFPTSSPTL
210 220 230 240 250
LIKSMFTTFG MEQCRRDDYD PDASLEYSEE ETYQQFLDFY EDVLPEFKNV
260 270 280 290 300
GKVIQFKVSC NLEPHLRGNV YVQYQSEEEC QAALSLFNGR WYAGRQLQCE
310 320 330 340 350
FCPVTRWKMA ICGLFEIQQC PRGKHCNFLH VFRNPNNEFW EANRDIYLSP
360 370 380 390 400
DRTGSSFGKN SERRERMGHH DDYYSRLRGR RNPSPDHSYK RNGESERKSS
410 420 430 440 450
RHRGKKSHKR TSKSRERHNS RSRGRNRDRS RDRSRGRGSR SRSRSRSRRS
460 470 480
RRSRSQSSSR SRSRGRRRSG NRDRTVQSPK SK
Length:482
Mass (Da):58,045
Last modified:May 1, 1997 - v2
Checksum:i1DACC8A6CA4727A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14172.1.
RefSeqiNP_005080.1. NM_005089.3.
UniGeneiHs.171909.

Genome annotation databases

EnsembliENST00000307771; ENSP00000303015; ENSG00000169249.
GeneIDi8233.
KEGGihsa:8233.
UCSCiuc004cxg.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14172.1.
RefSeqiNP_005080.1. NM_005089.3.
UniGeneiHs.171909.

3D structure databases

ProteinModelPortaliQ15696.
SMRiQ15696. Positions 228-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113865. 38 interactions.
IntActiQ15696. 6 interactions.
STRINGi9606.ENSP00000303015.

PTM databases

PhosphoSiteiQ15696.

Polymorphism and mutation databases

BioMutaiZRSR2.
DMDMi2833266.

Proteomic databases

MaxQBiQ15696.
PaxDbiQ15696.
PRIDEiQ15696.

Protocols and materials databases

DNASUi8233.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307771; ENSP00000303015; ENSG00000169249.
GeneIDi8233.
KEGGihsa:8233.
UCSCiuc004cxg.4. human.

Organism-specific databases

CTDi8233.
GeneCardsiGC0XP015808.
H-InvDBHIX0017758.
HGNCiHGNC:23019. ZRSR2.
HPAiHPA047500.
MIMi300028. gene.
neXtProtiNX_Q15696.
PharmGKBiPA162410930.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG304335.
GeneTreeiENSGT00530000063193.
HOGENOMiHOG000049279.
HOVERGENiHBG054605.
InParanoidiQ15696.
OMAiERMGHHD.
PhylomeDBiQ15696.
TreeFamiTF324447.

Miscellaneous databases

ChiTaRSiZRSR2. human.
GeneWikiiZRSR2.
GenomeRNAii8233.
NextBioi30981.
PROiQ15696.
SOURCEiSearch...

Gene expression databases

BgeeiQ15696.
CleanExiHS_ZRSR2.
ExpressionAtlasiQ15696. baseline and differential.
GenevisibleiQ15696. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR009145. U2_small.
IPR000571. Znf_CCCH.
[Graphical view]
PANTHERiPTHR12620. PTHR12620. 1 hit.
PfamiPF00642. zf-CCCH. 1 hit.
[Graphical view]
PRINTSiPR01848. U2AUXFACTOR.
SMARTiSM00360. RRM. 1 hit.
SM00356. ZnF_C3H1. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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].

Entry informationi

Entry nameiU2AFM_HUMAN
AccessioniPrimary (citable) accession number: Q15696
Secondary accession number(s): Q14D69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 24, 2015
This is version 135 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.