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Protein

Splicing factor U2AF 65 kDa subunit

Gene

U2af2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for the splicing of pre-mRNA. By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene.By similarity

GO - Molecular functioni

  1. C2H2 zinc finger domain binding Source: UniProtKB
  2. enzyme binding Source: MGI
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  3. positive regulation of RNA splicing Source: UniProtKB
  4. RNA splicing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_291263. mRNA 3'-end processing.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_321120. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_351784. Cleavage of Growing Transcript in the Termination Region.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor U2AF 65 kDa subunit
Alternative name(s):
U2 auxiliary factor 65 kDa subunit
U2 snRNP auxiliary factor large subunit
Gene namesi
Name:U2af2
Synonyms:U2af65
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98886. U2af2.

Subcellular locationi

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleoplasm Source: MGI
  3. Prp19 complex Source: Ensembl
  4. spliceosomal complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 475474Splicing factor U2AF 65 kDa subunitPRO_0000081989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei15 – 1515-hydroxylysine; by JMJD6By similarity
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei276 – 27615-hydroxylysine; by JMJD6By similarity

Post-translational modificationi

Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiP26369.
PaxDbiP26369.
PRIDEiP26369.

PTM databases

PhosphoSiteiP26369.

Miscellaneous databases

PMAP-CutDBP26369.

Expressioni

Gene expression databases

BgeeiP26369.
ExpressionAtlasiP26369. baseline and differential.
GenevestigatoriP26369.

Interactioni

Subunit structurei

Heterodimer with U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1. Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17. Interacts with PRPF19; the interaction is direct. Interacts with POLR2A (via the C-terminal domain); Interacts with PRPF19; the interaction is direct. Interacts with POLR2A (via the C-terminal domain); recruits PRPF19 and the Prp19 complex to the pre-mRNA (By similarity). Interacts with U2AF1L4.By similarity1 Publication

Protein-protein interaction databases

BioGridi204400. 1 interaction.
IntActiP26369. 3 interactions.
MINTiMINT-4139054.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi376 – 3838Combined sources
Helixi386 – 3883Combined sources
Beta strandi389 – 3913Combined sources
Helixi392 – 40716Combined sources
Beta strandi412 – 4165Combined sources
Turni427 – 4304Combined sources
Beta strandi431 – 4388Combined sources
Helixi439 – 44911Combined sources
Beta strandi454 – 4574Combined sources
Beta strandi460 – 4645Combined sources
Helixi466 – 4705Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M52NMR-A371-475[»]
3V4MX-ray1.80A/B372-475[»]
4RU2X-ray2.20B/D/F/H/J/L/N/P/R85-112[»]
ProteinModelPortaliP26369.
SMRiP26369. Positions 148-342, 371-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini149 – 23183RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini259 – 33779RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini385 – 46682RRM 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9392Required for interaction with PRPF19By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 6236Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG298004.
GeneTreeiENSGT00780000122028.
HOGENOMiHOG000180745.
HOVERGENiHBG062169.
InParanoidiP26369.
KOiK12837.
OMAiIPRPMDG.
OrthoDBiEOG7CNZFZ.
PhylomeDBiP26369.
TreeFamiTF314111.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006529. U2AF_lg.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01642. U2AF_lg. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD
60 70 80 90 100
QRSASRDRRR RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE
110 120 130 140 150
HITPMQYKAM QAAGQIPATA LLPTMTPDGL AVTPTPVPVV GSQMTRQARR
160 170 180 190 200
LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ APGNPVLAVQ INQDKNFAFL
210 220 230 240 250
EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE NPSVYVPGVV
260 270 280 290 300
STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK
310 320 330 340 350
GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSLPST
360 370 380 390 400
INQTPVTLQV PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE
410 420 430 440 450
DVRDECSKYG LVKSIEIPRP VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT
460 470
GRKFANRVVV TKYCDPDSYH RRDFW
Length:475
Mass (Da):53,517
Last modified:January 23, 2007 - v3
Checksum:i2D81375CD8FC7251
GO

Sequence cautioni

The sequence CAA45875.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64587 mRNA. Translation: CAA45874.1.
X64587 mRNA. Translation: CAA45875.1. Different initiation.
AK078496 mRNA. Translation: BAC37309.1.
CCDSiCCDS57476.1.
PIRiS22646.
RefSeqiNP_001192160.1. NM_001205231.1.
UniGeneiMm.360389.

Genome annotation databases

EnsembliENSMUST00000005041; ENSMUSP00000005041; ENSMUSG00000030435.
GeneIDi22185.
KEGGimmu:22185.
UCSCiuc009ezu.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64587 mRNA. Translation: CAA45874.1.
X64587 mRNA. Translation: CAA45875.1. Different initiation.
AK078496 mRNA. Translation: BAC37309.1.
CCDSiCCDS57476.1.
PIRiS22646.
RefSeqiNP_001192160.1. NM_001205231.1.
UniGeneiMm.360389.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M52NMR-A371-475[»]
3V4MX-ray1.80A/B372-475[»]
4RU2X-ray2.20B/D/F/H/J/L/N/P/R85-112[»]
ProteinModelPortaliP26369.
SMRiP26369. Positions 148-342, 371-475.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204400. 1 interaction.
IntActiP26369. 3 interactions.
MINTiMINT-4139054.

PTM databases

PhosphoSiteiP26369.

Proteomic databases

MaxQBiP26369.
PaxDbiP26369.
PRIDEiP26369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005041; ENSMUSP00000005041; ENSMUSG00000030435.
GeneIDi22185.
KEGGimmu:22185.
UCSCiuc009ezu.3. mouse.

Organism-specific databases

CTDi11338.
MGIiMGI:98886. U2af2.

Phylogenomic databases

eggNOGiNOG298004.
GeneTreeiENSGT00780000122028.
HOGENOMiHOG000180745.
HOVERGENiHBG062169.
InParanoidiP26369.
KOiK12837.
OMAiIPRPMDG.
OrthoDBiEOG7CNZFZ.
PhylomeDBiP26369.
TreeFamiTF314111.

Enzyme and pathway databases

ReactomeiREACT_291263. mRNA 3'-end processing.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_321120. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_351784. Cleavage of Growing Transcript in the Termination Region.

Miscellaneous databases

NextBioi302149.
PMAP-CutDBP26369.
PROiP26369.
SOURCEiSearch...

Gene expression databases

BgeeiP26369.
ExpressionAtlasiP26369. baseline and differential.
GenevestigatoriP26369.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006529. U2AF_lg.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01642. U2AF_lg. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the murine homologue of the human splicing factor U2AF65."
    Sailer A., Macdonald N.J., Weissmann C.
    Nucleic Acids Res. 20:2374-2374(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SL/AM.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. "Auxiliary splice factor U2AF26 and transcription factor Gfi1 cooperate directly in regulating CD45 alternative splicing."
    Heyd F., ten Dam G., Moeroey T.
    Nat. Immunol. 7:859-867(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH U2AF1L4.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiU2AF2_MOUSE
AccessioniPrimary (citable) accession number: P26369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.