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P26368

- U2AF2_HUMAN

UniProt

P26368 - U2AF2_HUMAN

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Protein

Splicing factor U2AF 65 kDa subunit

Gene

U2AF2

Organism
Homo sapiens (Human)
Status
Reviewed - 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 (PubMed:21536736). Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10.4 Publications

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA 3'-end processing Source: Reactome
  3. mRNA export from nucleus Source: Reactome
  4. mRNA processing Source: ProtInc
  5. mRNA splicing, via spliceosome Source: HGNC
  6. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  7. RNA splicing Source: Reactome
  8. termination of RNA polymerase II transcription Source: Reactome
  9. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor U2AF 65 kDa subunit
Alternative name(s):
U2 auxiliary factor 65 kDa subunit
Short name:
hU2AF(65)
Short name:
hU2AF65
U2 snRNP auxiliary factor large subunit
Gene namesi
Name:U2AF2
Synonyms:U2AF65
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:23156. U2AF2.

Subcellular locationi

GO - Cellular componenti

  1. nuclear speck Source: MGI
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi92 – 921W → A: Decreases affinity for UAF1 by 3 orders of magnitude. 1 Publication
Mutagenesisi96 – 961P → G: Decreases affinity for UAF1 by 2 orders of magnitude. 1 Publication
Mutagenesisi104 – 1041P → G: Decreases affinity for UAF1 by 2 orders of magnitude. 1 Publication
Mutagenesisi387 – 3882EE → RR: Reduces interaction with SF1. 1 Publication
Mutagenesisi391 – 3944DDEE → AAAA: Reduces interaction with SF1.
Mutagenesisi391 – 3944DDEE → RRKK: Reduces interaction with SF1.
Mutagenesisi396 – 3972EE → AA: No effect. 1 Publication
Mutagenesisi396 – 3972EE → GA: Reduces interaction with SF1. 1 Publication
Mutagenesisi396 – 3972EE → KK: Reduces interaction with SF1. 1 Publication
Mutagenesisi454 – 4541F → A: Reduces interaction with SF1. 1 Publication

Organism-specific databases

PharmGKBiPA134908683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 475474Splicing factor U2AF 65 kDa subunitPRO_0000081988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine5 Publications
Modified residuei2 – 21Phosphoserine3 Publications
Modified residuei15 – 1515-hydroxylysine; by JMJD61 Publication
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei276 – 27615-hydroxylysine; by JMJD61 Publication

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.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiP26368.
PaxDbiP26368.
PRIDEiP26368.

PTM databases

PhosphoSiteiP26368.

Miscellaneous databases

PMAP-CutDBP26368.

Expressioni

Gene expression databases

BgeeiP26368.
CleanExiHS_U2AF2.
ExpressionAtlasiP26368. baseline and differential.
GenevestigatoriP26368.

Organism-specific databases

HPAiCAB010910.
HPA041943.
HPA043562.

Interactioni

Subunit structurei

Interacts with U2AF1L4 (By similarity). 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); recruits PRPF19 and the Prp19 complex to the pre-mRNA.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN1P542534EBI-742339,EBI-930964
CHERPQ8IWX82EBI-742339,EBI-2555370
CPSF7Q8N6842EBI-742339,EBI-746909
MUC1P159412EBI-742339,EBI-2804728
PRPF3O433952EBI-742339,EBI-744322
RBM10P981752EBI-742339,EBI-721525
RBM5P527562EBI-742339,EBI-714003
SNRPAP090122EBI-742339,EBI-607085
SNW1Q135735EBI-742339,EBI-632715
SRPK2P783624EBI-742339,EBI-593303
SUGP1Q8IWZ83EBI-742339,EBI-2691671
U2AF1Q010818EBI-742339,EBI-632461

Protein-protein interaction databases

BioGridi116466. 132 interactions.
DIPiDIP-2154N.
IntActiP26368. 49 interactions.
MINTiMINT-1192370.
STRINGi9606.ENSP00000307863.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi104 – 1096Combined sources
Beta strandi150 – 1556Combined sources
Helixi162 – 17514Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi185 – 1917Combined sources
Beta strandi193 – 20412Combined sources
Helixi205 – 2117Combined sources
Helixi212 – 2143Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi261 – 2644Combined sources
Helixi272 – 2809Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi285 – 2928Combined sources
Turni294 – 2963Combined sources
Beta strandi299 – 30911Combined sources
Helixi312 – 3209Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi331 – 3344Combined sources
Beta strandi376 – 3838Combined sources
Helixi386 – 3894Combined sources
Helixi392 – 40615Combined sources
Turni407 – 4093Combined sources
Beta strandi414 – 4163Combined sources
Turni422 – 4243Combined sources
Turni427 – 4304Combined sources
Beta strandi431 – 4355Combined sources
Helixi439 – 44911Combined sources
Beta strandi454 – 4574Combined sources
Beta strandi460 – 4634Combined sources
Helixi466 – 4705Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMTX-ray2.20B85-112[»]
1O0PNMR-A372-475[»]
1OPINMR-A372-475[»]
1U2FNMR-A148-237[»]
2G4BX-ray2.50A148-336[»]
2HZCX-ray1.47A148-229[»]
2M0GNMR-B372-475[»]
2U2FNMR-A258-342[»]
2YH0NMR-A148-342[»]
2YH1NMR-A148-342[»]
3VAFX-ray2.49A/B148-336[»]
3VAGX-ray2.19A/B148-336[»]
3VAHX-ray2.50A/B148-336[»]
3VAIX-ray2.20A/B148-336[»]
3VAJX-ray1.90A/B148-336[»]
3VAKX-ray2.17A/B148-336[»]
3VALX-ray2.50A/B/D/I148-336[»]
3VAMX-ray2.40A/B148-336[»]
4FXWX-ray2.29A/C375-475[»]
ProteinModelPortaliP26368.
SMRiP26368. Positions 148-475.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26368.

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 PRPF191 PublicationAdd
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.
GeneTreeiENSGT00750000117711.
HOGENOMiHOG000180745.
HOVERGENiHBG062169.
InParanoidiP26368.
KOiK12837.
OMAiYARRETR.
OrthoDBiEOG7CNZFZ.
PhylomeDBiP26368.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26368-1) [UniParc]FASTAAdd to Basket

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.

« 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 NATLVSPPST
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):53,501
Last modified:January 23, 2007 - v4
Checksum:i26AD271CD8FC6211
GO
Isoform 2 (identifier: P26368-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     345-348: Missing.

Show »
Length:471
Mass (Da):53,121
Checksum:i3F59A02CD2B03F46
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei345 – 3484Missing in isoform 2. 1 PublicationVSP_035414

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64044 mRNA. Translation: CAA45409.1.
CH471135 Genomic DNA. Translation: EAW72404.1.
BC008740 mRNA. Translation: AAH08740.1.
BC030574 mRNA. Translation: AAH30574.1.
CCDSiCCDS12933.1. [P26368-1]
CCDS46197.1. [P26368-2]
PIRiS20250.
RefSeqiNP_001012496.1. NM_001012478.1. [P26368-2]
NP_009210.1. NM_007279.2. [P26368-1]
UniGeneiHs.528007.

Genome annotation databases

EnsembliENST00000308924; ENSP00000307863; ENSG00000063244. [P26368-1]
ENST00000450554; ENSP00000388475; ENSG00000063244. [P26368-2]
GeneIDi11338.
KEGGihsa:11338.
UCSCiuc002qlt.3. human. [P26368-2]
uc002qlu.3. human. [P26368-1]

Polymorphism databases

DMDMi267188.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64044 mRNA. Translation: CAA45409.1 .
CH471135 Genomic DNA. Translation: EAW72404.1 .
BC008740 mRNA. Translation: AAH08740.1 .
BC030574 mRNA. Translation: AAH30574.1 .
CCDSi CCDS12933.1. [P26368-1 ]
CCDS46197.1. [P26368-2 ]
PIRi S20250.
RefSeqi NP_001012496.1. NM_001012478.1. [P26368-2 ]
NP_009210.1. NM_007279.2. [P26368-1 ]
UniGenei Hs.528007.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JMT X-ray 2.20 B 85-112 [» ]
1O0P NMR - A 372-475 [» ]
1OPI NMR - A 372-475 [» ]
1U2F NMR - A 148-237 [» ]
2G4B X-ray 2.50 A 148-336 [» ]
2HZC X-ray 1.47 A 148-229 [» ]
2M0G NMR - B 372-475 [» ]
2U2F NMR - A 258-342 [» ]
2YH0 NMR - A 148-342 [» ]
2YH1 NMR - A 148-342 [» ]
3VAF X-ray 2.49 A/B 148-336 [» ]
3VAG X-ray 2.19 A/B 148-336 [» ]
3VAH X-ray 2.50 A/B 148-336 [» ]
3VAI X-ray 2.20 A/B 148-336 [» ]
3VAJ X-ray 1.90 A/B 148-336 [» ]
3VAK X-ray 2.17 A/B 148-336 [» ]
3VAL X-ray 2.50 A/B/D/I 148-336 [» ]
3VAM X-ray 2.40 A/B 148-336 [» ]
4FXW X-ray 2.29 A/C 375-475 [» ]
ProteinModelPortali P26368.
SMRi P26368. Positions 148-475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116466. 132 interactions.
DIPi DIP-2154N.
IntActi P26368. 49 interactions.
MINTi MINT-1192370.
STRINGi 9606.ENSP00000307863.

PTM databases

PhosphoSitei P26368.

Polymorphism databases

DMDMi 267188.

Proteomic databases

MaxQBi P26368.
PaxDbi P26368.
PRIDEi P26368.

Protocols and materials databases

DNASUi 11338.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308924 ; ENSP00000307863 ; ENSG00000063244 . [P26368-1 ]
ENST00000450554 ; ENSP00000388475 ; ENSG00000063244 . [P26368-2 ]
GeneIDi 11338.
KEGGi hsa:11338.
UCSCi uc002qlt.3. human. [P26368-2 ]
uc002qlu.3. human. [P26368-1 ]

Organism-specific databases

CTDi 11338.
GeneCardsi GC19P056165.
HGNCi HGNC:23156. U2AF2.
HPAi CAB010910.
HPA041943.
HPA043562.
MIMi 191318. gene.
neXtProti NX_P26368.
PharmGKBi PA134908683.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298004.
GeneTreei ENSGT00750000117711.
HOGENOMi HOG000180745.
HOVERGENi HBG062169.
InParanoidi P26368.
KOi K12837.
OMAi YARRETR.
OrthoDBi EOG7CNZFZ.
PhylomeDBi P26368.
TreeFami TF314111.

Enzyme and pathway databases

Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi U2AF2. human.
EvolutionaryTracei P26368.
GeneWikii U2AF2.
GenomeRNAii 11338.
NextBioi 43079.
PMAP-CutDB P26368.
PROi P26368.
SOURCEi Search...

Gene expression databases

Bgeei P26368.
CleanExi HS_U2AF2.
ExpressionAtlasi P26368. baseline and differential.
Genevestigatori P26368.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006529. U2AF_lg.
[Graphical view ]
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
TIGRFAMsi TIGR01642. U2AF_lg. 1 hit.
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and domain structure of the mammalian splicing factor U2AF."
    Zamore P.D., Patton J.G., Green M.R.
    Nature 355:609-614(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. 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] (ISOFORM 2).
    Tissue: Lymph and Skin.
  4. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-9; 196-203; 277-286 AND 463-471, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  5. "Large-scale proteomic analysis of the human spliceosome."
    Rappsilber J., Ryder U., Lamond A.I., Mann M.
    Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 261-286, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
  6. "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: INTERACTION WITH ZRSR2.
  7. "Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
    Zhang W.-J., Wu J.Y.
    Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCAF11.
  8. "Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly."
    Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J.
    EMBO J. 18:4549-4559(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SF1.
  9. "Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
    Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
    J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "U2AF-homology motif interactions are required for alternative splicing regulation by SPF45."
    Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., Sattler M.
    Nat. Struct. Mol. Biol. 14:620-629(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM17.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing."
    Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: FUNCTION, HYDROXYLATION AT LYS-15 AND LYS-276.
  18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing."
    Chen Y., Zhang L., Jones K.A.
    Genes Dev. 25:701-716(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNW1.
  21. "The RNA polymerase II C-terminal domain promotes splicing activation through recruitment of a U2AF65-Prp19 complex."
    David C.J., Boyne A.R., Millhouse S.R., Manley J.L.
    Genes Dev. 25:972-983(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POLR2A AND PRPF19.
  22. "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-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65))."
    Ito T., Muto Y., Green M.R., Yokoyama S.
    EMBO J. 18:4523-4534(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 148-237.
  26. "Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP."
    Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M.
    Mol. Cell 11:965-976(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 372-475 IN COMPLEX WITH SF1, MUTAGENESIS OF 387-GLU-GLU-388; 391-ASP--GLU-393; 396-GLU-GLU-397 AND PHE-454.
  27. "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 90-112 IN COMPLEX WITH U2AF1, MUTAGENESIS OF TRP-92; PRO-96 AND PRO-104.

Entry informationi

Entry nameiU2AF2_HUMAN
AccessioniPrimary (citable) accession number: P26368
Secondary accession number(s): Q96HC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 170 of the entry and version 4 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3