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UniProtKB/Swiss-Prot entry P26368


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name U2AF2_HUMAN
Primary accession number P26368
Secondary accession number Q96HC5
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 105)
Name and origin of the protein
Protein name Splicing factor U2AF 65 kDa subunit
Synonyms U2 auxiliary factor 65 kDa subunit
hU2AF65
hU2AF(65)
U2 snRNP auxiliary factor large subunit
Gene name
Name: U2AF2
Synonyms: U2AF65
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1038/355609a0; PubMed=1538748 [NCBI, ExPASy, EBI, Israel, Japan]
Zamore P.D., Patton J.G., Green M.R.;
"Cloning and domain structure of the mammalian splicing factor U2AF.";
Nature 355:609-614(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-9; 196-203; 277-286 AND 463-471, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (NOV-2006) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 261-286, MASS SPECTROMETRY, AND INTERACTION WITH THE SPLICEOSOME.
DOI=10.1101/gr.473902; PubMed=12176931 [NCBI, ExPASy, EBI, Israel, Japan]
Rappsilber J., Ryder U., Lamond A.I., Mann M.;
"Large-scale proteomic analysis of the human spliceosome.";
Genome Res. 12:1231-1245(2002).
[6]
INTERACTION WITH SFRS2IP.
PubMed=9447963 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang W.-J., Wu J.Y.;
"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing.";
Mol. Cell. Biol. 18:676-684(1998).
[7]
INTERACTION WITH SF1.
DOI=10.1093/emboj/18.16.4549; PubMed=10449420 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J.;
"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly.";
EMBO J. 18:4549-4559(1999).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
TISSUE=Hepatocyte;
DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.;
"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.";
Proteomics 5:3589-3599(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-53; SER-55 AND SER-79, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
STRUCTURE BY NMR OF 148-237.
DOI=10.1093/emboj/18.16.4523; PubMed=10449418 [NCBI, ExPASy, EBI, Israel, Japan]
Ito T., Muto Y., Green M.R., Yokoyama S.;
"Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65)).";
EMBO J. 18:4523-4534(1999).
[15]
STRUCTURE BY NMR OF 372-475 IN COMPLEX WITH SF1, AND MUTAGENESIS OF 387-GLU-GLU-388; 391-ASP--GLU-393; 396-GLU-GLU-397 AND PHE-454.
DOI=10.1016/S1097-2765(03)00115-1; PubMed=12718882 [NCBI, ExPASy, EBI, Israel, Japan]
Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M.;
"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP.";
Mol. Cell 11:965-976(2003).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 90-112 IN COMPLEX WITH U2AF1, AND MUTAGENESIS OF TRP-92; PRO-96 AND PRO-104.
DOI=10.1016/S0092-8674(01)00480-9; PubMed=11551507 [NCBI, ExPASy, EBI, Israel, Japan]
Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.;
"A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer.";
Cell 106:595-605(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X64044; CAA45409.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471135; EAW72404.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008740; AAH08740.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030574; AAH30574.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S20250; S20250.
RefSeq NP_001012496.1; -.
NP_009210.1; -.
UniGene Hs.528007
3D structure databases
PDB
1JMT; X-ray; 2.20 A; B=85-112.[ExPASy / RCSB / EBI]
1O0P; NMR; -; A=372-475.[ExPASy / RCSB / EBI]
1OPI; NMR; -; A=372-475.[ExPASy / RCSB / EBI]
1U2F; NMR; -; A=148-237.[ExPASy / RCSB / EBI]
2G4B; X-ray; 2.50 A; A=148-336.[ExPASy / RCSB / EBI]
2HZC; X-ray; 1.47 A; A=148-229.[ExPASy / RCSB / EBI]
2U2F; NMR; -; A=258-342.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JMT; -.
1O0P; -.
1OPI; -.
1U2F; -.
2G4B; -.
2HZC; -.
2U2F; -.
ModBase P26368.
Protein-protein interaction databases
DIP DIP:2154N; -.
PTM databases
PhosphoSite P26368; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_1788; Transcription.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.
Organism-specific databases
HGNC HGNC:23156; U2AF2.
GenAtlas U2AF2.
HPA CAB010910; -.
MIM 191318; gene. [NCBI / EBI]
PharmGKB PA134908683; -.
GeneCards P26368.
Gene expression databases
ArrayExpress P26368; -.
CleanEx HS_U2AF2; -.
GermOnline ENSG00000063244; Homo sapiens.
Ontologies
GO
GO:0005681; Cellular component: spliceosome (inferred from direct assay from HGNC).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred by curator from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
IPR006529; U2AF_lg.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
Pfam PF00076; RRM_1; 3.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 3.
SMART graphical view of domain structure.
TIGRFAMs TIGR01642; U2AF_lg; 1.
PROSITE PS50102; RRM; 3.
PROSITE graphical view of domain structure (profiles).
BLOCKS P26368.
ProtoNet P26368.
Genome annotation databases
Ensembl ENSG00000063244; Homo sapiens. [Contig view]
GeneID 11338; -.
KEGG son:SO_3453; -.
Phylogenomic databases
HOVERGEN P26368; -.
Other
NextBio 43079; -.
SOURCE U2AF2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding; Spliceosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   475  474     Splicing factor U2AF 65 kDa subunit. PRO_0000081988
DOMAIN   149   231  83     RRM 1. 
DOMAIN   259   337  79     RRM 2. 
DOMAIN   385   466  82     RRM 3. 
COMPBIAS   27    62  36     Arg/Ser-rich (RS domain). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   2     2        Phosphoserine. 
MOD_RES   53    53        Phosphoserine. 
MOD_RES   55    55        Phosphoserine. 
MOD_RES   79    79        Phosphoserine. 
VAR_SEQ   345   348        Missing (in isoform 2). VSP_035414
MUTAGEN   92    92        W->A: Decreases affinity for UAF1 by 3 orders of magnitude. 
MUTAGEN   96    96        P->G: Decreases affinity for UAF1 by 2 orders of magnitude. 
MUTAGEN   104   104        P->G: Decreases affinity for UAF1 by 2 orders of magnitude. 
MUTAGEN   387   388        EE->RR: Reduces interaction with SF1. 
MUTAGEN   391   394        DDEE->AAAA: Reduces interaction with SF1. 
MUTAGEN   391   394        DDEE->RRKK: Reduces interaction with SF1. 
MUTAGEN   396   397        EE->AA: No effect. 
MUTAGEN   396   397        EE->GA: Reduces interaction with SF1. 
MUTAGEN   396   397        EE->KK: Reduces interaction with SF1. 
MUTAGEN   454   454        F->A: Reduces interaction with SF1. 
HELIX   104   109  6      
STRAND   150   155  6      
HELIX   162   175  14      
STRAND   180   183  4      
STRAND   185   191  7      
STRAND   193   204  12      
HELIX   205   211  7      
HELIX   212   214  3      
STRAND   225   227  3      
TURN   236   259  24      
STRAND   261   264  4      
HELIX   272   280  9      
STRAND   285   292  8      
TURN   294   296  3      
STRAND   298   309  12      
HELIX   312   320  9      
STRAND   331   334  4      
STRAND   376   383  8      
TURN   386   390  5      
HELIX   392   406  15      
TURN   407   409  3      
STRAND   412   416  5      
STRAND   421   425  5      
STRAND   430   437  8      
HELIX   439   449  11      
STRAND   454   457  4      
STRAND   460   464  5      
HELIX   466   470  5      
Sequence information
Length: 475 AA [This is the length of the unprocessed precursor] Molecular weight: 53501 Da [This is the MW of the unprocessed precursor] CRC64: 26AD271CD8FC6211 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR 

        70         80         90        100        110        120 
RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA 

       130        140        150        160        170        180 
LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ 

       190        200        210        220        230        240 
APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE 

       250        260        270        280        290        300 
NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK 

       310        320        330        340        350        360 
GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSPPST INQTPVTLQV 

       370        380        390        400        410        420 
PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP 

       430        440        450        460        470 
VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW 

P26368 in FASTA format

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