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UniProtKB/Swiss-Prot entry Q15459


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

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Entry information
Entry name SF3A1_HUMAN
Primary accession number Q15459
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 94)
Name and origin of the protein
Protein name Splicing factor 3 subunit 1
Synonyms Spliceosome-associated protein 114
SAP 114
SF3a120
Gene name
Name: SF3A1
Synonyms: SAP114
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].
PubMed=7489498 [NCBI, ExPASy, EBI, Israel, Japan]
Kraemer A., Mulhauser F., Wersig C., Groning K., Bilbe G.;
"Mammalian splicing factor SF3a120 represents a new member of the SURP family of proteins and is homologous to the essential splicing factor PRP21p of Saccharomyces cerevisiae.";
RNA 1:260-272(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Lymph;
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).
[5]
CHARACTERIZATION OF THE SPLICEOSOME.
DOI=10.1016/S1097-2765(00)80318-4; PubMed=10882114 [NCBI, ExPASy, EBI, Israel, Japan]
Das R., Zhou Z., Reed R.;
"Functional association of U2 snRNP with the ATP-independent spliceosomal complex E.";
Mol. Cell 5:779-787(2000).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.";
RNA 8:426-439(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-456 AND TYR-759, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-359, 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-320; SER-329 AND SER-359, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-413 AND SER-451, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[14]
STRUCTURE BY NMR OF 704-789.
Structural genomics consortium (SGC);
"Solution structure of a human ubiquitin-like domain in SF3A1.";
Submitted (JUN-2005) to the PDB data bank.
[15]
VARIANT [LARGE SCALE ANALYSIS] TRP-511.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.
  • SUBUNIT: Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A3.
  • INTERACTION:
    O94817:ATG12; NbExp=1; IntAct=EBI-1054743, EBI-746742;
    P08047:SP1; NbExp=1; IntAct=EBI-1054743, EBI-298336;
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • TISSUE SPECIFICITY: Ubiquitously expressed.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • SIMILARITY: Contains 2 SURP motif repeats.
  • SIMILARITY: Contains 1 ubiquitin-like domain.
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
X85237; CAA59494.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456575; CAG30461.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004997; AAC23435.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001976; AAH01976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007684; AAH07684.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S60735; S60735.
RefSeq NP_001005409.1; -.
NP_005868.1; -.
UniGene Hs.406277
3D structure databases
PDB
1ZKH; NMR; -; A=704-789.[ExPASy / RCSB / EBI]
2DT6; NMR; -; A=48-110.[ExPASy / RCSB / EBI]
2DT7; NMR; -; B=134-217.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ZKH; -.
2DT6; -.
2DT7; -.
SMR Q15459; 134-217, 687-790.
ModBase Q15459.
Protein-protein interaction databases
DIP DIP:29164N; -.
IntAct Q15459; 11.
PTM databases
PhosphoSite Q15459; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_71; Gene Expression.
Organism-specific databases
GeneCards GC22M029054; -.
H-InvDB HIX0016367; -.
HGNC HGNC:10765; SF3A1.
GenAtlas SF3A1.
HPA HPA000690; -.
MIM 605595; gene. [NCBI / EBI]
PharmGKB PA35683; -.
GeneCards Q15459.
Gene expression databases
ArrayExpress Q15459; -.
CleanEx HS_SF3A1; -.
GermOnline ENSG00000099995; Homo sapiens.
Ontologies
GO
GO:0005684; Cellular component: U2-dependent spliceosome (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0000389; Biological process: nuclear mRNA 3'-splice site recognition (traceable author statement from HGNC).
GO:0006464; Biological process: protein modification process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000061; Surp.
IPR000626; Ubiquitin.
Graphical view of domain structure.
Pfam PF01805; Surp; 2.
PF00240; ubiquitin; 1.
Pfam graphical view of domain structure.
PRINTS PR00348; UBIQUITIN.
SMART SM00648; SWAP; 2.
SM00213; UBQ; 1.
SMART graphical view of domain structure.
PROSITE PS50128; SURP; 2.
PS50053; UBIQUITIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q15459; -.
Proteomics databases
PRIDE Q15459; -.
Genome annotation databases
Ensembl ENSG00000099995; Homo sapiens. [Contig view]
GeneID 10291; -.
KEGG hsa:10291; -.
Phylogenomic databases
HOGENOM Q15459; -.
HOVERGEN Q15459; -.
Other
NextBio 39000; -.
SOURCE SF3A1; Homo sapiens.
ProtoNet Q15459.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Repeat; Spliceosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   793  793     Splicing factor 3 subunit 1. PRO_0000114917
REPEAT   52    94  43     SURP motif 1. 
REPEAT   166   208  43     SURP motif 2. 
DOMAIN   707   793  87     Ubiquitin-like. 
COMPBIAS   10    16  7     Poly-Pro. 
COMPBIAS   118   122  5     Poly-Gln. 
COMPBIAS   260   267  8     Poly-Glu. 
COMPBIAS   369   372  4     Poly-Pro. 
COMPBIAS   557   560  4     Poly-Pro. 
COMPBIAS   672   675  4     Poly-Pro. 
MOD_RES   124   124        Phosphothreonine. 
MOD_RES   320   320        Phosphoserine. 
MOD_RES   329   329        Phosphoserine. 
MOD_RES   359   359        Phosphoserine. 
MOD_RES   413   413        Phosphoserine. 
MOD_RES   451   451        Phosphoserine. 
MOD_RES   456   456        Phosphotyrosine. 
MOD_RES   759   759        Phosphotyrosine. 
VARIANT   511   511  1     R -> W (in a colorectal cancer sample; somatic mutation). VAR_036290 
HELIX   48    63  16      
HELIX   66    74  9      
HELIX   79    84  6      
HELIX   91   103  13      
STRAND   705   710  6      
STRAND   715   721  7      
STRAND   726   731  6      
HELIX   737   747  11      
TURN   752   754  3      
STRAND   755   759  5      
STRAND   762   764  3      
HELIX   770   773  4      
STRAND   779   786  8      
Sequence information
Length: 793 AA [This is the length of the unprocessed precursor] Molecular weight: 88886 Da [This is the MW of the unprocessed precursor] CRC64: 7259F1EC4577305C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPAGPVQAVP PPPPVPTEPK QPTEEEASSK EDSAPSKPVV GIIYPPPEVR NIVDKTASFV 

        70         80         90        100        110        120 
ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ 

       130        140        150        160        170        180 
QQTTQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ 

       190        200        210        220        230        240 
FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL 

       250        260        270        280        290        300 
DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT 

       310        320        330        340        350        360 
PEELGARILI QERYEKFGES EEVEMEVESD EEDDKQEKAE EPPSQLDQDT QVQDMDEGSD 

       370        380        390        400        410        420 
DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP LPPAPAPDEY LVSPITGEKI 

       430        440        450        460        470        480 
PASKMQEHMR IGLLDPRWLE QRDRSIREKQ SDDEVYAPGL DIESSLKQLA ERRTDIFGVE 

       490        500        510        520        530        540 
ETAIGKKIGE EEIQKPEEKV TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD 

       550        560        570        580        590        600 
TKEKIGPSKP NEIPQQPPPP SSATNIPSSA PPITSVPRPP TMPPPVRTTV VSAVPVMPRP 

       610        620        630        640        650        660 
PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT AFVPAPPVAP 

       670        680        690        700        710        720 
VPAPAPMPPV HPPPPMEDEP TSKKLKTEDS LMPEEEFLRR NKGPVSIKVQ VPNMQDKTEW 

       730        740        750        760        770        780 
KLNGQVLVFT LPLTDQVSVI KVKIHEATGM PAGKQKLQYE GIFIKDSNSL AYYNMANGAV 

       790 
IHLALKERGG RKK 

Q15459 in FASTA format

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