ID SF3A1_HUMAN Reviewed; 793 AA.
AC Q15459;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 01-MAY-2013, entry version 139.
DE RecName: Full=Splicing factor 3A subunit 1;
DE AltName: Full=SF3a120;
DE AltName: Full=Spliceosome-associated protein 114;
DE Short=SAP 114;
GN Name=SF3A1; Synonyms=SAP114;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7489498;
RA Kraemer A., Mulhauser F., Wersig C., Groning K., Bilbe G.;
RT "Mammalian splicing factor SF3a120 represents a new member of the SURP
RT family of proteins and is homologous to the essential splicing factor
RT PRP21p of Saccharomyces cerevisiae.";
RL RNA 1:260-272(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION OF THE SPLICEOSOME.
RX PubMed=10882114; DOI=10.1016/S1097-2765(00)80318-4;
RA Das R., Zhou Z., Reed R.;
RT "Functional association of U2 snRNP with the ATP-independent
RT spliceosomal complex E.";
RL Mol. Cell 5:779-787(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-456 AND TYR-759, AND
RP MASS SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-359, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-413 AND
RP SER-451, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329; SER-359
RP AND SER-451, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-359; SER-413
RP AND SER-451, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329 AND
RP SER-359, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP STRUCTURE BY NMR OF 704-789.
RG Structural genomics consortium (SGC);
RT "Solution structure of a human ubiquitin-like domain in SF3A1.";
RL Submitted (JUN-2005) to the PDB data bank.
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-511.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Subunit of the splicing factor SF3A required for 'A'
CC complex assembly formed by the stable binding of U2 snRNP to the
CC branchpoint sequence (BPS) in pre-mRNA. Sequence independent
CC binding of SF3A/SF3B complex upstream of the branch site is
CC essential, it may anchor U2 snRNP to the pre-mRNA. May also be
CC involved in the assembly of the 'E' complex.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of
CC splicing factor SF3A which is composed of three subunits;
CC SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the
CC splicing factor SF3B and a 12S RNA unit to form the U2 small
CC nuclear ribonucleoproteins complex (U2 snRNP). Interacts with
CC SF3A3.
CC -!- INTERACTION:
CC Q9BXW4:MAP1LC3C; NbExp=3; IntAct=EBI-1054743, EBI-2603996;
CC P08047:SP1; NbExp=2; IntAct=EBI-1054743, EBI-298336;
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Contains 2 SURP motif repeats.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; X85237; CAA59494.1; -; mRNA.
DR EMBL; CR456575; CAG30461.1; -; mRNA.
DR EMBL; AC004997; AAC23435.1; -; Genomic_DNA.
DR EMBL; BC001976; AAH01976.1; -; mRNA.
DR EMBL; BC007684; AAH07684.1; -; mRNA.
DR IPI; IPI00017451; -.
DR PIR; S60735; S60735.
DR RefSeq; NP_001005409.1; NM_001005409.1.
DR RefSeq; NP_005868.1; NM_005877.4.
DR UniGene; Hs.406277; -.
DR UniGene; Hs.505597; -.
DR PDB; 1ZKH; NMR; -; A=704-789.
DR PDB; 2DT6; NMR; -; A=48-110.
DR PDB; 2DT7; NMR; -; B=134-217.
DR PDBsum; 1ZKH; -.
DR PDBsum; 2DT6; -.
DR PDBsum; 2DT7; -.
DR ProteinModelPortal; Q15459; -.
DR DIP; DIP-29164N; -.
DR IntAct; Q15459; 12.
DR MINT; MINT-144269; -.
DR STRING; 9606.ENSP00000215793; -.
DR PhosphoSite; Q15459; -.
DR DMDM; 2498882; -.
DR PaxDb; Q15459; -.
DR PeptideAtlas; Q15459; -.
DR PRIDE; Q15459; -.
DR DNASU; 10291; -.
DR Ensembl; ENST00000215793; ENSP00000215793; ENSG00000099995.
DR GeneID; 10291; -.
DR KEGG; hsa:10291; -.
DR UCSC; uc003ahl.3; human.
DR CTD; 10291; -.
DR GeneCards; GC22M030727; -.
DR HGNC; HGNC:10765; SF3A1.
DR HPA; HPA000690; -.
DR HPA; HPA030083; -.
DR MIM; 605595; gene.
DR neXtProt; NX_Q15459; -.
DR PharmGKB; PA35683; -.
DR eggNOG; NOG300902; -.
DR HOGENOM; HOG000238941; -.
DR HOVERGEN; HBG059993; -.
DR InParanoid; Q15459; -.
DR KO; K12825; -.
DR OMA; GMPPAKQ; -.
DR OrthoDB; EOG4N5VWN; -.
DR PhylomeDB; Q15459; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SF3A1; human.
DR EvolutionaryTrace; Q15459; -.
DR GenomeRNAi; 10291; -.
DR NextBio; 39000; -.
DR PMAP-CutDB; Q15459; -.
DR ArrayExpress; Q15459; -.
DR Bgee; Q15459; -.
DR CleanEx; HS_SF3A1; -.
DR Genevestigator; Q15459; -.
DR GermOnline; ENSG00000099995; Homo sapiens.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC.
DR InterPro; IPR022030; PRP21-like.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR000626; Ubiquitin.
DR InterPro; IPR019955; Ubiquitin_supergroup.
DR Pfam; PF12230; PRP21_like_P; 1.
DR Pfam; PF01805; Surp; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00648; SWAP; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF109905; SSF109905; 2.
DR PROSITE; PS50128; SURP; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat; Spliceosome.
FT CHAIN 1 793 Splicing factor 3A subunit 1.
FT /FTId=PRO_0000114917.
FT REPEAT 52 94 SURP motif 1.
FT REPEAT 166 208 SURP motif 2.
FT DOMAIN 707 793 Ubiquitin-like.
FT COMPBIAS 10 16 Poly-Pro.
FT COMPBIAS 118 122 Poly-Gln.
FT COMPBIAS 260 267 Poly-Glu.
FT COMPBIAS 369 372 Poly-Pro.
FT COMPBIAS 557 560 Poly-Pro.
FT COMPBIAS 672 675 Poly-Pro.
FT MOD_RES 55 55 N6-acetyllysine.
FT MOD_RES 320 320 Phosphoserine.
FT MOD_RES 329 329 Phosphoserine.
FT MOD_RES 359 359 Phosphoserine.
FT MOD_RES 413 413 Phosphoserine.
FT MOD_RES 451 451 Phosphoserine.
FT MOD_RES 456 456 Phosphotyrosine.
FT MOD_RES 759 759 Phosphotyrosine.
FT VARIANT 511 511 R -> W (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036290.
FT HELIX 48 63
FT HELIX 66 74
FT HELIX 79 84
FT HELIX 91 103
FT HELIX 161 177
FT HELIX 179 188
FT TURN 189 191
FT HELIX 193 198
FT HELIX 204 215
FT STRAND 705 710
FT STRAND 715 721
FT STRAND 726 731
FT HELIX 737 747
FT TURN 752 754
FT STRAND 755 759
FT STRAND 762 764
FT HELIX 770 773
FT STRAND 779 786
SQ SEQUENCE 793 AA; 88886 MW; 7259F1EC4577305C CRC64;
MPAGPVQAVP PPPPVPTEPK QPTEEEASSK EDSAPSKPVV GIIYPPPEVR NIVDKTASFV
ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ
QQTTQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ
FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL
DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT
PEELGARILI QERYEKFGES EEVEMEVESD EEDDKQEKAE EPPSQLDQDT QVQDMDEGSD
DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP LPPAPAPDEY LVSPITGEKI
PASKMQEHMR IGLLDPRWLE QRDRSIREKQ SDDEVYAPGL DIESSLKQLA ERRTDIFGVE
ETAIGKKIGE EEIQKPEEKV TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD
TKEKIGPSKP NEIPQQPPPP SSATNIPSSA PPITSVPRPP TMPPPVRTTV VSAVPVMPRP
PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT AFVPAPPVAP
VPAPAPMPPV HPPPPMEDEP TSKKLKTEDS LMPEEEFLRR NKGPVSIKVQ VPNMQDKTEW
KLNGQVLVFT LPLTDQVSVI KVKIHEATGM PAGKQKLQYE GIFIKDSNSL AYYNMANGAV
IHLALKERGG RKK
//
