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Database: UniProt
Entry: Q15459
LinkDB: Q15459
Original site: Q15459 
ID   SF3A1_HUMAN             Reviewed;         793 AA.
AC   Q15459; E9PAW1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   26-NOV-2014, entry version 156.
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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 IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329; SER-359
RP   AND SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-359; SER-413
RP   AND SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329 AND
RP   SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   [18]
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   [19]
RP   STRUCTURE BY NMR OF 48-110 AND 134-217 IN COMPLEX WITH SF3A3, SUBUNIT,
RP   SURP MOTIFS, AND MUTAGENESIS OF GLU-48; LYS-55; PHE-162 AND LEU-169.
RX   PubMed=17098193; DOI=10.1016/j.str.2006.09.009;
RA   Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P.,
RA   Muto Y., Yokoyama S.;
RT   "Solution structures of the SURP domains and the subunit-assembly
RT   mechanism within the splicing factor SF3a complex in 17S U2 snRNP.";
RL   Structure 14:1677-1689(2006).
RN   [20]
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. {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17098193}.
CC   -!- INTERACTION:
CC       Q9BXW4:MAP1LC3C; NbExp=3; IntAct=EBI-1054743, EBI-2603996;
CC       O75400:PRPF40A; NbExp=2; IntAct=EBI-1054743, EBI-473291;
CC       P98175:RBM10; NbExp=2; IntAct=EBI-1054743, EBI-721525;
CC       Q15428:SF3A2; NbExp=3; IntAct=EBI-1054743, EBI-2462271;
CC       Q12874:SF3A3; NbExp=2; IntAct=EBI-1054743, EBI-1051880;
CC       P08047:SP1; NbExp=2; IntAct=EBI-1054743, EBI-298336;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15459-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15459-2; Sequence=VSP_054090;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data.;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DOMAIN: SURP motif 2 mediates direct binding to SF3A3.
CC   -!- SIMILARITY: Contains 2 SURP motif repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00263}.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00214}.
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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   CCDS; CCDS13875.1; -. [Q15459-1]
DR   PIR; S60735; S60735.
DR   RefSeq; NP_005868.1; NM_005877.5. [Q15459-1]
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   SMR; Q15459; 48-110, 134-288, 704-789.
DR   BioGrid; 115580; 129.
DR   DIP; DIP-29164N; -.
DR   IntAct; Q15459; 28.
DR   MINT; MINT-144269; -.
DR   STRING; 9606.ENSP00000215793; -.
DR   PhosphoSite; Q15459; -.
DR   DMDM; 2498882; -.
DR   MaxQB; Q15459; -.
DR   PaxDb; Q15459; -.
DR   PeptideAtlas; Q15459; -.
DR   PRIDE; Q15459; -.
DR   DNASU; 10291; -.
DR   Ensembl; ENST00000215793; ENSP00000215793; ENSG00000099995. [Q15459-1]
DR   GeneID; 10291; -.
DR   KEGG; hsa:10291; -.
DR   UCSC; uc003ahl.3; human. [Q15459-1]
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   GeneTree; ENSGT00730000111077; -.
DR   HOGENOM; HOG000238941; -.
DR   HOVERGEN; HBG059993; -.
DR   InParanoid; Q15459; -.
DR   KO; K12825; -.
DR   OMA; VMQQQQT; -.
DR   OrthoDB; EOG7JDQX9; -.
DR   PhylomeDB; Q15459; -.
DR   TreeFam; TF105705; -.
DR   Reactome; REACT_467; mRNA Splicing - Major Pathway.
DR   ChiTaRS; SF3A1; human.
DR   EvolutionaryTrace; Q15459; -.
DR   GeneWiki; SF3A1; -.
DR   GenomeRNAi; 10291; -.
DR   NextBio; 39000; -.
DR   PMAP-CutDB; Q15459; -.
DR   PRO; PR:Q15459; -.
DR   Bgee; Q15459; -.
DR   CleanEx; HS_SF3A1; -.
DR   ExpressionAtlas; Q15459; baseline and differential.
DR   Genevestigator; Q15459; -.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:HGNC.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC.
DR   GO; GO:0006397; P:mRNA processing; IMP:HGNC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; TAS:Reactome.
DR   InterPro; IPR022030; PRP21-like.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR000626; Ubiquitin-like.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
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   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50128; SURP; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   mRNA processing; 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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
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   SITE        169    169       Critical for binding to SF3A3.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES     320    320       Phosphoserine.
FT                                {ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     329    329       Phosphoserine.
FT                                {ECO:0000269|PubMed:17081983,
FT                                ECO:0000269|PubMed:18318008,
FT                                ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:19367720,
FT                                ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:20068231,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     359    359       Phosphoserine.
FT                                {ECO:0000269|PubMed:17081983,
FT                                ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:20068231,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     413    413       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:20068231}.
FT   MOD_RES     451    451       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:20068231}.
FT   MOD_RES     456    456       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:15592455}.
FT   MOD_RES     759    759       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:15592455}.
FT   VAR_SEQ     106    170       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_054090.
FT   VARIANT     511    511       R -> W (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036290.
FT   MUTAGEN      48     48       E->F: SLURP 1 motif acquires binding to
FT                                SF3A3; when associated to Leu-55.
FT                                {ECO:0000269|PubMed:17098193}.
FT   MUTAGEN      55     55       K->L: SLURP 1 motif acquires binding to
FT                                SF3A3; when associated to Phe-48.
FT                                {ECO:0000269|PubMed:17098193}.
FT   MUTAGEN     162    162       F->E: No effect on binding to SF3A3.
FT                                {ECO:0000269|PubMed:17098193}.
FT   MUTAGEN     169    169       L->K: Abolishes binding to SF3A3.
FT                                {ECO:0000269|PubMed:17098193}.
FT   HELIX        48     63       {ECO:0000244|PDB:2DT6}.
FT   HELIX        66     74       {ECO:0000244|PDB:2DT6}.
FT   HELIX        79     84       {ECO:0000244|PDB:2DT6}.
FT   HELIX        91    103       {ECO:0000244|PDB:2DT6}.
FT   HELIX       161    177       {ECO:0000244|PDB:2DT7}.
FT   HELIX       179    188       {ECO:0000244|PDB:2DT7}.
FT   TURN        189    191       {ECO:0000244|PDB:2DT7}.
FT   HELIX       193    198       {ECO:0000244|PDB:2DT7}.
FT   HELIX       204    215       {ECO:0000244|PDB:2DT7}.
FT   STRAND      705    710       {ECO:0000244|PDB:1ZKH}.
FT   STRAND      715    721       {ECO:0000244|PDB:1ZKH}.
FT   STRAND      726    731       {ECO:0000244|PDB:1ZKH}.
FT   HELIX       737    747       {ECO:0000244|PDB:1ZKH}.
FT   TURN        752    754       {ECO:0000244|PDB:1ZKH}.
FT   STRAND      755    759       {ECO:0000244|PDB:1ZKH}.
FT   STRAND      762    764       {ECO:0000244|PDB:1ZKH}.
FT   HELIX       770    773       {ECO:0000244|PDB:1ZKH}.
FT   STRAND      779    786       {ECO:0000244|PDB:1ZKH}.
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
//
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