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Q15459

- SF3A1_HUMAN

UniProt

Q15459 - SF3A1_HUMAN

Protein

Splicing factor 3A subunit 1

Gene

SF3A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei169 – 1691Critical for binding to SF3A3

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-splice site recognition Source: HGNC
    3. mRNA processing Source: HGNC
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. RNA splicing Source: Reactome

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    ReactomeiREACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor 3A subunit 1
    Alternative name(s):
    SF3a120
    Spliceosome-associated protein 114
    Short name:
    SAP 114
    Gene namesi
    Name:SF3A1
    Synonyms:SAP114
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:10765. SF3A1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. spliceosomal complex Source: HGNC
    5. U2-type spliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481E → F: SLURP 1 motif acquires binding to SF3A3; when associated to Leu-55. 1 Publication
    Mutagenesisi55 – 551K → L: SLURP 1 motif acquires binding to SF3A3; when associated to Phe-48. 1 Publication
    Mutagenesisi162 – 1621F → E: No effect on binding to SF3A3. 1 Publication
    Mutagenesisi169 – 1691L → K: Abolishes binding to SF3A3. 1 Publication

    Organism-specific databases

    PharmGKBiPA35683.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 793793Splicing factor 3A subunit 1PRO_0000114917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551N6-acetyllysine1 Publication
    Modified residuei320 – 3201Phosphoserine2 Publications
    Modified residuei329 – 3291Phosphoserine7 Publications
    Modified residuei359 – 3591Phosphoserine4 Publications
    Modified residuei413 – 4131Phosphoserine2 Publications
    Modified residuei451 – 4511Phosphoserine3 Publications
    Modified residuei456 – 4561Phosphotyrosine1 Publication
    Modified residuei759 – 7591Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15459.
    PaxDbiQ15459.
    PeptideAtlasiQ15459.
    PRIDEiQ15459.

    PTM databases

    PhosphoSiteiQ15459.

    Miscellaneous databases

    PMAP-CutDBQ15459.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    ArrayExpressiQ15459.
    BgeeiQ15459.
    CleanExiHS_SF3A1.
    GenevestigatoriQ15459.

    Organism-specific databases

    HPAiHPA000690.
    HPA030083.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. 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 SF3A3.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAP1LC3CQ9BXW43EBI-1054743,EBI-2603996
    PRPF40AO754002EBI-1054743,EBI-473291
    RBM10P981752EBI-1054743,EBI-721525
    SF3A2Q154283EBI-1054743,EBI-2462271
    SF3A3Q128742EBI-1054743,EBI-1051880
    SP1P080472EBI-1054743,EBI-298336

    Protein-protein interaction databases

    BioGridi115580. 120 interactions.
    DIPiDIP-29164N.
    IntActiQ15459. 28 interactions.
    MINTiMINT-144269.
    STRINGi9606.ENSP00000215793.

    Structurei

    Secondary structure

    1
    793
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi48 – 6316
    Helixi66 – 749
    Helixi79 – 846
    Helixi91 – 10313
    Helixi161 – 17717
    Helixi179 – 18810
    Turni189 – 1913
    Helixi193 – 1986
    Helixi204 – 21512
    Beta strandi705 – 7106
    Beta strandi715 – 7217
    Beta strandi726 – 7316
    Helixi737 – 74711
    Turni752 – 7543
    Beta strandi755 – 7595
    Beta strandi762 – 7643
    Helixi770 – 7734
    Beta strandi779 – 7868

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZKHNMR-A704-789[»]
    2DT6NMR-A48-110[»]
    2DT7NMR-B134-217[»]
    ProteinModelPortaliQ15459.
    SMRiQ15459. Positions 48-110, 134-288, 704-789.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15459.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati52 – 9443SURP motif 1Add
    BLAST
    Repeati166 – 20843SURP motif 2Add
    BLAST
    Domaini707 – 79387Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 167Poly-Pro
    Compositional biasi118 – 1225Poly-Gln
    Compositional biasi260 – 2678Poly-Glu
    Compositional biasi369 – 3724Poly-Pro
    Compositional biasi557 – 5604Poly-Pro
    Compositional biasi672 – 6754Poly-Pro

    Domaini

    SURP motif 2 mediates direct binding to SF3A3.

    Sequence similaritiesi

    Contains 2 SURP motif repeats.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG300902.
    HOGENOMiHOG000238941.
    HOVERGENiHBG059993.
    InParanoidiQ15459.
    KOiK12825.
    OMAiVMQQQQT.
    OrthoDBiEOG7JDQX9.
    PhylomeDBiQ15459.
    TreeFamiTF105705.

    Family and domain databases

    InterProiIPR022030. PRP21-like.
    IPR000061. Surp.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF12230. PRP21_like_P. 1 hit.
    PF01805. Surp. 2 hits.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00648. SWAP. 2 hits.
    SM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF109905. SSF109905. 2 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50128. SURP. 2 hits.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15459-1) [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

    MPAGPVQAVP PPPPVPTEPK QPTEEEASSK EDSAPSKPVV GIIYPPPEVR    50
    NIVDKTASFV ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE 100
    FKEGKAQEPS AAIPKVMQQQ QQTTQQQLPQ KVQAQVIQET IVPKEPPPEF 150
    EFIADPPSIS AFDLDVVKLT AQFVARNGRQ FLTQLMQKEQ RNYQFDFLRP 200
    QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL DQVCYRVEWA 250
    KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT 300
    PEELGARILI QERYEKFGES EEVEMEVESD EEDDKQEKAE EPPSQLDQDT 350
    QVQDMDEGSD DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP 400
    LPPAPAPDEY LVSPITGEKI PASKMQEHMR IGLLDPRWLE QRDRSIREKQ 450
    SDDEVYAPGL DIESSLKQLA ERRTDIFGVE ETAIGKKIGE EEIQKPEEKV 500
    TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD TKEKIGPSKP 550
    NEIPQQPPPP SSATNIPSSA PPITSVPRPP TMPPPVRTTV VSAVPVMPRP 600
    PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT 650
    AFVPAPPVAP VPAPAPMPPV HPPPPMEDEP TSKKLKTEDS LMPEEEFLRR 700
    NKGPVSIKVQ VPNMQDKTEW KLNGQVLVFT LPLTDQVSVI KVKIHEATGM 750
    PAGKQKLQYE GIFIKDSNSL AYYNMANGAV IHLALKERGG RKK 793
    Length:793
    Mass (Da):88,886
    Last modified:November 1, 1996 - v1
    Checksum:i7259F1EC4577305C
    GO
    Isoform 2 (identifier: Q15459-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-170: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:728
    Mass (Da):81,678
    Checksum:i53E0FCDFB1CB4616
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti511 – 5111R → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036290

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei106 – 17065Missing in isoform 2. CuratedVSP_054090Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85237 mRNA. Translation: CAA59494.1.
    CR456575 mRNA. Translation: CAG30461.1.
    AC004997 Genomic DNA. Translation: AAC23435.1.
    BC001976 mRNA. Translation: AAH01976.1.
    BC007684 mRNA. Translation: AAH07684.1.
    CCDSiCCDS13875.1. [Q15459-1]
    CCDS46684.1. [Q15459-2]
    PIRiS60735.
    RefSeqiNP_001005409.1. NM_001005409.1. [Q15459-2]
    NP_005868.1. NM_005877.4. [Q15459-1]
    UniGeneiHs.406277.
    Hs.505597.

    Genome annotation databases

    EnsembliENST00000215793; ENSP00000215793; ENSG00000099995. [Q15459-1]
    GeneIDi10291.
    KEGGihsa:10291.
    UCSCiuc003ahl.3. human. [Q15459-1]

    Polymorphism databases

    DMDMi2498882.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85237 mRNA. Translation: CAA59494.1 .
    CR456575 mRNA. Translation: CAG30461.1 .
    AC004997 Genomic DNA. Translation: AAC23435.1 .
    BC001976 mRNA. Translation: AAH01976.1 .
    BC007684 mRNA. Translation: AAH07684.1 .
    CCDSi CCDS13875.1. [Q15459-1 ]
    CCDS46684.1. [Q15459-2 ]
    PIRi S60735.
    RefSeqi NP_001005409.1. NM_001005409.1. [Q15459-2 ]
    NP_005868.1. NM_005877.4. [Q15459-1 ]
    UniGenei Hs.406277.
    Hs.505597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZKH NMR - A 704-789 [» ]
    2DT6 NMR - A 48-110 [» ]
    2DT7 NMR - B 134-217 [» ]
    ProteinModelPortali Q15459.
    SMRi Q15459. Positions 48-110, 134-288, 704-789.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115580. 120 interactions.
    DIPi DIP-29164N.
    IntActi Q15459. 28 interactions.
    MINTi MINT-144269.
    STRINGi 9606.ENSP00000215793.

    PTM databases

    PhosphoSitei Q15459.

    Polymorphism databases

    DMDMi 2498882.

    Proteomic databases

    MaxQBi Q15459.
    PaxDbi Q15459.
    PeptideAtlasi Q15459.
    PRIDEi Q15459.

    Protocols and materials databases

    DNASUi 10291.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215793 ; ENSP00000215793 ; ENSG00000099995 . [Q15459-1 ]
    GeneIDi 10291.
    KEGGi hsa:10291.
    UCSCi uc003ahl.3. human. [Q15459-1 ]

    Organism-specific databases

    CTDi 10291.
    GeneCardsi GC22M030727.
    HGNCi HGNC:10765. SF3A1.
    HPAi HPA000690.
    HPA030083.
    MIMi 605595. gene.
    neXtProti NX_Q15459.
    PharmGKBi PA35683.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300902.
    HOGENOMi HOG000238941.
    HOVERGENi HBG059993.
    InParanoidi Q15459.
    KOi K12825.
    OMAi VMQQQQT.
    OrthoDBi EOG7JDQX9.
    PhylomeDBi Q15459.
    TreeFami TF105705.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SF3A1. human.
    EvolutionaryTracei Q15459.
    GeneWikii SF3A1.
    GenomeRNAii 10291.
    NextBioi 39000.
    PMAP-CutDB Q15459.
    PROi Q15459.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15459.
    Bgeei Q15459.
    CleanExi HS_SF3A1.
    Genevestigatori Q15459.

    Family and domain databases

    InterProi IPR022030. PRP21-like.
    IPR000061. Surp.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF12230. PRP21_like_P. 1 hit.
    PF01805. Surp. 2 hits.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00648. SWAP. 2 hits.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109905. SSF109905. 2 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50128. SURP. 2 hits.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Kraemer A., Mulhauser F., Wersig C., Groning K., Bilbe G.
      RNA 1:260-272(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence of human chromosome 22."
      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.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Cervix and Lymph.
    5. "Functional association of U2 snRNP with the ATP-independent spliceosomal complex E."
      Das R., Zhou Z., Reed R.
      Mol. Cell 5:779-787(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
    6. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      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.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-456 AND TYR-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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-329 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-413 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329; SER-359 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-359; SER-413 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-320; SER-329 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Solution structure of a human ubiquitin-like domain in SF3A1."
      Structural genomics consortium (SGC)
      Submitted (JUN-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 704-789.
    19. "Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP."
      Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P., Muto Y., Yokoyama S.
      Structure 14:1677-1689(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 48-110 AND 134-217 IN COMPLEX WITH SF3A3, SUBUNIT, SURP MOTIFS, MUTAGENESIS OF GLU-48; LYS-55; PHE-162 AND LEU-169.
    20. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-511.

    Entry informationi

    Entry nameiSF3A1_HUMAN
    AccessioniPrimary (citable) accession number: Q15459
    Secondary accession number(s): E9PAW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3