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Q12872

- SFSWA_HUMAN

UniProt

Q12872 - SFSWA_HUMAN

Protein

Splicing factor, suppressor of white-apricot homolog

Gene

SFSWAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (23 Mar 2010)
      Previous versions | rss
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    Functioni

    Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10.1 Publication

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA processing Source: ProtInc
    2. mRNA splice site selection Source: ProtInc
    3. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor, suppressor of white-apricot homolog
    Alternative name(s):
    Splicing factor, arginine/serine-rich 8
    Suppressor of white apricot protein homolog
    Gene namesi
    Name:SFSWAP
    Synonyms:SFRS8, SWAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10790. SFSWAP.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35706.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 951951Splicing factor, suppressor of white-apricot homologPRO_0000081934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei315 – 3151N6-acetyllysine1 Publication
    Modified residuei604 – 6041Phosphoserine3 Publications
    Modified residuei642 – 6421Phosphothreonine1 Publication
    Modified residuei909 – 9091Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ12872.
    PaxDbiQ12872.
    PRIDEiQ12872.

    PTM databases

    PhosphoSiteiQ12872.

    Expressioni

    Gene expression databases

    ArrayExpressiQ12872.
    BgeeiQ12872.
    CleanExiHS_SFRS8.
    GenevestigatoriQ12872.

    Organism-specific databases

    HPAiHPA039362.
    HPA040063.

    Interactioni

    Protein-protein interaction databases

    BioGridi112331. 3 interactions.
    IntActiQ12872. 2 interactions.
    STRINGi9606.ENSP00000261674.

    Structurei

    Secondary structure

    1
    951
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi192 – 1943
    Beta strandi198 – 2003
    Helixi206 – 22116
    Helixi224 – 23310
    Helixi241 – 2433
    Helixi249 – 26214
    Turni454 – 4563
    Helixi457 – 46913
    Helixi472 – 48110
    Helixi484 – 4863
    Beta strandi490 – 4923
    Helixi496 – 50914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E5ZNMR-A440-522[»]
    2E60NMR-A189-282[»]
    ProteinModelPortaliQ12872.
    SMRiQ12872. Positions 189-282, 455-522.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12872.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati211 – 25343SURP motif 1Add
    BLAST
    Repeati459 – 49941SURP motif 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi165 – 1684Poly-Glu
    Compositional biasi287 – 2904Poly-Asp
    Compositional biasi382 – 3854Poly-Pro
    Compositional biasi413 – 4164Poly-Pro
    Compositional biasi420 – 4245Poly-Pro
    Compositional biasi434 – 4407Poly-Thr
    Compositional biasi451 – 4544Poly-Pro
    Compositional biasi616 – 6194Poly-Ser
    Compositional biasi660 – 6634Poly-Ala
    Compositional biasi754 – 76310Poly-Lys
    Compositional biasi789 – 951163Arg/Ser-rich (RS domain)Add
    BLAST
    Compositional biasi850 – 8534Poly-Lys

    Sequence similaritiesi

    Contains 2 SURP motif repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG289028.
    HOVERGENiHBG079184.
    InParanoidiQ12872.
    OMAiPPCVVVE.
    OrthoDBiEOG786H2Z.
    PhylomeDBiQ12872.
    TreeFamiTF106264.

    Family and domain databases

    InterProiIPR000061. Surp.
    IPR019147. SWAP_N_domain.
    [Graphical view]
    PfamiPF09750. DRY_EERY. 1 hit.
    PF01805. Surp. 2 hits.
    [Graphical view]
    SMARTiSM00648. SWAP. 2 hits.
    [Graphical view]
    SUPFAMiSSF109905. SSF109905. 2 hits.
    PROSITEiPS50128. SURP. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12872-1) [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

    MYGASGGRAK PERKSGAKEE AGPGGAGGGG SRVELLVFGY ACKLFRDDER    50
    ALAQEQGQHL IPWMGDHKIL IDRYDGRGHL HDLSEYDAEY STWNRDYQLS 100
    EEEARIEALC DEERYLALHT DLLEEEARQE EEYKRLSEAL AEDGSYNAVG 150
    FTYGSDYYDP SEPTEEEEPS KQREKNEAEN LEENEEPFVA PLGLSVPSDV 200
    ELPPTAKMHA IIERTASFVC RQGAQFEIML KAKQARNSQF DFLRFDHYLN 250
    PYYKFIQKAM KEGRYTVLAE NKSDEKKKSG VSSDNEDDDD EEDGNYLHPS 300
    LFASKKCNRL EELMKPLKVV DPDHPLAALV RKAQADSSTP TPHNADGAPV 350
    QPSQVEYTAD STVAAMYYSY YMLPDGTYCL APPPPGIDVT TYYSTLPAGV 400
    TVSNSPGVTT TAPPPPGTTP LPPPTTAETS SGATSTTTTT SALAPVAAII 450
    PPPPDVQPVI DKLAEYVARN GLKFETSVRA KNDQRFEFLQ PWHQYNAYYE 500
    FKKQFFLQKE GGDSMQAVSA PEEAPTDSAP EKPSDAGEDG APEDAAEVGA 550
    RAGSGGKKEA SSSKTVPDGK LVKASFAPIS FAIKAKENDL LPLEKNRVKL 600
    DDDSDDDEES KEGQESSSSA ANTNPAVAPP CVVVEEKKPQ LTQEELEAKQ 650
    AKQKLEDRLA AAAREKLAQA SKESKEKQLQ AERKRKAALF LQTLKNPLPE 700
    AEAGKIEESP FSVEESSTTP CPLLTGGRPL PTLEVKPPDR PSSKSKDPPR 750
    EEEKEKKKKK HKKRSRTRSR SPKYHSSSKS RSRSHSKAKH SLPSAYRTVR 800
    RSRSRSRSPR RRAHSPERRR EERSVPTAYR VSRSPGASRK RTRSRSPHEK 850
    KKKRRSRSRT KSKARSQSVS PSKQAAPRPA APAAHSAHSA SVSPVESRGS 900
    SQERSRGVSQ EKEAQISSAI VSSVQSKITQ DLMAKVRAML AASKNLQTSA 950
    S 951
    Length:951
    Mass (Da):104,822
    Last modified:March 23, 2010 - v3
    Checksum:iA942D589F4B6BF47
    GO
    Isoform 2 (identifier: Q12872-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         801-801: R → RSRVTASPGTLRAEPCQSSASVTAAAEPGSYQAASTTTRFDSASSFEGKPGKT

    Note: No experimental confirmation available.

    Show »
    Length:1,003
    Mass (Da):110,012
    Checksum:iC67AFFE577FF7CA4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361R → P in AAA19604. (PubMed:8206918)Curated
    Sequence conflicti493 – 4931H → Y in AAA19604. (PubMed:8206918)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521L → Q.1 Publication
    Corresponds to variant rs1051207 [ dbSNP | Ensembl ].
    VAR_046442
    Natural varianti122 – 1221L → F.
    Corresponds to variant rs1051314 [ dbSNP | Ensembl ].
    VAR_046443
    Natural varianti136 – 1361L → F.1 Publication
    Corresponds to variant rs1131564 [ dbSNP | Ensembl ].
    VAR_046444
    Natural varianti421 – 4211L → P.3 Publications
    Corresponds to variant rs1982528 [ dbSNP | Ensembl ].
    VAR_021789
    Natural varianti512 – 5121G → S.
    Corresponds to variant rs34541796 [ dbSNP | Ensembl ].
    VAR_057248
    Natural varianti538 – 5381E → G.
    Corresponds to variant rs34744641 [ dbSNP | Ensembl ].
    VAR_057249
    Natural varianti887 – 8871A → E.
    Corresponds to variant rs34729193 [ dbSNP | Ensembl ].
    VAR_057250

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei801 – 8011R → RSRVTASPGTLRAEPCQSSA SVTAAAEPGSYQAASTTTRF DSASSFEGKPGKT in isoform 2. 1 PublicationVSP_044786

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08377 mRNA. Translation: AAA19604.1.
    AC117500 Genomic DNA. No translation available.
    AC131009 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98526.1.
    BC008707 mRNA. Translation: AAH08707.1.
    BC015953 mRNA. Translation: AAH15953.1.
    BC136678 mRNA. Translation: AAI36679.1.
    BC144364 mRNA. Translation: AAI44365.1.
    CCDSiCCDS58290.1. [Q12872-2]
    CCDS9273.1. [Q12872-1]
    PIRiA54037.
    B54037.
    C54037.
    RefSeqiNP_001248340.1. NM_001261411.1. [Q12872-2]
    NP_004583.2. NM_004592.3. [Q12872-1]
    UniGeneiHs.308171.

    Genome annotation databases

    EnsembliENST00000261674; ENSP00000261674; ENSG00000061936. [Q12872-1]
    ENST00000541286; ENSP00000437738; ENSG00000061936. [Q12872-2]
    GeneIDi6433.
    KEGGihsa:6433.
    UCSCiuc001uja.2. human. [Q12872-1]

    Polymorphism databases

    DMDMi292495067.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08377 mRNA. Translation: AAA19604.1 .
    AC117500 Genomic DNA. No translation available.
    AC131009 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98526.1 .
    BC008707 mRNA. Translation: AAH08707.1 .
    BC015953 mRNA. Translation: AAH15953.1 .
    BC136678 mRNA. Translation: AAI36679.1 .
    BC144364 mRNA. Translation: AAI44365.1 .
    CCDSi CCDS58290.1. [Q12872-2 ]
    CCDS9273.1. [Q12872-1 ]
    PIRi A54037.
    B54037.
    C54037.
    RefSeqi NP_001248340.1. NM_001261411.1. [Q12872-2 ]
    NP_004583.2. NM_004592.3. [Q12872-1 ]
    UniGenei Hs.308171.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E5Z NMR - A 440-522 [» ]
    2E60 NMR - A 189-282 [» ]
    ProteinModelPortali Q12872.
    SMRi Q12872. Positions 189-282, 455-522.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112331. 3 interactions.
    IntActi Q12872. 2 interactions.
    STRINGi 9606.ENSP00000261674.

    PTM databases

    PhosphoSitei Q12872.

    Polymorphism databases

    DMDMi 292495067.

    Proteomic databases

    MaxQBi Q12872.
    PaxDbi Q12872.
    PRIDEi Q12872.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261674 ; ENSP00000261674 ; ENSG00000061936 . [Q12872-1 ]
    ENST00000541286 ; ENSP00000437738 ; ENSG00000061936 . [Q12872-2 ]
    GeneIDi 6433.
    KEGGi hsa:6433.
    UCSCi uc001uja.2. human. [Q12872-1 ]

    Organism-specific databases

    CTDi 6433.
    GeneCardsi GC12P132196.
    H-InvDB HIX0036782.
    HGNCi HGNC:10790. SFSWAP.
    HPAi HPA039362.
    HPA040063.
    MIMi 601945. gene.
    neXtProti NX_Q12872.
    PharmGKBi PA35706.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289028.
    HOVERGENi HBG079184.
    InParanoidi Q12872.
    OMAi PPCVVVE.
    OrthoDBi EOG786H2Z.
    PhylomeDBi Q12872.
    TreeFami TF106264.

    Miscellaneous databases

    ChiTaRSi SFSWAP. human.
    EvolutionaryTracei Q12872.
    GenomeRNAii 6433.
    NextBioi 24987.
    PROi Q12872.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12872.
    Bgeei Q12872.
    CleanExi HS_SFRS8.
    Genevestigatori Q12872.

    Family and domain databases

    InterProi IPR000061. Surp.
    IPR019147. SWAP_N_domain.
    [Graphical view ]
    Pfami PF09750. DRY_EERY. 1 hit.
    PF01805. Surp. 2 hits.
    [Graphical view ]
    SMARTi SM00648. SWAP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF109905. SSF109905. 2 hits.
    PROSITEi PS50128. SURP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot."
      Denhez F., Lafyatis R.
      J. Biol. Chem. 269:16170-16179(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-52; PHE-136 AND PRO-421.
      Tissue: Placenta.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-421.
    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] (ISOFORMS 1 AND 2), VARIANT PRO-421.
      Tissue: Brain and Skin.
    5. "The mammalian homolog of suppressor-of-white-apricot regulates alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS."
      Sarkissian M., Winne A., Lafyatis R.
      J. Biol. Chem. 271:31106-31114(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-604 AND SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    10. "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-283 AND SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of the SURP1 and SURP2 domain in splicing factor, arginine/serine-rich 8."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 189-282 AND 434-522.

    Entry informationi

    Entry nameiSFSWA_HUMAN
    AccessioniPrimary (citable) accession number: Q12872
    Secondary accession number(s): B2RN45
    , B7ZM97, F5H6B8, Q6PJF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 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 12
      Human chromosome 12: 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