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O75494

- SRS10_HUMAN

UniProt

O75494 - SRS10_HUMAN

Protein

Serine/arginine-rich splicing factor 10

Gene

SRSF10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing. Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70. Required for splicing repression in M-phase cells and after heat shock. May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator.3 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB
    5. RS domain binding Source: UniProtKB
    6. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. cytoplasmic transport Source: UniProtKB
    2. mRNA export from nucleus Source: UniProtKB
    3. mRNA splice site selection Source: UniProtKB
    4. mRNA splicing, via spliceosome Source: UniProtKB
    5. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. RNA splicing, via transesterification reactions Source: UniProtKB
    8. spliceosomal tri-snRNP complex assembly Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/arginine-rich splicing factor 10
    Alternative name(s):
    40 kDa SR-repressor protein
    Short name:
    SRrp40
    FUS-interacting serine-arginine-rich protein 1
    Splicing factor SRp38
    Splicing factor, arginine/serine-rich 13A
    TLS-associated protein with Ser-Arg repeats
    Short name:
    TASR
    Short name:
    TLS-associated protein with SR repeats
    TLS-associated serine-arginine protein
    Short name:
    TLS-associated SR protein
    Gene namesi
    Name:SRSF10
    Synonyms:FUSIP1, FUSIP2, SFRS13A, TASR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16713. SRSF10.

    Subcellular locationi

    Nucleus speckle 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleoplasm Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28427.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 262262Serine/arginine-rich splicing factor 10PRO_0000081593Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei106 – 1061Phosphoserine1 Publication
    Modified residuei108 – 1081Phosphoserine1 Publication
    Modified residuei129 – 1291Phosphoserine1 Publication
    Modified residuei131 – 1311Phosphoserine3 Publications
    Modified residuei133 – 1331Phosphoserine4 Publications
    Modified residuei158 – 1581Phosphoserine1 Publication
    Modified residuei160 – 1601Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. Isoform 3 is phosphorylated on Ser-168 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75494.
    PaxDbiO75494.
    PRIDEiO75494.

    PTM databases

    PhosphoSiteiO75494.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiO75494.
    BgeeiO75494.
    GenevestigatoriO75494.

    Interactioni

    Subunit structurei

    The phosphorylated but not the dephosphorylated form interacts with TRA2B/SFRS10. The dephosphorylated form interacts with SNRNP70. Isoform 1 and isoform 3 interact with FUS C-terminus.2 Publications

    Protein-protein interaction databases

    BioGridi115990. 50 interactions.
    IntActiO75494. 16 interactions.
    MINTiMINT-5002282.

    Structurei

    3D structure databases

    ProteinModelPortaliO75494.
    SMRiO75494. Positions 10-116.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 8879RRMPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi106 – 260155Arg/Ser-rich (RS domain)Add
    BLAST

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG312850.
    HOVERGENiHBG107480.
    InParanoidiO75494.
    KOiK12900.
    OrthoDBiEOG73BVG8.
    PhylomeDBiO75494.
    TreeFamiTF351864.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75494-1) [UniParc]FASTAAdd to Basket

    Also known as: TASR-1

    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

    MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP    50
    RGFAYVQFED VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE 100
    GRNVYSSSRY DDYDRYRRSR SRSYERRRSR SRSFDYNYRR SYSPRNSRPT 150
    GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR SRSKSQPKKE MKAKSRSRSA 200
    SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR SQSRSRSKSR 250
    SRSWTSPKSS GH 262
    Length:262
    Mass (Da):31,301
    Last modified:November 1, 1998 - v1
    Checksum:i205F95D36CBBFAB4
    GO
    Isoform 2 (identifier: O75494-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         147-147: Missing.

    Show »
    Length:261
    Mass (Da):31,213
    Checksum:iA07499B11D4C7570
    GO
    Isoform 3 (identifier: O75494-3) [UniParc]FASTAAdd to Basket

    Also known as: TASR-2, SRp38-2

    The sequence of this isoform differs from the canonical sequence as follows:
         165-183: FKHRNRSFSRSKSNSRSRS → PNCSWNTQYSSAYYTSRKI
         184-262: Missing.

    Note: Contains a phosphoserine at position 168.By similarity

    Show »
    Length:183
    Mass (Da):22,222
    Checksum:i4AA87CAA9B51A131
    GO
    Isoform 4 (identifier: O75494-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         164-173: RFKHRNRSFS → SQVSKKKNER
         174-183: Missing.
         184-262: Missing.

    Note: Contains a phosphoserine at position 158. Contains a phosphoserine at position 160.

    Show »
    Length:173
    Mass (Da):21,000
    Checksum:i4AB40FBF24846495
    GO
    Isoform 5 (identifier: O75494-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         146-165: NSRPTGRPRRSRSHSDNDRF → KPNCSWNTQYSSAYYTSRKI
         166-173: Missing.
         174-183: Missing.
         184-262: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:165
    Mass (Da):20,117
    Checksum:i6CB98688C53A9F69
    GO
    Isoform 6 (identifier: O75494-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         147-147: Missing.
         165-183: FKHRNRSFSRSKSNSRSRS → PNCSWNTQYSSAYYTSRKI
         184-262: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:182
    Mass (Da):22,135
    Checksum:iF99356E1D895987D
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei146 – 16520NSRPT…DNDRF → KPNCSWNTQYSSAYYTSRKI in isoform 5. 1 PublicationVSP_043697Add
    BLAST
    Alternative sequencei147 – 1471Missing in isoform 2 and isoform 6. 1 PublicationVSP_010421
    Alternative sequencei164 – 17310RFKHRNRSFS → SQVSKKKNER in isoform 4. CuratedVSP_010422
    Alternative sequencei165 – 18319FKHRN…SRSRS → PNCSWNTQYSSAYYTSRKI in isoform 3 and isoform 6. 4 PublicationsVSP_010424Add
    BLAST
    Alternative sequencei166 – 1738Missing in isoform 5. 1 PublicationVSP_043698
    Alternative sequencei174 – 18310Missing in isoform 4 and isoform 5. 1 PublicationVSP_010423
    Alternative sequencei184 – 26279Missing in isoform 3, isoform 4, isoform 5 and isoform 6. 4 PublicationsVSP_010425Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047448 mRNA. Translation: AAC70918.1.
    AF067730 mRNA. Translation: AAC26727.1.
    AF449427 mRNA. Translation: AAL57514.1.
    AY150180 mRNA. Translation: AAN65380.1.
    AY150181 mRNA. Translation: AAN65381.1.
    AF419331 mRNA. Translation: AAL16665.1.
    AF419332 Genomic DNA. Translation: AAL16666.1.
    AY048592 Genomic DNA. Translation: AAL06098.1.
    AY048592 Genomic DNA. Translation: AAL06099.1.
    AK001286 mRNA. Translation: BAA91601.1.
    AK001656 mRNA. Translation: BAG50956.1.
    AK296175 mRNA. Translation: BAG58911.1.
    AL590609 Genomic DNA. Translation: CAI14807.1.
    AL590609 Genomic DNA. Translation: CAI14803.1.
    AL590609 Genomic DNA. Translation: CAI14805.1.
    AL590609 Genomic DNA. Translation: CAI14808.1.
    BC001107 mRNA. Translation: AAH01107.1.
    BC005039 mRNA. Translation: AAH05039.1.
    BC010074 mRNA. Translation: AAH10074.1.
    CCDSiCCDS30629.1. [O75494-3]
    CCDS30630.1. [O75494-1]
    CCDS53280.1. [O75494-5]
    CCDS53281.1. [O75494-6]
    CCDS53282.1. [O75494-2]
    CCDS53283.1. [O75494-4]
    RefSeqiNP_001177934.1. NM_001191005.1. [O75494-2]
    NP_001177935.1. NM_001191006.1. [O75494-4]
    NP_001177936.1. NM_001191007.1. [O75494-6]
    NP_001177938.1. NM_001191009.1. [O75494-5]
    NP_006616.1. NM_006625.4. [O75494-3]
    NP_473357.1. NM_054016.2. [O75494-1]
    UniGeneiHs.3530.

    Genome annotation databases

    EnsembliENST00000343255; ENSP00000344149; ENSG00000188529. [O75494-2]
    ENST00000344989; ENSP00000342913; ENSG00000188529. [O75494-3]
    ENST00000374452; ENSP00000363576; ENSG00000188529. [O75494-4]
    ENST00000453840; ENSP00000388991; ENSG00000188529. [O75494-6]
    ENST00000484146; ENSP00000419813; ENSG00000188529. [O75494-5]
    ENST00000492112; ENSP00000420195; ENSG00000188529. [O75494-1]
    GeneIDi10772.
    KEGGihsa:10772.
    UCSCiuc021oin.1. human. [O75494-4]
    uc021oio.1. human. [O75494-3]
    uc021oiq.1. human. [O75494-5]
    uc021oir.1. human. [O75494-1]
    uc021ois.1. human. [O75494-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047448 mRNA. Translation: AAC70918.1 .
    AF067730 mRNA. Translation: AAC26727.1 .
    AF449427 mRNA. Translation: AAL57514.1 .
    AY150180 mRNA. Translation: AAN65380.1 .
    AY150181 mRNA. Translation: AAN65381.1 .
    AF419331 mRNA. Translation: AAL16665.1 .
    AF419332 Genomic DNA. Translation: AAL16666.1 .
    AY048592 Genomic DNA. Translation: AAL06098.1 .
    AY048592 Genomic DNA. Translation: AAL06099.1 .
    AK001286 mRNA. Translation: BAA91601.1 .
    AK001656 mRNA. Translation: BAG50956.1 .
    AK296175 mRNA. Translation: BAG58911.1 .
    AL590609 Genomic DNA. Translation: CAI14807.1 .
    AL590609 Genomic DNA. Translation: CAI14803.1 .
    AL590609 Genomic DNA. Translation: CAI14805.1 .
    AL590609 Genomic DNA. Translation: CAI14808.1 .
    BC001107 mRNA. Translation: AAH01107.1 .
    BC005039 mRNA. Translation: AAH05039.1 .
    BC010074 mRNA. Translation: AAH10074.1 .
    CCDSi CCDS30629.1. [O75494-3 ]
    CCDS30630.1. [O75494-1 ]
    CCDS53280.1. [O75494-5 ]
    CCDS53281.1. [O75494-6 ]
    CCDS53282.1. [O75494-2 ]
    CCDS53283.1. [O75494-4 ]
    RefSeqi NP_001177934.1. NM_001191005.1. [O75494-2 ]
    NP_001177935.1. NM_001191006.1. [O75494-4 ]
    NP_001177936.1. NM_001191007.1. [O75494-6 ]
    NP_001177938.1. NM_001191009.1. [O75494-5 ]
    NP_006616.1. NM_006625.4. [O75494-3 ]
    NP_473357.1. NM_054016.2. [O75494-1 ]
    UniGenei Hs.3530.

    3D structure databases

    ProteinModelPortali O75494.
    SMRi O75494. Positions 10-116.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115990. 50 interactions.
    IntActi O75494. 16 interactions.
    MINTi MINT-5002282.

    PTM databases

    PhosphoSitei O75494.

    Proteomic databases

    MaxQBi O75494.
    PaxDbi O75494.
    PRIDEi O75494.

    Protocols and materials databases

    DNASUi 10772.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343255 ; ENSP00000344149 ; ENSG00000188529 . [O75494-2 ]
    ENST00000344989 ; ENSP00000342913 ; ENSG00000188529 . [O75494-3 ]
    ENST00000374452 ; ENSP00000363576 ; ENSG00000188529 . [O75494-4 ]
    ENST00000453840 ; ENSP00000388991 ; ENSG00000188529 . [O75494-6 ]
    ENST00000484146 ; ENSP00000419813 ; ENSG00000188529 . [O75494-5 ]
    ENST00000492112 ; ENSP00000420195 ; ENSG00000188529 . [O75494-1 ]
    GeneIDi 10772.
    KEGGi hsa:10772.
    UCSCi uc021oin.1. human. [O75494-4 ]
    uc021oio.1. human. [O75494-3 ]
    uc021oiq.1. human. [O75494-5 ]
    uc021oir.1. human. [O75494-1 ]
    uc021ois.1. human. [O75494-2 ]

    Organism-specific databases

    CTDi 10772.
    GeneCardsi GC01M024293.
    HGNCi HGNC:16713. SRSF10.
    MIMi 605221. gene.
    neXtProti NX_O75494.
    PharmGKBi PA28427.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG312850.
    HOVERGENi HBG107480.
    InParanoidi O75494.
    KOi K12900.
    OrthoDBi EOG73BVG8.
    PhylomeDBi O75494.
    TreeFami TF351864.

    Miscellaneous databases

    GeneWikii FUSIP1.
    NextBioi 40903.
    PROi O75494.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75494.
    Bgeei O75494.
    Genevestigatori O75494.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing."
      Yang L., Embree L.J., Tsai S., Hickstein D.D.
      J. Biol. Chem. 273:27761-27764(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH FUS.
      Tissue: Leukemia.
    2. "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins."
      Yang L., Embree L.J., Hickstein D.D.
      Mol. Cell. Biol. 20:3345-3354(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing."
      Cowper A.E., Caceres J.F., Mayeda A., Screaton G.R.
      J. Biol. Chem. 276:48908-48914(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "The SR protein SRp38 represses splicing in M Phase cells."
      Shin C., Manley J.L.
      Cell 111:407-417(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, PHOSPHORYLATION.
    5. "Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins."
      Clinton J.M., Chansky H.A., Odell D.D., Zielinska-Kwiatkowska A., Hickstein D.D., Yang L.
      Gene 284:141-147(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), TISSUE SPECIFICITY.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
      Tissue: Thalamus.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 3).
      Tissue: Muscle, Placenta and Uterus.
    9. "Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock."
      Shin C., Feng Y., Manley J.L.
      Nature 427:553-558(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH SNRNP70 AND TRA2B.
    10. "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.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-131 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-131; SER-133; SER-158 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-106; SER-108; SER-131 AND SER-133, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-160 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSRS10_HUMAN
    AccessioniPrimary (citable) accession number: O75494
    Secondary accession number(s): A6NFM6
    , A6NI42, A6NIU7, B4DJP9, O60572, Q5JRH9, Q5JRI0, Q5JRI2, Q5JRI3, Q5JRI4, Q96G09, Q96P17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 148 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3