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Q07955

- SRSF1_HUMAN

UniProt

Q07955 - SRSF1_HUMAN

Protein

Serine/arginine-rich splicing factor 1

Gene

SRSF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.1 Publication

    GO - Molecular functioni

    1. mRNA binding Source: MGI
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. cardiac muscle contraction Source: Ensembl
    2. gene expression Source: Reactome
    3. in utero embryonic development Source: Ensembl
    4. mRNA 3'-end processing Source: Reactome
    5. mRNA 5'-splice site recognition Source: UniProtKB
    6. mRNA export from nucleus Source: Reactome
    7. mRNA processing Source: ProtInc
    8. mRNA splice site selection Source: ProtInc
    9. mRNA splicing, via spliceosome Source: UniProtKB
    10. RNA splicing Source: Reactome
    11. termination of RNA polymerase II transcription Source: Reactome
    12. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Biological processi

    mRNA processing, mRNA splicing, mRNA transport, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/arginine-rich splicing factor 1
    Alternative name(s):
    Alternative-splicing factor 1
    Short name:
    ASF-1
    Splicing factor, arginine/serine-rich 1
    pre-mRNA-splicing factor SF2, P33 subunit
    Gene namesi
    Name:SRSF1
    Synonyms:ASF, SF2, SF2P33, SFRS1
    ORF Names:OK/SW-cl.3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:10780. SRSF1.

    Subcellular locationi

    Cytoplasm. Nucleus speckle
    Note: In nuclear speckles. Shuttles between the nucleus and the cytoplasm.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. nuclear speck Source: MGI
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 592FV → SR in FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding. 1 Publication
    Mutagenesisi93 – 931R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109. 2 Publications
    Mutagenesisi97 – 971R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109. 2 Publications
    Mutagenesisi109 – 1091R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97. 2 Publications
    Mutagenesisi162 – 1632FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. 2 Publications
    Mutagenesisi162 – 1621F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. 2 Publications
    Mutagenesisi162 – 1621F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. 2 Publications
    Mutagenesisi180 – 1801F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. 2 Publications
    Mutagenesisi182 – 24867Missing in MR-B; strongly inhibits splicing. 1 PublicationAdd
    BLAST
    Mutagenesisi182 – 19918Missing in MR-E; loss of ability to activate splicing. 1 PublicationAdd
    BLAST
    Mutagenesisi192 – 24857Missing in MR-A; loss of ability to activate splicing. 1 PublicationAdd
    BLAST
    Mutagenesisi192 – 1998Missing in MR-D; loss of ability to activate splicing. 1 Publication
    Mutagenesisi199 – 22426Missing in RS-A; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd
    BLAST
    Mutagenesisi215 – 24834Missing in RS-C; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd
    BLAST
    Mutagenesisi226 – 24823Missing in RS-B; retains both splice activation and splice site switching activity. 1 PublicationAdd
    BLAST

    Organism-specific databases

    PharmGKBiPA35696.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 248247Serine/arginine-rich splicing factor 1PRO_0000081911Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei38 – 381N6-acetyllysine1 Publication
    Modified residuei93 – 931Asymmetric dimethylarginine1 Publication
    Modified residuei97 – 971Asymmetric dimethylarginine1 Publication
    Modified residuei109 – 1091Asymmetric dimethylarginine1 Publication
    Modified residuei179 – 1791N6-acetyllysine1 Publication
    Modified residuei199 – 1991Phosphoserine3 Publications
    Modified residuei201 – 2011PhosphoserineBy similarity
    Modified residuei205 – 2051Phosphoserine1 Publication
    Modified residuei231 – 2311Phosphoserine1 Publication
    Modified residuei234 – 2341Phosphoserine1 Publication
    Modified residuei238 – 2381Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed.8 Publications
    Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ07955.
    PaxDbiQ07955.
    PeptideAtlasiQ07955.
    PRIDEiQ07955.

    PTM databases

    PhosphoSiteiQ07955.

    Miscellaneous databases

    PMAP-CutDBQ07955.

    Expressioni

    Gene expression databases

    ArrayExpressiQ07955.
    BgeeiQ07955.
    CleanExiHS_SFRS1.
    GenevestigatoriQ07955.

    Organism-specific databases

    HPAiCAB013073.

    Interactioni

    Subunit structurei

    Consists of two polypeptides of p32 and p33. In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Interacts with SRPK1. Identified in the spliceosome C complex. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus). Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CIR1Q86X953EBI-398920,EBI-627102
    NFYAP235115EBI-398920,EBI-389739
    NXF1Q9UBU95EBI-398920,EBI-398874
    SRPK1Q96SB43EBI-398920,EBI-539478
    Srpk1O705515EBI-398920,EBI-593343From a different organism.
    Srpk2O547813EBI-398920,EBI-593325From a different organism.
    TRAF5O004632EBI-398920,EBI-523498

    Protein-protein interaction databases

    BioGridi112324. 141 interactions.
    DIPiDIP-2155N.
    IntActiQ07955. 49 interactions.
    MINTiMINT-5000565.
    STRINGi9606.ENSP00000258962.

    Structurei

    Secondary structure

    1
    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 228
    Helixi29 – 368
    Helixi37 – 393
    Beta strandi42 – 476
    Beta strandi50 – 545
    Beta strandi57 – 626
    Helixi64 – 7411
    Beta strandi85 – 873
    Beta strandi110 – 1134
    Beta strandi122 – 1276
    Helixi134 – 1418
    Helixi142 – 1443
    Beta strandi147 – 1526
    Beta strandi158 – 1647
    Helixi165 – 17410
    Turni175 – 1773
    Beta strandi179 – 1813
    Beta strandi183 – 1853
    Beta strandi187 – 1893
    Beta strandi191 – 1977
    Beta strandi202 – 2043
    Beta strandi206 – 2083

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X4ANMR-A1-96[»]
    2M7SNMR-A106-195[»]
    2M8DNMR-B107-196[»]
    2O3DNMR-A107-215[»]
    3BEGX-ray2.90B105-219[»]
    4C0OX-ray2.56C/D106-230[»]
    ProteinModelPortaliQ07955.
    SMRiQ07955. Positions 6-102, 116-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07955.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 9176RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini121 – 19575RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni198 – 24750Interacts with SAFB1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi94 – 11320Gly-rich (hinge region)Add
    BLAST
    Compositional biasi198 – 24750Arg/Ser-rich (RS domain)Add
    BLAST

    Domaini

    The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling.1 Publication

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated
    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOVERGENiHBG002295.
    InParanoidiQ07955.
    KOiK12890.
    OrthoDBiEOG76X620.
    PhylomeDBiQ07955.
    TreeFamiTF106261.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR029538. SRSF1.
    [Graphical view]
    PANTHERiPTHR10548:SF87. PTHR10548:SF87. 1 hit.
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform ASF-1 (identifier: Q07955-1) [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

    MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR    50
    RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG 100
    GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA 150
    DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP 200
    SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRT 248
    Length:248
    Mass (Da):27,745
    Last modified:January 23, 2007 - v2
    Checksum:iC28A0B2F112EA713
    GO
    Isoform ASF-2 (identifier: Q07955-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         185-248: GETAYIRVKV...PRHSRSRSRT → FCLSNREKLP...NCFVQNGLKC

    Show »
    Length:292
    Mass (Da):31,999
    Checksum:iC9502AC70F373EAC
    GO
    Isoform ASF-3 (identifier: Q07955-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         185-201: GETAYIRVKVDGPRSPS → VGYTRILFFDQNWIQWS
         202-248: Missing.

    Note: May be due to intron retention.

    Show »
    Length:201
    Mass (Da):22,460
    Checksum:iB9AC6495A491613D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891P → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035488

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei185 – 24864GETAY…SRSRT → FCLSNREKLPTSGLKLMGPE VQVMEDLDLEAVVVAEAVAE ATAGVAVTPQGEAEDHHAIL PVIADLALVHKMIGDTFCRT HVVYSFPLFSTIFSFFNSNC FVQNGLKC in isoform ASF-2. 1 PublicationVSP_005856Add
    BLAST
    Alternative sequencei185 – 20117GETAY…PRSPS → VGYTRILFFDQNWIQWS in isoform ASF-3. 1 PublicationVSP_005857Add
    BLAST
    Alternative sequencei202 – 24847Missing in isoform ASF-3. 1 PublicationVSP_005858Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M72709 mRNA. Translation: AAA35565.1.
    M72709 mRNA. Translation: AAA35564.1.
    M69040 mRNA. Translation: AAA03476.1.
    AB062124 mRNA. Translation: BAB93456.1.
    AK312781 mRNA. Translation: BAG35644.1.
    CH471109 Genomic DNA. Translation: EAW94485.1.
    CH471109 Genomic DNA. Translation: EAW94486.1.
    BC010264 mRNA. Translation: AAH10264.1.
    BC033785 mRNA. Translation: AAH33785.1.
    CCDSiCCDS11600.1. [Q07955-1]
    CCDS58580.1. [Q07955-3]
    PIRiA40040.
    B40040.
    C40040.
    RefSeqiNP_001071634.1. NM_001078166.1. [Q07955-3]
    NP_008855.1. NM_006924.4. [Q07955-1]
    UniGeneiHs.68714.

    Genome annotation databases

    EnsembliENST00000258962; ENSP00000258962; ENSG00000136450. [Q07955-1]
    ENST00000581979; ENSP00000463223; ENSG00000136450. [Q07955-3]
    ENST00000582730; ENSP00000462215; ENSG00000136450. [Q07955-3]
    GeneIDi6426.
    KEGGihsa:6426.
    UCSCiuc002ivi.3. human. [Q07955-1]
    uc002ivj.3. human. [Q07955-3]

    Polymorphism databases

    DMDMi730773.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M72709 mRNA. Translation: AAA35565.1 .
    M72709 mRNA. Translation: AAA35564.1 .
    M69040 mRNA. Translation: AAA03476.1 .
    AB062124 mRNA. Translation: BAB93456.1 .
    AK312781 mRNA. Translation: BAG35644.1 .
    CH471109 Genomic DNA. Translation: EAW94485.1 .
    CH471109 Genomic DNA. Translation: EAW94486.1 .
    BC010264 mRNA. Translation: AAH10264.1 .
    BC033785 mRNA. Translation: AAH33785.1 .
    CCDSi CCDS11600.1. [Q07955-1 ]
    CCDS58580.1. [Q07955-3 ]
    PIRi A40040.
    B40040.
    C40040.
    RefSeqi NP_001071634.1. NM_001078166.1. [Q07955-3 ]
    NP_008855.1. NM_006924.4. [Q07955-1 ]
    UniGenei Hs.68714.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X4A NMR - A 1-96 [» ]
    2M7S NMR - A 106-195 [» ]
    2M8D NMR - B 107-196 [» ]
    2O3D NMR - A 107-215 [» ]
    3BEG X-ray 2.90 B 105-219 [» ]
    4C0O X-ray 2.56 C/D 106-230 [» ]
    ProteinModelPortali Q07955.
    SMRi Q07955. Positions 6-102, 116-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112324. 141 interactions.
    DIPi DIP-2155N.
    IntActi Q07955. 49 interactions.
    MINTi MINT-5000565.
    STRINGi 9606.ENSP00000258962.

    PTM databases

    PhosphoSitei Q07955.

    Polymorphism databases

    DMDMi 730773.

    Proteomic databases

    MaxQBi Q07955.
    PaxDbi Q07955.
    PeptideAtlasi Q07955.
    PRIDEi Q07955.

    Protocols and materials databases

    DNASUi 6426.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258962 ; ENSP00000258962 ; ENSG00000136450 . [Q07955-1 ]
    ENST00000581979 ; ENSP00000463223 ; ENSG00000136450 . [Q07955-3 ]
    ENST00000582730 ; ENSP00000462215 ; ENSG00000136450 . [Q07955-3 ]
    GeneIDi 6426.
    KEGGi hsa:6426.
    UCSCi uc002ivi.3. human. [Q07955-1 ]
    uc002ivj.3. human. [Q07955-3 ]

    Organism-specific databases

    CTDi 6426.
    GeneCardsi GC17M056079.
    H-InvDB HIX0173551.
    HGNCi HGNC:10780. SRSF1.
    HPAi CAB013073.
    MIMi 600812. gene.
    neXtProti NX_Q07955.
    PharmGKBi PA35696.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOVERGENi HBG002295.
    InParanoidi Q07955.
    KOi K12890.
    OrthoDBi EOG76X620.
    PhylomeDBi Q07955.
    TreeFami TF106261.

    Enzyme and pathway databases

    Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi SRSF1. human.
    EvolutionaryTracei Q07955.
    GeneWikii ASF/SF2.
    GenomeRNAii 6426.
    NextBioi 24955.
    PMAP-CutDB Q07955.
    PROi Q07955.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07955.
    Bgeei Q07955.
    CleanExi HS_SFRS1.
    Genevestigatori Q07955.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR029538. SRSF1.
    [Graphical view ]
    PANTHERi PTHR10548:SF87. PTHR10548:SF87. 1 hit.
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators."
      Ge H., Zuo P., Manley J.L.
      Cell 66:373-382(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ASF-1 AND ASF-2), PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING.
    2. "Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators."
      Krainer A.R., Mayeda A., Kozak D., Binns G.
      Cell 66:383-394(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ASF-1), PROTEIN SEQUENCE OF 144-161 AND 167-175.
    3. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ASF-1).
      Tissue: Colon adenocarcinoma.
    4. "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] (ISOFORM ASF-1).
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 ASF-1 AND ASF-3).
      Tissue: Brain and Placenta.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-28; 31-38; 52-65; 75-83; 123-138 AND 143-164, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    8. "SR proteins: a conserved family of pre-mRNA splicing factors."
      Zahler A.M., Lane W.S., Stolk J.A., Roth M.B.
      Genes Dev. 6:837-847(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 123-140.
    9. "Two members of a conserved family of nuclear phosphoproteins are involved in pre-mRNA splicing."
      Mayeda A., Zahler A.M., Krainer A.R., Roth M.B.
      Proc. Natl. Acad. Sci. U.S.A. 89:1301-1304(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Specific interactions between proteins implicated in splice site selection and regulated alternative splicing."
      Wu J.Y., Maniatis T.
      Cell 75:1061-1070(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION IN SPLICEOSOME ASSEMBLY.
    11. "Functional domains of the human splicing factor ASF/SF2."
      Zuo P., Manley J.L.
      EMBO J. 12:4727-4737(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS, CHARACTERIZATION OF FUNCTIONAL DOMAINS.
    12. "Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors."
      Kohtz J.D., Jamison S.F., Will C.L., Zuo P., Luehrmann R., Garcia-Blanco M.A., Manley J.L.
      Nature 368:119-124(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECRUITMENT OF U1-70K TO PRE-MRNA.
    13. "The human splicing factor ASF/SF2 can specifically recognize pre-mRNA 5' splice sites."
      Zuo P., Manley J.L.
      Proc. Natl. Acad. Sci. U.S.A. 91:3363-3367(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECOGNITION OF PRE-MRNA 5'SPLICE SITES.
    14. "The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities."
      Tacke R., Manley J.L.
      EMBO J. 14:3540-3551(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING SPECIFICITY.
    15. "A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
      Tronchere H., Wang J., Fu X.D.
      Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZRSR2.
    16. "A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm."
      Caceres J.F., Screaton G.R., Krainer A.R.
      Genes Dev. 12:55-66(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-162 AND PHE-180.
    17. "A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2."
      Ge H., Si Y., Wolffe A.P.
      Mol. Cell 2:751-759(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSIP1.
    18. Cited for: INTERACTION WITH SAFB/SAFB1.
    19. "Identification and characterization of a novel serine-arginine-rich splicing regulatory protein."
      Barnard D.C., Patton J.G.
      Mol. Cell. Biol. 20:3049-3057(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SREK1.
    20. "Nuclear export and retention signals in the RS domain of SR proteins."
      Cazalla D., Zhu J., Manche L., Huber E., Krainer A.R., Caceres J.F.
      Mol. Cell. Biol. 22:6871-6882(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    21. "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.
    22. "SR splicing factors serve as adapter proteins for TAP-dependent mRNA export."
      Huang Y., Gattoni R., Stevenin J., Steitz J.A.
      Mol. Cell 11:837-843(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NXF1.
    23. "Processive phosphorylation of alternative splicing factor/splicing factor 2."
      Aubol B.E., Chakrabarti S., Ngo J., Shaffer J., Nolen B., Fu X.-D., Ghosh G., Adams J.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SERINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH SRPK1.
    24. "A novel SR-related protein is required for the second step of pre-mRNA splicing."
      Cazalla D., Newton K., Caceres J.F.
      Mol. Cell. Biol. 25:2969-2980(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RSRC1.
    25. "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.
    26. "Ordered multi-site phosphorylation of the splicing factor ASF/SF2 by SRPK1."
      Ma C.T., Velazquez-Dones A., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.
      J. Mol. Biol. 376:55-68(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
    27. "Adaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1."
      Hagopian J.C., Ma C.T., Meade B.R., Albuquerque C.P., Ngo J.C., Ghosh G., Jennings P.A., Fu X.D., Adams J.A.
      J. Mol. Biol. 382:894-909(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-205; SER-231; SER-234 AND SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1."
      Huynh N., Ma C.T., Giang N., Hagopian J., Ngo J., Adams J., Ghosh G.
      Biochemistry 48:11432-11440(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
    30. "Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1."
      Ma C.T., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.
      J. Mol. Biol. 390:618-634(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY SRPK1, THE MECHANISM OF PHOSPHORYATION.
    31. "Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
      Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
      Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    32. "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-38 AND LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF."
      Sinha R., Allemand E., Zhang Z., Karni R., Myers M.P., Krainer A.R.
      Mol. Cell. Biol. 30:2762-2774(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-93; ARG-97 AND ARG-109, MUTAGENESIS OF ARG-93; ARG-97 AND ARG-109, SUBCELLULAR LOCATION.
    34. "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-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "NSrp70 is a novel nuclear speckle-related protein that modulates alternative pre-mRNA splicing in vivo."
      Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.
      Nucleic Acids Res. 39:4300-4314(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCDC55.
    37. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    38. "Solution structure of RRM domain in splicing factor SF2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-98.
    39. "A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1."
      Ngo J.C., Giang K., Chakrabarti S., Ma C.T., Huynh N., Hagopian J.C., Dorrestein P.C., Fu X.D., Adams J.A., Ghosh G.
      Mol. Cell 29:563-576(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 105-219 IN COMPLEX WITH SRPK1, MECHANISM OF ITS PHOSPHORYLATION BY SRPK1, DOMAIN RRM.
    40. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-89.

    Entry informationi

    Entry nameiSRSF1_HUMAN
    AccessioniPrimary (citable) accession number: Q07955
    Secondary accession number(s): B2R6Z7, D3DTZ3, Q13809
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 180 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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