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Q6PDM2

- SRSF1_MOUSE

UniProt

Q6PDM2 - SRSF1_MOUSE

Protein

Serine/arginine-rich splicing factor 1

Gene

Srsf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (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 By similarity. Specifically regulates alternative splicing of cardiac isoforms of CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling at the juvenile to adult transition. The inappropriate accumulation of a neonatal and neuronal isoform of CAMKD2 in the adult heart results in aberrant calcium handling and defective excitation-contraction coupling in cardiomyocytes. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.By similarity1 Publication

    GO - Molecular functioni

    1. mRNA binding Source: MGI
    2. nucleotide binding Source: InterPro
    3. protein binding Source: IntAct
    4. RNA binding Source: UniProtKB
    5. RS domain binding Source: MGI

    GO - Biological processi

    1. cardiac muscle contraction Source: MGI
    2. in utero embryonic development Source: MGI
    3. mRNA 5'-splice site recognition Source: UniProtKB
    4. mRNA transport Source: UniProtKB-KW
    5. RNA splicing Source: MGI

    Keywords - Biological processi

    mRNA processing, mRNA splicing, mRNA transport, Transport

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/arginine-rich splicing factor 1
    Alternative name(s):
    ASF/SF2
    Pre-mRNA-splicing factor SRp30a
    Splicing factor, arginine/serine-rich 1
    Gene namesi
    Name:Srsf1
    Synonyms:Sfrs1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:98283. Srsf1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Nucleus speckle By similarity
    Note: Shuttles between the nucleus and the cytoplasm.By similarity

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. exon-exon junction complex Source: Ensembl
    4. nuclear speck Source: MGI
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 248247Serine/arginine-rich splicing factor 1PRO_0000081912Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineSequence Analysis
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei38 – 381N6-acetyllysineBy similarity
    Modified residuei93 – 931Asymmetric dimethylarginineBy similarity
    Modified residuei97 – 971Asymmetric dimethylarginineBy similarity
    Modified residuei109 – 1091Asymmetric dimethylarginineBy similarity
    Modified residuei179 – 1791N6-acetyllysineBy similarity
    Modified residuei199 – 1991Phosphoserine2 Publications
    Modified residuei201 – 2011Phosphoserine2 Publications
    Modified residuei205 – 2051PhosphoserineBy similarity
    Modified residuei231 – 2311PhosphoserineBy similarity
    Modified residuei234 – 2341PhosphoserineBy similarity
    Modified residuei238 – 2381PhosphoserineBy similarity

    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 By similarity.By similarity
    Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6PDM2.
    PaxDbiQ6PDM2.
    PRIDEiQ6PDM2.

    PTM databases

    PhosphoSiteiQ6PDM2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6PDM2.
    BgeeiQ6PDM2.
    CleanExiMM_SFRS1.
    GenevestigatoriQ6PDM2.

    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. 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) By similarity. Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hexim1Q8R4094EBI-2550360,EBI-6261031
    Polr2aP087752EBI-2550360,EBI-2549849
    Tial1P703183EBI-2550360,EBI-299820
    Traf5P701912EBI-2550360,EBI-523899

    Protein-protein interaction databases

    BioGridi225922. 8 interactions.
    DIPiDIP-48723N.
    IntActiQ6PDM2. 10 interactions.
    MINTiMINT-1867664.

    Structurei

    Secondary structure

    1
    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi122 – 1276
    Helixi134 – 1418
    Helixi142 – 1443
    Beta strandi147 – 1526
    Beta strandi156 – 1649
    Helixi165 – 17410
    Beta strandi175 – 1817
    Beta strandi187 – 19610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X4CNMR-A113-207[»]
    ProteinModelPortaliQ6PDM2.
    SMRiQ6PDM2. Positions 6-102, 116-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6PDM2.

    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 SAFB1By similarityAdd
    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 By similarity.By similarity

    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.
    GeneTreeiENSGT00700000104103.
    HOVERGENiHBG002295.
    InParanoidiB2KGJ5.
    KOiK12890.
    OrthoDBiEOG76X620.
    PhylomeDBiQ6PDM2.
    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 1 (identifier: Q6PDM2-1) [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 - v3
    Checksum:iC28A0B2F112EA713
    GO
    Isoform 2 (identifier: Q6PDM2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         185-203: GETAYIRVKVDGPRSPSYG → VGYTLILFFGQNWIQFS
         204-248: Missing.

    Note: May be due to intron retention.

    Show »
    Length:201
    Mass (Da):22,320
    Checksum:i16B6D495BD77613F
    GO
    Isoform 3 (identifier: Q6PDM2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         185-199: GETAYIRVKVDGPRS → TYLKRWIKNALD
         200-248: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:196
    Mass (Da):21,807
    Checksum:i6723D202662FF71D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191S → A in BAC25546. (PubMed:16141072)Curated
    Sequence conflicti162 – 1643FVR → CVP in BAC25546. (PubMed:16141072)Curated
    Sequence conflicti185 – 1851G → W in BAC25546. (PubMed:16141072)Curated
    Sequence conflicti191 – 1966RVKVDG → PRIVDR in BAC25546. (PubMed:16141072)Curated
    Sequence conflicti209 – 2102SR → VC in BAC25546. (PubMed:16141072)Curated
    Sequence conflicti226 – 2283YSP → DSR in BAC25546. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei185 – 20319GETAY…SPSYG → VGYTLILFFGQNWIQFS in isoform 2. 1 PublicationVSP_013770Add
    BLAST
    Alternative sequencei185 – 19915GETAY…DGPRS → TYLKRWIKNALD in isoform 3. CuratedVSP_013771Add
    BLAST
    Alternative sequencei200 – 24849Missing in isoform 3. CuratedVSP_013772Add
    BLAST
    Alternative sequencei204 – 24845Missing in isoform 2. 1 PublicationVSP_013773Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018176 mRNA. Translation: BAC25546.1.
    AK078715 mRNA. Translation: BAC37367.1.
    AK150535 mRNA. Translation: BAE29641.1.
    AL593853 Genomic DNA. Translation: CAI24416.1.
    CU406964 Genomic DNA. Translation: CAQ51705.1.
    BC046773 mRNA. Translation: AAH46773.1.
    BC058627 mRNA. Translation: AAH58627.1.
    CCDSiCCDS36273.1. [Q6PDM2-1]
    CCDS36274.1. [Q6PDM2-2]
    PIRiS26404.
    RefSeqiNP_001071635.1. NM_001078167.2. [Q6PDM2-2]
    NP_775550.2. NM_173374.4. [Q6PDM2-1]
    XP_006543028.1. XM_006542965.1. [Q6PDM2-1]
    UniGeneiMm.391719.

    Genome annotation databases

    EnsembliENSMUST00000079866; ENSMUSP00000133517; ENSMUSG00000018379. [Q6PDM2-2]
    ENSMUST00000139129; ENSMUSP00000120595; ENSMUSG00000018379. [Q6PDM2-1]
    GeneIDi102641923.
    110809.
    KEGGimmu:102641923.
    mmu:110809.
    UCSCiuc007kvc.1. mouse. [Q6PDM2-1]
    uc007kvd.1. mouse. [Q6PDM2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK018176 mRNA. Translation: BAC25546.1 .
    AK078715 mRNA. Translation: BAC37367.1 .
    AK150535 mRNA. Translation: BAE29641.1 .
    AL593853 Genomic DNA. Translation: CAI24416.1 .
    CU406964 Genomic DNA. Translation: CAQ51705.1 .
    BC046773 mRNA. Translation: AAH46773.1 .
    BC058627 mRNA. Translation: AAH58627.1 .
    CCDSi CCDS36273.1. [Q6PDM2-1 ]
    CCDS36274.1. [Q6PDM2-2 ]
    PIRi S26404.
    RefSeqi NP_001071635.1. NM_001078167.2. [Q6PDM2-2 ]
    NP_775550.2. NM_173374.4. [Q6PDM2-1 ]
    XP_006543028.1. XM_006542965.1. [Q6PDM2-1 ]
    UniGenei Mm.391719.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X4C NMR - A 113-207 [» ]
    ProteinModelPortali Q6PDM2.
    SMRi Q6PDM2. Positions 6-102, 116-197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 225922. 8 interactions.
    DIPi DIP-48723N.
    IntActi Q6PDM2. 10 interactions.
    MINTi MINT-1867664.

    PTM databases

    PhosphoSitei Q6PDM2.

    Proteomic databases

    MaxQBi Q6PDM2.
    PaxDbi Q6PDM2.
    PRIDEi Q6PDM2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079866 ; ENSMUSP00000133517 ; ENSMUSG00000018379 . [Q6PDM2-2 ]
    ENSMUST00000139129 ; ENSMUSP00000120595 ; ENSMUSG00000018379 . [Q6PDM2-1 ]
    GeneIDi 102641923.
    110809.
    KEGGi mmu:102641923.
    mmu:110809.
    UCSCi uc007kvc.1. mouse. [Q6PDM2-1 ]
    uc007kvd.1. mouse. [Q6PDM2-2 ]

    Organism-specific databases

    CTDi 6426.
    MGIi MGI:98283. Srsf1.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00700000104103.
    HOVERGENi HBG002295.
    InParanoidi B2KGJ5.
    KOi K12890.
    OrthoDBi EOG76X620.
    PhylomeDBi Q6PDM2.
    TreeFami TF106261.

    Miscellaneous databases

    EvolutionaryTracei Q6PDM2.
    NextBioi 364697.
    PROi Q6PDM2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PDM2.
    Bgeei Q6PDM2.
    CleanExi MM_SFRS1.
    Genevestigatori Q6PDM2.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Bone marrow macrophage, Eye and Medulla oblongata.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Embryonic brain.
    4. Lubec G., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-28.
      Tissue: Brain.
    5. "Characterization and comparison of four serine- and arginine-rich (SR) protein kinases."
      Nayler O., Stamm S., Ullrich A.
      Biochem. J. 326:693-700(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CLK1; CLK2; CLK3 AND CLK4.
    6. "ASF/SF2-regulated CaMKIIdelta alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle."
      Xu X., Yang D., Ding J.-H., Wang W., Chu P.-H., Dalton N.D., Wang H.-Y., Bermingham J.R. Jr., Ye Z., Liu F., Rosenfeld M.G., Manley J.L., Ross J. Jr., Chen J., Xiao R.-P., Cheng H., Fu X.-D.
      Cell 120:59-72(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    8. "Solution structure of RRM domain in splicing factor 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 113-207.

    Entry informationi

    Entry nameiSRSF1_MOUSE
    AccessioniPrimary (citable) accession number: Q6PDM2
    Secondary accession number(s): B2KGJ5
    , Q3UCH2, Q5SXC5, Q8BJV3, Q8C1H9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3