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Q96SB4

- SRPK1_HUMAN

UniProt

Q96SB4 - SRPK1_HUMAN

Protein

SRSF protein kinase 1

Gene

SRPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using 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 first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 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 RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation.16 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.6 Publications

    Cofactori

    Magnesium.6 Publications

    Enzyme regulationi

    Activated by phosphorylation on Ser-51 and Ser-555.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091ATP1 PublicationPROSITE-ProRule annotation
    Active sitei213 – 2131Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi86 – 949ATP1 PublicationPROSITE-ProRule annotation
    Nucleotide bindingi166 – 1683ATP1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein kinase activity Source: ProtInc
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB
    2. innate immune response Source: BHF-UCL
    3. intracellular signal transduction Source: UniProtKB
    4. mRNA processing Source: UniProtKB-KW
    5. negative regulation of viral genome replication Source: BHF-UCL
    6. positive regulation of viral genome replication Source: BHF-UCL
    7. protein phosphorylation Source: UniProtKB
    8. regulation of mRNA processing Source: UniProtKB
    9. regulation of mRNA splicing, via spliceosome Source: UniProtKB
    10. RNA splicing Source: ProtInc
    11. sperm chromatin condensation Source: UniProtKB
    12. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Chromosome partition, Differentiation, Host-virus interaction, mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ96SB4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SRSF protein kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    SFRS protein kinase 1
    Serine/arginine-rich protein-specific kinase 1
    Short name:
    SR-protein-specific kinase 1
    Gene namesi
    Name:SRPK1Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11305. SRPK1.

    Subcellular locationi

    Isoform 2 : Cytoplasm. Nucleus. Nucleus matrix. Microsome
    Note: Shuttles between the nucleus and the cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus. KAT5/TIP60 inhibits its nuclear translocation.
    Isoform 1 : Cytoplasm. Nucleus matrix. Microsome
    Note: Mainly localized in the microsomal fraction and the cytoplasm, and to a lesser extent in the nuclear matrix.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB-KW
    3. nuclear matrix Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi37 – 371S → A: No effect on protein phosphorylation. 1 Publication
    Mutagenesisi51 – 511S → A: Protein phosphorylation impaired at this position. 1 Publication
    Mutagenesisi222 – 2221S → A: No effect on protein phosphorylation. 1 Publication
    Mutagenesisi311 – 3111S → G: No effect on protein phosphorylation. 1 Publication
    Mutagenesisi436 – 4361S → G: No effect on protein phosphorylation. 1 Publication
    Mutagenesisi555 – 5551S → A: Protein phosphorylation impaired at this position. 1 Publication
    Mutagenesisi619 – 6191S → A: No effect on protein phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA36129.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 655655SRSF protein kinase 1PRO_0000086674Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511Phosphoserine; by CK25 Publications
    Modified residuei309 – 3091PhosphoserineBy similarity
    Modified residuei311 – 3111Phosphoserine1 Publication
    Modified residuei555 – 5551Phosphoserine; by CK21 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96SB4.
    PaxDbiQ96SB4.
    PRIDEiQ96SB4.

    PTM databases

    PhosphoSiteiQ96SB4.

    Expressioni

    Tissue specificityi

    Isoform 2 is predominantly expressed in the testis but is also present at lower levels in heart, ovary, small intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1 is only seen in the testis, at lower levels than isoform 2. Highly expressed in different erythroid and lymphoid cell lines, with isoform 2 being far more abundant than isoform 1.3 Publications

    Gene expression databases

    ArrayExpressiQ96SB4.
    BgeeiQ96SB4.
    CleanExiHS_SRPK1.
    GenevestigatoriQ96SB4.

    Organism-specific databases

    HPAiHPA016431.
    HPA056486.

    Interactioni

    Subunit structurei

    Monomer. Isoform 2 is found in a multisubunit complex containing seven proteins, named toposome, which separates entangled circular chromatin DNA during chromosome segregation. Isoform 2 interacts with HHV-1 ICP27 protein. Isoform 2 interacts with DNAJB1/HSP40 and AHSA1/AHA1 and this mediates formation of a complex with the Hsp70 /Hsp90 machinery. Isoform 1 is found in a complex with: DHX9, MOV10, MATR3, HNRNPU, NCL, DDX21, HSD17B4, PABPC1, HNRNPM, IGF2BP1, SYNCRIP, RPL3, VIM, YBX1, NPM1, HNRNPA2B1, HNRNPC, RPLP0, RPL7A and RALY. Isoform 2 binds to IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Isoform 1 and isoform 2 interact with SAFB which inhibits its activity. Isoform 2 interacts with SAFB2 which inhibits its activity.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A7Y3Z34EBI-539478,EBI-7321730From a different organism.
    DGCR8Q8WYQ53EBI-539478,EBI-528411
    LUC7LQ9NQ292EBI-539478,EBI-473747
    LUC7L2Q9Y3832EBI-539478,EBI-352851
    PRPF38AQ8NAV12EBI-539478,EBI-715374
    RBM39Q144982EBI-539478,EBI-395290
    RBM8AQ9Y5S92EBI-539478,EBI-447231
    RNPS1Q152872EBI-539478,EBI-395959
    SAFBQ154242EBI-5773439,EBI-348298
    SafbO884532EBI-539478,EBI-539530From a different organism.
    SRPK3Q9UPE12EBI-539478,EBI-6381269
    SRSF1Q079553EBI-539478,EBI-398920
    SRSF7Q166292EBI-539478,EBI-398885
    SRSF8Q9BRL62EBI-539478,EBI-6380719
    TP53P046373EBI-539478,EBI-366083
    YTHDC1Q96MU73EBI-539478,EBI-2849854

    Protein-protein interaction databases

    BioGridi112610. 206 interactions.
    DIPiDIP-33888N.
    IntActiQ96SB4. 218 interactions.
    MINTiMINT-262701.
    STRINGi9606.ENSP00000391069.

    Structurei

    Secondary structure

    1
    655
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni77 – 793
    Beta strandi80 – 889
    Beta strandi90 – 9910
    Turni100 – 1034
    Beta strandi104 – 1118
    Helixi115 – 13319
    Helixi139 – 1435
    Beta strandi147 – 1559
    Beta strandi158 – 1658
    Beta strandi168 – 1714
    Helixi172 – 1787
    Turni179 – 1813
    Helixi186 – 20520
    Helixi216 – 2183
    Beta strandi219 – 2213
    Helixi225 – 23511
    Helixi485 – 4906
    Beta strandi493 – 4953
    Helixi498 – 5003
    Beta strandi502 – 5065
    Helixi515 – 5173
    Helixi520 – 5245
    Helixi531 – 54616
    Beta strandi557 – 5593
    Helixi561 – 57313
    Helixi578 – 5836
    Helixi587 – 5893
    Beta strandi595 – 5995
    Helixi608 – 6147
    Helixi620 – 63011
    Helixi631 – 6344
    Helixi638 – 6403
    Helixi644 – 6485
    Helixi651 – 6544

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WAKX-ray1.73A42-655[»]
    1WBPX-ray2.40A42-655[»]
    3BEGX-ray2.90A58-255[»]
    A474-655[»]
    ProteinModelPortaliQ96SB4.
    SMRiQ96SB4. Positions 63-263, 477-655.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96SB4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 653574Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000171558.
    HOVERGENiHBG108512.
    KOiK15409.
    OrthoDBiEOG70S74X.
    PhylomeDBiQ96SB4.
    TreeFamiTF105334.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 2 hits.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 22 Publications (identifier: Q96SB4-2) [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

    MERKVLALQA RKKRTKAKKD KAQRKSETQH RGSAPHSESD LPEQEEEILG    50
    SDDDEQEDPN DYCKGGYHLV KIGDLFNGRY HVIRKLGWGH FSTVWLSWDI 100
    QGKKFVAMKV VKSAEHYTET ALDEIRLLKS VRNSDPNDPN REMVVQLLDD 150
    FKISGVNGTH ICMVFEVLGH HLLKWIIKSN YQGLPLPCVK KIIQQVLQGL 200
    DYLHTKCRII HTDIKPENIL LSVNEQYIRR LAAEATEWQR SGAPPPSGSA 250
    VSTAPQPKPA DKMSKNKKKK LKKKQKRQAE LLEKRMQEIE EMEKESGPGQ 300
    KRPNKQEESE SPVERPLKEN PPNKMTQEKL EESSTIGQDQ TLMERDTEGG 350
    AAEINCNGVI EVINYTQNSN NETLRHKEDL HNANDCDVQN LNQESSFLSS 400
    QNGDSSTSQE TDSCTPITSE VSDTMVCQSS STVGQSFSEQ HISQLQESIR 450
    AEIPCEDEQE QEHNGPLDNK GKSTAGNFLV NPLEPKNAEK LKVKIADLGN 500
    ACWVHKHFTE DIQTRQYRSL EVLIGSGYNT PADIWSTACM AFELATGDYL 550
    FEPHSGEEYT RDEDHIALII ELLGKVPRKL IVAGKYSKEF FTKKGDLKHI 600
    TKLKPWGLFE VLVEKYEWSQ EEAAGFTDFL LPMLELIPEK RATAAECLRH 650
    PWLNS 655
    Length:655
    Mass (Da):74,325
    Last modified:October 14, 2008 - v2
    Checksum:i900E980FE1C16B9A
    GO
    Isoform 1 (identifier: Q96SB4-3) [UniParc]FASTAAdd to Basket

    Also known as: 1a

    The sequence of this isoform differs from the canonical sequence as follows:
         4-4: K → KGERWSGLRH...FALHPSLSPA

    Note: Due to intron retention.

    Show »
    Length:826
    Mass (Da):92,412
    Checksum:i9E4D86DE22A10D32
    GO

    Sequence cautioni

    The sequence CAI20544.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI20545.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101I → T in AAH38292. (PubMed:15489334)Curated
    Sequence conflicti360 – 3601I → L AA sequence (PubMed:12134018)Curated
    Sequence conflicti363 – 3631I → L AA sequence (PubMed:12134018)Curated
    Sequence conflicti400 – 4012SQ → LP in AAA20530. (PubMed:8208298)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721I → T.
    Corresponds to variant rs35519113 [ dbSNP | Ensembl ].
    VAR_051669

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei4 – 41K → KGERWSGLRHEGQWSPGRGP GQRRELRLTAAVRFPDVRRP STEVAPPHTPCLWAAGPRPS FRASSGAGRSRPLFPARPAR ALGPLQGPALGGRRRPPPAR PLTRPETPPAHPARALLCAP WAASPTPAASPSPQPPPRQA PQPGLAPLLGLHPHLGRLLS STFALHPSLSPA in isoform 1. 1 PublicationVSP_042130

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09564 mRNA. Translation: AAA20530.1.
    AJ318054 mRNA. Translation: CAC39299.1.
    Z99128 Genomic DNA. Translation: CAI20544.1. Sequence problems.
    Z99128 Genomic DNA. Translation: CAI20545.1. Sequence problems.
    BC038292 mRNA. Translation: AAH38292.1.
    CCDSiCCDS47415.1. [Q96SB4-2]
    PIRiS45337.
    RefSeqiNP_003128.3. NM_003137.4. [Q96SB4-2]
    UniGeneiHs.443861.

    Genome annotation databases

    EnsembliENST00000373825; ENSP00000362931; ENSG00000096063. [Q96SB4-2]
    GeneIDi6732.
    KEGGihsa:6732.
    UCSCiuc003olh.3. human. [Q96SB4-2]

    Polymorphism databases

    DMDMi209572680.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09564 mRNA. Translation: AAA20530.1 .
    AJ318054 mRNA. Translation: CAC39299.1 .
    Z99128 Genomic DNA. Translation: CAI20544.1 . Sequence problems.
    Z99128 Genomic DNA. Translation: CAI20545.1 . Sequence problems.
    BC038292 mRNA. Translation: AAH38292.1 .
    CCDSi CCDS47415.1. [Q96SB4-2 ]
    PIRi S45337.
    RefSeqi NP_003128.3. NM_003137.4. [Q96SB4-2 ]
    UniGenei Hs.443861.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WAK X-ray 1.73 A 42-655 [» ]
    1WBP X-ray 2.40 A 42-655 [» ]
    3BEG X-ray 2.90 A 58-255 [» ]
    A 474-655 [» ]
    ProteinModelPortali Q96SB4.
    SMRi Q96SB4. Positions 63-263, 477-655.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112610. 206 interactions.
    DIPi DIP-33888N.
    IntActi Q96SB4. 218 interactions.
    MINTi MINT-262701.
    STRINGi 9606.ENSP00000391069.

    Chemistry

    BindingDBi Q96SB4.
    ChEMBLi CHEMBL4375.
    GuidetoPHARMACOLOGYi 2208.

    PTM databases

    PhosphoSitei Q96SB4.

    Polymorphism databases

    DMDMi 209572680.

    Proteomic databases

    MaxQBi Q96SB4.
    PaxDbi Q96SB4.
    PRIDEi Q96SB4.

    Protocols and materials databases

    DNASUi 6732.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373825 ; ENSP00000362931 ; ENSG00000096063 . [Q96SB4-2 ]
    GeneIDi 6732.
    KEGGi hsa:6732.
    UCSCi uc003olh.3. human. [Q96SB4-2 ]

    Organism-specific databases

    CTDi 6732.
    GeneCardsi GC06M035801.
    H-InvDB HIX0005813.
    HGNCi HGNC:11305. SRPK1.
    HPAi HPA016431.
    HPA056486.
    MIMi 601939. gene.
    neXtProti NX_Q96SB4.
    PharmGKBi PA36129.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000171558.
    HOVERGENi HBG108512.
    KOi K15409.
    OrthoDBi EOG70S74X.
    PhylomeDBi Q96SB4.
    TreeFami TF105334.

    Enzyme and pathway databases

    SignaLinki Q96SB4.

    Miscellaneous databases

    EvolutionaryTracei Q96SB4.
    GeneWikii SRPK1.
    GenomeRNAii 6732.
    NextBioi 26262.
    PROi Q96SB4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96SB4.
    Bgeei Q96SB4.
    CleanExi HS_SRPK1.
    Genevestigatori Q96SB4.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A serine kinase regulates intracellular localization of splicing factors in the cell cycle."
      Gui J.F., Lane W.S., Fu X.-D.
      Nature 369:678-682(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
      Tissue: Cervix carcinoma.
    2. "Cloning and characterization of an alternatively spliced form of SR protein kinase 1 that interacts specifically with scaffold attachment factor-B."
      Nikolakaki E., Kohen R., Hartmann A.M., Stamm S., Georgatsou E., Giannakouros T.
      J. Biol. Chem. 276:40175-40182(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SAFB.
      Tissue: Testis1 Publication.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: TestisImported.
    5. "Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein."
      Daub H., Blencke S., Habenberger P., Kurtenbach A., Dennenmoser J., Wissing J., Ullrich A., Cotten M.
      J. Virol. 76:8124-8137(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 330-345 AND 353-375, FUNCTION IN PHOSPHORYLATION OF HEPATITIS B VIRUS CORE PROTEIN.
    6. "Identification of toposome, a novel multisubunit complex containing topoisomerase IIalpha."
      Lee C.G., Hague L.K., Li H., Donnelly R.
      Cell Cycle 3:638-647(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 376-400 AND 616-636, FUNCTION, IDENTIFICATION IN A TOPOSOME COMPLEX.
    7. "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: FUNCTION, INTERACTION WITH ZRSR2.
    8. "SRPK1 and LBR protein kinases show identical substrate specificities."
      Papoutsopoulou S., Nikolakaki E., Giannakouros T.
      Biochem. Biophys. Res. Commun. 255:602-607(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LBR.
    9. "SR protein-specific kinase 1 is highly expressed in testis and phosphorylates protamine 1."
      Papoutsopoulou S., Nikolakaki E., Chalepakis G., Kruft V., Chevaillier P., Giannakouros T.
      Nucleic Acids Res. 27:2972-2980(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PRM1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "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: FUNCTION, INTERACTION WITH SFRS1.
    11. "Protein kinase CK2 phosphorylates and activates the SR protein-specific kinase 1."
      Mylonis I., Giannakouros T.
      Biochem. Biophys. Res. Commun. 301:650-656(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-51 AND SER-555, MUTAGENESIS OF SER-37; SER-51; SER-222; SER-311; SER-436; SER-555 AND SER-619.
    12. "Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a pathway independent of the phosphorylation of the viral core protein."
      Zheng Y., Fu X.D., Ou J.H.
      Virology 342:150-158(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEGATIVE REGULATION OF HEPATITIS B VIRUS (HBV) REPLICATION.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
    15. "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: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
    16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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].
    19. "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: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
    20. "The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2."
      Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T., Georgatsou E.
      FEBS J. 276:5212-5227(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAFB/SAFB1 AND SAFB2.
    21. "Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
      Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
      Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNAJB1/HSP40 AND AHSA1/AHA1.
    22. "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: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
    23. "Arginine methylation of the ICP27 RGG box regulates the functional interactions of ICP27 with SRPK1 and Aly/REF during herpes simplex virus 1 infection."
      Souki S.K., Sandri-Goldin R.M.
      J. Virol. 83:8970-8975(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-1 ICP27 PROTEIN.
    24. "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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION OF ISOFORM 1 IN A COMPLEX WITH DHX9; MOV10; MATR3; HNRNPU; NCL; DDX21; HSD17B4; PABPC1; HNRNPM; IGF2BP1; SYNCRIP; RPL3; VIM; YBX1; NPM1; HNRNPA2B1; HNRNPC; RPLP0; RPL7A AND RALY.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
      Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
      EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    28. "Serine-arginine protein kinases: a small protein kinase family with a large cellular presence."
      Giannakouros T., Nikolakaki E., Mylonis I., Georgatsou E.
      FEBS J. 278:570-586(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    29. "Phosphorylation mechanism and structure of serine-arginine protein kinases."
      Ghosh G., Adams J.A.
      FEBS J. 278:587-597(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    30. "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-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2."
      Ngo J.C.K., Chakrabarti S., Ding J.-H., Velazquez-Dones A., Nolen B., Aubol B.E., Adams J.A., Fu X.-D., Ghosh G.
      Mol. Cell 20:77-89(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-438 IN COMPLEX WITH ATP AND SUBSTRATE PEPTIDE, FUNCTION, INTERACTION WITH SFRS1.
    32. Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 42-655, SUBUNIT.
    33. "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 58-655 IN COMPLEX WITH SRSF1, MECHANISM OF PHOSPHORYLATION OF SRSF1.

    Entry informationi

    Entry nameiSRPK1_HUMAN
    AccessioniPrimary (citable) accession number: Q96SB4
    Secondary accession number(s): Q12890
    , Q5R364, Q5R365, Q8IY12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 132 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 6
      Human chromosome 6: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3