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P78362

- SRPK2_HUMAN

UniProt

P78362 - SRPK2_HUMAN

Protein

SRSF protein kinase 2

Gene

SRPK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (13 Jul 2010)
      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. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. 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.8 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.2 Publications

    Cofactori

    Magnesium.2 Publications

    Enzyme regulationi

    Activated by phosphorylation on Ser-52 and Ser-588.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101ATPBy similarityPROSITE-ProRule annotation
    Sitei139 – 1402Cleavage; by caspase-3
    Active sitei214 – 2141Proton acceptorPROSITE-ProRule annotation
    Sitei403 – 4042Cleavage; by caspase-3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi87 – 959ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: BHF-UCL
    2. ATP binding Source: UniProtKB
    3. magnesium ion binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: BHF-UCL
    2. cell differentiation Source: UniProtKB-KW
    3. innate immune response Source: BHF-UCL
    4. intracellular signal transduction Source: UniProtKB
    5. negative regulation of viral genome replication Source: BHF-UCL
    6. nuclear speck organization Source: BHF-UCL
    7. positive regulation of cell cycle Source: BHF-UCL
    8. positive regulation of cell proliferation Source: BHF-UCL
    9. positive regulation of gene expression Source: BHF-UCL
    10. positive regulation of neuron apoptotic process Source: BHF-UCL
    11. positive regulation of viral genome replication Source: BHF-UCL
    12. protein phosphorylation Source: UniProtKB
    13. regulation of mRNA splicing, via spliceosome Source: UniProtKB
    14. RNA splicing Source: UniProtKB
    15. spliceosomal complex assembly Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation, mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP78362.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SRSF protein kinase 2 (EC:2.7.11.1)
    Alternative name(s):
    SFRS protein kinase 2
    Serine/arginine-rich protein-specific kinase 2
    Short name:
    SR-protein-specific kinase 2
    Cleaved into the following 2 chains:
    Gene namesi
    Name:SRPK2Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:11306. SRPK2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleolus Source: HPA
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36130.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 688688SRSF protein kinase 2PRO_0000086677Add
    BLAST
    Chaini1 – 139139SRSF protein kinase 2 N-terminalPRO_0000414751Add
    BLAST
    Chaini140 – 688549SRSF protein kinase 2 C-terminalPRO_0000414752Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521Phosphoserine; by CK2By similarity
    Modified residuei380 – 3801Phosphoserine2 Publications
    Modified residuei492 – 4921Phosphothreonine; by PKB/AKT11 Publication
    Modified residuei494 – 4941Phosphoserine3 Publications
    Modified residuei497 – 4971Phosphoserine4 Publications
    Modified residuei588 – 5881Phosphoserine; by CK2By similarity

    Post-translational modificationi

    Phosphorylation at Thr-492 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage.6 Publications
    Proteolytically cleaved at Asp-139 and Asp-403 by caspase-3 during apoptotic cell death. Cleavage at Asp-139 which is the major site of cleavage, produces a small N-terminal fragment that translocates into nucleus and promotes VP16-induced apoptosis.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP78362.
    PaxDbiP78362.
    PRIDEiP78362.

    PTM databases

    PhosphoSiteiP78362.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.1 Publication

    Gene expression databases

    ArrayExpressiP78362.
    BgeeiP78362.
    CleanExiHS_SRPK2.
    GenevestigatoriP78362.

    Organism-specific databases

    HPAiHPA015522.
    HPA020876.

    Interactioni

    Subunit structurei

    Interacts with PKB/AKT1 in a phosphorylation-dependent manner. The phosphorylated form (by PKB/AKT1) interacts with YWHAB and YWHAE. Interaction with YWHAB suppresses its cleavage by caspases and inhibits the release of its N-terminal pro-apoptotic fragment. Interacts with SFN. Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARGLU1Q9NWB62EBI-593303,EBI-2808785
    HNRNPCP079102EBI-593303,EBI-357966
    LUC7LQ9NQ292EBI-593303,EBI-473747
    LUC7L2Q9Y3832EBI-593303,EBI-352851
    MMTAG2Q9BU762EBI-593303,EBI-742459
    PRPF38AQ8NAV12EBI-593303,EBI-715374
    RBM23Q86U062EBI-593303,EBI-780319
    RBM39Q144984EBI-593303,EBI-395290
    RBM8AQ9Y5S92EBI-593303,EBI-447231
    SNRNP27Q8WVK22EBI-593303,EBI-2512550
    SNRNP70P086213EBI-593303,EBI-1049228
    SRSF7Q166292EBI-593303,EBI-398885
    SRSF8Q9BRL62EBI-593303,EBI-6380719
    U2AF1Q010814EBI-593303,EBI-632461
    U2AF2P263684EBI-593303,EBI-742339
    YTHDC1Q96MU73EBI-593303,EBI-2849854
    YWHABP319462EBI-593303,EBI-359815

    Protein-protein interaction databases

    BioGridi112611. 214 interactions.
    IntActiP78362. 223 interactions.
    MINTiMINT-1468300.
    STRINGi9606.ENSP00000377262.

    Structurei

    Secondary structure

    1
    688
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni78 – 803
    Beta strandi81 – 899
    Beta strandi91 – 10010
    Turni101 – 1044
    Beta strandi105 – 1128
    Helixi116 – 13419
    Helixi140 – 1445
    Beta strandi150 – 1567
    Beta strandi159 – 1668
    Helixi173 – 1797
    Turni180 – 1823
    Helixi187 – 20620
    Helixi217 – 2193
    Beta strandi220 – 2223
    Helixi226 – 2338
    Helixi518 – 5203
    Turni521 – 5233
    Beta strandi526 – 5283
    Helixi531 – 5333
    Helixi548 – 5503
    Helixi553 – 5575
    Helixi564 – 57916
    Helixi594 – 60613
    Helixi611 – 6144
    Helixi620 – 6234
    Beta strandi630 – 6323
    Helixi641 – 6499
    Helixi653 – 66614
    Helixi671 – 6733
    Helixi677 – 6815
    Helixi684 – 6863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X7GX-ray2.50A51-688[»]
    ProteinModelPortaliP78362.
    SMRiP78362. Positions 64-283, 508-688.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78362.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 684604Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108512.
    KOiK08831.
    OMAiYCPEVKL.
    OrthoDBiEOG70S74X.
    PhylomeDBiP78362.
    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.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78362-1) [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

    MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPPPLPDP TPPEPEEEIL    50
    GSDDEEQEDP ADYCKGGYHP VKIGDLFNGR YHVIRKLGWG HFSTVWLCWD 100
    MQGKRFVAMK VVKSAQHYTE TALDEIKLLK CVRESDPSDP NKDMVVQLID 150
    DFKISGMNGI HVCMVFEVLG HHLLKWIIKS NYQGLPVRCV KSIIRQVLQG 200
    LDYLHSKCKI IHTDIKPENI LMCVDDAYVR RMAAEATEWQ KAGAPPPSGS 250
    AVSTAPQQKP IGKISKNKKK KLKKKQKRQA ELLEKRLQEI EELEREAERK 300
    IIEENITSAA PSNDQDGEYC PEVKLKTTGL EEAAEAETAK DNGEAEDQEE 350
    KEDAEKENIE KDEDDVDQEL ANIDPTWIES PKTNGHIENG PFSLEQQLDD 400
    EDDDEEDCPN PEEYNLDEPN AESDYTYSSS YEQFNGELPN GRHKIPESQF 450
    PEFSTSLFSG SLEPVACGSV LSEGSPLTEQ EESSPSHDRS RTVSASSTGD 500
    LPKAKTRAAD LLVNPLDPRN ADKIRVKIAD LGNACWVHKH FTEDIQTRQY 550
    RSIEVLIGAG YSTPADIWST ACMAFELATG DYLFEPHSGE DYSRDEDHIA 600
    HIIELLGSIP RHFALSGKYS REFFNRRGEL RHITKLKPWS LFDVLVEKYG 650
    WPHEDAAQFT DFLIPMLEMV PEKRASAGEC LRHPWLNS 688
    Length:688
    Mass (Da):77,527
    Last modified:July 13, 2010 - v3
    Checksum:iACCAF2A887444EC2
    GO
    Isoform 2 (identifier: P78362-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MSVNSEKSSSSER → MSSRKVLAIQARKRRPKREKHPKK

    Show »
    Length:699
    Mass (Da):79,029
    Checksum:i70B084ABA32CC3DB
    GO

    Sequence cautioni

    The sequence AAQ63886.1 differs from that shown. Reason: The cDNA appears to contain a duplicated region.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371P → R in AAH68547. (PubMed:15489334)Curated
    Sequence conflicti236 – 2372AT → P in AAC05299. (PubMed:9472028)Curated
    Sequence conflicti521 – 5211A → R in AAC05299. (PubMed:9472028)Curated
    Sequence conflicti601 – 6011H → L in AAC29141. (PubMed:12853948)Curated
    Sequence conflicti608 – 6092SI → KV in AAC29141. (PubMed:12853948)Curated
    Sequence conflicti612 – 6165HFALS → KYAML in AAC29141. (PubMed:12853948)Curated
    Sequence conflicti621 – 6211R → K in AAC29141. (PubMed:12853948)Curated
    Sequence conflicti625 – 6273NRR → TRK in AAC29141. (PubMed:12853948)Curated
    Sequence conflicti640 – 6401S → G in AAH68547. (PubMed:15489334)Curated
    Sequence conflicti681 – 6811Missing in AAC05299. (PubMed:9472028)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431P → L.1 Publication
    Corresponds to variant rs34699980 [ dbSNP | Ensembl ].
    VAR_041114
    Natural varianti243 – 2431G → D in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_041115
    Natural varianti426 – 4261T → P.1 Publication
    Corresponds to variant rs55743527 [ dbSNP | Ensembl ].
    VAR_041116
    Natural varianti486 – 4861S → F.1 Publication
    Corresponds to variant rs56112661 [ dbSNP | Ensembl ].
    VAR_041117
    Natural varianti515 – 5151P → T.1 Publication
    Corresponds to variant rs56017595 [ dbSNP | Ensembl ].
    VAR_041118
    Natural varianti608 – 6081S → N.
    Corresponds to variant rs1050413 [ dbSNP | Ensembl ].
    VAR_060390
    Natural varianti615 – 6151L → I.
    Corresponds to variant rs1050418 [ dbSNP | Ensembl ].
    VAR_057111

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MSVNS…SSSER → MSSRKVLAIQARKRRPKREK HPKK in isoform 2. 1 PublicationVSP_039386Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U88666 mRNA. Translation: AAC05299.1.
    AC005070 Genomic DNA. Translation: AAC29140.1.
    AC005070 Genomic DNA. Translation: AAC29141.1.
    AC004884 Genomic DNA. No translation available.
    AC073138 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83359.1.
    BC035214 mRNA. Translation: AAH35214.1.
    BC068547 mRNA. Translation: AAH68547.1.
    BE781215 mRNA. No translation available.
    AY354201 mRNA. Translation: AAQ63886.1. Sequence problems.
    CCDSiCCDS34724.1. [P78362-2]
    CCDS5735.1. [P78362-1]
    RefSeqiNP_001265202.1. NM_001278273.1. [P78362-1]
    NP_872633.1. NM_182691.2. [P78362-1]
    NP_872634.1. NM_182692.2. [P78362-2]
    UniGeneiHs.285197.

    Genome annotation databases

    EnsembliENST00000357311; ENSP00000349863; ENSG00000135250. [P78362-1]
    ENST00000393651; ENSP00000377262; ENSG00000135250. [P78362-2]
    ENST00000489828; ENSP00000419791; ENSG00000135250. [P78362-1]
    GeneIDi6733.
    KEGGihsa:6733.
    UCSCiuc003vct.4. human. [P78362-1]
    uc003vcv.4. human. [P78362-2]

    Polymorphism databases

    DMDMi300669676.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U88666 mRNA. Translation: AAC05299.1 .
    AC005070 Genomic DNA. Translation: AAC29140.1 .
    AC005070 Genomic DNA. Translation: AAC29141.1 .
    AC004884 Genomic DNA. No translation available.
    AC073138 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83359.1 .
    BC035214 mRNA. Translation: AAH35214.1 .
    BC068547 mRNA. Translation: AAH68547.1 .
    BE781215 mRNA. No translation available.
    AY354201 mRNA. Translation: AAQ63886.1 . Sequence problems.
    CCDSi CCDS34724.1. [P78362-2 ]
    CCDS5735.1. [P78362-1 ]
    RefSeqi NP_001265202.1. NM_001278273.1. [P78362-1 ]
    NP_872633.1. NM_182691.2. [P78362-1 ]
    NP_872634.1. NM_182692.2. [P78362-2 ]
    UniGenei Hs.285197.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X7G X-ray 2.50 A 51-688 [» ]
    ProteinModelPortali P78362.
    SMRi P78362. Positions 64-283, 508-688.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112611. 214 interactions.
    IntActi P78362. 223 interactions.
    MINTi MINT-1468300.
    STRINGi 9606.ENSP00000377262.

    Chemistry

    BindingDBi P78362.
    ChEMBLi CHEMBL5668.
    GuidetoPHARMACOLOGYi 2209.

    PTM databases

    PhosphoSitei P78362.

    Polymorphism databases

    DMDMi 300669676.

    Proteomic databases

    MaxQBi P78362.
    PaxDbi P78362.
    PRIDEi P78362.

    Protocols and materials databases

    DNASUi 6733.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357311 ; ENSP00000349863 ; ENSG00000135250 . [P78362-1 ]
    ENST00000393651 ; ENSP00000377262 ; ENSG00000135250 . [P78362-2 ]
    ENST00000489828 ; ENSP00000419791 ; ENSG00000135250 . [P78362-1 ]
    GeneIDi 6733.
    KEGGi hsa:6733.
    UCSCi uc003vct.4. human. [P78362-1 ]
    uc003vcv.4. human. [P78362-2 ]

    Organism-specific databases

    CTDi 6733.
    GeneCardsi GC07M104751.
    H-InvDB HIX0006976.
    HGNCi HGNC:11306. SRPK2.
    HPAi HPA015522.
    HPA020876.
    MIMi 602980. gene.
    neXtProti NX_P78362.
    PharmGKBi PA36130.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108512.
    KOi K08831.
    OMAi YCPEVKL.
    OrthoDBi EOG70S74X.
    PhylomeDBi P78362.
    TreeFami TF105334.

    Enzyme and pathway databases

    SignaLinki P78362.

    Miscellaneous databases

    ChiTaRSi SRPK2. human.
    EvolutionaryTracei P78362.
    GeneWikii SRPK2.
    GenomeRNAii 6733.
    NextBioi 26266.
    PROi P78362.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78362.
    Bgeei P78362.
    CleanExi HS_SRPK2.
    Genevestigatori P78362.

    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. "SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells."
      Wang H.-Y., Lin W., Dyck J.A., Yeakley J.M., Songyang Z., Cantley L.C., Fu X.-D.
      J. Cell Biol. 140:737-750(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Fetal brain1 Publication.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-99 (ISOFORM 2).
      Tissue: Retinoblastoma, SkinImported and TestisImported.
    5. Sha J.H., Zhou Z.M., Li J.M.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-537 (ISOFORM 1).
      Tissue: TestisImported.
    6. "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: FUNCTION IN PHOSPHORYLATION OF HEPATITIS B VIRUS CORE PROTEIN.
    7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1."
      Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J., Persson J.L., Ye K.
      Cancer Res. 68:4559-4570(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ACIN1, INTERACTION WITH ACIN1.
    11. "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-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome."
      Mathew R., Hartmuth K., Moehlmann S., Urlaub H., Ficner R., Luehrmann R.
      Nat. Struct. Mol. Biol. 15:435-443(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DDX23/PRP28, ASSOCIATION WITH U4/U6-U5 TRI-SNRNPS.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons."
      Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.
      J. Biol. Chem. 284:24512-24525(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-492 BY PKB/AKT1, INTERACTION WITH PKB/AKT1; YWHAB; YWHAE AND SFN.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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-380; SER-494 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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: FUNCTION IN PHOSPHORYLATION OF SRSF2, SUBCELLULAR LOCATION.
    20. "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.
    21. "The N-terminal fragment from caspase-cleaved serine/arginine protein-specific kinase2 (SRPK2) translocates into the nucleus and promotes apoptosis."
      Hong Y., Jang S.W., Ye K.
      J. Biol. Chem. 286:777-786(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CASPASE-3 CLEAVAGE AT ASP-139 AND ASP-403, SUBCELLULAR LOCATION.
    22. "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-494 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-43; ASP-243; PRO-426; PHE-486 AND THR-515.

    Entry informationi

    Entry nameiSRPK2_HUMAN
    AccessioniPrimary (citable) accession number: P78362
    Secondary accession number(s): A8MVX2
    , O75220, O75221, Q6NUL0, Q6V1X2, Q8IYQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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