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P78362 (SRPK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:SRPK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.8 Ref.10 Ref.12 Ref.15 Ref.19 Ref.21

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.6

Cofactor

Magnesium. Ref.1 Ref.6

Enzyme regulation

Activated by phosphorylation on Ser-52 and Ser-588 By similarity. UniProtKB Q96SB4

Subunit structure

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). Ref.10 Ref.15

Subcellular location

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. Ref.1 Ref.19 Ref.21

Tissue specificity

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

Post-translational modification

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.

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. Ref.21

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
mRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from direct assay Ref.1. Source: UniProtKB

angiogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred by curator PubMed 12417631. Source: BHF-UCL

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay PubMed 12417631. Source: BHF-UCL

nuclear speck organization

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell cycle

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay Ref.10. Source: BHF-UCL

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of viral genome replication

Inferred from direct assay PubMed 20498328. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of mRNA splicing, via spliceosome

Traceable author statement Ref.20. Source: UniProtKB

spliceosomal complex assembly

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_function14-3-3 protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

ATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78362-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P78362-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 688688SRSF protein kinase 2
PRO_0000086677
Chain1 – 139139SRSF protein kinase 2 N-terminal
PRO_0000414751
Chain140 – 688549SRSF protein kinase 2 C-terminal
PRO_0000414752

Regions

Domain81 – 684604Protein kinase
Nucleotide binding87 – 959ATP By similarity UniProtKB Q9UPE1

Sites

Active site2141Proton acceptor By similarity
Binding site1101ATP By similarity UniProtKB Q9UPE1
Site139 – 1402Cleavage; by caspase-3
Site403 – 4042Cleavage; by caspase-3

Amino acid modifications

Modified residue521Phosphoserine; by CK2 By similarity UniProtKB Q96SB4
Modified residue3801Phosphoserine Ref.11 Ref.17
Modified residue4921Phosphothreonine; by PKB/AKT1 Ref.15
Modified residue4941Phosphoserine Ref.13 Ref.17 Ref.22
Modified residue4971Phosphoserine Ref.9 Ref.13 Ref.17 Ref.22
Modified residue5881Phosphoserine; by CK2 By similarity UniProtKB Q96SB4

Natural variations

Alternative sequence1 – 1313MSVNS…SSSER → MSSRKVLAIQARKRRPKREK HPKK in isoform 2.
VSP_039386
Natural variant431P → L. Ref.23
Corresponds to variant rs34699980 [ dbSNP | Ensembl ].
VAR_041114
Natural variant2431G → D in a glioblastoma multiforme sample; somatic mutation. Ref.23
VAR_041115
Natural variant4261T → P. Ref.23
Corresponds to variant rs55743527 [ dbSNP | Ensembl ].
VAR_041116
Natural variant4861S → F. Ref.23
Corresponds to variant rs56112661 [ dbSNP | Ensembl ].
VAR_041117
Natural variant5151P → T. Ref.23
Corresponds to variant rs56017595 [ dbSNP | Ensembl ].
VAR_041118
Natural variant6081S → N.
Corresponds to variant rs1050413 [ dbSNP | Ensembl ].
VAR_060390
Natural variant6151L → I.
Corresponds to variant rs1050418 [ dbSNP | Ensembl ].
VAR_057111

Experimental info

Sequence conflict1371P → R in AAH68547. Ref.4
Sequence conflict236 – 2372AT → P in AAC05299. Ref.1
Sequence conflict5211A → R in AAC05299. Ref.1
Sequence conflict6011H → L in AAC29141. Ref.2
Sequence conflict608 – 6092SI → KV in AAC29141. Ref.2
Sequence conflict612 – 6165HFALS → KYAML in AAC29141. Ref.2
Sequence conflict6211R → K in AAC29141. Ref.2
Sequence conflict625 – 6273NRR → TRK in AAC29141. Ref.2
Sequence conflict6401S → G in AAH68547. Ref.4
Sequence conflict6811Missing in AAC05299. Ref.1

Secondary structure

......................................................... 688
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 13, 2010. Version 3.
Checksum: ACCAF2A887444EC2

FASTA68877,527
        10         20         30         40         50         60 
MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPPPLPDP TPPEPEEEIL GSDDEEQEDP 

        70         80         90        100        110        120 
ADYCKGGYHP VKIGDLFNGR YHVIRKLGWG HFSTVWLCWD MQGKRFVAMK VVKSAQHYTE 

       130        140        150        160        170        180 
TALDEIKLLK CVRESDPSDP NKDMVVQLID DFKISGMNGI HVCMVFEVLG HHLLKWIIKS 

       190        200        210        220        230        240 
NYQGLPVRCV KSIIRQVLQG LDYLHSKCKI IHTDIKPENI LMCVDDAYVR RMAAEATEWQ 

       250        260        270        280        290        300 
KAGAPPPSGS AVSTAPQQKP IGKISKNKKK KLKKKQKRQA ELLEKRLQEI EELEREAERK 

       310        320        330        340        350        360 
IIEENITSAA PSNDQDGEYC PEVKLKTTGL EEAAEAETAK DNGEAEDQEE KEDAEKENIE 

       370        380        390        400        410        420 
KDEDDVDQEL ANIDPTWIES PKTNGHIENG PFSLEQQLDD EDDDEEDCPN PEEYNLDEPN 

       430        440        450        460        470        480 
AESDYTYSSS YEQFNGELPN GRHKIPESQF PEFSTSLFSG SLEPVACGSV LSEGSPLTEQ 

       490        500        510        520        530        540 
EESSPSHDRS RTVSASSTGD LPKAKTRAAD LLVNPLDPRN ADKIRVKIAD LGNACWVHKH 

       550        560        570        580        590        600 
FTEDIQTRQY RSIEVLIGAG YSTPADIWST ACMAFELATG DYLFEPHSGE DYSRDEDHIA 

       610        620        630        640        650        660 
HIIELLGSIP RHFALSGKYS REFFNRRGEL RHITKLKPWS LFDVLVEKYG WPHEDAAQFT 

       670        680 
DFLIPMLEMV PEKRASAGEC LRHPWLNS 

« Hide

Isoform 2 [UniParc].

Checksum: 70B084ABA32CC3DB
Show »

FASTA69979,029

References

« Hide 'large scale' references
[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 brain.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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, Skin and Testis.
[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: Testis.
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001265202.1. NM_001278273.1.
NP_872633.1. NM_182691.2.
NP_872634.1. NM_182692.2.
UniGeneHs.285197.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X7GX-ray2.50A51-688[»]
ProteinModelPortalP78362.
SMRP78362. Positions 64-688.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112611. 213 interactions.
IntActP78362. 223 interactions.
MINTMINT-1468300.
STRING9606.ENSP00000377262.

Chemistry

BindingDBP78362.
ChEMBLCHEMBL5668.
GuidetoPHARMACOLOGY2209.

PTM databases

PhosphoSiteP78362.

Polymorphism databases

DMDM300669676.

Proteomic databases

PaxDbP78362.
PRIDEP78362.

Protocols and materials databases

DNASU6733.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357311; ENSP00000349863; ENSG00000135250. [P78362-1]
ENST00000393651; ENSP00000377262; ENSG00000135250. [P78362-2]
ENST00000489828; ENSP00000419791; ENSG00000135250. [P78362-1]
GeneID6733.
KEGGhsa:6733.
UCSCuc003vct.4. human. [P78362-1]
uc003vcv.4. human. [P78362-2]

Organism-specific databases

CTD6733.
GeneCardsGC07M104751.
H-InvDBHIX0006976.
HGNCHGNC:11306. SRPK2.
HPAHPA015522.
HPA020876.
MIM602980. gene.
neXtProtNX_P78362.
PharmGKBPA36130.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108512.
KOK08831.
OMAPSNEQDD.
OrthoDBEOG70S74X.
PhylomeDBP78362.
TreeFamTF105334.

Enzyme and pathway databases

SignaLinkP78362.

Gene expression databases

ArrayExpressP78362.
BgeeP78362.
CleanExHS_SRPK2.
GenevestigatorP78362.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRPK2. human.
EvolutionaryTraceP78362.
GeneWikiSRPK2.
GenomeRNAi6733.
NextBio26266.
PROP78362.
SOURCESearch...

Entry information

Entry nameSRPK2_HUMAN
AccessionPrimary (citable) accession number: P78362
Secondary accession number(s): A8MVX2 expand/collapse secondary AC list , O75220, O75221, Q6NUL0, Q6V1X2, Q8IYQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM