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Q96SB4 (SRPK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. 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 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 names
Name:SRPK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
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. 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/isoform2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.19 Ref.21 Ref.22 Ref.25 Ref.31

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.2 Ref.5 Ref.6 Ref.10 Ref.11

Cofactor

Magnesium. Ref.1 Ref.2 Ref.5 Ref.6 Ref.10 Ref.11

Enzyme regulation

Activated by phosphorylation on Ser-51 and Ser-555. Ref.11

Subunit structure

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. Ref.2 Ref.6 Ref.7 Ref.10 Ref.20 Ref.21 Ref.23 Ref.31 Ref.32

Subcellular location

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. Ref.2 Ref.9 Ref.21 Ref.25 Ref.27

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. Ref.2 Ref.9 Ref.21 Ref.25 Ref.27

Tissue specificity

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. Ref.2 Ref.9 Ref.25

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processChromosome partition
Differentiation
Host-virus interaction
mRNA processing
mRNA splicing
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement Ref.1. Source: ProtInc

chromosome segregation

Inferred from direct assay Ref.6. Source: UniProtKB

innate immune response

Inferred by curator PubMed 12417631. Source: BHF-UCL

intracellular signal transduction

Inferred from direct assay Ref.2. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of viral genome replication

Inferred from direct assay PubMed 12417631. 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.2Ref.7. Source: UniProtKB

regulation of mRNA processing

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of mRNA splicing, via spliceosome

Traceable author statement Ref.28. Source: UniProtKB

sperm chromatin condensation

Traceable author statement Ref.28. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from direct assay Ref.2. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.2. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20. Source: IntAct

protein kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 Ref.1 Ref.2 (identifier: Q96SB4-2)

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 1 Ref.2 (identifier: Q96SB4-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655SRSF protein kinase 1
PRO_0000086674

Regions

Domain80 – 653574Protein kinase
Nucleotide binding86 – 949ATP
Nucleotide binding166 – 1683ATP

Sites

Active site2131Proton acceptor
Binding site1091ATP

Amino acid modifications

Modified residue511Phosphoserine; by CK2 Ref.11 Ref.13 Ref.16 Ref.17 Ref.24
Modified residue3091Phosphoserine By similarity
Modified residue3111Phosphoserine Ref.30
Modified residue5551Phosphoserine; by CK2 Ref.11

Natural variations

Alternative sequence41K → KGERWSGLRHEGQWSPGRGP GQRRELRLTAAVRFPDVRRP STEVAPPHTPCLWAAGPRPS FRASSGAGRSRPLFPARPAR ALGPLQGPALGGRRRPPPAR PLTRPETPPAHPARALLCAP WAASPTPAASPSPQPPPRQA PQPGLAPLLGLHPHLGRLLS STFALHPSLSPA in isoform 1.
VSP_042130
Natural variant721I → T.
Corresponds to variant rs35519113 [ dbSNP | Ensembl ].
VAR_051669

Experimental info

Mutagenesis371S → A: No effect on protein phosphorylation. Ref.11
Mutagenesis511S → A: Protein phosphorylation impaired at this position. Ref.11
Mutagenesis2221S → A: No effect on protein phosphorylation. Ref.11
Mutagenesis3111S → G: No effect on protein phosphorylation. Ref.11
Mutagenesis4361S → G: No effect on protein phosphorylation. Ref.11
Mutagenesis5551S → A: Protein phosphorylation impaired at this position. Ref.11
Mutagenesis6191S → A: No effect on protein phosphorylation. Ref.11
Sequence conflict2101I → T in AAH38292. Ref.4
Sequence conflict3601I → L AA sequence Ref.5
Sequence conflict3631I → L AA sequence Ref.5
Sequence conflict400 – 4012SQ → LP in AAA20530. Ref.1

Secondary structure

.............................................................. 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 900E980FE1C16B9A

FASTA65574,325
        10         20         30         40         50         60 
MERKVLALQA RKKRTKAKKD KAQRKSETQH RGSAPHSESD LPEQEEEILG SDDDEQEDPN 

        70         80         90        100        110        120 
DYCKGGYHLV KIGDLFNGRY HVIRKLGWGH FSTVWLSWDI QGKKFVAMKV VKSAEHYTET 

       130        140        150        160        170        180 
ALDEIRLLKS VRNSDPNDPN REMVVQLLDD FKISGVNGTH ICMVFEVLGH HLLKWIIKSN 

       190        200        210        220        230        240 
YQGLPLPCVK KIIQQVLQGL DYLHTKCRII HTDIKPENIL LSVNEQYIRR LAAEATEWQR 

       250        260        270        280        290        300 
SGAPPPSGSA VSTAPQPKPA DKMSKNKKKK LKKKQKRQAE LLEKRMQEIE EMEKESGPGQ 

       310        320        330        340        350        360 
KRPNKQEESE SPVERPLKEN PPNKMTQEKL EESSTIGQDQ TLMERDTEGG AAEINCNGVI 

       370        380        390        400        410        420 
EVINYTQNSN NETLRHKEDL HNANDCDVQN LNQESSFLSS QNGDSSTSQE TDSCTPITSE 

       430        440        450        460        470        480 
VSDTMVCQSS STVGQSFSEQ HISQLQESIR AEIPCEDEQE QEHNGPLDNK GKSTAGNFLV 

       490        500        510        520        530        540 
NPLEPKNAEK LKVKIADLGN ACWVHKHFTE DIQTRQYRSL EVLIGSGYNT PADIWSTACM 

       550        560        570        580        590        600 
AFELATGDYL FEPHSGEEYT RDEDHIALII ELLGKVPRKL IVAGKYSKEF FTKKGDLKHI 

       610        620        630        640        650 
TKLKPWGLFE VLVEKYEWSQ EEAAGFTDFL LPMLELIPEK RATAAECLRH PWLNS 

« Hide

Isoform 1 (1a) [UniParc].

Checksum: 9E4D86DE22A10D32
Show »

FASTA82692,412

References

« Hide 'large scale' references
[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: Testis.
[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. expand/collapse author list , 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: Testis.
[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]"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-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]"The ratio of SRPK1/SRPK1a regulates erythroid differentiation in K562 leukaemic cells."
Sanidas I., Kotoula V., Ritou E., Daans J., Lenz C., Mairhofer M., Daniilidou M., Kolbus A., Kruft V., Ponsaerts P., Nikolakaki E.
Biochim. Biophys. Acta 1803:1319-1331(2010) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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]"SR protein kinase 1 is resilient to inactivation."
Ngo J.C., Gullingsrud J., Giang K., Yeh M.J., Fu X.D., Adams J.A., McCammon J.A., Ghosh G.
Structure 15:123-133(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47415.1. [Q96SB4-2]
PIRS45337.
RefSeqNP_003128.3. NM_003137.4. [Q96SB4-2]
UniGeneHs.443861.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WAKX-ray1.73A42-655[»]
1WBPX-ray2.40A42-655[»]
3BEGX-ray2.90A58-255[»]
A474-655[»]
ProteinModelPortalQ96SB4.
SMRQ96SB4. Positions 63-263, 477-655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112610. 206 interactions.
IntActQ96SB4. 218 interactions.
MINTMINT-262701.
STRING9606.ENSP00000391069.

Chemistry

BindingDBQ96SB4.
ChEMBLCHEMBL4375.
GuidetoPHARMACOLOGY2208.

PTM databases

PhosphoSiteQ96SB4.

Polymorphism databases

DMDM209572680.

Proteomic databases

MaxQBQ96SB4.
PaxDbQ96SB4.
PRIDEQ96SB4.

Protocols and materials databases

DNASU6732.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373825; ENSP00000362931; ENSG00000096063. [Q96SB4-2]
GeneID6732.
KEGGhsa:6732.
UCSCuc003olh.3. human. [Q96SB4-2]

Organism-specific databases

CTD6732.
GeneCardsGC06M035801.
H-InvDBHIX0005813.
HGNCHGNC:11305. SRPK1.
HPAHPA016431.
HPA056486.
MIM601939. gene.
neXtProtNX_Q96SB4.
PharmGKBPA36129.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000171558.
HOVERGENHBG108512.
KOK15409.
OrthoDBEOG70S74X.
PhylomeDBQ96SB4.
TreeFamTF105334.

Enzyme and pathway databases

SignaLinkQ96SB4.

Gene expression databases

ArrayExpressQ96SB4.
BgeeQ96SB4.
CleanExHS_SRPK1.
GenevestigatorQ96SB4.

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

EvolutionaryTraceQ96SB4.
GeneWikiSRPK1.
GenomeRNAi6732.
NextBio26262.
PROQ96SB4.
SOURCESearch...

Entry information

Entry nameSRPK1_HUMAN
AccessionPrimary (citable) accession number: Q96SB4
Secondary accession number(s): Q12890 expand/collapse secondary AC list , Q5R364, Q5R365, Q8IY12
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 131 of the entry and version 2 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 6

Human chromosome 6: entries, gene names and cross-references to MIM