SRSF protein kinase 1 - Mus musculus (Mouse)

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O70551 (SRPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Srpk1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. 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. 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. Can induce splicing of exon 10 in MAPT/TAU By similarity. Ref.1 Ref.2
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.2
Cofactor	Magnesium. Ref.1 Ref.2
Enzyme regulation	Activated by phosphorylation on Ser-51 and Ser-548 By similarity. UniProtKB Q96SB4
Subunit structure	Monomer. Found in a multisubunit complex containing seven proteins, named toposome, which separates entangled circular chromatin DNA during chromosome segregation. Interacts with HHV-1 ICP27 protein. Interacts with DNAJB1/HSP40 and AHSA1/AHA1 and this mediates formation of a complex with the Hsp70 /Hsp90 machinery. Binds to IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Interacts with SAFB/SAFB1 and SAFB2 which inhibits its activity By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Nucleus matrix By similarity. Microsome By similarity. 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 By similarity. Ref.1
Tissue specificity	Predominantly expressed in the testis but is also present at lower levels in heart, spleen, liver, brain, kidney, lung and skeletal muscle. Present in all germinal cells in the seminiferous tubules but not in mature spermatozoa. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Chromosome partition Differentiation mRNA processing mRNA splicing
Cellular component	Cytoplasm Endoplasmic reticulum Microsome Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay Ref.1. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW regulation of mRNA processing Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.1. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRSF1	Q07955	5	EBI-593343,EBI-398920	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 648

648

SRSF protein kinase 1

PRO_0000086675

Regions

Domain

80 – 646

567

Protein kinase

Nucleotide binding

86 – 94

ATP By similarity UniProtKB Q9UPE1

Sites

Active site

213

Proton acceptor By similarity UniProtKB Q9UPE1

Binding site

109

ATP By similarity UniProtKB Q9UPE1

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.8 UniProtKB Q96SB4

Modified residue

309

Phosphoserine Ref.7

Modified residue

311

Phosphoserine Ref.7

Modified residue

448

Phosphothreonine Ref.5 Ref.6 Ref.7

Modified residue

450

Phosphoserine Ref.5 Ref.6 Ref.7

Modified residue

548

Phosphoserine; by CK2 By similarity UniProtKB Q96SB4

Modified residue

578

N6-acetyllysine By similarity

Experimental info

Sequence conflict

113

S → I in CAA11833. Ref.2

Sequence conflict

155

G → V in CAA11833. Ref.2

Sequence conflict

256

Q → T in CAA11833. Ref.2

Sequence conflict

279

A → P in BAA25299. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O70551 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: CB779C163A11ECEB
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FASTA

648

73,088

        10         20         30         40         50         60 
MERKVLALQA RKKRTKAKKD KAQRKPETQH RGSAPHSESD IPEQEEEILG SDDDEQEDPN 

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

       130        140        150        160        170        180 
ALDEIRLLKS VRNSDPNDPN GEMVVQLLDD 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 SPVDRPLTEN PPNKMTQEKL EESNSIGQDQ TLTERGGEGG APEINCNGVI 

       370        380        390        400        410        420 
GVVNYPENSN NETLRHKEDL HNANDCDVHT LKQEPSFLNS SNGDSSPSQD TDSCTPTASE 

       430        440        450        460        470        480 
TMVCQSSAEQ SLTRQDITQL EESIRADTPS GDEQEPNGAL DSKGKFSAGN FLINPLEPKN 

       490        500        510        520        530        540 
AEKLQVKIAD LGNACWVHKH FTEDIQTRQY RSLEVLIGSG YNTPADIWST ACMAFELATG 

       550        560        570        580        590        600 
DYLFEPHSGE DYTRDEDHIA LIIELLGKVP RKLIVAGKYS KEFFTKKGDL KHITKLKPWG 

       610        620        630        640 
LLEVLVEKYE WPQEEAAGFT DFLLPMLELM PEKRATAAEC LRHPWLNS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel SR-protein-specific kinase, SRPK2, disassembles nuclear speckles." Kuroyanagi N., Onogi H., Wakabayashi T., Hagiwara M. Biochem. Biophys. Res. Commun. 242:357-364(1998) [PubMed: 9446799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Brain.
[2]	"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: 10390541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Embryo.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland and Testis.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 573-581, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND SER-450, MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND SER-450, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-311; THR-448 AND SER-450, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012290 mRNA. Translation: BAA25299.1. AJ224115 mRNA. Translation: CAA11833.1. BC005707 mRNA. Translation: AAH05707.1. BC050761 mRNA. Translation: AAH50761.1.
IPI	IPI00387234.
PIR	JC5930.
RefSeq	NP_058075.2. NM_016795.3.
UniGene	Mm.15252. Mm.479188.
3D structure databases
ProteinModelPortal	O70551.
SMR	O70551. Positions 63-648.
ModBase	Search...
Protein-protein interaction databases
IntAct	O70551. 1 interaction.
STRING	O70551.
PTM databases
PhosphoSite	O70551.
Proteomic databases
PRIDE	O70551.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000130643; ENSMUSP00000116259; ENSMUSG00000004865.
GeneID	20815.
KEGG	mmu:20815.
Organism-specific databases
CTD	6732.
MGI	MGI:106908. Srpk1.
Phylogenomic databases
eggNOG	roNOG04128.
GeneTree	ENSGT00530000063566.
HOGENOM	HBG755340.
HOVERGEN	HBG108512.
InParanoid	O70551.
OMA	HISQLQE.
PhylomeDB	O70551.
Gene expression databases
ArrayExpress	O70551.
Bgee	O70551.
CleanEx	MM_SRPK1.
Genevestigator	O70551.
GermOnline	ENSMUSG00000004865. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
KO	K15409.
Pfam	PF00069. Pkinase. 2 hits. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	299541.
SOURCE	Search...

Entry information

Entry name

SRPK1_MOUSE

Accession

Primary (citable) accession number: O70551
Secondary accession number(s): O70193, Q99JT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents