Serine/threonine-protein kinase VRK1

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Reviewed, UniProtKB/Swiss-Prot Q99986 (VRK1_HUMAN)

Last modified June 16, 2009. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase VRK1
    EC=2.7.11.1
Alternative name(s):
    Vaccinia-related kinase 1

Gene names

Name:

VRK1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Serine/threonine kinase that phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Active in presence of Mn²⁺, Mg²⁺ and Zn²⁺, but is not functional with Ca²⁺ or Cu²⁺. Has a higher affinity for Mn²⁺ than for Mg²⁺. Ref.4
Subcellular location	Nucleus. Note: Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis. Ref.3
Tissue specificity	Widely expressed. Highly expressed in fetal liver, testis and thymus. Ref.1
Post-translational modification	Autophosphorylated at various serine and threonine residues. Autophosphorylation does not impair its ability to phosphorylate p53/TP53. Ref.3 Ref.4
Sequence similarities	Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. VRK subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.3 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATF2	P15336	1	EBI-1769146,EBI-1170906
JUN	P05412	3	EBI-1769146,EBI-852823
PLK3	Q9H4B4	6	EBI-1769146,EBI-751877
RAN	P62826	4	EBI-1769146,EBI-286642
Tp53	P02340	1	EBI-1769146,EBI-474016	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Serine/threonine-protein kinase VRK1

PRO_0000086803

Regions

Domain

37 – 317

281

Protein kinase

Nucleotide binding

43 – 51

ATP By similarity

Sites

Active site

177

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

355

Phosphothreonine; by autocatalysis

Experimental info

Mutagenesis

S → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

102

T → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

125

S → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

150

S → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

158

S → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

239

S → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

305

T → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

312

T → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

355

T → A: Does not abolish autophosphorylation. Ref.3

Mutagenesis

390

T → A: Does not abolish autophosphorylation. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

Q99986-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 5640C624BF059949
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FASTA

396

45,476

        10         20         30         40         50         60 
MPRVKAAQAG RQSSAKRHLA EQFAVGEIIT DMAKKEWKVG LPIGQGGFGC IYLADMNSSE 

        70         80         90        100        110        120 
SVGSDAPCVV KVEPSDNGPL FTELKFYQRA AKPEQIQKWI RTRKLKYLGV PKYWGSGLHD 

       130        140        150        160        170        180 
KNGKSYRFMI MDRFGSDLQK IYEANAKRFS RKTVLQLSLR ILDILEYIHE HEYVHGDIKA 

       190        200        210        220        230        240 
SNLLLNYKNP DQVYLVDYGL AYRYCPEGVH KEYKEDPKRC HDGTIEFTSI DAHNGVAPSR 

       250        260        270        280        290        300 
RGDLEILGYC MIQWLTGHLP WEDNLKDPKY VRDSKIRYRE NIASLMDKCF PEKNKPGEIA 

       310        320        330        340        350        360 
KYMETVKLLD YTEKPLYENL RDILLQGLKA IGSKDDGKLD LSVVENGGLK AKTITKKRKK 

       370        380        390 
EIEESKEPGV EDTEWSNTQT EEAIQTRSRT RKRVQK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to Vaccinia virus B1R kinase." Nezu J., Oku A., Jones M.H., Shimane M. Genomics 45:327-331(1997) [PubMed: 9344656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Fetal liver.
[2]	"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]. Tissue: Brain and Lung.
[3]	"The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein." Lopez-Borges S., Lazo P.A. Oncogene 19:3656-3664(2000) [PubMed: 10951572] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF SER-14; THR-102; SER-125; SER-150; SER-158; SER-239; THR-305; THR-312; THR-355 AND THR-390.
[4]	"Kinetic properties of p53 phosphorylation by the human vaccinia-related kinase 1." Barcia R., Lopez-Borges S., Vega F.M., Lazo P.A. Arch. Biochem. Biophys. 399:1-5(2002) [PubMed: 11883897] [Abstract] Cited for: AUTOPHOSPHORYLATION, ENZYME REGULATION.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases
	AB000449 mRNA. Translation: BAA19108.1. BC103761 mRNA. Translation: AAI03762.1. BC112075 mRNA. Translation: AAI12076.1. BC113510 mRNA. Translation: AAI13511.1.
IPI	IPI00019640.
RefSeq	NP_003375.1.
UniGene	Hs.422662
3D structure databases
HSSP	HSSP built from PDB template 1CKI based on UniProtKB Q06486.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99986. 11 interactions.
PTM databases
PhosphoSite	Q99986.
Proteomic databases
PeptideAtlas	Q99986.
PRIDE	Q99986.
Genome annotation databases
Ensembl	ENSG00000100749. Homo sapiens. [Contig view]
GeneID	7443.
KEGG	hsa:7443.
Organism-specific databases
GeneCards	GC14P096333.
H-InvDB	HIX0037640.
HGNC	HGNC:12718. VRK1.
HPA	HPA000660.
MIM	602168. gene.
PharmGKB	PA37330.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q99986.
HOVERGEN	Q99986.
OMA	Q99986. NKPGEIA.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Gene expression databases
ArrayExpress	Q99986.
Bgee	Q99986.
CleanEx	HS_VRK1.
GermOnline	ENSG00000100749. Homo sapiens.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser_thr_pkin_AS. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	29150.
SOURCE	Search...

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Entry information

Entry name

VRK1_HUMAN

Accession

Primary (citable) accession number: Q99986
Secondary accession number(s): Q3SYL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

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

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents