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Q99986

- VRK1_HUMAN

UniProt

Q99986 - VRK1_HUMAN

Protein

Serine/threonine-protein kinase VRK1

Gene

VRK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    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+. RAN inhibits its autophosphorylation and its ability to phosphorylate histone H3.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711ATPPROSITE-ProRule annotation
    Active sitei177 – 1771Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi43 – 519ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histone kinase activity (H3-S10 specific) Source: UniProt
    3. histone kinase activity (H3-T3 specific) Source: UniProt
    4. nucleosomal histone binding Source: UniProt
    5. protein binding Source: IntAct
    6. protein kinase activity Source: UniProt
    7. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. Golgi disassembly Source: UniProtKB
    2. histone H3-S10 phosphorylation Source: UniProt
    3. histone H3-T3 phosphorylation Source: UniProt
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB-KW
    6. mitotic nuclear envelope disassembly Source: Reactome
    7. mitotic nuclear envelope reassembly Source: Reactome
    8. protein autophosphorylation Source: UniProtKB
    9. protein phosphorylation Source: UniProt

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    SignaLinkiQ99986.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase VRK1 (EC:2.7.11.1)
    Alternative name(s):
    Vaccinia-related kinase 1
    Gene namesi
    Name:VRK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:12718. VRK1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmcytoskeletonspindle By similarity
    Note: Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. Golgi stack Source: UniProtKB
    4. nucleolus Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProt
    7. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Pontocerebellar hypoplasia 1A (PCH1A) [MIM:607596]: A disorder characterized by an abnormally small cerebellum and brainstem, central and peripheral motor dysfunction from birth, gliosis and spinal cord anterior horn cells degeneration resembling infantile spinal muscular atrophy. Additional features include muscle hypotonia, congenital contractures and respiratory insufficiency that is evident at birth.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141S → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi102 – 1021T → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi125 – 1251S → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi150 – 1501S → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi158 – 1581S → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi179 – 1791K → A: Does not affect phosphorylation at S-342. 1 Publication
    Mutagenesisi239 – 2391S → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi305 – 3051T → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi312 – 3121T → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi342 – 3421S → A: Abolishes phosphorylation by PLK3 and induction of Golgi fragmentation during mitosis. Strongly reduced autophosphorylation. 2 Publications
    Mutagenesisi353 – 3531T → A: Strongly reduced autophosphorylation. 1 Publication
    Mutagenesisi355 – 3551T → A: Does not abolish autophosphorylation. 1 Publication
    Mutagenesisi390 – 3901T → A: Does not abolish autophosphorylation. 1 Publication

    Organism-specific databases

    MIMi607596. phenotype.
    Orphaneti2254. Pontocerebellar hypoplasia type 1.
    PharmGKBiPA37330.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396Serine/threonine-protein kinase VRK1PRO_0000086803Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei342 – 3421Phosphoserine; by PLK33 Publications
    Modified residuei355 – 3551Phosphothreonine; by autocatalysis2 Publications

    Post-translational modificationi

    Autophosphorylated at various serine and threonine residues. Autophosphorylation does not impair its ability to phosphorylate p53/TP53. Phosphorylation by PLK3 leads to induction of Golgi fragmentation during mitosis.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99986.
    PaxDbiQ99986.
    PeptideAtlasiQ99986.
    PRIDEiQ99986.

    PTM databases

    PhosphoSiteiQ99986.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in fetal liver, testis and thymus.1 Publication

    Gene expression databases

    BgeeiQ99986.
    CleanExiHS_VRK1.
    GenevestigatoriQ99986.

    Organism-specific databases

    HPAiHPA000660.
    HPA017929.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATF2P153365EBI-1769146,EBI-1170906
    COILP384329EBI-1769146,EBI-945751
    JUNP054124EBI-1769146,EBI-852823
    PLK3Q9H4B412EBI-1769146,EBI-751877
    RANP6282612EBI-1769146,EBI-286642
    TP53P046379EBI-1769146,EBI-366083
    TP53BP1Q128888EBI-1769146,EBI-396540

    Protein-protein interaction databases

    BioGridi113282. 16 interactions.
    IntActiQ99986. 14 interactions.
    MINTiMINT-3060185.
    STRINGi9606.ENSP00000216639.

    Structurei

    Secondary structure

    1
    396
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2 – 43
    Beta strandi11 – 133
    Beta strandi22 – 243
    Beta strandi28 – 303
    Beta strandi36 – 427
    Beta strandi46 – 494
    Beta strandi50 – 567
    Beta strandi59 – 613
    Beta strandi67 – 748
    Helixi78 – 9013
    Helixi93 – 10210
    Beta strandi113 – 1219
    Beta strandi124 – 1329
    Beta strandi134 – 1374
    Helixi138 – 1447
    Turni145 – 1473
    Helixi151 – 17020
    Helixi180 – 1823
    Beta strandi183 – 1886
    Beta strandi193 – 1953
    Helixi198 – 2003
    Beta strandi202 – 2054
    Helixi206 – 2083
    Turni225 – 2273
    Helixi230 – 2334
    Helixi240 – 25617
    Helixi262 – 2643
    Helixi268 – 28013
    Helixi282 – 2898
    Beta strandi291 – 2944
    Helixi297 – 30711
    Beta strandi311 – 3133
    Helixi317 – 33014
    Beta strandi355 – 3573

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KTYNMR-A1-360[»]
    2KULNMR-A1-360[»]
    2LAVNMR-A1-361[»]
    2RSVNMR-A1-396[»]
    3OP5X-ray2.40A/B/C/D3-364[»]
    ProteinModelPortaliQ99986.
    SMRiQ99986. Positions 1-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99986.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 317281Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG330134.
    HOGENOMiHOG000069991.
    HOVERGENiHBG007532.
    InParanoidiQ99986.
    KOiK08816.
    OMAiYCMVQWL.
    OrthoDBiEOG7KSX83.
    PhylomeDBiQ99986.
    TreeFamiTF106473.

    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. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99986-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRVKAAQAG RQSSAKRHLA EQFAVGEIIT DMAKKEWKVG LPIGQGGFGC    50
    IYLADMNSSE SVGSDAPCVV KVEPSDNGPL FTELKFYQRA AKPEQIQKWI 100
    RTRKLKYLGV PKYWGSGLHD KNGKSYRFMI MDRFGSDLQK IYEANAKRFS 150
    RKTVLQLSLR ILDILEYIHE HEYVHGDIKA SNLLLNYKNP DQVYLVDYGL 200
    AYRYCPEGVH KEYKEDPKRC HDGTIEFTSI DAHNGVAPSR RGDLEILGYC 250
    MIQWLTGHLP WEDNLKDPKY VRDSKIRYRE NIASLMDKCF PEKNKPGEIA 300
    KYMETVKLLD YTEKPLYENL RDILLQGLKA IGSKDDGKLD LSVVENGGLK 350
    AKTITKKRKK EIEESKEPGV EDTEWSNTQT EEAIQTRSRT RKRVQK 396
    Length:396
    Mass (Da):45,476
    Last modified:May 1, 1997 - v1
    Checksum:i5640C624BF059949
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000449 mRNA. Translation: BAA19108.1.
    BC103761 mRNA. Translation: AAI03762.1.
    BC112075 mRNA. Translation: AAI12076.1.
    BC113510 mRNA. Translation: AAI13511.1.
    CCDSiCCDS9947.1.
    RefSeqiNP_003375.1. NM_003384.2.
    UniGeneiHs.422662.

    Genome annotation databases

    EnsembliENST00000216639; ENSP00000216639; ENSG00000100749.
    GeneIDi7443.
    KEGGihsa:7443.
    UCSCiuc001yft.3. human.

    Polymorphism databases

    DMDMi45593726.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000449 mRNA. Translation: BAA19108.1 .
    BC103761 mRNA. Translation: AAI03762.1 .
    BC112075 mRNA. Translation: AAI12076.1 .
    BC113510 mRNA. Translation: AAI13511.1 .
    CCDSi CCDS9947.1.
    RefSeqi NP_003375.1. NM_003384.2.
    UniGenei Hs.422662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KTY NMR - A 1-360 [» ]
    2KUL NMR - A 1-360 [» ]
    2LAV NMR - A 1-361 [» ]
    2RSV NMR - A 1-396 [» ]
    3OP5 X-ray 2.40 A/B/C/D 3-364 [» ]
    ProteinModelPortali Q99986.
    SMRi Q99986. Positions 1-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113282. 16 interactions.
    IntActi Q99986. 14 interactions.
    MINTi MINT-3060185.
    STRINGi 9606.ENSP00000216639.

    Chemistry

    BindingDBi Q99986.
    ChEMBLi CHEMBL1293199.
    GuidetoPHARMACOLOGYi 2275.

    PTM databases

    PhosphoSitei Q99986.

    Polymorphism databases

    DMDMi 45593726.

    Proteomic databases

    MaxQBi Q99986.
    PaxDbi Q99986.
    PeptideAtlasi Q99986.
    PRIDEi Q99986.

    Protocols and materials databases

    DNASUi 7443.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216639 ; ENSP00000216639 ; ENSG00000100749 .
    GeneIDi 7443.
    KEGGi hsa:7443.
    UCSCi uc001yft.3. human.

    Organism-specific databases

    CTDi 7443.
    GeneCardsi GC14P097263.
    HGNCi HGNC:12718. VRK1.
    HPAi HPA000660.
    HPA017929.
    MIMi 602168. gene.
    607596. phenotype.
    neXtProti NX_Q99986.
    Orphaneti 2254. Pontocerebellar hypoplasia type 1.
    PharmGKBi PA37330.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG330134.
    HOGENOMi HOG000069991.
    HOVERGENi HBG007532.
    InParanoidi Q99986.
    KOi K08816.
    OMAi YCMVQWL.
    OrthoDBi EOG7KSX83.
    PhylomeDBi Q99986.
    TreeFami TF106473.

    Enzyme and pathway databases

    Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    SignaLinki Q99986.

    Miscellaneous databases

    EvolutionaryTracei Q99986.
    GeneWikii VRK1.
    GenomeRNAii 7443.
    NextBioi 29150.
    PROi Q99986.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99986.
    CleanExi HS_VRK1.
    Genevestigatori Q99986.

    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. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-355, ENZYME REGULATION.
    5. "Characterization of three paralogous members of the Mammalian vaccinia related kinase family."
      Nichols R.J., Traktman P.
      J. Biol. Chem. 279:7934-7946(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    6. "Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK."
      Sevilla A., Santos C.R., Vega F.M., Lazo P.A.
      J. Biol. Chem. 279:27458-27465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines."
      Blanco S., Klimcakova L., Vega F.M., Lazo P.A.
      FEBS J. 273:2487-2504(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus."
      Nichols R.J., Wiebe M.S., Traktman P.
      Mol. Biol. Cell 17:2451-2464(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities."
      Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.
      Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAN, ENZYME REGULATION.
    10. "Spinal muscular atrophy with pontocerebellar hypoplasia is caused by a mutation in the VRK1 gene."
      Renbaum P., Kellerman E., Jaron R., Geiger D., Segel R., Lee M., King M.C., Levy-Lahad E.
      Am. J. Hum. Genet. 85:281-289(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PCH1A.
    11. "Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a downstream target in a pathway that induces Golgi fragmentation."
      Lopez-Sanchez I., Sanz-Garcia M., Lazo P.A.
      Mol. Cell. Biol. 29:1189-1201(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-342, MUTAGENESIS OF LYS-179 AND SER-342.
    12. "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-342, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Human vaccinia-related kinase 1."
      Structural genomics consortium (SGC)
      Submitted (SEP-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3-364 IN COMPLEX WITH INHIBITOR.
    15. "NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity."
      Shin J., Chakraborty G., Bharatham N., Kang C., Tochio N., Koshiba S., Kigawa T., Kim W., Kim K.T., Yoon H.S.
      J. Biol. Chem. 286:22131-22138(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-342 AND THR-353, AUTOPHOSPHORYLATION.

    Entry informationi

    Entry nameiVRK1_HUMAN
    AccessioniPrimary (citable) accession number: Q99986
    Secondary accession number(s): Q3SYL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3