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Q8IV63

- VRK3_HUMAN

UniProt

Q8IV63 - VRK3_HUMAN

Protein

Inactive serine/threonine-protein kinase VRK3

Gene

VRK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (10 Oct 2003)
      Previous versions | rss
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    Functioni

    Inactive kinase that suppresses ERK activity by promoting phosphatase activity of DUSP3 which specifically dephosphorylates and inactivates ERK in the nucleus.By similarity

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. protein kinase activity Source: InterPro

    GO - Biological processi

    1. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
    2. positive regulation of phosphoprotein phosphatase activity Source: Ensembl

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ8IV63.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inactive serine/threonine-protein kinase VRK3
    Alternative name(s):
    Serine/threonine-protein pseudokinase VRK3
    Vaccinia-related kinase 3
    Gene namesi
    Name:VRK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:18996. VRK3.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134923990.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 474474Inactive serine/threonine-protein kinase VRK3PRO_0000086808Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphoserine1 Publication
    Modified residuei59 – 591Phosphoserine1 Publication
    Modified residuei82 – 821Phosphoserine3 Publications
    Modified residuei83 – 831Phosphoserine3 Publications
    Modified residuei90 – 901Phosphoserine1 Publication
    Modified residuei115 – 1151Phosphoserine1 Publication
    Modified residuei122 – 1221Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IV63.
    PaxDbiQ8IV63.
    PRIDEiQ8IV63.

    PTM databases

    PhosphoSiteiQ8IV63.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IV63.
    BgeeiQ8IV63.
    CleanExiHS_VRK3.
    GenevestigatoriQ8IV63.

    Organism-specific databases

    HPAiHPA016040.

    Interactioni

    Subunit structurei

    Interacts with DUSP3 By similarity. Interacts with RAN.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi119394. 5 interactions.
    IntActiQ8IV63. 5 interactions.
    MINTiMINT-8247443.
    STRINGi9606.ENSP00000324636.

    Structurei

    Secondary structure

    1
    474
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi157 – 1593
    Beta strandi165 – 17511
    Beta strandi178 – 1858
    Beta strandi200 – 2067
    Helixi211 – 22111
    Helixi224 – 23310
    Beta strandi246 – 2505
    Turni251 – 2533
    Beta strandi254 – 2607
    Helixi266 – 2727
    Helixi274 – 2763
    Helixi280 – 29920
    Beta strandi311 – 3155
    Beta strandi318 – 3247
    Helixi327 – 3293
    Helixi335 – 3373
    Turni354 – 3563
    Helixi359 – 3624
    Helixi369 – 38517
    Helixi391 – 3933
    Helixi397 – 40913
    Helixi426 – 43611
    Helixi446 – 45914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JIIX-ray2.00A/B146-474[»]
    ProteinModelPortaliQ8IV63.
    SMRiQ8IV63. Positions 145-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IV63.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini166 – 457292Protein kinasePROSITE-ProRule annotationsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi49 – 6416Nuclear localization signal1 PublicationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotations

    Phylogenomic databases

    eggNOGiNOG298316.
    HOGENOMiHOG000293191.
    HOVERGENiHBG047756.
    InParanoidiQ8IV63.
    KOiK08816.
    OMAiYEEKPPY.
    OrthoDBiEOG7KSX83.
    PhylomeDBiQ8IV63.
    TreeFamiTF106473.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR026870. Zinc_ribbon_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF13240. zinc_ribbon_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IV63-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MISFCPDCGK SIQAAFKFCP YCGNSLPVEE HVGSQTFVNP HVSSFQGSKR    50
    GLNSSFETSP KKVKWSSTVT SPRLSLFSDG DSSESEDTLS SSERSKGSGS 100
    RPPTPKSSPQ KTRKSPQVTR GSPQKTSCSP QKTRQSPQTL KRSRVTTSLE 150
    ALPTGTVLTD KSGRQWKLKS FQTRDNQGIL YEAAPTSTLT CDSGPQKQKF 200
    SLKLDAKDGR LFNEQNFFQR AAKPLQVNKW KKLYSTPLLA IPTCMGFGVH 250
    QDKYRFLVLP SLGRSLQSAL DVSPKHVLSE RSVLQVACRL LDALEFLHEN 300
    EYVHGNVTAE NIFVDPEDQS QVTLAGYGFA FRYCPSGKHV AYVEGSRSPH 350
    EGDLEFISMD LHKGCGPSRR SDLQSLGYCM LKWLYGFLPW TNCLPNTEDI 400
    MKQKQKFVDK PGPFVGPCGH WIRPSETLQK YLKVVMALTY EEKPPYAMLR 450
    NNLEALLQDL RVSPYDPIGL PMVP 474
    Length:474
    Mass (Da):52,881
    Last modified:October 10, 2003 - v2
    Checksum:i86B9B91050A7F0CC
    GO
    Isoform 2 (identifier: Q8IV63-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         407-412: FVDKPG → LPWDSF
         413-474: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:412
    Mass (Da):45,904
    Checksum:iB8EA8340E4FB9824
    GO
    Isoform 3 (identifier: Q8IV63-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         47-96: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:424
    Mass (Da):47,501
    Checksum:iD17A379F153ED44E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591S → F.1 Publication
    Corresponds to variant rs2033262 [ dbSNP | Ensembl ].
    VAR_041295
    Natural varianti105 – 1051P → T.1 Publication
    Corresponds to variant rs11547882 [ dbSNP | Ensembl ].
    VAR_041296
    Natural varianti170 – 1701S → P.
    Corresponds to variant rs11547881 [ dbSNP | Ensembl ].
    VAR_051682
    Natural varianti171 – 1711F → L.1 Publication
    Corresponds to variant rs11547883 [ dbSNP | Ensembl ].
    VAR_041297
    Natural varianti188 – 1881T → A.
    Corresponds to variant rs11879620 [ dbSNP | Ensembl ].
    VAR_051683
    Natural varianti268 – 2681S → L.1 Publication
    Corresponds to variant rs10410075 [ dbSNP | Ensembl ].
    VAR_041298
    Natural varianti288 – 2881C → Y.1 Publication
    Corresponds to variant rs10409482 [ dbSNP | Ensembl ].
    VAR_041299
    Natural varianti304 – 3041H → L.
    Corresponds to variant rs35261919 [ dbSNP | Ensembl ].
    VAR_051684
    Natural varianti370 – 3701R → C.1 Publication
    Corresponds to variant rs35331034 [ dbSNP | Ensembl ].
    VAR_041300
    Natural varianti371 – 3711S → G.1 Publication
    Corresponds to variant rs56407496 [ dbSNP | Ensembl ].
    VAR_041301

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei47 – 9650Missing in isoform 3. 1 PublicationVSP_043409Add
    BLAST
    Alternative sequencei407 – 4126FVDKPG → LPWDSF in isoform 2. 1 PublicationVSP_008544
    Alternative sequencei413 – 47462Missing in isoform 2. 1 PublicationVSP_008545Add
    BLAST

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti161 – 1611K → E in AAP47180. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031052 mRNA. Translation: BAA90769.1.
    AF514788 mRNA. Translation: AAP47180.1.
    AK292918 mRNA. Translation: BAF85607.1.
    AK303010 mRNA. Translation: BAG64141.1.
    AC011452 Genomic DNA. No translation available.
    BC023556 mRNA. Translation: AAH23556.1.
    BC095449 mRNA. Translation: AAH95449.1.
    CCDSiCCDS12791.1. [Q8IV63-1]
    CCDS33076.1. [Q8IV63-3]
    RefSeqiNP_001020949.1. NM_001025778.1. [Q8IV63-3]
    NP_057524.3. NM_016440.3. [Q8IV63-1]
    XP_005259028.1. XM_005258971.1. [Q8IV63-1]
    XP_005259029.1. XM_005258972.1. [Q8IV63-3]
    XP_005259031.1. XM_005258974.2. [Q8IV63-2]
    XP_006723300.1. XM_006723237.1. [Q8IV63-1]
    XP_006723301.1. XM_006723238.1. [Q8IV63-3]
    UniGeneiHs.443330.

    Genome annotation databases

    EnsembliENST00000316763; ENSP00000324636; ENSG00000105053. [Q8IV63-1]
    ENST00000377011; ENSP00000366210; ENSG00000105053. [Q8IV63-3]
    ENST00000594092; ENSP00000472541; ENSG00000105053. [Q8IV63-2]
    ENST00000594948; ENSP00000473171; ENSG00000105053. [Q8IV63-1]
    ENST00000599538; ENSP00000469880; ENSG00000105053. [Q8IV63-1]
    ENST00000601341; ENSP00000470156; ENSG00000105053. [Q8IV63-3]
    GeneIDi51231.
    KEGGihsa:51231.
    UCSCiuc002prg.2. human. [Q8IV63-1]
    uc002pri.1. human. [Q8IV63-3]
    uc002prk.2. human. [Q8IV63-2]

    Polymorphism databases

    DMDMi45593724.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031052 mRNA. Translation: BAA90769.1 .
    AF514788 mRNA. Translation: AAP47180.1 .
    AK292918 mRNA. Translation: BAF85607.1 .
    AK303010 mRNA. Translation: BAG64141.1 .
    AC011452 Genomic DNA. No translation available.
    BC023556 mRNA. Translation: AAH23556.1 .
    BC095449 mRNA. Translation: AAH95449.1 .
    CCDSi CCDS12791.1. [Q8IV63-1 ]
    CCDS33076.1. [Q8IV63-3 ]
    RefSeqi NP_001020949.1. NM_001025778.1. [Q8IV63-3 ]
    NP_057524.3. NM_016440.3. [Q8IV63-1 ]
    XP_005259028.1. XM_005258971.1. [Q8IV63-1 ]
    XP_005259029.1. XM_005258972.1. [Q8IV63-3 ]
    XP_005259031.1. XM_005258974.2. [Q8IV63-2 ]
    XP_006723300.1. XM_006723237.1. [Q8IV63-1 ]
    XP_006723301.1. XM_006723238.1. [Q8IV63-3 ]
    UniGenei Hs.443330.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JII X-ray 2.00 A/B 146-474 [» ]
    ProteinModelPortali Q8IV63.
    SMRi Q8IV63. Positions 145-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119394. 5 interactions.
    IntActi Q8IV63. 5 interactions.
    MINTi MINT-8247443.
    STRINGi 9606.ENSP00000324636.

    PTM databases

    PhosphoSitei Q8IV63.

    Polymorphism databases

    DMDMi 45593724.

    Proteomic databases

    MaxQBi Q8IV63.
    PaxDbi Q8IV63.
    PRIDEi Q8IV63.

    Protocols and materials databases

    DNASUi 51231.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316763 ; ENSP00000324636 ; ENSG00000105053 . [Q8IV63-1 ]
    ENST00000377011 ; ENSP00000366210 ; ENSG00000105053 . [Q8IV63-3 ]
    ENST00000594092 ; ENSP00000472541 ; ENSG00000105053 . [Q8IV63-2 ]
    ENST00000594948 ; ENSP00000473171 ; ENSG00000105053 . [Q8IV63-1 ]
    ENST00000599538 ; ENSP00000469880 ; ENSG00000105053 . [Q8IV63-1 ]
    ENST00000601341 ; ENSP00000470156 ; ENSG00000105053 . [Q8IV63-3 ]
    GeneIDi 51231.
    KEGGi hsa:51231.
    UCSCi uc002prg.2. human. [Q8IV63-1 ]
    uc002pri.1. human. [Q8IV63-3 ]
    uc002prk.2. human. [Q8IV63-2 ]

    Organism-specific databases

    CTDi 51231.
    GeneCardsi GC19M050479.
    HGNCi HGNC:18996. VRK3.
    HPAi HPA016040.
    neXtProti NX_Q8IV63.
    PharmGKBi PA134923990.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298316.
    HOGENOMi HOG000293191.
    HOVERGENi HBG047756.
    InParanoidi Q8IV63.
    KOi K08816.
    OMAi YEEKPPY.
    OrthoDBi EOG7KSX83.
    PhylomeDBi Q8IV63.
    TreeFami TF106473.

    Enzyme and pathway databases

    SignaLinki Q8IV63.

    Miscellaneous databases

    ChiTaRSi VRK3. human.
    EvolutionaryTracei Q8IV63.
    GenomeRNAii 51231.
    NextBioi 54332.
    PROi Q8IV63.

    Gene expression databases

    ArrayExpressi Q8IV63.
    Bgeei Q8IV63.
    CleanExi HS_VRK3.
    Genevestigatori Q8IV63.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR026870. Zinc_ribbon_dom.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF13240. zinc_ribbon_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Vaccinia related kinase 3 (VRK3)."
      Nezu J.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Cloning and characterization of a novel human VRK3 gene."
      Ni X., Xie Y., Mao Y.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Testis and Trachea.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Skin.
    6. "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, NUCLEAR LOCALIZATION SIGNAL.
    7. "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: INTERACTION WITH RAN.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-82; SER-83 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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-82 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-82; SER-83; SER-115 AND SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site."
      Scheeff E.D., Eswaran J., Bunkoczi G., Knapp S., Manning G.
      Structure 17:128-138(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 146-474, FUNCTION, LACK OF CATALYTIC ACTIVITY.
    13. "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.
      , 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] PHE-59; THR-105; LEU-171; LEU-268; TYR-288; CYS-370 AND GLY-371.

    Entry informationi

    Entry nameiVRK3_HUMAN
    AccessioniPrimary (citable) accession number: Q8IV63
    Secondary accession number(s): A6NEG5
    , A8KA53, Q502Y2, Q9P2V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: October 10, 2003
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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