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Q9WVS7

- MP2K5_MOUSE

UniProt

Q9WVS7 - MP2K5_MOUSE

Protein

Dual specificity mitogen-activated protein kinase kinase 5

Gene

Map2k5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei195 – 1951ATPPROSITE-ProRule annotation
    Active sitei283 – 2831Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi172 – 1809ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: UniProtKB-KW
    5. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. cellular response to growth factor stimulus Source: Ensembl
    3. ERK5 cascade Source: Ensembl
    4. heart development Source: MGI
    5. MAPK cascade Source: MGI
    6. negative regulation of cell migration involved in sprouting angiogenesis Source: Ensembl
    7. negative regulation of chemokine (C-X-C motif) ligand 2 production Source: Ensembl
    8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    9. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    10. negative regulation of heterotypic cell-cell adhesion Source: Ensembl
    11. negative regulation of interleukin-8 biosynthetic process Source: Ensembl
    12. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    13. negative regulation of response to cytokine stimulus Source: Ensembl
    14. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    15. positive regulation of cell growth Source: Ensembl
    16. positive regulation of epithelial cell proliferation Source: Ensembl
    17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_216232. Signalling to ERK5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity mitogen-activated protein kinase kinase 5 (EC:2.7.12.2)
    Short name:
    MAP kinase kinase 5
    Short name:
    MAPKK 5
    Alternative name(s):
    MAPK/ERK kinase 5
    Short name:
    MEK 5
    Gene namesi
    Name:Map2k5
    Synonyms:Mek5, Mkk5, Prkmk5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1346345. Map2k5.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleus Source: Ensembl
    3. spindle Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201R → A: Loss of MAPK7 binding; when associated with A-21. 1 Publication
    Mutagenesisi21 – 211I → A: Loss of MAPK7 binding; when associated with A-20. 1 Publication
    Mutagenesisi64 – 641D → A: Loss of MAP3K2/MAP3K3 binding; when associated with A-65. 1 Publication
    Mutagenesisi65 – 651E → A: Loss of MAP3K2/MAP3K3 binding; when associated with A-64. 1 Publication
    Mutagenesisi67 – 671G → A: Loss of MAP3K2/MAP3K3 binding; when associated with A-68. 1 Publication
    Mutagenesisi68 – 681D → A: Loss of MAP3K2/MAP3K3 binding; when associated with A-67. 1 Publication
    Mutagenesisi311 – 3111S → A: Dominant negative form; when associated with V-315. 1 Publication
    Mutagenesisi311 – 3111S → D: Dominant active form; when associated with D-315. 1 Publication
    Mutagenesisi315 – 3151T → D: Dominant active form; when associated with D-311. 1 Publication
    Mutagenesisi315 – 3151T → V: Dominant negative form; when associated with A-311. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Dual specificity mitogen-activated protein kinase kinase 5PRO_0000086384Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei311 – 3111PhosphoserineBy similarity
    Modified residuei315 – 3151PhosphothreonineBy similarity

    Post-translational modificationi

    Activated by phosphorylation on Ser/Thr by MAP kinase kinase kinases.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9WVS7.
    PRIDEiQ9WVS7.

    PTM databases

    PhosphoSiteiQ9WVS7.

    Expressioni

    Gene expression databases

    BgeeiQ9WVS7.
    CleanExiMM_MAP2K5.
    GenevestigatoriQ9WVS7.

    Interactioni

    Subunit structurei

    Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with SQSTM1 and PRKCZ or PRKCI.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Map3k2Q610834EBI-446144,EBI-446134
    Map3k3Q6108415EBI-446144,EBI-446250
    Nap1l1P2865620EBI-446144,EBI-645055
    Sqstm1Q643373EBI-446144,EBI-645025

    Protein-protein interaction databases

    IntActiQ9WVS7. 10 interactions.
    MINTiMINT-1728345.

    Structurei

    Secondary structure

    1
    448
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 226
    Beta strandi28 – 347
    Beta strandi36 – 383
    Helixi41 – 5111
    Beta strandi60 – 623
    Beta strandi70 – 745
    Helixi75 – 9521
    Beta strandi102 – 1065

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WI0NMR-A8-107[»]
    ProteinModelPortaliQ9WVS7.
    SMRiQ9WVS7. Positions 16-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WVS7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 9780OPRAdd
    BLAST
    Domaini166 – 419254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 258Interaction with MAPK7
    Regioni64 – 685Interaction with MAP3K2/MAP3K3
    Regioni117 – 13115Interaction with MAPK7Add
    BLAST

    Domaini

    Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues of the OPR domain. This domain also mediates interactions with SQSTM1 and PARD6A.2 Publications

    Sequence similaritiesi

    Contains 1 OPR domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00690000101918.
    HOGENOMiHOG000234206.
    HOVERGENiHBG108518.
    InParanoidiQ9WVS7.
    KOiK04463.
    OMAiEVVSMWV.
    OrthoDBiEOG7HF1KZ.
    PhylomeDBiQ9WVS7.
    TreeFamiTF106468.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00564. PB1. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00666. PB1. 1 hit.
    SM00220. S_TKc. 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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9WVS7-1) [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

    MLWLALGPFC AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ    50
    VLPEATTTAF EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE 100
    PLQIFPRACK PPGERNIHGL KVNTRAGPSQ HTSPVVSDSL PSNSLKKSSA 150
    ELRKILANGQ MNEQDIRYRD TLGHGNGGTV YKAHHVPSGK ILAVKVILLD 200
    ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC TEFMDGGSLD 250
    VYRKIPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTGGQVKLC 300
    DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA 350
    LGRFPYPQIQ KNQGSLMPLQ LLQCIVDEDS PVLPLGEFSE PFVHFITQCM 400
    RKQPKERPAP EELMGHPFIV QFNDGNSTVV SMWVCRALEE RRSQQGPP 448
    Length:448
    Mass (Da):50,105
    Last modified:November 1, 1999 - v1
    Checksum:i50C50E8F0F712BE7
    GO
    Isoform 2 (identifier: Q9WVS7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         359-367: Missing.

    Show »
    Length:439
    Mass (Da):49,105
    Checksum:iABAFCC35482F0EF6
    GO
    Isoform 3 (identifier: Q9WVS7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         183-186: AHHV → LLHI
         187-448: Missing.

    Show »
    Length:186
    Mass (Da):20,737
    Checksum:i9978D2D647198D15
    GO
    Isoform 4 (identifier: Q9WVS7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         108-118: ACKPPGERNIH → GYRRGSRLREY
         119-448: Missing.

    Show »
    Length:118
    Mass (Da):13,589
    Checksum:iCACEC8FE6518544A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei108 – 11811ACKPPGERNIH → GYRRGSRLREY in isoform 4. 1 PublicationVSP_015836Add
    BLAST
    Alternative sequencei119 – 448330Missing in isoform 4. 1 PublicationVSP_015837Add
    BLAST
    Alternative sequencei183 – 1864AHHV → LLHI in isoform 3. 1 PublicationVSP_015838
    Alternative sequencei187 – 448262Missing in isoform 3. 1 PublicationVSP_015839Add
    BLAST
    Alternative sequencei359 – 3679Missing in isoform 2. 1 PublicationVSP_015840

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB019374 mRNA. Translation: BAA82040.1.
    AK020716 mRNA. Translation: BAB32187.1.
    BC013697 mRNA. Translation: AAH13697.1.
    BC028260 mRNA. Translation: AAH28260.1.
    CCDSiCCDS23269.1. [Q9WVS7-1]
    RefSeqiNP_035970.1. NM_011840.2. [Q9WVS7-1]
    XP_006511208.1. XM_006511145.1. [Q9WVS7-2]
    UniGeneiMm.325746.

    Genome annotation databases

    EnsembliENSMUST00000034920; ENSMUSP00000034920; ENSMUSG00000058444. [Q9WVS7-1]
    GeneIDi23938.
    KEGGimmu:23938.
    UCSCiuc009qaw.1. mouse. [Q9WVS7-1]
    uc009qaz.1. mouse. [Q9WVS7-4]
    uc012guv.1. mouse. [Q9WVS7-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB019374 mRNA. Translation: BAA82040.1 .
    AK020716 mRNA. Translation: BAB32187.1 .
    BC013697 mRNA. Translation: AAH13697.1 .
    BC028260 mRNA. Translation: AAH28260.1 .
    CCDSi CCDS23269.1. [Q9WVS7-1 ]
    RefSeqi NP_035970.1. NM_011840.2. [Q9WVS7-1 ]
    XP_006511208.1. XM_006511145.1. [Q9WVS7-2 ]
    UniGenei Mm.325746.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WI0 NMR - A 8-107 [» ]
    ProteinModelPortali Q9WVS7.
    SMRi Q9WVS7. Positions 16-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WVS7. 10 interactions.
    MINTi MINT-1728345.

    PTM databases

    PhosphoSitei Q9WVS7.

    Proteomic databases

    PaxDbi Q9WVS7.
    PRIDEi Q9WVS7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034920 ; ENSMUSP00000034920 ; ENSMUSG00000058444 . [Q9WVS7-1 ]
    GeneIDi 23938.
    KEGGi mmu:23938.
    UCSCi uc009qaw.1. mouse. [Q9WVS7-1 ]
    uc009qaz.1. mouse. [Q9WVS7-4 ]
    uc012guv.1. mouse. [Q9WVS7-2 ]

    Organism-specific databases

    CTDi 5607.
    MGIi MGI:1346345. Map2k5.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00690000101918.
    HOGENOMi HOG000234206.
    HOVERGENi HBG108518.
    InParanoidi Q9WVS7.
    KOi K04463.
    OMAi EVVSMWV.
    OrthoDBi EOG7HF1KZ.
    PhylomeDBi Q9WVS7.
    TreeFami TF106468.

    Enzyme and pathway databases

    Reactomei REACT_216232. Signalling to ERK5.

    Miscellaneous databases

    ChiTaRSi MAP2K5. mouse.
    EvolutionaryTracei Q9WVS7.
    NextBioi 303741.
    PROi Q9WVS7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9WVS7.
    CleanExi MM_MAP2K5.
    Genevestigatori Q9WVS7.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00564. PB1. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00666. PB1. 1 hit.
    SM00220. S_TKc. 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. "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus."
      Kamakura S., Moriguchi T., Nishida E.
      J. Biol. Chem. 274:26563-26571(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF SER-311 AND THR-315.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Strain: C57BL/6J.
      Tissue: Head and Hypothalamus.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins."
      Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., Michaelsen E., Bjoerkoey G., Johansen T.
      J. Biol. Chem. 278:34568-34581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1; PRKCZ; PRKCI; PARD6A AND MAP3K3, DOMAIN.
    5. "PB1 domain-dependent signaling complex is required for extracellular signal-regulated kinase 5 activation."
      Nakamura K., Uhlik M.T., Johnson N.L., Hahn K.M., Johnson G.L.
      Mol. Cell. Biol. 26:2065-2079(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH MAP3K2 AND MAPK7, MUTAGENESIS OF ARG-20; ILE-21; ASP-64; GLU-65; GLY-67 AND ASP-68.
    6. "Solution structure of the PB1 domain of mouse mitogen activated protein kinase kinase 5 (MAP2K5)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 7-107.

    Entry informationi

    Entry nameiMP2K5_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVS7
    Secondary accession number(s): Q8CFM3, Q8K360, Q9D222
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3