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Q13163

- MP2K5_HUMAN

UniProt

Q13163 - MP2K5_HUMAN

Protein

Dual specificity mitogen-activated protein kinase kinase 5

Gene

MAP2K5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      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 – 1951ATP
    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: UniProtKB
    4. protein kinase activity Source: ProtInc
    5. protein serine/threonine kinase activity Source: UniProtKB-KW
    6. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

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

    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

    BRENDAi2.7.12.2. 2681.
    ReactomeiREACT_12020. Signalling to ERK5.
    SignaLinkiQ13163.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6845. MAP2K5.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi195 – 1951K → M: Inactivation. 1 Publication
    Mutagenesisi311 – 3111S → A: Inactivation. 1 Publication
    Mutagenesisi315 – 3151T → A: Inactivation. 1 Publication

    Organism-specific databases

    PharmGKBiPA30590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Dual specificity mitogen-activated protein kinase kinase 5PRO_0000086383Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei311 – 3111Phosphoserine2 Publications
    Modified residuei315 – 3151Phosphothreonine1 Publication

    Post-translational modificationi

    Activated by phosphorylation on Ser/Thr by MAP kinase kinase kinases.By similarity
    Yersinia yopJ may acetylate Ser/Thr residues, preventing phosphorylation and activation, thus blocking the MAPK signaling pathway.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13163.
    PaxDbiQ13163.
    PRIDEiQ13163.

    PTM databases

    PhosphoSiteiQ13163.

    Expressioni

    Tissue specificityi

    Expressed in many adult tissues. Abundant in heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ13163.
    BgeeiQ13163.
    CleanExiHS_MAP2K5.
    GenevestigatoriQ13163.

    Organism-specific databases

    HPAiCAB022094.
    HPA027347.
    HPA027755.

    Interactioni

    Subunit structurei

    Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with SQSTM1 and PRKCZ or PRKCI By similarity. Interacts with Yersinia yopJ.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRB2P629932EBI-307294,EBI-401755
    MAP3K3Q997592EBI-307294,EBI-307281
    MAPK7Q131642EBI-307294,EBI-1213983

    Protein-protein interaction databases

    BioGridi111593. 19 interactions.
    DIPiDIP-27558N.
    IntActiQ13163. 13 interactions.
    MINTiMINT-1155433.
    STRINGi9606.ENSP00000178640.

    Structurei

    Secondary structure

    1
    448
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 237
    Turni24 – 263
    Beta strandi27 – 337
    Helixi41 – 5111
    Beta strandi58 – 636
    Beta strandi65 – 673
    Beta strandi69 – 724
    Helixi75 – 9319
    Turni94 – 963
    Beta strandi102 – 1076

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NPTX-ray1.75A/C5-108[»]
    2O2VX-ray1.83A5-108[»]
    4IC7X-ray2.60B/E16-130[»]
    ProteinModelPortaliQ13163.
    SMRiQ13163. Positions 16-130, 160-437.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13163.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 9780OPRAdd
    BLAST
    Domaini166 – 409244Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 258Interaction with MAPK7By similarity
    Regioni64 – 685Interaction with MAP3K2/MAP3K3By similarity
    Regioni117 – 13115Interaction with MAPK7By similarityAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234206.
    HOVERGENiHBG108518.
    InParanoidiQ13163.
    KOiK04463.
    OMAiEVVSMWV.
    OrthoDBiEOG7HF1KZ.
    PhylomeDBiQ13163.
    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 B (identifier: Q13163-1) [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

    MLWLALGPFP AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ    50
    VLPEATTTAF EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE 100
    PLQIFPRACK PPGERNIHGL KVNTRAGPSQ HSSPAVSDSL PSNSLKKSSA 150
    ELKKILANGQ MNEQDIRYRD TLGHGNGGTV YKAYHVPSGK ILAVKVILLD 200
    ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC TEFMDGGSLD 250
    VYRKMPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTRGQVKLC 300
    DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA 350
    LGRFPYPQIQ KNQGSLMPLQ LLQCIVDEDS PVLPVGEFSE PFVHFITQCM 400
    RKQPKERPAP EELMGHPFIV QFNDGNAAVV SMWVCRALEE RRSQQGPP 448
    Length:448
    Mass (Da):50,112
    Last modified:November 28, 2006 - v2
    Checksum:iF23BB327E2A9C7DC
    GO
    Isoform A (identifier: Q13163-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         349-358: Missing.

    Show »
    Length:438
    Mass (Da):48,968
    Checksum:i21246312F1640EE2
    GO
    Isoform C (identifier: Q13163-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         349-358: Missing.
         444-448: QQGPP → LASLPSPSPSV

    Note: Incomplete sequence.

    Show »
    Length:444
    Mass (Da):49,497
    Checksum:i574D15B06FD49134
    GO
    Isoform 4 (identifier: Q13163-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVL → MMEGHFPQS

    Note: No experimental confirmation available.

    Show »
    Length:412
    Mass (Da):46,131
    Checksum:i7B00956329FCAEDB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181H → R.1 Publication
    Corresponds to variant rs56241934 [ dbSNP | Ensembl ].
    VAR_040823
    Natural varianti427 – 4271A → V.1 Publication
    VAR_040824
    Natural varianti428 – 4281A → T.1 Publication
    Corresponds to variant rs55811347 [ dbSNP | Ensembl ].
    VAR_046070

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4545MLWLA…FRDVL → MMEGHFPQS in isoform 4. 1 PublicationVSP_043333Add
    BLAST
    Alternative sequencei349 – 35810Missing in isoform A and isoform C. 2 PublicationsVSP_021825
    Alternative sequencei444 – 4485QQGPP → LASLPSPSPSV in isoform C. 1 PublicationVSP_021826

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25265 mRNA. Translation: AAA96146.1.
    U71087 mRNA. Translation: AAB16851.1.
    U71088 mRNA. Translation: AAB16852.2.
    BT006780 mRNA. Translation: AAP35426.1.
    AK293459 mRNA. Translation: BAG56954.1.
    CR542229 mRNA. Translation: CAG47025.1.
    AC009292 Genomic DNA. No translation available.
    AC016355 Genomic DNA. No translation available.
    AC103753 Genomic DNA. No translation available.
    BC008838 mRNA. Translation: AAH08838.1.
    CCDSiCCDS10224.1. [Q13163-1]
    CCDS42051.1. [Q13163-2]
    CCDS55970.1. [Q13163-4]
    RefSeqiNP_001193733.1. NM_001206804.1. [Q13163-4]
    NP_002748.1. NM_002757.3. [Q13163-2]
    NP_660143.1. NM_145160.2. [Q13163-1]
    UniGeneiHs.114198.

    Genome annotation databases

    EnsembliENST00000178640; ENSP00000178640; ENSG00000137764. [Q13163-1]
    ENST00000354498; ENSP00000346493; ENSG00000137764. [Q13163-4]
    ENST00000395476; ENSP00000378859; ENSG00000137764. [Q13163-2]
    GeneIDi5607.
    KEGGihsa:5607.
    UCSCiuc002aqu.3. human. [Q13163-1]
    uc002aqv.3. human. [Q13163-2]
    uc010ujw.2. human. [Q13163-4]

    Polymorphism databases

    DMDMi118572669.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25265 mRNA. Translation: AAA96146.1 .
    U71087 mRNA. Translation: AAB16851.1 .
    U71088 mRNA. Translation: AAB16852.2 .
    BT006780 mRNA. Translation: AAP35426.1 .
    AK293459 mRNA. Translation: BAG56954.1 .
    CR542229 mRNA. Translation: CAG47025.1 .
    AC009292 Genomic DNA. No translation available.
    AC016355 Genomic DNA. No translation available.
    AC103753 Genomic DNA. No translation available.
    BC008838 mRNA. Translation: AAH08838.1 .
    CCDSi CCDS10224.1. [Q13163-1 ]
    CCDS42051.1. [Q13163-2 ]
    CCDS55970.1. [Q13163-4 ]
    RefSeqi NP_001193733.1. NM_001206804.1. [Q13163-4 ]
    NP_002748.1. NM_002757.3. [Q13163-2 ]
    NP_660143.1. NM_145160.2. [Q13163-1 ]
    UniGenei Hs.114198.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NPT X-ray 1.75 A/C 5-108 [» ]
    2O2V X-ray 1.83 A 5-108 [» ]
    4IC7 X-ray 2.60 B/E 16-130 [» ]
    ProteinModelPortali Q13163.
    SMRi Q13163. Positions 16-130, 160-437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111593. 19 interactions.
    DIPi DIP-27558N.
    IntActi Q13163. 13 interactions.
    MINTi MINT-1155433.
    STRINGi 9606.ENSP00000178640.

    Chemistry

    BindingDBi Q13163.
    ChEMBLi CHEMBL4948.
    GuidetoPHARMACOLOGYi 2066.

    PTM databases

    PhosphoSitei Q13163.

    Polymorphism databases

    DMDMi 118572669.

    Proteomic databases

    MaxQBi Q13163.
    PaxDbi Q13163.
    PRIDEi Q13163.

    Protocols and materials databases

    DNASUi 5607.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000178640 ; ENSP00000178640 ; ENSG00000137764 . [Q13163-1 ]
    ENST00000354498 ; ENSP00000346493 ; ENSG00000137764 . [Q13163-4 ]
    ENST00000395476 ; ENSP00000378859 ; ENSG00000137764 . [Q13163-2 ]
    GeneIDi 5607.
    KEGGi hsa:5607.
    UCSCi uc002aqu.3. human. [Q13163-1 ]
    uc002aqv.3. human. [Q13163-2 ]
    uc010ujw.2. human. [Q13163-4 ]

    Organism-specific databases

    CTDi 5607.
    GeneCardsi GC15P067835.
    HGNCi HGNC:6845. MAP2K5.
    HPAi CAB022094.
    HPA027347.
    HPA027755.
    MIMi 602520. gene.
    neXtProti NX_Q13163.
    PharmGKBi PA30590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234206.
    HOVERGENi HBG108518.
    InParanoidi Q13163.
    KOi K04463.
    OMAi EVVSMWV.
    OrthoDBi EOG7HF1KZ.
    PhylomeDBi Q13163.
    TreeFami TF106468.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 2681.
    Reactomei REACT_12020. Signalling to ERK5.
    SignaLinki Q13163.

    Miscellaneous databases

    ChiTaRSi MAP2K5. human.
    EvolutionaryTracei Q13163.
    GeneWikii MAP2K5.
    GenomeRNAii 5607.
    NextBioi 21792.
    PROi Q13163.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13163.
    Bgeei Q13163.
    CleanExi HS_MAP2K5.
    Genevestigatori Q13163.

    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. "Components of a new human protein kinase signal transduction pathway."
      Zhou G., Bao Z.Q., Dixon J.E.
      J. Biol. Chem. 270:12665-12669(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH ERK5 AND MAPK7, MUTAGENESIS OF LYS-195; SER-311 AND THR-315, PHOSPHORYLATION AT SER-311 AND THR-315.
      Tissue: Fetal brain.
    2. "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C."
      Kato Y., Kravchenko V.V., Tapping R.I., Han J., Ulevitch R.J., Lee J.-D.
      EMBO J. 16:7054-7066(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), FUNCTION.
      Tissue: Placenta.
    3. Lee J.D.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS OF ISOFORM C.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    5. "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] (ISOFORM 4).
      Tissue: Cerebellum.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM B).
      Tissue: Brain.
    9. "Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation."
      Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., Orth K.
      Science 312:1211-1214(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YOPJ, ACETYLATION.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Crystal structure of the complex of human mitogen activated protein kinase kinase 5 phox domain (MAP2K5-Phox) with human mitogen activated protein kinase kinase kinase 3 (MAP3K2B-Phox)."
      Structural genomics consortium (SGC)
      Submitted (NOV-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 4-108 IN COMPLEX WITH MAP3K2.
    14. "Crystal structure of the complex of human mitogen activated protein kinase kinase 5 phox domain (MAP2K5-Phox) with human mitogen activated protein kinase kinase kinase 3 (MAP3K3B-Phox)."
      Structural genomics consortium (SGC)
      Submitted (NOV-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 4-108 IN COMPLEX WITH MAP3K3.
    15. "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] ARG-118; VAL-427 AND THR-428.

    Entry informationi

    Entry nameiMP2K5_HUMAN
    AccessioniPrimary (citable) accession number: Q13163
    Secondary accession number(s): B4DE43, Q92961, Q92962
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 149 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 15
      Human chromosome 15: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3