Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y2U5

- M3K2_HUMAN

UniProt

Q9Y2U5 - M3K2_HUMAN

Protein

Mitogen-activated protein kinase kinase kinase 2

Gene

MAP3K2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of a protein kinase signal transduction cascade. Regulates the JNK and ERK5 pathways by phosphorylating and activating MAP2K5 and MAP2K7 By similarity. Plays a role in caveolae kiss-and-run dynamics.By similarity2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by phosphorylation on Thr-524.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei385 – 3851ATPPROSITE-ProRule annotation
    Active sitei483 – 4831Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi362 – 37110ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase kinase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein kinase activity Source: MGI
    6. protein kinase binding Source: UniProtKB
    7. protein serine/threonine kinase activity Source: ProtInc

    GO - Biological processi

    1. activation of JUN kinase activity Source: ProtInc
    2. activation of MAPK activity Source: ProtInc
    3. cellular response to mechanical stimulus Source: UniProtKB
    4. positive regulation of transcription, DNA-templated Source: UniProtKB
    5. protein phosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.12.2. 2681.
    SignaLinkiQ9Y2U5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase 2 (EC:2.7.11.25)
    Alternative name(s):
    MAPK/ERK kinase kinase 2
    Short name:
    MEK kinase 2
    Short name:
    MEKK 2
    Gene namesi
    Name:MAP3K2
    Synonyms:MAPKKK2, MEKK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6854. MAP3K2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Upon EGF stimulation, translocates into the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Ensembl
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30598.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 619619Mitogen-activated protein kinase kinase kinase 2PRO_0000086243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Phosphoserine1 Publication
    Modified residuei153 – 1531Phosphoserine4 Publications
    Modified residuei159 – 1591Phosphoserine1 Publication
    Modified residuei164 – 1641Phosphoserine1 Publication
    Modified residuei239 – 2391Phosphoserine1 Publication
    Modified residuei297 – 2971Phosphoserine1 Publication
    Modified residuei331 – 3311Phosphoserine3 Publications
    Modified residuei344 – 3441Phosphoserine3 Publications

    Post-translational modificationi

    Autophosphorylated.By similarity
    Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y2U5.
    PaxDbiQ9Y2U5.
    PRIDEiQ9Y2U5.

    PTM databases

    PhosphoSiteiQ9Y2U5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2U5.
    BgeeiQ9Y2U5.
    CleanExiHS_MAP3K2.
    GenevestigatoriQ9Y2U5.

    Organism-specific databases

    HPAiHPA021540.

    Interactioni

    Subunit structurei

    Interacts with PKN2; the interaction activates PKN2 kinase activity in a MAP3K2-independent kinase activity By similarity. Self-associates. Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts (via the kinase catalytic domain) with STK38. Interacts with XIAP/BIRC4.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STUB1Q9UNE79EBI-357393,EBI-357085

    Protein-protein interaction databases

    BioGridi115969. 23 interactions.
    IntActiQ9Y2U5. 9 interactions.
    MINTiMINT-272127.
    STRINGi9606.ENSP00000343463.

    Structurei

    Secondary structure

    1
    619
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 507
    Beta strandi53 – 597
    Helixi65 – 7612
    Beta strandi80 – 867
    Beta strandi89 – 924
    Helixi96 – 10813
    Beta strandi114 – 1218

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CU1NMR-A43-132[»]
    2NPTX-ray1.75B/D26-123[»]
    ProteinModelPortaliQ9Y2U5.
    SMRiQ9Y2U5. Positions 35-122, 328-616.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2U5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 12280OPRAdd
    BLAST
    Domaini357 – 617261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG006303.
    InParanoidiQ9Y2U5.
    KOiK04420.
    OMAiRSVHMKS.
    OrthoDBiEOG747PHJ.
    PhylomeDBiQ9Y2U5.
    TreeFamiTF105113.

    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.
    [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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y2U5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDQQALNSI MQDLAVLHKA SRPALSLQET RKAKSSSPKK QNDVRVKFEH    50
    RGEKRILQFP RPVKLEDLRS KAKIAFGQSM DLHYTNNELV IPLTTQDDLD 100
    KAVELLDRSI HMKSLKILLV INGSTQATNL EPLPSLEDLD NTVFGAERKK 150
    RLSIIGPTSR DRSSPPPGYI PDELHQVARN GSFTSINSEG EFIPESMDQM 200
    LDPLSLSSPE NSGSGSCPSL DSPLDGESYP KSRMPRAQSY PDNHQEFSDY 250
    DNPIFEKFGK GGTYPRRYHV SYHHQEYNDG RKTFPRARRT QGTSLRSPVS 300
    FSPTDHSLST SSGSSIFTPE YDDSRIRRRG SDIDNPTLTV MDISPPSRSP 350
    RAPTNWRLGK LLGQGAFGRV YLCYDVDTGR ELAVKQVQFD PDSPETSKEV 400
    NALECEIQLL KNLLHERIVQ YYGCLRDPQE KTLSIFMEYM PGGSIKDQLK 450
    AYGALTENVT RKYTRQILEG VHYLHSNMIV HRDIKGANIL RDSTGNVKLG 500
    DFGASKRLQT ICLSGTGMKS VTGTPYWMSP EVISGEGYGR KADIWSVACT 550
    VVEMLTEKPP WAEFEAMAAI FKIATQPTNP KLPPHVSDYT RDFLKRIFVE 600
    AKLRPSADEL LRHMFVHYH 619
    Length:619
    Mass (Da):69,741
    Last modified:May 16, 2006 - v2
    Checksum:iE034580D349F097F
    GO

    Sequence cautioni

    The sequence BAC11348.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → GTR in BAD92200. 1 PublicationCurated
    Sequence conflicti103 – 1031V → L in AAD28547. 1 PublicationCurated
    Sequence conflicti103 – 1031V → L in AAF63496. 1 PublicationCurated
    Sequence conflicti198 – 1981D → E in AAD28547. 1 PublicationCurated
    Sequence conflicti198 – 1981D → E in AAF63496. 1 PublicationCurated
    Sequence conflicti225 – 2251D → G in AAD28547. 1 PublicationCurated
    Sequence conflicti275 – 2773QEY → KD in AAD28547. 1 PublicationCurated
    Sequence conflicti293 – 2964TSLR → NQLT in AAD28547. 1 PublicationCurated
    Sequence conflicti293 – 2964TSLR → NQLT in AAF63496. 1 PublicationCurated
    Sequence conflicti413 – 4131L → F in AAD28547. 1 PublicationCurated
    Sequence conflicti459 – 4591V → G in AAD28547. 1 PublicationCurated
    Sequence conflicti480 – 4801V → L in AAD28547. 1 PublicationCurated
    Sequence conflicti536 – 5361E → Q in AAD28547. 1 PublicationCurated
    Sequence conflicti536 – 5361E → Q in AAF63496. 1 PublicationCurated
    Sequence conflicti579 – 5791N → S in BAC11348. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101I → V.1 Publication
    Corresponds to variant rs55767983 [ dbSNP | Ensembl ].
    VAR_040682
    Natural varianti112 – 1121M → I in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040683
    Natural varianti140 – 1401D → G.1 Publication
    Corresponds to variant rs56307783 [ dbSNP | Ensembl ].
    VAR_040684

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF111105 mRNA. Translation: AAD28547.1.
    AF239798 mRNA. Translation: AAF63496.1.
    AB208963 mRNA. Translation: BAD92200.1.
    AC068282 Genomic DNA. Translation: AAY15043.1.
    AC110926 Genomic DNA. Translation: AAY15070.1.
    CH471103 Genomic DNA. Translation: EAW95315.1.
    BC136293 mRNA. Translation: AAI36294.1.
    AK075004 mRNA. Translation: BAC11348.1. Different initiation.
    CCDSiCCDS46404.1.
    RefSeqiNP_006600.3. NM_006609.4.
    UniGeneiHs.145605.

    Genome annotation databases

    EnsembliENST00000344908; ENSP00000343463; ENSG00000169967.
    ENST00000409947; ENSP00000387246; ENSG00000169967.
    GeneIDi10746.
    KEGGihsa:10746.
    UCSCiuc002toj.2. human.

    Polymorphism databases

    DMDMi97536681.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF111105 mRNA. Translation: AAD28547.1 .
    AF239798 mRNA. Translation: AAF63496.1 .
    AB208963 mRNA. Translation: BAD92200.1 .
    AC068282 Genomic DNA. Translation: AAY15043.1 .
    AC110926 Genomic DNA. Translation: AAY15070.1 .
    CH471103 Genomic DNA. Translation: EAW95315.1 .
    BC136293 mRNA. Translation: AAI36294.1 .
    AK075004 mRNA. Translation: BAC11348.1 . Different initiation.
    CCDSi CCDS46404.1.
    RefSeqi NP_006600.3. NM_006609.4.
    UniGenei Hs.145605.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CU1 NMR - A 43-132 [» ]
    2NPT X-ray 1.75 B/D 26-123 [» ]
    ProteinModelPortali Q9Y2U5.
    SMRi Q9Y2U5. Positions 35-122, 328-616.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115969. 23 interactions.
    IntActi Q9Y2U5. 9 interactions.
    MINTi MINT-272127.
    STRINGi 9606.ENSP00000343463.

    Chemistry

    BindingDBi Q9Y2U5.
    ChEMBLi CHEMBL5914.
    GuidetoPHARMACOLOGYi 2077.

    PTM databases

    PhosphoSitei Q9Y2U5.

    Polymorphism databases

    DMDMi 97536681.

    Proteomic databases

    MaxQBi Q9Y2U5.
    PaxDbi Q9Y2U5.
    PRIDEi Q9Y2U5.

    Protocols and materials databases

    DNASUi 10746.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344908 ; ENSP00000343463 ; ENSG00000169967 .
    ENST00000409947 ; ENSP00000387246 ; ENSG00000169967 .
    GeneIDi 10746.
    KEGGi hsa:10746.
    UCSCi uc002toj.2. human.

    Organism-specific databases

    CTDi 10746.
    GeneCardsi GC02M128057.
    H-InvDB HIX0002433.
    HGNCi HGNC:6854. MAP3K2.
    HPAi HPA021540.
    MIMi 609487. gene.
    neXtProti NX_Q9Y2U5.
    PharmGKBi PA30598.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG006303.
    InParanoidi Q9Y2U5.
    KOi K04420.
    OMAi RSVHMKS.
    OrthoDBi EOG747PHJ.
    PhylomeDBi Q9Y2U5.
    TreeFami TF105113.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 2681.
    SignaLinki Q9Y2U5.

    Miscellaneous databases

    EvolutionaryTracei Q9Y2U5.
    GeneWikii MAP3K2.
    GenomeRNAii 10746.
    NextBioi 40805.
    PROi Q9Y2U5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2U5.
    Bgeei Q9Y2U5.
    CleanExi HS_MAP3K2.
    Genevestigatori Q9Y2U5.

    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.
    [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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MEKK2 is involved in transducing T-cell co-stimulatory signals to the JNK cascade."
      Su B., Yang J.H., Xia Y., Karin M.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human MEKK2b cDNA."
      Wang C., Lo H.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Testis.
    7. "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] OF 180-619.
      Tissue: Teratocarcinoma.
    8. "Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation."
      Cheng J., Yang J., Xia Y., Karin M., Su B.
      Mol. Cell. Biol. 20:2334-2342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP2K7 AND MAPK8.
    9. "MEK5 and ERK5 are localized in the nuclei of resting as well as stimulated cells, while MEKK2 translocates from the cytosol to the nucleus upon stimulation."
      Raviv Z., Kalie E., Seger R.
      J. Cell Sci. 117:1773-1784(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae."
      Pelkmans L., Zerial M.
      Nature 436:128-133(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2."
      Winsauer G., Resch U., Hofer-Warbinek R., Schichl Y.M., de Martin R.
      Cell. Signal. 20:2107-2112(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY XIAP/BIRC4, INTERACTION WITH XIAP/BIRC4.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38)."
      Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N., Hosoi Y., Miyagawa K.
      Oncogene 27:1930-1938(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STK38, SELF-ASSOCIATION.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-159 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-153; SER-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-239; SER-331 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "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-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Solution structure of the PB1 domain of human protein kinase MEKK2B."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 43-132.
    23. "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] VAL-110; ILE-112 AND GLY-140.

    Entry informationi

    Entry nameiM3K2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2U5
    Secondary accession number(s): B9EG87
    , Q53QL9, Q53S75, Q59GZ6, Q8NC32, Q9NYK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 153 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 2
      Human chromosome 2: 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