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O35099

- M3K5_MOUSE

UniProt

O35099 - M3K5_MOUSE

Protein

Mitogen-activated protein kinase kinase kinase 5

Gene

Map3k5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1).5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by various stressors, including oxidative stress, endoplasmic reticulum stress, and calcium overload, as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) and lipopolysaccharide (LPS). Homophilic association of MAP3K5/ASK1 through the C-terminal coiled-coil domains and the heteromeric complex formation of MAP3K5/ASK1 with the reduced form of thioredoxin (TXN), constitutes an inactive form of the kinase. Upon ROS-induced dissociation of TXN from MAP3K5/ASK1, TRAF2 and TRAF6 are reciprocally recruited to MAP3K5/ASK1 and form the active MAP3K5/ASK1 signalosome, in which TRAF2 and TRAF6 appear to facilitate the active configuration of MAP3K5/ASK1. MAP3K5/ASK1 activity is also regulated through several phosphorylation and dephosphorylation events. Thr-845 is an activating phosphorylation site that is autophosphorylated and phosphorylated by MAP3K6/ASK2 and dephosphorylated by PPP5C. Ser-90 and Ser-1040 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2. Phosphorylation of Ser-973 induces association of MAP3K5/ASK1 with the 14-3-3 family proteins, which suppresses MAP3K5/ASK1 activity. Calcium/calmodulin-activated protein phosphatase calcineurin (PPP3CA) has been shown to directly dephosphorylate this site. SOCS1 binds to ASK1 by recognizing phosphorylation of Tyr-725 and induces MAP3K5/ASK1 degradation in endothelial cells. Also dephosphorylated and activated by PGAM5. Contains an N-terminal autoinhibitory domain.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei716 – 7161ATPPROSITE-ProRule annotation
    Active sitei810 – 8101Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi693 – 7019ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    3. magnesium ion binding Source: UniProtKB
    4. MAP kinase kinase kinase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: MGI
    2. cellular response to hydrogen peroxide Source: Ensembl
    3. cellular response to reactive nitrogen species Source: MGI
    4. innate immune response Source: UniProtKB-KW
    5. intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
    6. JNK cascade Source: Ensembl
    7. MAPK cascade Source: UniProtKB
    8. positive regulation of apoptotic process Source: UniProtKB
    9. programmed necrotic cell death Source: MGI
    10. regulation of cell death Source: MGI
    11. response to ischemia Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity, Stress response

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.12.2. 3474.
    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase 5 (EC:2.7.11.25)
    Alternative name(s):
    Apoptosis signal-regulating kinase 1
    Short name:
    ASK-1
    MAPK/ERK kinase kinase 5
    Short name:
    MEK kinase 5
    Short name:
    MEKK 5
    Gene namesi
    Name:Map3k5
    Synonyms:Ask1, Mekk5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1346876. Map3k5.

    Subcellular locationi

    Cytoplasm By similarity. Endoplasmic reticulum By similarity
    Note: Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13801380Mitogen-activated protein kinase kinase kinase 5PRO_0000086250Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei90 – 901Phosphoserine; by PIM1, PKB/AKT1 and PKB/AKT2By similarity
    Modified residuei725 – 7251PhosphotyrosineBy similarity
    Modified residuei820 – 8201Phosphothreonine; by autocatalysisBy similarity
    Modified residuei845 – 8451Phosphothreonine; by autocatalysis, MELK and MAP3K63 Publications
    Modified residuei849 – 8491Phosphothreonine; by autocatalysis1 Publication
    Modified residuei965 – 9651PhosphoserineBy similarity
    Modified residuei973 – 9731PhosphoserineBy similarity
    Modified residuei983 – 9831Phosphothreonine
    Modified residuei1036 – 10361PhosphoserineBy similarity
    Modified residuei1040 – 10401PhosphoserineBy similarity

    Post-translational modificationi

    Ser-90 and Ser-1040 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2 By similarity. Phosphorylated at Ser-973 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity By similarity. Calcineurin (CN) dephosphorylates this site. Also dephosphorylated and activated by PGAM5 By similarity. Phosphorylated at Thr-845 through autophosphorylation and by MAP3K6/ASK2 which leads to activation. Thr-845 is dephosphorylated by PPP5C.By similarity4 Publications
    Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent ubiquitination leading to proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO35099.
    PaxDbiO35099.
    PRIDEiO35099.

    PTM databases

    PhosphoSiteiO35099.

    Expressioni

    Tissue specificityi

    Expressed in various adult mouse tissues including heart, brain, lung, liver and kidney.1 Publication

    Gene expression databases

    ArrayExpressiO35099.
    BgeeiO35099.
    CleanExiMM_MAP3K5.
    GenevestigatoriO35099.

    Interactioni

    Subunit structurei

    Homodimer when inactive By similarity. Binds both upstream activators and downstream substrates in multimolecular complexes. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF By similarity. This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis By similarity. Interacts with SOCS1 which recognizes phosphorylation of Tyr-725 and induces MAP3K5/ASK1 degradation in endothelial cells By similarity. Interacts with the 14-3-3 family proteins such as YWHAB, YWHAE, YWHAQ, YWHAH, YWHAZ and SFN By similarity. Interacts with ARRB2, BIRC2, DAB2IP, IGF1R, MAP3K6/ASK2, PIM1, PGAM5, PPP5C, SOCS1, STUB1, TRAF2 and TXN By similarity. Interacts with ERN1 in a TRAF2-dependent manner By similarity. Interacts with calcineurin subunit PPP3R1, PPM1L and TRAF6. Interacts (via N-terminus) with RAF1 and this interaction inhibits the proapoptotic function of MAP3K5. Interacts with DAB2IP (via N-terminus C2 domain); the interaction occurs in a TNF-alpha-dependent manner By similarity.Interacts with DUSP13/DUSP13A; may positively regulate apoptosis By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ppp3r1Q638103EBI-777493,EBI-6666164

    Protein-protein interaction databases

    BioGridi204961. 7 interactions.
    DIPiDIP-38055N.
    IntActiO35099. 6 interactions.
    MINTiMINT-151480.
    STRINGi10090.ENSMUSP00000093485.

    Structurei

    3D structure databases

    ProteinModelPortaliO35099.
    SMRiO35099. Positions 648-947.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini687 – 945259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1252 – 129241Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117243.
    HOGENOMiHOG000293286.
    HOVERGENiHBG006305.
    InParanoidiQ14AY5.
    KOiK04426.
    OMAiTELHCKK.
    OrthoDBiEOG7WDN1P.
    TreeFamiTF105115.

    Family and domain databases

    InterProiIPR025136. DUF4071.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR013761. SAM/pointed.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF13281. DUF4071. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O35099-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTEAGEGIT FSVPPFASVG FCTIPEGGSC RRGGGAATAA EGEPSLQPLL     50
    VPPPPPPPGS FWNVESAAAP GTSCPTTAPG SSATRGRGNS GSGGGRRTTV 100
    AYVINEASQG QLVVAESEAL QSLREACEAV GATLETLHFG KLDFGETAVL 150
    DRFYNADIAV VEMSDAFRQP SLFYHLGVRE SFSMANNIIL YCDTNSDSLQ 200
    SLKEIICQKN TVCTGNYTFI PYMVTPHNKV YCCDSSFMKG LTELMQPNFE 250
    LLLGPICLPL VDRFVQLLKV AQASSSQYFR ESILSDIRKA RNLYTGKELA 300
    AELARIRQRV DNIEVLTADI VINLLLSYRD IQDYDSIVKL VETLEKLPTF 350
    DLASHHHVKF HYAFALNRRN LPGDRAKALD IMIPMVQSEE QVASDMYCLV 400
    GRIYKDMFLD SNFTDTESRD HGASWFKKAF ESEPTLQSGI NYAVLLLAAG 450
    HQFESSFELR KVGVKLSSLL GKKGNLEKLQ SYWEVGFFLG ASVLANDHLR 500
    VIQASEKLFR LKTPAWYLKS IVETILIYKH FVKLTTEQPS AKQELVDFWM 550
    DFLVEATKTD VTVVRFPVLI LEPTKIYQPS YLSINNEVEE KTISIWHVLP 600
    DDKKGIHEWN FGASSVRGVS ISKFEERCCF LYVLHNSDDF QIYFCTELHC 650
    KRFFEMVNTI TEEKGRGAED GDCEGDSLEY DYEYDENGDR VVLGKGTYGI 700
    VYAGRDLSNQ VRIAIKEIPE RDSRYSQPLH EEIALHKHLK HKNIVQYLGS 750
    FSENGFIKIF MEQVPGGSLS ALLRSKWGPL KDNEQTIGFY TKQILEGLKY 800
    LHDNQIVHRD IKGDNVLINT YSGVLKISDF GTSKRLAGIN PCTETFTGTL 850
    QYMAPEIIDK GPRGYGKAAD IWSLGCTIIE MATGKPPFYE LGEPQAAMFK 900
    VGMFKVHPEI PESMSAEAKA FILKCFEPDP DKRACANDLL IDEFLKVSSK 950
    KKKTQPKLSA LSTGSNEYLR SISLPVPVLV EDTSSSSEYG SVSPDTELKA 1000
    DPFSFKARAK SCGEKDGKGI RTLFLGIPDE NFEDHSAPPS PEEKDSGFFM 1050
    LRKDSERRAT LHRILTEDQD KVVRNLMESL AQGAEEPKLK WEHITTLISS 1100
    LREFVRSTDR KIIATTLSKL KLELDFDSHG ISQVQVVLFG FQDAVNKVLR 1150
    NHNIKPHWMF ALDSIIRKAV QTAITILVPE LRPHFSLASE SDTADPEDLD 1200
    VEDEHEELSS NQTVRRPQAI TEDAVATSGV STLSSTVSHD SQNAHRSLNV 1250
    QLGRMKIETN RLLEELVRKE RELQALLHQA IEEKDQEIRH LKLKSQPIDI 1300
    PGFPVCHLNS PGTTTEDSEL PGWLRENGAD EDTISRFLAE DYTLVDVLYY 1350
    VTRDDLKCLR LRGGMLCTLW KAIIDFRNKC 1380
    Length:1,380
    Mass (Da):154,512
    Last modified:July 27, 2011 - v3
    Checksum:iBE68D225EBBCDF38
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1661A → T in BAA23648. (PubMed:9367868)Curated
    Sequence conflicti368 – 3703RRN → TRT in BAA23648. (PubMed:9367868)Curated
    Sequence conflicti1090 – 10901K → N in BAA23648. (PubMed:9367868)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006787 mRNA. Translation: BAA23648.3.
    BC116627 mRNA. Translation: AAI16628.1.
    BC133697 mRNA. Translation: AAI33698.1.
    CCDSiCCDS35857.1.
    PIRiJC5778.
    RefSeqiNP_032606.4. NM_008580.4.
    UniGeneiMm.6595.

    Genome annotation databases

    EnsembliENSMUST00000095806; ENSMUSP00000093485; ENSMUSG00000071369.
    GeneIDi26408.
    KEGGimmu:26408.
    UCSCiuc007enm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006787 mRNA. Translation: BAA23648.3 .
    BC116627 mRNA. Translation: AAI16628.1 .
    BC133697 mRNA. Translation: AAI33698.1 .
    CCDSi CCDS35857.1.
    PIRi JC5778.
    RefSeqi NP_032606.4. NM_008580.4.
    UniGenei Mm.6595.

    3D structure databases

    ProteinModelPortali O35099.
    SMRi O35099. Positions 648-947.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204961. 7 interactions.
    DIPi DIP-38055N.
    IntActi O35099. 6 interactions.
    MINTi MINT-151480.
    STRINGi 10090.ENSMUSP00000093485.

    PTM databases

    PhosphoSitei O35099.

    Proteomic databases

    MaxQBi O35099.
    PaxDbi O35099.
    PRIDEi O35099.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000095806 ; ENSMUSP00000093485 ; ENSMUSG00000071369 .
    GeneIDi 26408.
    KEGGi mmu:26408.
    UCSCi uc007enm.2. mouse.

    Organism-specific databases

    CTDi 4217.
    MGIi MGI:1346876. Map3k5.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117243.
    HOGENOMi HOG000293286.
    HOVERGENi HBG006305.
    InParanoidi Q14AY5.
    KOi K04426.
    OMAi TELHCKK.
    OrthoDBi EOG7WDN1P.
    TreeFami TF105115.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 3474.
    Reactomei REACT_188970. Oxidative Stress Induced Senescence.

    Miscellaneous databases

    NextBioi 304389.
    PROi O35099.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35099.
    Bgeei O35099.
    CleanExi MM_MAP3K5.
    Genevestigatori O35099.

    Family and domain databases

    InterProi IPR025136. DUF4071.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR013761. SAM/pointed.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF13281. DUF4071. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    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. "Molecular cloning and characterization of the mouse apoptosis signal-regulating kinase 1."
      Tobiume K., Inage T., Takeda K., Enomoto S., Miyazono K., Ichijo H.
      Biochem. Biophys. Res. Commun. 239:905-910(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. Tobiume K., Inage T., Takeda K., Enomoto S., Miyazono K., Ichijo H.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 22-26; 123; 273; 755; 1001-1011; 1220-1222 AND 1274-1280.
    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].
    4. "ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis."
      Tobiume K., Matsuzawa A., Takahashi T., Nishitoh H., Morita K., Takeda K., Minowa O., Miyazono K., Noda T., Ichijo H.
      EMBO Rep. 2:222-228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer."
      Tobiume K., Saitoh M., Ichijo H.
      J. Cell. Physiol. 191:95-104(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-845 AND THR-849, ENZYME REGULATION.
    6. Cited for: FUNCTION.
    7. "ROS-dependent activation of the TRAF6-ASK1-p38 pathway is selectively required for TLR4-mediated innate immunity."
      Matsuzawa A., Saegusa K., Noguchi T., Sadamitsu C., Nishitoh H., Nagai S., Koyasu S., Matsumoto K., Takeda K., Ichijo H.
      Nat. Immunol. 6:587-592(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH TRAF6.
    8. "A balance between Raf-1 and Fas expression sets the pace of erythroid differentiation."
      Rubiolo C., Piazzolla D., Meissl K., Beug H., Huber J.C., Kolbus A., Baccarini M.
      Blood 108:152-159(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Direct interaction and reciprocal regulation between ASK1 and calcineurin-NFAT control cardiomyocyte death and growth."
      Liu Q., Wilkins B.J., Lee Y.J., Ichijo H., Molkentin J.D.
      Mol. Cell. Biol. 26:3785-3797(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP3R1, PHOSPHORYLATION AT SER-973, ENZYME REGULATION, FUNCTION.
    10. "Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase 2Cepsilon."
      Saito J., Toriumi S., Awano K., Ichijo H., Sasaki K., Kobayashi T., Tamura S.
      Biochem. J. 405:591-596(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPM1L.
    11. "Murine protein serine/threonine kinase 38 activates apoptosis signal-regulating kinase 1 via Thr 838 phosphorylation."
      Jung H., Seong H.A., Ha H.
      J. Biol. Chem. 283:34541-34553(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-845.
    12. "Apoptosis signal-regulating kinase 1 in stress and immune response."
      Takeda K., Noguchi T., Naguro I., Ichijo H.
      Annu. Rev. Pharmacol. Toxicol. 48:199-225(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
    13. "The roles of ASK family proteins in stress responses and diseases."
      Hattori K., Naguro I., Runchel C., Ichijo H.
      Cell Commun. Signal. 7:9-9(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
    14. "S100 proteins modulate protein phosphatase 5 function: a link between CA2+ signal transduction and protein dephosphorylation."
      Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M., Kobayashi R.
      J. Biol. Chem. 287:13787-13798(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C, PHOSPHORYLATION AT THR-845, DEPHOSPHORYLATION AT THR-845 BY PPP5C.

    Entry informationi

    Entry nameiM3K5_MOUSE
    AccessioniPrimary (citable) accession number: O35099
    Secondary accession number(s): Q14AY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3