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)

Q99683

- M3K5_HUMAN

UniProt

Q99683 - M3K5_HUMAN

Protein

Mitogen-activated protein kinase kinase kinase 5

Gene

MAP3K5

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 158 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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).18 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    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-838 is an activating phosphorylation site that is autophosphorylated and phosphorylated by MAP3K6/ASK2 and dephosphorylated by PPP5C. Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2. Phosphorylation of Ser-966 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-718 and induces MAP3K5/ASK1 degradation in endothelial cells. Also dephosphorylated and activated by PGAM5. Contains an N-terminal autoinhibitory domain.14 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei709 – 7091ATP
    Active sitei803 – 8031Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi686 – 6949ATPPROSITE-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 activity Source: UniProtKB
    8. protein phosphatase binding Source: BHF-UCL

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
    2. activation of JUN kinase activity Source: ProtInc
    3. activation of MAPKK activity Source: BHF-UCL
    4. apoptotic signaling pathway Source: ProtInc
    5. cellular response to hydrogen peroxide Source: BHF-UCL
    6. innate immune response Source: UniProtKB-KW
    7. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
    8. JNK cascade Source: UniProtKB
    9. MAPK cascade Source: UniProtKB
    10. positive regulation of apoptotic process Source: UniProtKB
    11. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    12. positive regulation of neuron death Source: ParkinsonsUK-UCL
    13. protein phosphorylation Source: ParkinsonsUK-UCL
    14. response to ischemia Source: Ensembl
    15. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Host-virus interaction, Immunity, Innate immunity, Stress response

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.12.2. 2681.
    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    SignaLinkiQ99683.

    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, MAPKKK5, MEKK5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6857. MAP3K5.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. protein kinase complex Source: ParkinsonsUK-UCL

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi709 – 7091K → M: Loss of kinase activity. Inhibits activation of JNK and apoptosis mediated by TNFRSF6 and DAXX. 2 Publications
    Mutagenesisi709 – 7091K → R: Loss of kinase activity. Abolishes DAXX-mediated apoptosis. 2 Publications
    Mutagenesisi966 – 9661S → A: Enhanced induction of apoptosis, increased kinase activity, and loss of YWHAG binding. 2 Publications
    Mutagenesisi1033 – 10331S → A: Enhanced induction of apoptosis and increased kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA30601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13741374Mitogen-activated protein kinase kinase kinase 5PRO_0000086249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Phosphoserine; by PIM1, PKB/AKT1 and PKB/AKT24 Publications
    Modified residuei718 – 7181Phosphotyrosine2 Publications
    Modified residuei813 – 8131Phosphothreonine; by autocatalysis2 Publications
    Modified residuei838 – 8381Phosphothreonine; by autocatalysis, MELK and MAP3K67 Publications
    Modified residuei842 – 8421Phosphothreonine; by autocatalysis2 Publications
    Modified residuei958 – 9581Phosphoserine1 Publication
    Modified residuei966 – 9661Phosphoserine4 Publications
    Modified residuei976 – 9761PhosphothreonineBy similarity
    Modified residuei1029 – 10291Phosphoserine3 Publications
    Modified residuei1033 – 10331Phosphoserine6 Publications

    Post-translational modificationi

    Phosphorylated at Thr-838 through autophosphorylation and by MAP3K6/ASK2 which leads to activation. Thr-838 is dephosphorylated by PPP5C. Ser-83 and Ser-1033 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 and AKT2. Phosphorylated at Ser-966 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity. Calcineurin (CN) dephosphorylates this site. Also dephosphorylated and activated by PGAM5.16 Publications
    Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent ubiquitination leading to proteasomal degradation.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ99683.
    PaxDbiQ99683.
    PRIDEiQ99683.

    PTM databases

    PhosphoSiteiQ99683.

    Expressioni

    Tissue specificityi

    Abundantly expressed in heart and pancreas.

    Inductioni

    By TNF. Inhibited by HIV-1 Nef.

    Gene expression databases

    ArrayExpressiQ99683.
    BgeeiQ99683.
    CleanExiHS_MAP3K5.
    GenevestigatoriQ99683.

    Organism-specific databases

    HPAiCAB007824.

    Interactioni

    Subunit structurei

    Homodimer when inactive. Binds both upstream activators and downstream substrates in multimolecular complexes. Associates with and inhibited by HIV-1 Nef. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF. This complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Interacts with SOCS1 which recognizes phosphorylation of Tyr-718 and induces MAP3K5/ASK1 degradation in endothelial cells. Interacts with the 14-3-3 family proteins such as YWHAB, YWHAE, YWHAQ, YWHAH, YWHAZ and SFN. Interacts with ARRB2, BIRC2, DAB2IP, IGF1R, MAP3K6/ASK2, PGAM5, PIM1, PPP5C, SOCS1, STUB1, TRAF2, TRAF6 and TXN. Interacts with ERN1 in a TRAF2-dependent manner. Interacts with calcineurin subunit PPP3R1 and with PPM1L By similarity. 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. Interacts with DUSP13/DUSP13A; may positively regulate apoptosis.By similarity28 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1P317492EBI-476263,EBI-296087
    APPP050672EBI-476263,EBI-77613
    ARRB1P494073EBI-476263,EBI-743313
    ARRB2P321212EBI-476263,EBI-714559
    DAB2IPQ5VWQ82EBI-476263,EBI-2871881
    DAXXQ9UER77EBI-476263,EBI-77321
    FASP254452EBI-476263,EBI-494743
    MAP2K3P467342EBI-476263,EBI-602462
    Map3k6Q9WTR23EBI-476263,EBI-1254790From a different organism.
    MCRS1Q96EZ83EBI-476263,EBI-348259
    PPP3R1P630982EBI-476263,EBI-915984
    SMN2Q166373EBI-476263,EBI-395421
    TXNP105992EBI-476263,EBI-594644
    YWHABP319463EBI-476263,EBI-359815
    YWHAZP631043EBI-476263,EBI-347088
    ZNF622Q969S314EBI-476263,EBI-2687480

    Protein-protein interaction databases

    BioGridi110381. 74 interactions.
    DIPiDIP-29516N.
    IntActiQ99683. 39 interactions.
    MINTiMINT-99796.
    STRINGi9606.ENSP00000351908.

    Structurei

    Secondary structure

    1
    1374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi673 – 6753
    Beta strandi681 – 6833
    Beta strandi685 – 6884
    Beta strandi693 – 6997
    Turni700 – 7023
    Beta strandi705 – 7128
    Helixi725 – 7295
    Beta strandi740 – 7467
    Beta strandi749 – 7557
    Beta strandi758 – 7614
    Helixi762 – 7687
    Helixi777 – 79620
    Helixi806 – 8083
    Beta strandi809 – 8124
    Turni813 – 8153
    Beta strandi818 – 8203
    Turni823 – 8253
    Beta strandi827 – 8293
    Helixi843 – 8453
    Helixi848 – 8536
    Helixi854 – 8574
    Helixi860 – 87617
    Helixi882 – 8843
    Helixi887 – 89711
    Helixi909 – 91810
    Turni923 – 9253
    Helixi929 – 9335
    Helixi936 – 9383

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CLQX-ray2.30A/B659-951[»]
    3VW6X-ray2.40A/B671-939[»]
    4BF2X-ray2.11A/B660-977[»]
    4BHNX-ray2.30A/B660-977[»]
    4BIBX-ray2.43A/B660-977[»]
    4BICX-ray2.62A/B660-977[»]
    4BIDX-ray2.80A/B660-977[»]
    4BIEX-ray2.36A/B660-977[»]
    ProteinModelPortaliQ99683.
    SMRiQ99683. Positions 650-962.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99683.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini680 – 938259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1245 – 128541Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG006305.
    InParanoidiQ99683.
    KOiK04426.
    OMAiTELHCKK.
    OrthoDBiEOG7WDN1P.
    PhylomeDBiQ99683.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99683-1) [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

    MSTEADEGIT FSVPPFAPSG FCTIPEGGIC RRGGAAAVGE GEEHQLPPPP     50
    PGSFWNVESA AAPGIGCPAA TSSSSATRGR GSSVGGGSRR TTVAYVINEA 100
    SQGQLVVAES EALQSLREAC ETVGATLETL HFGKLDFGET TVLDRFYNAD 150
    IAVVEMSDAF RQPSLFYHLG VRESFSMANN IILYCDTNSD SLQSLKEIIC 200
    QKNTMCTGNY TFVPYMITPH NKVYCCDSSF MKGLTELMQP NFELLLGPIC 250
    LPLVDRFIQL LKVAQASSSQ YFRESILNDI RKARNLYTGK ELAAELARIR 300
    QRVDNIEVLT ADIVINLLLS YRDIQDYDSI VKLVETLEKL PTFDLASHHH 350
    VKFHYAFALN RRNLPGDRAK ALDIMIPMVQ SEGQVASDMY CLVGRIYKDM 400
    FLDSNFTDTE SRDHGASWFK KAFESEPTLQ SGINYAVLLL AAGHQFESSF 450
    ELRKVGVKLS SLLGKKGNLE KLQSYWEVGF FLGASVLAND HMRVIQASEK 500
    LFKLKTPAWY LKSIVETILI YKHFVKLTTE QPVAKQELVD FWMDFLVEAT 550
    KTDVTVVRFP VLILEPTKIY QPSYLSINNE VEEKTISIWH VLPDDKKGIH 600
    EWNFSASSVR GVSISKFEER CCFLYVLHNS DDFQIYFCTE LHCKKFFEMV 650
    NTITEEKGRS TEEGDCESDL LEYDYEYDEN GDRVVLGKGT YGIVYAGRDL 700
    SNQVRIAIKE IPERDSRYSQ PLHEEIALHK HLKHKNIVQY LGSFSENGFI 750
    KIFMEQVPGG SLSALLRSKW GPLKDNEQTI GFYTKQILEG LKYLHDNQIV 800
    HRDIKGDNVL INTYSGVLKI SDFGTSKRLA GINPCTETFT GTLQYMAPEI 850
    IDKGPRGYGK AADIWSLGCT IIEMATGKPP FYELGEPQAA MFKVGMFKVH 900
    PEIPESMSAE AKAFILKCFE PDPDKRACAN DLLVDEFLKV SSKKKKTQPK 950
    LSALSAGSNE YLRSISLPVP VLVEDTSSSS EYGSVSPDTE LKVDPFSFKT 1000
    RAKSCGERDV KGIRTLFLGI PDENFEDHSA PPSPEEKDSG FFMLRKDSER 1050
    RATLHRILTE DQDKIVRNLM ESLAQGAEEP KLKWEHITTL IASLREFVRS 1100
    TDRKIIATTL SKLKLELDFD SHGISQVQVV LFGFQDAVNK VLRNHNIKPH 1150
    WMFALDSIIR KAVQTAITIL VPELRPHFSL ASESDTADQE DLDVEDDHEE 1200
    QPSNQTVRRP QAVIEDAVAT SGVSTLSSTV SHDSQSAHRS LNVQLGRMKI 1250
    ETNRLLEELV RKEKELQALL HRAIEEKDQE IKHLKLKSQP IEIPELPVFH 1300
    LNSSGTNTED SELTDWLRVN GADEDTISRF LAEDYTLLDV LYYVTRDDLK 1350
    CLRLRGGMLC TLWKAIIDFR NKQT 1374
    Length:1,374
    Mass (Da):154,537
    Last modified:May 1, 1997 - v1
    Checksum:i265BDC65968AF985
    GO
    Isoform 2 (identifier: Q99683-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-753: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:621
    Mass (Da):69,839
    Checksum:i7EFE3AD82F6AB9FF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1006 – 10061G → R.1 Publication
    Corresponds to variant rs45626535 [ dbSNP | Ensembl ].
    VAR_040693
    Natural varianti1214 – 12141I → T.1 Publication
    Corresponds to variant rs56379668 [ dbSNP | Ensembl ].
    VAR_040694
    Natural varianti1250 – 12501I → V.1 Publication
    Corresponds to variant rs35551087 [ dbSNP | Ensembl ].
    VAR_040695
    Natural varianti1314 – 13141T → I.1 Publication
    Corresponds to variant rs45599539 [ dbSNP | Ensembl ].
    VAR_040696
    Natural varianti1315 – 13151D → N.1 Publication
    Corresponds to variant rs41288957 [ dbSNP | Ensembl ].
    VAR_040697

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 753753Missing in isoform 2. 1 PublicationVSP_056182Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67156 mRNA. Translation: AAC50894.1.
    D84476 mRNA. Translation: BAA12684.2.
    AK294507 mRNA. Translation: BAG57723.1.
    AL024508, AL121933 Genomic DNA. Translation: CAI20176.1.
    AL121933, AL024508 Genomic DNA. Translation: CAI15470.1.
    BC054503 mRNA. Translation: AAH54503.1.
    BC088829 mRNA. Translation: AAH88829.1.
    CCDSiCCDS5179.1.
    RefSeqiNP_005914.1. NM_005923.3.
    UniGeneiHs.186486.

    Genome annotation databases

    EnsembliENST00000355845; ENSP00000348104; ENSG00000197442.
    ENST00000359015; ENSP00000351908; ENSG00000197442.
    GeneIDi4217.
    KEGGihsa:4217.
    UCSCiuc003qhc.3. human.

    Polymorphism databases

    DMDMi6685617.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67156 mRNA. Translation: AAC50894.1 .
    D84476 mRNA. Translation: BAA12684.2 .
    AK294507 mRNA. Translation: BAG57723.1 .
    AL024508 , AL121933 Genomic DNA. Translation: CAI20176.1 .
    AL121933 , AL024508 Genomic DNA. Translation: CAI15470.1 .
    BC054503 mRNA. Translation: AAH54503.1 .
    BC088829 mRNA. Translation: AAH88829.1 .
    CCDSi CCDS5179.1.
    RefSeqi NP_005914.1. NM_005923.3.
    UniGenei Hs.186486.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CLQ X-ray 2.30 A/B 659-951 [» ]
    3VW6 X-ray 2.40 A/B 671-939 [» ]
    4BF2 X-ray 2.11 A/B 660-977 [» ]
    4BHN X-ray 2.30 A/B 660-977 [» ]
    4BIB X-ray 2.43 A/B 660-977 [» ]
    4BIC X-ray 2.62 A/B 660-977 [» ]
    4BID X-ray 2.80 A/B 660-977 [» ]
    4BIE X-ray 2.36 A/B 660-977 [» ]
    ProteinModelPortali Q99683.
    SMRi Q99683. Positions 650-962.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110381. 74 interactions.
    DIPi DIP-29516N.
    IntActi Q99683. 39 interactions.
    MINTi MINT-99796.
    STRINGi 9606.ENSP00000351908.

    Chemistry

    BindingDBi Q99683.
    ChEMBLi CHEMBL5285.
    GuidetoPHARMACOLOGYi 2080.

    PTM databases

    PhosphoSitei Q99683.

    Polymorphism databases

    DMDMi 6685617.

    Proteomic databases

    MaxQBi Q99683.
    PaxDbi Q99683.
    PRIDEi Q99683.

    Protocols and materials databases

    DNASUi 4217.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355845 ; ENSP00000348104 ; ENSG00000197442 .
    ENST00000359015 ; ENSP00000351908 ; ENSG00000197442 .
    GeneIDi 4217.
    KEGGi hsa:4217.
    UCSCi uc003qhc.3. human.

    Organism-specific databases

    CTDi 4217.
    GeneCardsi GC06M136919.
    HGNCi HGNC:6857. MAP3K5.
    HPAi CAB007824.
    MIMi 602448. gene.
    neXtProti NX_Q99683.
    PharmGKBi PA30601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG006305.
    InParanoidi Q99683.
    KOi K04426.
    OMAi TELHCKK.
    OrthoDBi EOG7WDN1P.
    PhylomeDBi Q99683.
    TreeFami TF105115.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 2681.
    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    SignaLinki Q99683.

    Miscellaneous databases

    ChiTaRSi MAP3K5. human.
    EvolutionaryTracei Q99683.
    GeneWikii ASK1.
    GenomeRNAii 4217.
    NextBioi 16633.
    PROi Q99683.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99683.
    Bgeei Q99683.
    CleanExi HS_MAP3K5.
    Genevestigatori Q99683.

    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 a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase."
      Wang X.S., Diener K., Jannuzzi D., Trollinger D., Tan T.-H., Lichenstein H., Zukowski M., Yao Z.
      J. Biol. Chem. 271:31607-31611(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. "Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways."
      Ichijo H., Nishida E., Irie K., ten Dijke P., Saitoh M., Moriguchi T., Takagi M., Matsumoto K., Miyazono K., Gotoh Y.
      Science 275:90-94(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Eye and Lung.
    6. "Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1."
      Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., Kawabata M., Miyazono K., Ichijo H.
      EMBO J. 17:2596-2606(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXN, ENZYME REGULATION, FUNCTION.
    7. Cited for: ENZYME REGULATION, INTERACTION WITH TRAF2, FUNCTION.
    8. "Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx."
      Chang H.Y., Nishitoh H., Yang X., Ichijo H., Baltimore D.
      Science 281:1860-1863(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAXX, MUTAGENESIS OF LYS-709.
    9. "Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins."
      Zhang L., Chen J., Fu H.
      Proc. Natl. Acad. Sci. U.S.A. 96:8511-8515(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 14-3-3 PROTEINS, ENZYME REGULATION, MUTAGENESIS OF SER-966, FUNCTION.
    10. "Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation."
      Hatai T., Matsuzawa A., Inoshita S., Mochida Y., Kuroda T., Sakamaki K., Kuida K., Yonehara S., Ichijo H., Takeda K.
      J. Biol. Chem. 275:26576-26581(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS.
    11. "Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin."
      Liu H., Nishitoh H., Ichijo H., Kyriakis J.M.
      Mol. Cell. Biol. 20:2198-2208(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH TRAF2, ENZYME REGULATION, FUNCTION.
    12. "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3."
      McDonald P.H., Chow C.W., Miller W.E., Laporte S.A., Field M.E., Lin F.-T., Davis R.J., Lefkowitz R.J.
      Science 290:1574-1577(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    13. "Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in response to oxidative stress."
      Morita K., Saitoh M., Tobiume K., Matsuura H., Enomoto S., Nishitoh H., Ichijo H.
      EMBO J. 20:6028-6036(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP5C, DEPHOSPHORYLATION AT THR-838, SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION.
    14. "Apoptosis signal-regulating kinase 1 (ASK1) is an intracellular inducer of keratinocyte differentiation."
      Sayama K., Hanakawa Y., Shirakata Y., Yamasaki K., Sawada Y., Sun L., Yamanishi K., Ichijo H., Hashimoto K.
      J. Biol. Chem. 276:999-1004(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN KERATINOCYTE DIFFERENTIATION.
    15. "Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1."
      Kim A.H., Khursigara G., Sun X., Franke T.F., Chao M.V.
      Mol. Cell. Biol. 21:893-901(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-83, ENZYME REGULATION, FUNCTION.
    16. "HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell."
      Geleziunas R., Xu W., Takeda K., Ichijo H., Greene W.C.
      Nature 410:834-838(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 NEF, INHIBITION BY HIV-1 NEF.
    17. "Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism."
      Chen J., Fujii K., Zhang L., Roberts T., Fu H.
      Proc. Natl. Acad. Sci. U.S.A. 98:7783-7788(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAF1.
    18. Cited for: INTERACTION WITH TRAF2 AND ERN1, ENZYME REGULATION, FUNCTION IN ER STRESS RESPONSE.
    19. "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: FUNCTION, HOMODIMERIZATION, ENZYME REGULATION, PHOSPHORYLATION AT THR-838.
    20. "Type 1 insulin-like growth factor receptor (IGF-IR) signaling inhibits apoptosis signal-regulating kinase 1 (ASK1)."
      Galvan V., Logvinova A., Sperandio S., Ichijo H., Bredesen D.E.
      J. Biol. Chem. 278:13325-13332(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGF1R, PHOSPHORYLATION, ENZYME REGULATION, SUBCELLULAR LOCATION.
    21. "AKT2 inhibition of cisplatin-induced JNK/p38 and Bax activation by phosphorylation of ASK1: implication of AKT2 in chemoresistance."
      Yuan Z.Q., Feldman R.I., Sussman G.E., Coppola D., Nicosia S.V., Cheng J.Q.
      J. Biol. Chem. 278:23432-23440(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-83, ENZYME REGULATION, FUNCTION.
    22. "AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3."
      Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.
      J. Clin. Invest. 111:1933-1943(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP.
    23. "Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-3 proteins."
      Subramanian R.R., Zhang H., Wang H., Ichijo H., Miyashita T., Fu H.
      Exp. Cell Res. 294:581-591(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YWHAB; YWHAE; YWHAH; YWHAQ; YWHAZ AND SFN, FUNCTION, SUBCELLULAR LOCATION.
    24. "Activation of apoptosis signal-regulating kinase 1 by reactive oxygen species through dephosphorylation at serine 967 and 14-3-3 dissociation."
      Goldman E.H., Chen L., Fu H.
      J. Biol. Chem. 279:10442-10449(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-966, ENZYME REGULATION, FUNCTION.
    25. "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
      Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
      J. Biol. Chem. 279:44955-44965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP.
    26. "Negative control of apoptosis signal-regulating kinase 1 through phosphorylation of Ser-1034."
      Fujii K., Goldman E.H., Park H.R., Zhang L., Chen J., Fu H.
      Oncogene 23:5099-5104(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-966 AND SER-1033, MUTAGENESIS OF SER-966 AND SER-1033, INTERACTION WITH YWHAG.
    27. "C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis."
      Hwang J.R., Zhang C., Patterson C.
      Cell Stress Chaperones 10:147-156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STUB1, UBIQUITINATION.
    28. "Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomain-interacting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation."
      Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.
      J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
    29. "Recruitment of tumor necrosis factor receptor-associated factor family proteins to apoptosis signal-regulating kinase 1 signalosome is essential for oxidative stress-induced cell death."
      Noguchi T., Takeda K., Matsuzawa A., Saegusa K., Nakano H., Gohda J., Inoue J., Ichijo H.
      J. Biol. Chem. 280:37033-37040(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH TRAF2, FUNCTION.
    30. "SOCS1 inhibits tumor necrosis factor-induced activation of ASK1-JNK inflammatory signaling by mediating ASK1 degradation."
      He Y., Zhang W., Zhang R., Zhang H., Min W.
      J. Biol. Chem. 281:5559-5566(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-718, INTERACTION WITH SOCS1, ENZYME REGULATION.
    31. "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.
    32. "Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-activated protein kinase kinase kinase in a heteromeric complex with ASK1."
      Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I., Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.
      J. Biol. Chem. 282:7522-7531(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH MAP3K5, PHOSPHORYLATION AT THR-838, MUTAGENESIS OF LYS-709.
    33. "Tumor necrosis factor receptor 2 signaling induces selective c-IAP1-dependent ASK1 ubiquitination and terminates mitogen-activated protein kinase signaling."
      Zhao Y., Conze D.B., Hanover J.A., Ashwell J.D.
      J. Biol. Chem. 282:7777-7782(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC2, UBIQUITINATION, FUNCTION.
    34. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
      Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
      J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP.
    35. "Thioredoxin and TRAF family proteins regulate reactive oxygen species-dependent activation of ASK1 through reciprocal modulation of the N-terminal homophilic interaction of ASK1."
      Fujino G., Noguchi T., Matsuzawa A., Yamauchi S., Saitoh M., Takeda K., Ichijo H.
      Mol. Cell. Biol. 27:8152-8163(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF2; TRAF6 AND TXN.
    36. "The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus."
      Guo C., Whitmarsh A.J.
      J. Biol. Chem. 283:15903-15911(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    37. "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-838.
    38. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    39. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    40. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis."
      Gu J.J., Wang Z., Reeves R., Magnuson N.S.
      Oncogene 28:4261-4271(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-83 BY PIM1, INTERACTION WITH PIM1.
    42. "Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1."
      Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S., Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.
      Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PGAM5, PHOSPHORYLATION AT THR-838; SER-966 AND SER-1033.
    43. "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.
    44. "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.
    45. "Positive regulation of apoptosis signal-regulating kinase 1 by dual-specificity phosphatase 13A."
      Park J.E., Park B.C., Kim H.A., Song M., Park S.G., Lee D.H., Kim H.J., Choi H.K., Kim J.T., Cho S.
      Cell. Mol. Life Sci. 67:2619-2629(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DUSP13.
    46. "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
      Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
      Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-838, DEPHOSPHORYLATION AT THR-838 BY PPP5C.
    47. "Structural and functional characterization of the human protein kinase ASK1."
      Bunkoczi G., Salah E., Filippakopoulos P., Fedorov O., Muller S., Sobott F., Parker S.A., Zhang H., Min W., Turk B.E., Knapp S.
      Structure 15:1215-1226(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-951, PHOSPHORYLATION AT THR-813; THR-838 AND THR-842.
    48. "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-1006; THR-1214; VAL-1250; ILE-1314 AND ASN-1315.

    Entry informationi

    Entry nameiM3K5_HUMAN
    AccessioniPrimary (citable) accession number: Q99683
    Secondary accession number(s): A6NIA0
    , B4DGB2, Q5THN3, Q99461
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 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 6
      Human chromosome 6: 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