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O35099

- M3K5_MOUSE

UniProt

O35099 - M3K5_MOUSE

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Protein
Mitogen-activated protein kinase kinase kinase 5
Gene
Map3k5, Ask1, Mekk5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 7161ATP By similarity
Active sitei810 – 8101Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi693 – 7019ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. JNK cascade Source: Ensembl
  2. MAPK cascade Source: UniProtKB
  3. activation of MAPK activity Source: MGI
  4. cellular response to hydrogen peroxide Source: Ensembl
  5. cellular response to reactive nitrogen species Source: MGI
  6. innate immune response Source: UniProtKB-KW
  7. intrinsic apoptotic signaling pathway in response to oxidative stress Source: MGI
  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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901Phosphoserine; by PIM1, PKB/AKT1 and PKB/AKT2 By similarity
Modified residuei725 – 7251Phosphotyrosine By similarity
Modified residuei820 – 8201Phosphothreonine; by autocatalysis By similarity
Modified residuei845 – 8451Phosphothreonine; by autocatalysis, MELK and MAP3K63 Publications
Modified residuei849 – 8491Phosphothreonine; by autocatalysis1 Publication
Modified residuei965 – 9651Phosphoserine By similarity
Modified residuei973 – 9731Phosphoserine By similarity
Modified residuei983 – 9831Phosphothreonine
Modified residuei1036 – 10361Phosphoserine By similarity
Modified residuei1040 – 10401Phosphoserine By 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.4 Publications
Ubiquitinated By similarity. 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.4 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini687 – 945259Protein kinase
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1252 – 129241 Reviewed prediction
Add
BLAST

Sequence similaritiesi

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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661A → T in BAA23648. 1 Publication
Sequence conflicti368 – 3703RRN → TRT in BAA23648. 1 Publication
Sequence conflicti1090 – 10901K → N in BAA23648. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

Similar proteinsi