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Mitogen-activated protein kinase kinase kinase 7 (EC 2 7 11 25)

 M3K7_RAT                Reviewed;         606 AA.
P0C8E4;
04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 1.
18-JUL-2018, entry version 86.
RecName: Full=Mitogen-activated protein kinase kinase kinase 7;
EC=2.7.11.25 {ECO:0000250|UniProtKB:O43318};
Name=Map3k7;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-331.
TISSUE=Hypothalamus, and Prostate;
Amgen EST program;
"Amgen rat EST program.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-606.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-439, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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 signal transduction of TRAF6,
various cytokines including interleukin-1 (IL-1), transforming
growth factor-beta (TGFB), TGFB-related factors like BMP2 and
BMP4, toll-like receptors (TLR), tumor necrosis factor receptor
CD40 and B-cell receptor (BCR). Ceramides are also able to
activate MAP3K7/TAK1. 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 MAP2K1/MEK1,
MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn
activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B
kinase complex (IKK). Both p38 MAPK and JNK pathways control the
transcription factors activator protein-1 (AP-1), while nuclear
factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB
and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-
induced apoptosis. In osmotic stress signaling, plays a major role
in the activation of MAPK8/JNK1, but not that of NF-kappa-B (By
similarity). Promotes TRIM5 capsid-specific restriction activity
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:O43318}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by proinflammatory cytokines and in
response to physical and chemical stresses, including osmotic
stress, oxidative stress, arsenic and ultraviolet light
irradiation. Activated by 'Lys-63'-linked polyubiquitination and
by autophosphorylation. Association with TAB1/MAP3K7IP1 and
TAB2/MAP3K7IP2 promotes activation through autophosphorylation,
whereas PPM1B/PP2CB, PP2A and PPP6C dephosphorylation leads to
inactivation (By similarity). {ECO:0000250}.
-!- SUBUNIT: Can form homodimer. Binds both upstream activators and
downstream substrates in multimolecular complexes. Interacts with
TAB1/MAP3K7IP1, TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3. Identified in
the TRIKA2 complex composed of MAP3K7/TAK1, TAB1/MAP3K7IP1 and
TAB2/MAP3K7IP2. Interacts with PPM1L and PPM1B/PP2CB. Interaction
with PP2A and PPP6C leads to its repressed activity. Interacts
with TRAF6 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts
with TAOK1 and TAOK2; interaction with TAOK2 interferes with
MAP3K7 interaction with IKKA, thus preventing NF-kappa-B
activation. Interacts with WDR34 (via WD domains). Interacts with
CYLD and RBCK1. Interacts with TGFBR1; induces MAP3K7/TAK1
activation by TRAF6. Interacts with MAPK8IP1 and SMAD6. Interacts
with isoform 1 of VRK2. Interacts with DAB2; the interaction is
induced by TGF-beta stimulation and may mediate TGF-beta
stimulated JNK activation. Interacts with TRIM5. Part of a complex
containing ITCH, NDFIP1 and MAP3K7. Interacts with PLEKHM1 (via
N- and C-terminus). Found in a complex with SH3RF1, RAC2,
MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2.
{ECO:0000250|UniProtKB:O43318, ECO:0000250|UniProtKB:Q62073}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Note=Although the majority of
MAP3K7/TAK1 is found in the cytosol, when complexed with
TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the
cell membrane. {ECO:0000250}.
-!- PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation
at Ser-192 and subsequent activation. Association with
TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63
polyubiquitin chain, promotes autophosphorylation and subsequent
activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB
and at Thr-187 by PP2A and PPP6C leads to inactivation (By
similarity). {ECO:0000250}.
-!- PTM: 'Lys-48'-linked polyubiquitination at Lys-72 is induced by
TNFalpha, and leads to proteasomal degradation. Undergoes 'Lys-
48'-linked polyubiquitination catalyzed by ITCH. 'Lys-63'-linked
polyubiquitination at Lys-158 by TRIM8 does not lead to
proteasomal degradation but contributes to autophosphorylation and
activation. Deubiquitinated by CYLD, a protease that selectively
cleaves 'Lys-63'-linked ubiquitin chains.
{ECO:0000250|UniProtKB:O43318, ECO:0000250|UniProtKB:Q62073}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AABR03040223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CB583299; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CB771642; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CK481792; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; DN936104; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; NP_001101390.2; NM_001107920.2.
RefSeq; XP_003750801.1; XM_003750753.4.
UniGene; Rn.24019; -.
SMR; P0C8E4; -.
BioGrid; 260325; 1.
STRING; 10116.ENSRNOP00000007657; -.
iPTMnet; P0C8E4; -.
PhosphoSitePlus; P0C8E4; -.
PaxDb; P0C8E4; -.
PRIDE; P0C8E4; -.
Ensembl; ENSRNOT00000007654; ENSRNOP00000007654; ENSRNOG00000005724.
Ensembl; ENSRNOT00000007657; ENSRNOP00000007657; ENSRNOG00000047516.
GeneID; 100910771; -.
GeneID; 313121; -.
KEGG; rno:100910771; -.
KEGG; rno:313121; -.
UCSC; RGD:1309438; rat.
CTD; 6885; -.
RGD; 1309438; Map3k7.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140790; -.
HOGENOM; HOG000231735; -.
HOVERGEN; HBG003485; -.
InParanoid; P0C8E4; -.
KO; K04427; -.
OMA; PARSHPW; -.
OrthoDB; EOG091G03QO; -.
PhylomeDB; P0C8E4; -.
TreeFam; TF105116; -.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-202424; Downstream TCR signaling.
Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
Reactome; R-RNO-4086398; Ca2+ pathway.
Reactome; R-RNO-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-RNO-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
Reactome; R-RNO-9020702; Interleukin-1 signaling.
Reactome; R-RNO-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-RNO-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-RNO-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
PRO; PR:P0C8E4; -.
Proteomes; UP000002494; Chromosome 5.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000005724; -.
Genevisible; P0C8E4; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:RGD.
GO; GO:0000186; P:activation of MAPKK activity; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007252; P:I-kappaB phosphorylation; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IDA:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:RGD.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017421; MAPKKK7.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR26392:SF74; PTHR26392:SF74; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF038168; MAPKKK7; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Apoptosis; ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
Isopeptide bond; Kinase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 606 Mitogen-activated protein kinase kinase
kinase 7.
/FTId=PRO_0000353138.
DOMAIN 36 291 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 42 50 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 300 Interaction with MAPK8IP1. {ECO:0000250}.
COMPBIAS 8 14 Poly-Ser.
ACT_SITE 156 156 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 63 63 ATP.
MOD_RES 184 184 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:O43318}.
MOD_RES 187 187 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:O43318}.
MOD_RES 192 192 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O43318}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000250|UniProtKB:O43318}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000250|UniProtKB:O43318}.
CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O43318}.
SEQUENCE 606 AA; 67200 MW; E24987277A616DCD CRC64;
MSTASAASSS SSSSASEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV
AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE
PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC
DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM
WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY
PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ
SDSGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIV ATTAYTKPKR GHRKTASFGN
ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPARSLP
WTPDDSTDTN GSDNSIPMAY LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI
ALLLQRKQEL VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ
KRQGTS


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