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

 Q923A8_MOUSE            Unreviewed;       606 AA.
Q923A8;
01-DEC-2001, integrated into UniProtKB/TrEMBL.
01-DEC-2001, sequence version 1.
18-JUL-2018, entry version 146.
RecName: Full=Mitogen-activated protein kinase kinase kinase 7 {ECO:0000256|PIRNR:PIRNR038168};
EC=2.7.11.25 {ECO:0000256|PIRNR:PIRNR038168};
Name=Map3k7 {ECO:0000313|EMBL:AAH06665.1,
ECO:0000313|Ensembl:ENSMUSP00000040307, ECO:0000313|MGI:MGI:1346877};
ORFNames=mCG_121930 {ECO:0000313|EMBL:EDL05512.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH06665.1};
[1] {ECO:0000313|EMBL:EDL05512.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Mixed {ECO:0000313|EMBL:EDL05512.1};
PubMed=12040188; DOI=10.1126/science.1069193;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
"A comparison of whole-genome shotgun-derived mouse chromosome 16 and
the human genome.";
Science 296:1661-1671(2002).
[2] {ECO:0000313|EMBL:AAH06665.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N {ECO:0000313|EMBL:AAH06665.1};
TISSUE=Mammary tumor. C3 {ECO:0000313|EMBL:AAH06665.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
Makowski K.A., Bosak S., Malek J.;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3] {ECO:0000313|EMBL:EDL05512.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Mixed {ECO:0000313|EMBL:EDL05512.1};
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000213|PubMed:17242355}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5] {ECO:0000213|PubMed:19144319}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6] {ECO:0000313|Ensembl:ENSMUSP00000040307, ECO:0000313|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000040307,
ECO:0000313|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7] {ECO:0000213|PubMed:21183079}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8] {ECO:0000313|Ensembl:ENSMUSP00000040307}
IDENTIFICATION.
STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000040307};
Ensembl;
Submitted (JUN-2011) to UniProtKB.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000256|PIRNR:PIRNR038168}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|PIRNR:PIRNR038168};
-!- 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. {ECO:0000256|PIRNR:PIRNR038168}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038168}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000256|PIRNR:PIRNR038168}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL833781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006665; AAH06665.1; -; mRNA.
EMBL; CH466538; EDL05512.1; -; Genomic_DNA.
RefSeq; NP_033342.1; NM_009316.1.
UniGene; Mm.258589; -.
IntAct; Q923A8; 5.
Ensembl; ENSMUST00000037607; ENSMUSP00000040307; ENSMUSG00000028284.
GeneID; 26409; -.
UCSC; uc008seq.2; mouse.
CTD; 6885; -.
MGI; MGI:1346877; Map3k7.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140790; -.
HOGENOM; HOG000231735; -.
HOVERGEN; HBG003485; -.
OMA; PARSHPW; -.
OrthoDB; EOG091G03QO; -.
TreeFam; TF105116; -.
ChiTaRS; Map3k7; mouse.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028284; -.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IEA:Ensembl.
GO; GO:0008385; C:IkappaB kinase complex; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
GO; GO:0007252; P:I-kappaB phosphorylation; IEA:UniProtKB-UniRule.
GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0002726; P:positive regulation of T cell cytokine production; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
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 {ECO:0000256|PIRNR:PIRNR038168};
ATP-binding {ECO:0000256|PIRNR:PIRNR038168};
Cell membrane {ECO:0000256|PIRNR:PIRNR038168};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000000589};
Cytoplasm {ECO:0000256|PIRNR:PIRNR038168};
Kinase {ECO:0000256|PIRNR:PIRNR038168};
Magnesium {ECO:0000256|PIRNR:PIRNR038168};
Membrane {ECO:0000256|PIRNR:PIRNR038168};
Metal-binding {ECO:0000256|PIRNR:PIRNR038168};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038168};
Proteomics identification {ECO:0000213|EPD:Q923A8,
ECO:0000213|MaxQB:Q923A8, ECO:0000213|PeptideAtlas:Q923A8};
Reference proteome {ECO:0000313|Proteomes:UP000000589};
Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038168};
Stress response {ECO:0000256|PIRNR:PIRNR038168};
Transcription {ECO:0000256|PIRNR:PIRNR038168};
Transcription regulation {ECO:0000256|PIRNR:PIRNR038168};
Transferase {ECO:0000256|PIRNR:PIRNR038168}.
DOMAIN 36 291 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
COILED 533 564 {ECO:0000256|SAM:Coils}.
SEQUENCE 606 AA; 67194 MW; AB8664F389272102 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
SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIV ATAAYSKPKR GHRKTASFGN
ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPARSHP
WTPDDSTDTN GSDNSIPMAY LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI
ALLLQRKQEL VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ
KRQGTS


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