Full text data of MAP3K6
MAP3K6
(ASK2, MAPKKK6, MEKK6)
[Confidence: low (only semi-automatic identification from reviews)]
Mitogen-activated protein kinase kinase kinase 6; 2.7.11.25 (Apoptosis signal-regulating kinase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Mitogen-activated protein kinase kinase kinase 6; 2.7.11.25 (Apoptosis signal-regulating kinase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95382
ID M3K6_HUMAN Reviewed; 1288 AA.
AC O95382; A2ACE8; A2VDG4; A2VDG5; Q59HF4; Q5SSD4; Q75PK3; Q96B75;
read moreDT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 6;
DE EC=2.7.11.25;
DE AltName: Full=Apoptosis signal-regulating kinase 2;
GN Name=MAP3K6; Synonyms=ASK2, MAPKKK6, MEKK6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP INTERACTION WITH MAP3K5, AND VARIANT ILE-455.
RX PubMed=17210579; DOI=10.1074/jbc.M607177200;
RA Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I.,
RA Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.;
RT "Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-
RT activated protein kinase kinase kinase in a heteromeric complex with
RT ASK1.";
RL J. Biol. Chem. 282:7522-7531(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 435-1288 (ISOFORMS 1/3), AND VARIANTS
RP ILE-455 AND ASN-969.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1288 (ISOFORM 3), AND
RP VARIANT LYS-622.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-1288, FUNCTION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH MAP3K5.
RX PubMed=9875215; DOI=10.1006/bbrc.1998.9749;
RA Wang X.S., Diener K., Tan T.-H., Yao Z.;
RT "MAPKKK6, a novel mitogen-activated protein kinase kinase kinase, that
RT associates with MAPKKK5.";
RL Biochem. Biophys. Res. Commun. 253:33-37(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 AND SER-1129, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984; SER-1129 AND
RP SER-1149, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] THR-869.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-544; LYS-622; GLY-668; LEU-673;
RP LEU-925; ILE-968 AND THR-1061.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Component of a protein kinase signal transduction
CC cascade. Activates the JNK, but not ERK or p38 kinase pathways.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- ENZYME REGULATION: Activated by phosphorylation on Thr-806.
CC Catalytically active only when complexed with MAP3K5, with MAP3K5
CC supporting the stability and the active configuration of MAP3K6
CC and MAP3K6 activating MAP3K5 by direct phosphorylation.
CC -!- SUBUNIT: Binds both upstream activators and downstream substrates
CC in multimolecular complexes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95382-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95382-2; Sequence=VSP_026201, VSP_026203, VSP_026204;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O95382-3; Sequence=VSP_026202;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05304.1; Type=Erroneous initiation;
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DR EMBL; AB167411; BAD12485.1; -; mRNA.
DR EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015914; AAH15914.1; -; mRNA.
DR EMBL; BC129950; AAI29951.1; -; mRNA.
DR EMBL; BC129951; AAI29952.1; -; mRNA.
DR EMBL; AB208805; BAD92042.1; -; mRNA.
DR EMBL; AF100318; AAD05304.1; ALT_INIT; mRNA.
DR RefSeq; NP_004663.3; NM_004672.3.
DR RefSeq; XP_005246086.1; XM_005246029.1.
DR UniGene; Hs.194694; -.
DR ProteinModelPortal; O95382; -.
DR SMR; O95382; 605-950.
DR IntAct; O95382; 7.
DR MINT; MINT-7997495; -.
DR STRING; 9606.ENSP00000350195; -.
DR BindingDB; O95382; -.
DR ChEMBL; CHEMBL1163123; -.
DR GuidetoPHARMACOLOGY; 2081; -.
DR PhosphoSite; O95382; -.
DR PaxDb; O95382; -.
DR PRIDE; O95382; -.
DR Ensembl; ENST00000357582; ENSP00000350195; ENSG00000142733.
DR Ensembl; ENST00000374040; ENSP00000363152; ENSG00000142733.
DR Ensembl; ENST00000493901; ENSP00000419591; ENSG00000142733.
DR GeneID; 9064; -.
DR KEGG; hsa:9064; -.
DR UCSC; uc001bny.1; human.
DR CTD; 9064; -.
DR GeneCards; GC01M027681; -.
DR H-InvDB; HIX0000314; -.
DR HGNC; HGNC:6858; MAP3K6.
DR HPA; HPA051192; -.
DR MIM; 604468; gene.
DR neXtProt; NX_O95382; -.
DR PharmGKB; PA30602; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG006305; -.
DR InParanoid; O95382; -.
DR KO; K04425; -.
DR OMA; KMQYYWD; -.
DR PhylomeDB; O95382; -.
DR BRENDA; 2.7.11.25; 2681.
DR SignaLink; O95382; -.
DR GenomeRNAi; 9064; -.
DR NextBio; 33967; -.
DR PRO; PR:O95382; -.
DR ArrayExpress; O95382; -.
DR Bgee; O95382; -.
DR CleanEx; HS_MAP3K6; -.
DR Genevestigator; O95382; -.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR InterPro; IPR025136; DUF4071.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13281; DUF4071; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Complete proteome;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 1288 Mitogen-activated protein kinase kinase
FT kinase 6.
FT /FTId=PRO_0000086251.
FT DOMAIN 648 906 Protein kinase.
FT NP_BIND 654 662 ATP (By similarity).
FT COILED 1004 1029 Potential.
FT COILED 1166 1205 Potential.
FT ACT_SITE 771 771 Proton acceptor (By similarity).
FT BINDING 677 677 ATP (By similarity).
FT MOD_RES 806 806 Phosphothreonine (By similarity).
FT MOD_RES 984 984 Phosphoserine.
FT MOD_RES 1129 1129 Phosphoserine.
FT MOD_RES 1149 1149 Phosphoserine.
FT VAR_SEQ 1 277 Missing (in isoform 2).
FT /FTId=VSP_026201.
FT VAR_SEQ 161 168 Missing (in isoform 3).
FT /FTId=VSP_026202.
FT VAR_SEQ 1065 1074 RLRAQGLGPA -> WMNGEDKGSF (in isoform 2).
FT /FTId=VSP_026203.
FT VAR_SEQ 1075 1288 Missing (in isoform 2).
FT /FTId=VSP_026204.
FT VARIANT 455 455 T -> I (in dbSNP:rs1138294).
FT /FTId=VAR_032832.
FT VARIANT 499 499 R -> C (in dbSNP:rs11247641).
FT /FTId=VAR_046050.
FT VARIANT 544 544 R -> W (in dbSNP:rs55671988).
FT /FTId=VAR_046051.
FT VARIANT 622 622 N -> K (in dbSNP:rs35659744).
FT /FTId=VAR_032833.
FT VARIANT 668 668 R -> G (in dbSNP:rs55869163).
FT /FTId=VAR_046052.
FT VARIANT 673 673 R -> L (in dbSNP:rs56359841).
FT /FTId=VAR_046053.
FT VARIANT 869 869 P -> T (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035629.
FT VARIANT 925 925 S -> L (in a breast pleomorphic lobular
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_046054.
FT VARIANT 968 968 T -> I (in an ovarian endometrioid cancer
FT sample; somatic mutation).
FT /FTId=VAR_046055.
FT VARIANT 969 969 S -> N (in dbSNP:rs17856498).
FT /FTId=VAR_032834.
FT VARIANT 1061 1061 A -> T (in dbSNP:rs55990440).
FT /FTId=VAR_046056.
FT VARIANT 1233 1233 G -> A (in dbSNP:rs17162549).
FT /FTId=VAR_046057.
FT CONFLICT 435 440 MQYYWD -> ALWVPV (in Ref. 3; AAI29952).
FT CONFLICT 435 440 MQYYWD -> HTWVPV (in Ref. 3; AAI29951).
SQ SEQUENCE 1288 AA; 142596 MW; 013AF3729698080F CRC64;
MAGPCPRSGA ERAGSCWQDP LAVALSRGRQ LAAPPGRGCA RSRPLSVVYV LTREPQPGLE
PREGTEAEPL PLRCLREACA QVPRPRPPPQ LRSLPFGTLE LGDTAALDAF YNADVVVLEV
SSSLVQPSLF YHLGVRESFS MTNNVLLCSQ ADLPDLQALR EDVFQKNSDC VGSYTLIPYV
VTATGRVLCG DAGLLRGLAD GLVQAGVGTE ALLTPLVGRL ARLLEATPTD SCGYFRETIR
RDIRQARERF SGPQLRQELA RLQRRLDSVE LLSPDIIMNL LLSYRDVQDY SAIIELVETL
QALPTCDVAE QHNVCFHYTF ALNRRNRPGD RAKALSVLLP LVQLEGSVAP DLYCMCGRIY
KDMFFSSGFQ DAGHREQAYH WYRKAFDVEP SLHSGINAAV LLIAAGQHFE DSKELRLIGM
KLGCLLARKG CVEKMQYYWD VGFYLGAQIL ANDPTQVVLA AEQLYKLNAP IWYLVSVMET
FLLYQHFRPT PEPPGGPPRR AHFWLHFLLQ SCQPFKTACA QGDQCLVLVL EMNKVLLPAK
LEVRGTDPVS TVTLSLLEPE TQDIPSSWTF PVASICGVSA SKRDERCCFL YALPPAQDVQ
LCFPSVGHCQ WFCGLIQAWV TNPDSTAPAE EAEGAGEMLE FDYEYTETGE RLVLGKGTYG
VVYAGRDRHT RVRIAIKEIP ERDSRFSQPL HEEIALHRRL RHKNIVRYLG SASQGGYLKI
FMEEVPGGSL SSLLRSVWGP LKDNESTISF YTRQILQGLG YLHDNHIVHR DIKGDNVLIN
TFSGLLKISD FGTSKRLAGI TPCTETFTGT LQYMAPEIID QGPRGYGKAA DIWSLGCTVI
EMATGRPPFH ELGSPQAAMF QVGMYKVHPP MPSSLSAEAQ AFLLRTFEPD PRLRASAQTL
LGDPFLQPGK RSRSPSSPRH APRPSDAPSA SPTPSANSTT QSQTFPCPQA PSQHPPSPPK
RCLSYGGTSQ LRVPEEPAAE EPASPEESSG LSLLHQESKR RAMLAAVLEQ ELPALAENLH
QEQKQEQGAR LGRNHVEELL RCLGAHIHTP NRRQLAQELR ALQGRLRAQG LGPALLHRPL
FAFPDAVKQI LRKRQIRPHW MFVLDSLLSR AVRAALGVLG PEVEKEAVSP RSEELSNEGD
SQQSPGQQSP LPVEPEQGPA PLMVQLSLLR AETDRLREIL AGKEREYQAL VQRALQRLNE
EARTYVLAPE PPTALSTDQG LVQWLQELNV DSGTIQMLLN HSFTLHTLLT YATRDDLIYT
RIRGGMVCRI WRAILAQRAG STPVTSGP
//
ID M3K6_HUMAN Reviewed; 1288 AA.
AC O95382; A2ACE8; A2VDG4; A2VDG5; Q59HF4; Q5SSD4; Q75PK3; Q96B75;
read moreDT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 6;
DE EC=2.7.11.25;
DE AltName: Full=Apoptosis signal-regulating kinase 2;
GN Name=MAP3K6; Synonyms=ASK2, MAPKKK6, MEKK6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP INTERACTION WITH MAP3K5, AND VARIANT ILE-455.
RX PubMed=17210579; DOI=10.1074/jbc.M607177200;
RA Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I.,
RA Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.;
RT "Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-
RT activated protein kinase kinase kinase in a heteromeric complex with
RT ASK1.";
RL J. Biol. Chem. 282:7522-7531(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 435-1288 (ISOFORMS 1/3), AND VARIANTS
RP ILE-455 AND ASN-969.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1288 (ISOFORM 3), AND
RP VARIANT LYS-622.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-1288, FUNCTION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH MAP3K5.
RX PubMed=9875215; DOI=10.1006/bbrc.1998.9749;
RA Wang X.S., Diener K., Tan T.-H., Yao Z.;
RT "MAPKKK6, a novel mitogen-activated protein kinase kinase kinase, that
RT associates with MAPKKK5.";
RL Biochem. Biophys. Res. Commun. 253:33-37(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 AND SER-1129, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984; SER-1129 AND
RP SER-1149, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] THR-869.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-544; LYS-622; GLY-668; LEU-673;
RP LEU-925; ILE-968 AND THR-1061.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Component of a protein kinase signal transduction
CC cascade. Activates the JNK, but not ERK or p38 kinase pathways.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- ENZYME REGULATION: Activated by phosphorylation on Thr-806.
CC Catalytically active only when complexed with MAP3K5, with MAP3K5
CC supporting the stability and the active configuration of MAP3K6
CC and MAP3K6 activating MAP3K5 by direct phosphorylation.
CC -!- SUBUNIT: Binds both upstream activators and downstream substrates
CC in multimolecular complexes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95382-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95382-2; Sequence=VSP_026201, VSP_026203, VSP_026204;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O95382-3; Sequence=VSP_026202;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD05304.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AB167411; BAD12485.1; -; mRNA.
DR EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015914; AAH15914.1; -; mRNA.
DR EMBL; BC129950; AAI29951.1; -; mRNA.
DR EMBL; BC129951; AAI29952.1; -; mRNA.
DR EMBL; AB208805; BAD92042.1; -; mRNA.
DR EMBL; AF100318; AAD05304.1; ALT_INIT; mRNA.
DR RefSeq; NP_004663.3; NM_004672.3.
DR RefSeq; XP_005246086.1; XM_005246029.1.
DR UniGene; Hs.194694; -.
DR ProteinModelPortal; O95382; -.
DR SMR; O95382; 605-950.
DR IntAct; O95382; 7.
DR MINT; MINT-7997495; -.
DR STRING; 9606.ENSP00000350195; -.
DR BindingDB; O95382; -.
DR ChEMBL; CHEMBL1163123; -.
DR GuidetoPHARMACOLOGY; 2081; -.
DR PhosphoSite; O95382; -.
DR PaxDb; O95382; -.
DR PRIDE; O95382; -.
DR Ensembl; ENST00000357582; ENSP00000350195; ENSG00000142733.
DR Ensembl; ENST00000374040; ENSP00000363152; ENSG00000142733.
DR Ensembl; ENST00000493901; ENSP00000419591; ENSG00000142733.
DR GeneID; 9064; -.
DR KEGG; hsa:9064; -.
DR UCSC; uc001bny.1; human.
DR CTD; 9064; -.
DR GeneCards; GC01M027681; -.
DR H-InvDB; HIX0000314; -.
DR HGNC; HGNC:6858; MAP3K6.
DR HPA; HPA051192; -.
DR MIM; 604468; gene.
DR neXtProt; NX_O95382; -.
DR PharmGKB; PA30602; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG006305; -.
DR InParanoid; O95382; -.
DR KO; K04425; -.
DR OMA; KMQYYWD; -.
DR PhylomeDB; O95382; -.
DR BRENDA; 2.7.11.25; 2681.
DR SignaLink; O95382; -.
DR GenomeRNAi; 9064; -.
DR NextBio; 33967; -.
DR PRO; PR:O95382; -.
DR ArrayExpress; O95382; -.
DR Bgee; O95382; -.
DR CleanEx; HS_MAP3K6; -.
DR Genevestigator; O95382; -.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR InterPro; IPR025136; DUF4071.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13281; DUF4071; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Complete proteome;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 1288 Mitogen-activated protein kinase kinase
FT kinase 6.
FT /FTId=PRO_0000086251.
FT DOMAIN 648 906 Protein kinase.
FT NP_BIND 654 662 ATP (By similarity).
FT COILED 1004 1029 Potential.
FT COILED 1166 1205 Potential.
FT ACT_SITE 771 771 Proton acceptor (By similarity).
FT BINDING 677 677 ATP (By similarity).
FT MOD_RES 806 806 Phosphothreonine (By similarity).
FT MOD_RES 984 984 Phosphoserine.
FT MOD_RES 1129 1129 Phosphoserine.
FT MOD_RES 1149 1149 Phosphoserine.
FT VAR_SEQ 1 277 Missing (in isoform 2).
FT /FTId=VSP_026201.
FT VAR_SEQ 161 168 Missing (in isoform 3).
FT /FTId=VSP_026202.
FT VAR_SEQ 1065 1074 RLRAQGLGPA -> WMNGEDKGSF (in isoform 2).
FT /FTId=VSP_026203.
FT VAR_SEQ 1075 1288 Missing (in isoform 2).
FT /FTId=VSP_026204.
FT VARIANT 455 455 T -> I (in dbSNP:rs1138294).
FT /FTId=VAR_032832.
FT VARIANT 499 499 R -> C (in dbSNP:rs11247641).
FT /FTId=VAR_046050.
FT VARIANT 544 544 R -> W (in dbSNP:rs55671988).
FT /FTId=VAR_046051.
FT VARIANT 622 622 N -> K (in dbSNP:rs35659744).
FT /FTId=VAR_032833.
FT VARIANT 668 668 R -> G (in dbSNP:rs55869163).
FT /FTId=VAR_046052.
FT VARIANT 673 673 R -> L (in dbSNP:rs56359841).
FT /FTId=VAR_046053.
FT VARIANT 869 869 P -> T (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035629.
FT VARIANT 925 925 S -> L (in a breast pleomorphic lobular
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_046054.
FT VARIANT 968 968 T -> I (in an ovarian endometrioid cancer
FT sample; somatic mutation).
FT /FTId=VAR_046055.
FT VARIANT 969 969 S -> N (in dbSNP:rs17856498).
FT /FTId=VAR_032834.
FT VARIANT 1061 1061 A -> T (in dbSNP:rs55990440).
FT /FTId=VAR_046056.
FT VARIANT 1233 1233 G -> A (in dbSNP:rs17162549).
FT /FTId=VAR_046057.
FT CONFLICT 435 440 MQYYWD -> ALWVPV (in Ref. 3; AAI29952).
FT CONFLICT 435 440 MQYYWD -> HTWVPV (in Ref. 3; AAI29951).
SQ SEQUENCE 1288 AA; 142596 MW; 013AF3729698080F CRC64;
MAGPCPRSGA ERAGSCWQDP LAVALSRGRQ LAAPPGRGCA RSRPLSVVYV LTREPQPGLE
PREGTEAEPL PLRCLREACA QVPRPRPPPQ LRSLPFGTLE LGDTAALDAF YNADVVVLEV
SSSLVQPSLF YHLGVRESFS MTNNVLLCSQ ADLPDLQALR EDVFQKNSDC VGSYTLIPYV
VTATGRVLCG DAGLLRGLAD GLVQAGVGTE ALLTPLVGRL ARLLEATPTD SCGYFRETIR
RDIRQARERF SGPQLRQELA RLQRRLDSVE LLSPDIIMNL LLSYRDVQDY SAIIELVETL
QALPTCDVAE QHNVCFHYTF ALNRRNRPGD RAKALSVLLP LVQLEGSVAP DLYCMCGRIY
KDMFFSSGFQ DAGHREQAYH WYRKAFDVEP SLHSGINAAV LLIAAGQHFE DSKELRLIGM
KLGCLLARKG CVEKMQYYWD VGFYLGAQIL ANDPTQVVLA AEQLYKLNAP IWYLVSVMET
FLLYQHFRPT PEPPGGPPRR AHFWLHFLLQ SCQPFKTACA QGDQCLVLVL EMNKVLLPAK
LEVRGTDPVS TVTLSLLEPE TQDIPSSWTF PVASICGVSA SKRDERCCFL YALPPAQDVQ
LCFPSVGHCQ WFCGLIQAWV TNPDSTAPAE EAEGAGEMLE FDYEYTETGE RLVLGKGTYG
VVYAGRDRHT RVRIAIKEIP ERDSRFSQPL HEEIALHRRL RHKNIVRYLG SASQGGYLKI
FMEEVPGGSL SSLLRSVWGP LKDNESTISF YTRQILQGLG YLHDNHIVHR DIKGDNVLIN
TFSGLLKISD FGTSKRLAGI TPCTETFTGT LQYMAPEIID QGPRGYGKAA DIWSLGCTVI
EMATGRPPFH ELGSPQAAMF QVGMYKVHPP MPSSLSAEAQ AFLLRTFEPD PRLRASAQTL
LGDPFLQPGK RSRSPSSPRH APRPSDAPSA SPTPSANSTT QSQTFPCPQA PSQHPPSPPK
RCLSYGGTSQ LRVPEEPAAE EPASPEESSG LSLLHQESKR RAMLAAVLEQ ELPALAENLH
QEQKQEQGAR LGRNHVEELL RCLGAHIHTP NRRQLAQELR ALQGRLRAQG LGPALLHRPL
FAFPDAVKQI LRKRQIRPHW MFVLDSLLSR AVRAALGVLG PEVEKEAVSP RSEELSNEGD
SQQSPGQQSP LPVEPEQGPA PLMVQLSLLR AETDRLREIL AGKEREYQAL VQRALQRLNE
EARTYVLAPE PPTALSTDQG LVQWLQELNV DSGTIQMLLN HSFTLHTLLT YATRDDLIYT
RIRGGMVCRI WRAILAQRAG STPVTSGP
//
MIM
604468
*RECORD*
*FIELD* NO
604468
*FIELD* TI
*604468 MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; MAP3K6
;;MAPKKK6;;
APOPTOSIS SIGNAL-REGULATING KINASE 2; ASK2
read more*FIELD* TX
Mitogen-activated protein kinase (MAPK) cascades consist of a 3-kinase
module: MAPK, MAPK kinase (MAP2K, MAPKK, or MKK), and MKK kinase (MAP3K,
MAPKKK, or MEKK). These kinase cascades relay signals from the cell
surface to the nucleus, resulting in gene transcription. Growth factors
and mitogens activate the extracellular-regulated kinase (ERK) pathway,
while stress stimuli and proinflammatory cytokines activate 2 closely
related but distinct parallel pathways, the c-Jun N-terminal kinase
(JNK), or stress-activated kinase (SAPK), pathway and the p38 kinase
pathway. Multiple upstream kinases, the MAP3Ks, have been identified.
MAP3K5 (602448) activates the JNK and p38 pathways and induces apoptosis
when overexpressed in stably transfected cells. Using a portion of
MAP3K5 as bait in a yeast 2-hybrid system, Wang et al. (1998) isolated a
partial cDNA encoding a novel protein kinase, MAP3K6, which they called
MAPKKK6. They isolated a full-length human skeletal muscle MAP3K6 cDNA
encoding a predicted 1,280-amino acid serine/threonine kinase containing
all 11 kinase subdomains. MAP3K6 and MAP3K5 share 45% amino acid
sequence identity; their catalytic domains share 82% identity. The
authors confirmed the interaction of MAP3K6 with MAP3K5 in vivo using
coimmunoprecipitation. Recombinant MAP3K6 weakly activated the JNK but
not the ERK or p38 kinase pathways. Northern blot analysis detected an
approximately 5.0-kb MAP3K6 transcript in several tissues, with the
highest expression in heart and skeletal muscle.
*FIELD* RF
1. Wang, X. S.; Diener, K.; Tan, T.-H.; Yao, Z.: MAPKKK6, a novel
mitogen-activated protein kinase kinase kinase, that associates with
MAPKKK5. Biochem. Biophys. Res. Commun. 253: 33-37, 1998.
*FIELD* CD
Patti M. Sherman: 1/27/2000
*FIELD* ED
mgross: 07/26/2010
mgross: 1/28/2000
psherman: 1/27/2000
*RECORD*
*FIELD* NO
604468
*FIELD* TI
*604468 MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; MAP3K6
;;MAPKKK6;;
APOPTOSIS SIGNAL-REGULATING KINASE 2; ASK2
read more*FIELD* TX
Mitogen-activated protein kinase (MAPK) cascades consist of a 3-kinase
module: MAPK, MAPK kinase (MAP2K, MAPKK, or MKK), and MKK kinase (MAP3K,
MAPKKK, or MEKK). These kinase cascades relay signals from the cell
surface to the nucleus, resulting in gene transcription. Growth factors
and mitogens activate the extracellular-regulated kinase (ERK) pathway,
while stress stimuli and proinflammatory cytokines activate 2 closely
related but distinct parallel pathways, the c-Jun N-terminal kinase
(JNK), or stress-activated kinase (SAPK), pathway and the p38 kinase
pathway. Multiple upstream kinases, the MAP3Ks, have been identified.
MAP3K5 (602448) activates the JNK and p38 pathways and induces apoptosis
when overexpressed in stably transfected cells. Using a portion of
MAP3K5 as bait in a yeast 2-hybrid system, Wang et al. (1998) isolated a
partial cDNA encoding a novel protein kinase, MAP3K6, which they called
MAPKKK6. They isolated a full-length human skeletal muscle MAP3K6 cDNA
encoding a predicted 1,280-amino acid serine/threonine kinase containing
all 11 kinase subdomains. MAP3K6 and MAP3K5 share 45% amino acid
sequence identity; their catalytic domains share 82% identity. The
authors confirmed the interaction of MAP3K6 with MAP3K5 in vivo using
coimmunoprecipitation. Recombinant MAP3K6 weakly activated the JNK but
not the ERK or p38 kinase pathways. Northern blot analysis detected an
approximately 5.0-kb MAP3K6 transcript in several tissues, with the
highest expression in heart and skeletal muscle.
*FIELD* RF
1. Wang, X. S.; Diener, K.; Tan, T.-H.; Yao, Z.: MAPKKK6, a novel
mitogen-activated protein kinase kinase kinase, that associates with
MAPKKK5. Biochem. Biophys. Res. Commun. 253: 33-37, 1998.
*FIELD* CD
Patti M. Sherman: 1/27/2000
*FIELD* ED
mgross: 07/26/2010
mgross: 1/28/2000
psherman: 1/27/2000