M4K3_HUMAN
ID M4K3_HUMAN Reviewed; 894 AA.
AC Q8IVH8; Q6IQ39; Q8IVH7; Q9UDM5; Q9Y6R5;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Germinal center kinase-related protein kinase;
DE Short=GLK;
DE AltName: Full=MAPK/ERK kinase kinase kinase 3;
DE Short=MEK kinase kinase 3;
DE Short=MEKKK 3;
GN Name=MAP4K3; Synonyms=RAB8IPL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAN75849.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF LYS-48.
RC TISSUE=Macrophage, and Skeletal muscle;
RX PubMed=9275185; DOI=10.1073/pnas.94.18.9687;
RA Diener K., Wang X.S., Chen C., Meyer C.F., Keesler G., Zukowski M.,
RA Tan T.-H., Yao Z.;
RT "Activation of the c-Jun N-terminal kinase pathway by a novel protein
RT kinase related to human germinal center kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9687-9692(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
RA Gorry M.C., Zhang Y., Marks J.J., Suppe B., Hart S., Cortelli J.,
RA Pallos D., Hart T.C.;
RT "Physical/genetic map of the 2p22-2p21 region on chromosome 2.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE OF 1-712 (ISOFORM 1).
RA Edwards J., Wohldmann P., Hawkins M., Harkins R.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-200; GLN-424 AND SER-669.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: May play a role in the response to environmental stress.
CC Appears to act upstream of the JUN N-terminal pathway.
CC {ECO:0000269|PubMed:9275185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:9275185};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9275185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9275185};
CC -!- SUBUNIT: Interacts with SH3GL2. Interaction appears to regulate MAP4K3-
CC mediated JNK activation (By similarity).
CC {ECO:0000250|UniProtKB:Q924I2}.
CC -!- INTERACTION:
CC Q8IVH8; P62993: GRB2; NbExp=2; IntAct=EBI-1758170, EBI-401755;
CC Q8IVH8; Q13094: LCP2; NbExp=5; IntAct=EBI-1758170, EBI-346946;
CC Q8IVH8; Q04759: PRKCQ; NbExp=4; IntAct=EBI-1758170, EBI-374762;
CC Q8IVH8; Q02111: Prkcq; Xeno; NbExp=4; IntAct=EBI-1758170, EBI-2639157;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000303|PubMed:9275185, ECO:0000305};
CC IsoId=Q8IVH8-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:9275185, ECO:0000305};
CC IsoId=Q8IVH8-2; Sequence=VSP_007052;
CC Name=3 {ECO:0000303|PubMed:9275185, ECO:0000305};
CC IsoId=Q8IVH8-3; Sequence=VSP_007053;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined,
CC with high levels in heart, brain, placenta, skeletal muscle, kidney and
CC pancreas and lower levels in lung and liver.
CC {ECO:0000269|PubMed:9275185}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AF000145; AAC15472.1; -; mRNA.
DR EMBL; AF445413; AAN75849.1; -; Genomic_DNA.
DR EMBL; AF445385; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445386; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445387; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445388; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445390; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445391; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445392; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445393; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445394; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445395; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445396; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445397; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445398; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445399; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445400; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445401; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445402; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445403; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445404; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445405; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445406; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445407; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445408; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445409; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445410; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445411; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445412; AAN75849.1; JOINED; Genomic_DNA.
DR EMBL; AF445413; AAN75850.1; -; Genomic_DNA.
DR EMBL; AF445385; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445386; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445387; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445388; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445390; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445391; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445392; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445393; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445394; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445395; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445397; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445398; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445399; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445400; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445401; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445402; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445403; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445404; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445405; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445406; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445407; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445408; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445409; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445410; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445411; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; AF445412; AAN75850.1; JOINED; Genomic_DNA.
DR EMBL; CH471053; EAX00346.1; -; Genomic_DNA.
DR EMBL; BC071579; AAH71579.1; -; mRNA.
DR EMBL; AC007684; AAF19240.1; -; Genomic_DNA.
DR CCDS; CCDS1803.1; -. [Q8IVH8-1]
DR CCDS; CCDS58707.1; -. [Q8IVH8-3]
DR RefSeq; NP_001257354.1; NM_001270425.1. [Q8IVH8-3]
DR RefSeq; NP_003609.2; NM_003618.3. [Q8IVH8-1]
DR PDB; 5J5T; X-ray; 2.85 A; A=13-380.
DR PDBsum; 5J5T; -.
DR AlphaFoldDB; Q8IVH8; -.
DR SMR; Q8IVH8; -.
DR BioGRID; 114063; 74.
DR DIP; DIP-48924N; -.
DR IntAct; Q8IVH8; 18.
DR MINT; Q8IVH8; -.
DR STRING; 9606.ENSP00000263881; -.
DR BindingDB; Q8IVH8; -.
DR ChEMBL; CHEMBL5432; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8IVH8; -.
DR GuidetoPHARMACOLOGY; 2087; -.
DR iPTMnet; Q8IVH8; -.
DR PhosphoSitePlus; Q8IVH8; -.
DR SwissPalm; Q8IVH8; -.
DR BioMuta; MAP4K3; -.
DR DMDM; 29427817; -.
DR CPTAC; CPTAC-864; -.
DR CPTAC; CPTAC-865; -.
DR EPD; Q8IVH8; -.
DR jPOST; Q8IVH8; -.
DR MassIVE; Q8IVH8; -.
DR MaxQB; Q8IVH8; -.
DR PaxDb; Q8IVH8; -.
DR PeptideAtlas; Q8IVH8; -.
DR PRIDE; Q8IVH8; -.
DR ProteomicsDB; 70709; -. [Q8IVH8-1]
DR ProteomicsDB; 70710; -. [Q8IVH8-2]
DR ProteomicsDB; 70711; -. [Q8IVH8-3]
DR Antibodypedia; 29616; 362 antibodies from 33 providers.
DR DNASU; 8491; -.
DR Ensembl; ENST00000263881.8; ENSP00000263881.3; ENSG00000011566.15. [Q8IVH8-1]
DR Ensembl; ENST00000341681.9; ENSP00000345434.5; ENSG00000011566.15. [Q8IVH8-3]
DR GeneID; 8491; -.
DR KEGG; hsa:8491; -.
DR MANE-Select; ENST00000263881.8; ENSP00000263881.3; NM_003618.4; NP_003609.2.
DR UCSC; uc002rro.4; human. [Q8IVH8-1]
DR CTD; 8491; -.
DR DisGeNET; 8491; -.
DR GeneCards; MAP4K3; -.
DR HGNC; HGNC:6865; MAP4K3.
DR HPA; ENSG00000011566; Low tissue specificity.
DR MIM; 604921; gene.
DR neXtProt; NX_Q8IVH8; -.
DR OpenTargets; ENSG00000011566; -.
DR PharmGKB; PA30611; -.
DR VEuPathDB; HostDB:ENSG00000011566; -.
DR eggNOG; KOG0576; Eukaryota.
DR GeneTree; ENSGT00940000155483; -.
DR InParanoid; Q8IVH8; -.
DR OMA; VIKLEPX; -.
DR PhylomeDB; Q8IVH8; -.
DR TreeFam; TF105121; -.
DR PathwayCommons; Q8IVH8; -.
DR SignaLink; Q8IVH8; -.
DR SIGNOR; Q8IVH8; -.
DR BioGRID-ORCS; 8491; 19 hits in 1117 CRISPR screens.
DR ChiTaRS; MAP4K3; human.
DR GenomeRNAi; 8491; -.
DR Pharos; Q8IVH8; Tchem.
DR PRO; PR:Q8IVH8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IVH8; protein.
DR Bgee; ENSG00000011566; Expressed in secondary oocyte and 199 other tissues.
DR ExpressionAtlas; Q8IVH8; baseline and differential.
DR Genevisible; Q8IVH8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0034612; P:response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR DisProt; DP02822; -.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..894
FT /note="Mitogen-activated protein kinase kinase kinase
FT kinase 3"
FT /id="PRO_0000086277"
FT DOMAIN 16..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 556..867
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 410..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:9275185"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JP0"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..12
FT /note="MNPGFDLSRRNP -> MA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9275185"
FT /id="VSP_007052"
FT VAR_SEQ 352..372
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007053"
FT VARIANT 200
FT /note="V -> L (in dbSNP:rs35957290)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040743"
FT VARIANT 424
FT /note="H -> Q (in dbSNP:rs56317466)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040744"
FT VARIANT 669
FT /note="T -> S (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040745"
FT MUTAGEN 48
FT /note="K->E: Loss of kinase activity and ability to
FT activate JNK family."
FT /evidence="ECO:0000269|PubMed:9275185"
FT CONFLICT 392
FT /note="N -> D (in Ref. 1; AAC15472)"
FT /evidence="ECO:0000305"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:5J5T"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 110..129
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5J5T"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:5J5T"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:5J5T"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:5J5T"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:5J5T"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:5J5T"
SQ SEQUENCE 894 AA; 101316 MW; 6EB77BBB34E5B733 CRC64;
MNPGFDLSRR NPQEDFELIQ RIGSGTYGDV YKARNVNTGE LAAIKVIKLE PGEDFAVVQQ
EIIMMKDCKH PNIVAYFGSY LRRDKLWICM EFCGGGSLQD IYHVTGPLSE LQIAYVSRET
LQGLYYLHSK GKMHRDIKGA NILLTDNGHV KLADFGVSAQ ITATIAKRKS FIGTPYWMAP
EVAAVERKGG YNQLCDLWAV GITAIELAEL QPPMFDLHPM RALFLMTKSN FQPPKLKDKM
KWSNSFHHFV KMALTKNPKK RPTAEKLLQH PFVTQHLTRS LAIELLDKVN NPDHSTYHDF
DDDDPEPLVA VPHRIHSTSR NVREEKTRSE ITFGQVKFDP PLRKETEPHH ELPDSDGFLD
SSEEIYYTAR SNLDLQLEYG QGHQGGYFLG ANKSLLKSVE EELHQRGHVA HLEDDEGDDD
ESKHSTLKAK IPPPLPPKPK SIFIPQEMHS TEDENQGTIK RCPMSGSPAK PSQVPPRPPP
PRLPPHKPVA LGNGMSSFQL NGERDGSLCQ QQNEHRGTNL SRKEKKDVPK PISNGLPPTP
KVHMGACFSK VFNGCPLKIH CASSWINPDT RDQYLIFGAE EGIYTLNLNE LHETSMEQLF
PRRCTWLYVM NNCLLSISGK ASQLYSHNLP GLFDYARQMQ KLPVAIPAHK LPDRILPRKF
SVSAKIPETK WCQKCCVVRN PYTGHKYLCG ALQTSIVLLE WVEPMQKFML IKHIDFPIPC
PLRMFEMLVV PEQEYPLVCV GVSRGRDFNQ VVRFETVNPN STSSWFTESD TPQTNVTHVT
QLERDTILVC LDCCIKIVNL QGRLKSSRKL SSELTFDFQI ESIVCLQDSV LAFWKHGMQG
RSFRSNEVTQ EISDSTRIFR LLGSDRVVVL ESRPTDNPTA NSNLYILAGH ENSY
