GenomeNet

Database: UniProt/SWISS-PROT
Entry: M3K14_HUMAN
LinkDB: M3K14_HUMAN
Original site: M3K14_HUMAN 
ID   M3K14_HUMAN             Reviewed;         947 AA.
AC   Q99558; A8K2D8; D3DX67; Q8IYN1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   16-JAN-2019, entry version 188.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 14;
DE            EC=2.7.11.25;
DE   AltName: Full=NF-kappa-beta-inducing kinase;
DE            Short=HsNIK;
DE   AltName: Full=Serine/threonine-protein kinase NIK;
GN   Name=MAP3K14; Synonyms=NIK;
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], MUTAGENESIS OF 429-LYS-LYS-430, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9020361; DOI=10.1038/385540a0;
RA   Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.;
RT   "MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and
RT   IL-1.";
RL   Nature 385:540-544(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
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   [6]
RP   INTERACTION WITH PELI3.
RX   PubMed=12874243; DOI=10.4049/jimmunol.171.3.1500;
RA   Jensen L.E., Whitehead A.S.;
RT   "Pellino3, a novel member of the Pellino protein family, promotes
RT   activation of c-Jun and Elk-1 and may act as a scaffolding protein.";
RL   J. Immunol. 171:1500-1506(2003).
RN   [7]
RP   INTERACTION WITH GRB10.
RX   PubMed=12853971; DOI=10.1038/sj.onc.1206532;
RA   Chen D., Xu L.G., Chen L., Li L., Zhai Z., Shu H.B.;
RT   "NIK is a component of the EGF/heregulin receptor signaling
RT   complexes.";
RL   Oncogene 22:4348-4355(2003).
RN   [8]
RP   FUNCTION, UBIQUITINATION, AND INTERACTION WITH TRAF3.
RX   PubMed=15084608; DOI=10.1074/jbc.M403286200;
RA   Liao G., Zhang M., Harhaj E.W., Sun S.C.;
RT   "Regulation of the NF-kappaB-inducing kinase by tumor necrosis factor
RT   receptor-associated factor 3-induced degradation.";
RL   J. Biol. Chem. 279:26243-26250(2004).
RN   [9]
RP   INTERACTION WITH ARRB1 AND ARRB2.
RX   PubMed=15173580; DOI=10.1073/pnas.0402851101;
RA   Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J.;
RT   "beta-Arrestin inhibits NF-kappaB activity by means of its interaction
RT   with the NF-kappaB inhibitor IkappaBalpha.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004).
RN   [10]
RP   INTERACTION WITH NIBP.
RX   PubMed=15951441; DOI=10.1074/jbc.M501670200;
RA   Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V.,
RA   Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.;
RT   "NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-
RT   (kappa)B activation.";
RL   J. Biol. Chem. 280:29233-29241(2005).
RN   [11]
RP   PHOSPHORYLATION BY CHUK/IKKA.
RX   PubMed=20501937; DOI=10.1126/scisignal.2000778;
RA   Razani B., Zarnegar B., Ytterberg A.J., Shiba T., Dempsey P.W.,
RA   Ware C.F., Loo J.A., Cheng G.;
RT   "Negative feedback in noncanonical NF-kappaB signaling modulates NIK
RT   stability through IKKalpha-mediated phosphorylation.";
RL   Sci. Signal. 3:RA41-RA41(2010).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 330-680.
RX   PubMed=22718757; DOI=10.1074/jbc.M112.366658;
RA   Liu J., Sudom A., Min X., Cao Z., Gao X., Ayres M., Lee F., Cao P.,
RA   Johnstone S., Plotnikova O., Walker N., Chen G., Wang Z.;
RT   "Structure of the nuclear factor kappaB-inducing kinase (NIK) kinase
RT   domain reveals a constitutively active conformation.";
RL   J. Biol. Chem. 287:27326-27334(2012).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 308-673.
RX   PubMed=22921830; DOI=10.1016/j.str.2012.07.013;
RA   de Leon-Boenig G., Bowman K.K., Feng J.A., Crawford T., Everett C.,
RA   Franke Y., Oh A., Stanley M., Staben S.T., Starovasnik M.A.,
RA   Wallweber H.J., Wu J., Wu L.C., Johnson A.R., Hymowitz S.G.;
RT   "The crystal structure of the catalytic domain of the NF-kappaB
RT   inducing kinase reveals a narrow but flexible active site.";
RL   Structure 20:1704-1714(2012).
RN   [14]
RP   VARIANTS [LARGE SCALE ANALYSIS] ASN-140; LYS-514; ALA-764; ILE-852 AND
RP   HIS-928.
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).
RN   [15]
RP   PHOSPHORYLATION AT THR-559, UBIQUITINATION, INTERACTION WITH ZFP91,
RP   AND MUTAGENESIS OF 429-LYS-LYS-430 AND THR-559.
RX   PubMed=20682767; DOI=10.1074/jbc.M110.129551;
RA   Jin X., Jin H.R., Jung H.S., Lee S.J., Lee J.H., Lee J.J.;
RT   "An atypical E3 ligase zinc finger protein 91 stabilizes and activates
RT   NF-kappaB-inducing kinase via Lys63-linked ubiquitination.";
RL   J. Biol. Chem. 285:30539-30547(2010).
CC   -!- FUNCTION: Lymphotoxin beta-activated kinase which seems to be
CC       exclusively involved in the activation of NF-kappa-B and its
CC       transcriptional activity. Promotes proteolytic processing of
CC       NFKB2/P100, which leads to activation of NF-kappa-B via the non-
CC       canonical pathway. Could act in a receptor-selective manner.
CC       {ECO:0000269|PubMed:15084608}.
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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.25;
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=2.7.11.25;
CC   -!- SUBUNIT: Interacts with TRAF2, TRAF5, TRAF6, IKKA and NFKB2/P100
CC       (By similarity). Interacts with TRAF3 and PELI3. Interacts with
CC       NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2.
CC       Interacts with GRB10. Interacts with ZFP91. {ECO:0000250,
CC       ECO:0000269|PubMed:12853971, ECO:0000269|PubMed:12874243,
CC       ECO:0000269|PubMed:15084608, ECO:0000269|PubMed:15173580,
CC       ECO:0000269|PubMed:15951441, ECO:0000269|PubMed:20682767}.
CC   -!- INTERACTION:
CC       P05186:ALPL; NbExp=4; IntAct=EBI-358011, EBI-1054354;
CC       Q16543:CDC37; NbExp=2; IntAct=EBI-358011, EBI-295634;
CC       O15111:CHUK; NbExp=6; IntAct=EBI-358011, EBI-81249;
CC       Q60680-2:Chuk (xeno); NbExp=3; IntAct=EBI-358011, EBI-646264;
CC       P08238:HSP90AB1; NbExp=2; IntAct=EBI-358011, EBI-352572;
CC       O14920:IKBKB; NbExp=3; IntAct=EBI-358011, EBI-81266;
CC       Q12933:TRAF2; NbExp=7; IntAct=EBI-358011, EBI-355744;
CC       Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-358011, EBI-359276;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in testis, small intestine,
CC       spleen, thymus, peripheral blood leukocytes, prostate, ovary and
CC       colon. {ECO:0000269|PubMed:9020361}.
CC   -!- PTM: Autophosphorylated. Phosphorylation at Thr-559 is required to
CC       activates its kinase activity and 'Lys-63'-linked
CC       polyubiquitination. Phosphorylated by CHUK/IKKA leading to MAP3K14
CC       destabilization. {ECO:0000269|PubMed:20501937,
CC       ECO:0000269|PubMed:20682767}.
CC   -!- PTM: Ubiquitinated. Undergoes both 'Lys-48'- and 'Lys-63'-linked
CC       polyubiquitination. 'Lys-48'-linked polyubiquitination leads to
CC       its degradation by the proteasome, while 'Lys-63'-linked
CC       polyubiquitination stabilizes and activates it.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000305}.
DR   EMBL; Y10256; CAA71306.1; -; mRNA.
DR   EMBL; AK290203; BAF82892.1; -; mRNA.
DR   EMBL; DQ314874; ABC40733.1; -; Genomic_DNA.
DR   EMBL; CH471178; EAW51529.1; -; Genomic_DNA.
DR   EMBL; CH471178; EAW51530.1; -; Genomic_DNA.
DR   EMBL; BC035576; AAH35576.1; -; mRNA.
DR   CCDS; CCDS74079.1; -.
DR   RefSeq; NP_003945.2; NM_003954.4.
DR   RefSeq; XP_011523743.1; XM_011525441.2.
DR   UniGene; Hs.404183; -.
DR   UniGene; Hs.668927; -.
DR   UniGene; Hs.735695; -.
DR   PDB; 4DN5; X-ray; 2.50 A; A/B=330-680.
DR   PDB; 4G3D; X-ray; 2.90 A; A/B/D/E=308-673.
DR   PDB; 4IDT; X-ray; 2.40 A; A/B=330-680.
DR   PDB; 4IDV; X-ray; 2.90 A; A/B/C/D=330-680.
DR   PDBsum; 4DN5; -.
DR   PDBsum; 4G3D; -.
DR   PDBsum; 4IDT; -.
DR   PDBsum; 4IDV; -.
DR   ProteinModelPortal; Q99558; -.
DR   SMR; Q99558; -.
DR   BioGrid; 114487; 35.
DR   CORUM; Q99558; -.
DR   DIP; DIP-27522N; -.
DR   IntAct; Q99558; 30.
DR   MINT; Q99558; -.
DR   BindingDB; Q99558; -.
DR   ChEMBL; CHEMBL5888; -.
DR   GuidetoPHARMACOLOGY; 2074; -.
DR   iPTMnet; Q99558; -.
DR   PhosphoSitePlus; Q99558; -.
DR   BioMuta; MAP3K14; -.
DR   DMDM; 92090612; -.
DR   PeptideAtlas; Q99558; -.
DR   PRIDE; Q99558; -.
DR   ProteomicsDB; 78326; -.
DR   DNASU; 9020; -.
DR   Ensembl; ENST00000344686; ENSP00000478552; ENSG00000006062.
DR   Ensembl; ENST00000376926; ENSP00000482657; ENSG00000006062.
DR   Ensembl; ENST00000648527; ENSP00000497704; ENSG00000006062.
DR   GeneID; 9020; -.
DR   KEGG; hsa:9020; -.
DR   UCSC; uc032fjy.2; human.
DR   CTD; 9020; -.
DR   DisGeNET; 9020; -.
DR   EuPathDB; HostDB:ENSG00000006062.13; -.
DR   GeneCards; MAP3K14; -.
DR   HGNC; HGNC:6853; MAP3K14.
DR   HPA; HPA027269; -.
DR   HPA; HPA027270; -.
DR   MalaCards; MAP3K14; -.
DR   MIM; 604655; gene.
DR   neXtProt; NX_Q99558; -.
DR   OpenTargets; ENSG00000006062; -.
DR   Orphanet; 447731; NIK deficiency.
DR   PharmGKB; PA30597; -.
DR   GeneTree; ENSGT00940000156497; -.
DR   HOGENOM; HOG000113436; -.
DR   HOVERGEN; HBG052384; -.
DR   InParanoid; Q99558; -.
DR   KO; K04466; -.
DR   OMA; EQESCTV; -.
DR   OrthoDB; 372069at2759; -.
DR   PhylomeDB; Q99558; -.
DR   Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR   SignaLink; Q99558; -.
DR   SIGNOR; Q99558; -.
DR   ChiTaRS; MAP3K14; human.
DR   GeneWiki; MAP3K14; -.
DR   GenomeRNAi; 9020; -.
DR   PRO; PR:Q99558; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000006062; Expressed in 141 organ(s), highest expression level in esophagogastric junction muscularis propria.
DR   CleanEx; HS_MAP3K14; -.
DR   ExpressionAtlas; Q99558; baseline and differential.
DR   Genevisible; Q99558; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; TAS:Reactome.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004704; F:NF-kappaB-inducing kinase activity; ISS:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; EXP:Reactome.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017425; MAPKKK14.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24361:SF226; PTHR24361:SF226; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF038175; MAPKKK14; 1.
DR   SMART; SM00220; S_TKc; 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   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN         1    947       Mitogen-activated protein kinase kinase
FT                                kinase 14.
FT                                /FTId=PRO_0000086266.
FT   DOMAIN      400    655       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     406    414       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      401    653       Interaction with ZFP91.
FT                                {ECO:0000269|PubMed:20682767}.
FT   ACT_SITE    515    515       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     429    429       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     559    559       Phosphothreonine.
FT                                {ECO:0000269|PubMed:20682767}.
FT   VARIANT     140    140       S -> N (in dbSNP:rs11574819).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040711.
FT   VARIANT     255    255       T -> M (in dbSNP:rs11574820).
FT                                /FTId=VAR_051641.
FT   VARIANT     514    514       G -> K (in a lung neuroendocrine
FT                                carcinoma sample; somatic mutation;
FT                                requires 2 nucleotide substitutions).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040712.
FT   VARIANT     674    674       H -> Y (in dbSNP:rs11867907).
FT                                /FTId=VAR_051642.
FT   VARIANT     764    764       T -> A (in dbSNP:rs56302559).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040713.
FT   VARIANT     852    852       T -> I (in an ovarian mucinous carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040714.
FT   VARIANT     928    928       P -> H (in dbSNP:rs56036201).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040715.
FT   MUTAGEN     429    430       KK->AA: Loss of autophosphorylation and
FT                                'Lys-63'-linked ubiquitination.
FT                                {ECO:0000269|PubMed:20682767,
FT                                ECO:0000269|PubMed:9020361}.
FT   MUTAGEN     559    559       T->A: Abolishes 'Lys-63'-linked
FT                                ubiquitination.
FT                                {ECO:0000269|PubMed:20682767}.
FT   CONFLICT     25     25       A -> P (in Ref. 1; CAA71306).
FT                                {ECO:0000305}.
FT   CONFLICT    348    348       G -> S (in Ref. 1; CAA71306).
FT                                {ECO:0000305}.
FT   CONFLICT    880    880       R -> G (in Ref. 2; BAF82892).
FT                                {ECO:0000305}.
FT   HELIX       335    341       {ECO:0000244|PDB:4IDT}.
FT   STRAND      345    347       {ECO:0000244|PDB:4IDT}.
FT   HELIX       350    363       {ECO:0000244|PDB:4IDT}.
FT   STRAND      364    366       {ECO:0000244|PDB:4IDT}.
FT   STRAND      377    381       {ECO:0000244|PDB:4IDT}.
FT   TURN        395    397       {ECO:0000244|PDB:4IDT}.
FT   STRAND      398    408       {ECO:0000244|PDB:4IDT}.
FT   STRAND      410    419       {ECO:0000244|PDB:4IDT}.
FT   TURN        420    422       {ECO:0000244|PDB:4IDT}.
FT   STRAND      425    432       {ECO:0000244|PDB:4IDT}.
FT   HELIX       433    435       {ECO:0000244|PDB:4IDT}.
FT   HELIX       439    442       {ECO:0000244|PDB:4IDT}.
FT   TURN        443    446       {ECO:0000244|PDB:4IDT}.
FT   STRAND      455    461       {ECO:0000244|PDB:4IDT}.
FT   STRAND      464    469       {ECO:0000244|PDB:4IDT}.
FT   HELIX       477    484       {ECO:0000244|PDB:4IDT}.
FT   HELIX       489    507       {ECO:0000244|PDB:4IDT}.
FT   TURN        508    510       {ECO:0000244|PDB:4IDT}.
FT   HELIX       518    520       {ECO:0000244|PDB:4IDT}.
FT   STRAND      521    523       {ECO:0000244|PDB:4IDT}.
FT   STRAND      530    532       {ECO:0000244|PDB:4IDT}.
FT   HELIX       535    537       {ECO:0000244|PDB:4IDV}.
FT   STRAND      543    547       {ECO:0000244|PDB:4G3D}.
FT   TURN        550    553       {ECO:0000244|PDB:4G3D}.
FT   HELIX       560    562       {ECO:0000244|PDB:4IDT}.
FT   HELIX       565    568       {ECO:0000244|PDB:4IDT}.
FT   HELIX       576    591       {ECO:0000244|PDB:4IDT}.
FT   TURN        595    599       {ECO:0000244|PDB:4IDT}.
FT   HELIX       605    610       {ECO:0000244|PDB:4IDT}.
FT   HELIX       614    617       {ECO:0000244|PDB:4IDT}.
FT   HELIX       624    633       {ECO:0000244|PDB:4IDT}.
FT   TURN        638    640       {ECO:0000244|PDB:4IDT}.
FT   HELIX       644    658       {ECO:0000244|PDB:4IDT}.
SQ   SEQUENCE   947 AA;  104042 MW;  C9D10F67FF7F48AC CRC64;
     MAVMEMACPG APGSAVGQQK ELPKAKEKTP PLGKKQSSVY KLEAVEKSPV FCGKWEILND
     VITKGTAKEG SEAGPAAISI IAQAECENSQ EFSPTFSERI FIAGSKQYSQ SESLDQIPNN
     VAHATEGKMA RVCWKGKRRS KARKKRKKKS SKSLAHAGVA LAKPLPRTPE QESCTIPVQE
     DESPLGAPYV RNTPQFTKPL KEPGLGQLCF KQLGEGLRPA LPRSELHKLI SPLQCLNHVW
     KLHHPQDGGP LPLPTHPFPY SRLPHPFPFH PLQPWKPHPL ESFLGKLACV DSQKPLPDPH
     LSKLACVDSP KPLPGPHLEP SCLSRGAHEK FSVEEYLVHA LQGSVSSGQA HSLTSLAKTW
     AARGSRSREP SPKTEDNEGV LLTEKLKPVD YEYREEVHWA THQLRLGRGS FGEVHRMEDK
     QTGFQCAVKK VRLEVFRAEE LMACAGLTSP RIVPLYGAVR EGPWVNIFME LLEGGSLGQL
     VKEQGCLPED RALYYLGQAL EGLEYLHSRR ILHGDVKADN VLLSSDGSHA ALCDFGHAVC
     LQPDGLGKSL LTGDYIPGTE THMAPEVVLG RSCDAKVDVW SSCCMMLHML NGCHPWTQFF
     RGPLCLKIAS EPPPVREIPP SCAPLTAQAI QEGLRKEPIH RVSAAELGGK VNRALQQVGG
     LKSPWRGEYK EPRHPPPNQA NYHQTLHAQP RELSPRAPGP RPAEETTGRA PKLQPPLPPE
     PPEPNKSPPL TLSKEESGMW EPLPLSSLEP APARNPSSPE RKATVPEQEL QQLEIELFLN
     SLSQPFSLEE QEQILSCLSI DSLSLSDDSE KNPSKASQSS RDTLSSGVHS WSSQAEARSS
     SWNMVLARGR PTDTPSYFNG VKVQIQSLNG EHLHIREFHR VKVGDIATGI SSQIPAAAFS
     LVTKDGQPVR YDMEVPDSGI DLQCTLAPDG SFAWSWRVKH GQLENRP
//
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