GenomeNet

Database: UniProt/SWISS-PROT
Entry: MK06_HUMAN
LinkDB: MK06_HUMAN
Original site: MK06_HUMAN 
ID   MK06_HUMAN              Reviewed;         721 AA.
AC   Q16659; B2R945; B5BU65; Q68DH4; Q8IYN8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-FEB-2019, entry version 178.
DE   RecName: Full=Mitogen-activated protein kinase 6;
DE            Short=MAP kinase 6;
DE            Short=MAPK 6;
DE            EC=2.7.11.24;
DE   AltName: Full=Extracellular signal-regulated kinase 3;
DE            Short=ERK-3;
DE   AltName: Full=MAP kinase isoform p97;
DE            Short=p97-MAPK;
GN   Name=MAPK6; Synonyms=ERK3, PRKM6;
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].
RC   TISSUE=Fetal skeletal muscle;
RX   PubMed=7969157; DOI=10.1128/MCB.14.12.8202;
RA   Zhu A.X., Zhao Y., Moller D.E., Flier J.S.;
RT   "Cloning and characterization of p97MAPK, a novel human homolog of rat
RT   ERK-3.";
RL   Mol. Cell. Biol. 14:8202-8211(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Smooth muscle;
RX   PubMed=8875998;
RA   Meloche S., Beatty B.G., Pellerin J.;
RT   "Primary structure, expression and chromosomal locus of a human
RT   homolog of rat ERK3.";
RL   Oncogene 13:1575-1579(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oral cancer;
RA   Saranath D., Mahale A., Rai R., Dedhia P.;
RT   "ERK-3 cDNA clone isolated from human oral cancer.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Esophageal carcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA   Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA   Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA   Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA   Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA   Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA   Isogai T., Imai J., Watanabe S., Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in
RT   vitro-expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-290.
RC   TISSUE=Placenta;
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   [8]
RP   UBIQUITINATION AT MET-1.
RX   PubMed=15226418; DOI=10.1128/MCB.24.14.6140-6150.2004;
RA   Coulombe P., Rodier G., Bonneil E., Thibault P., Meloche S.;
RT   "N-Terminal ubiquitination of extracellular signal-regulated kinase 3
RT   and p21 directs their degradation by the proteasome.";
RL   Mol. Cell. Biol. 24:6140-6150(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION
RP   BY 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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   PHOSPHORYLATION AT SER-189.
RX   PubMed=21177870; DOI=10.1074/jbc.M110.181529;
RA   Deleris P., Trost M., Topisirovic I., Tanguay P.L., Borden K.L.,
RA   Thibault P., Meloche S.;
RT   "Activation loop phosphorylation of ERK3/ERK4 by group I p21-activated
RT   kinases (PAKs) defines a novel PAK-ERK3/4-MAPK-activated protein
RT   kinase 5 signaling pathway.";
RL   J. Biol. Chem. 286:6470-6478(2011).
RN   [13]
RP   INTERACTION WITH UBE3A AND NEURL4.
RX   PubMed=22645313; DOI=10.1128/MCB.00201-12;
RA   Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M.,
RA   Harper J.W., Howley P.M.;
RT   "Identification and proteomic analysis of distinct UBE3A/E6AP protein
RT   complexes.";
RL   Mol. Cell. Biol. 32:3095-3106(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-386; SER-452;
RP   SER-556; SER-558; SER-665 AND SER-684, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-290.
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: Atypical MAPK protein. Phosphorylates microtubule-
CC       associated protein 2 (MAP2) and MAPKAPK5. The precise role of the
CC       complex formed with MAPKAPK5 is still unclear, but the complex
CC       follows a complex set of phosphorylation events: upon interaction
CC       with atypical MAPKAPK5, ERK3/MAPK6 is phosphorylated at Ser-189
CC       and then mediates phosphorylation and activation of MAPKAPK5,
CC       which in turn phosphorylates ERK3/MAPK6. May promote entry in the
CC       cell cycle (By similarity). {ECO:0000250}.
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=2.7.11.24;
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=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation at Ser-189.
CC   -!- SUBUNIT: Heterodimer with ERK4/MAPK4. Interacts with (via FRIEDE
CC       motif) MAPKAPK5 (By similarity). Interacts with UBE3A; this
CC       interaction may be indirect and mediated by HERC2, possibly via
CC       HERC2 interaction with NEURL4. {ECO:0000250,
CC       ECO:0000269|PubMed:22645313}.
CC   -!- INTERACTION:
CC       Q9H6Z9:EGLN3; NbExp=6; IntAct=EBI-1384105, EBI-1175354;
CC       Q8IW41:MAPKAPK5; NbExp=7; IntAct=EBI-1384105, EBI-1201460;
CC       Q8IW41-2:MAPKAPK5; NbExp=4; IntAct=EBI-1384105, EBI-11958803;
CC       P12504:vif (xeno); NbExp=2; IntAct=EBI-1384105, EBI-779991;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Translocates to the cytoplasm following
CC       interaction with MAPKAPK5. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highest expression in the skeletal muscle,
CC       followed by the brain. Also found in heart, placenta, lung, liver,
CC       pancreas, kidney and skin fibroblasts.
CC   -!- DOMAIN: In contrast to classical MAPKs, the TXY motif within the
CC       activation loop is replaced by the SEG motif, whose
CC       phosphorylation activates the MAP kinases. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-189 by PAK1, PAK2 and PAK3 resulting in
CC       catalytic activation. Phosphorylated by MAPKAPK5 at other sites.
CC       {ECO:0000269|PubMed:21177870}.
CC   -!- PTM: Ubiquitination at Met-1 leads to degradation by the
CC       proteasome pathway. {ECO:0000269|PubMed:15226418}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MAPK6ID43349ch15q21.html";
DR   EMBL; X80692; CAA56709.1; -; mRNA.
DR   EMBL; L77964; AAA98769.1; -; mRNA.
DR   EMBL; AF420474; AAL17605.1; -; mRNA.
DR   EMBL; AK313633; BAG36392.1; -; mRNA.
DR   EMBL; CR749401; CAH18246.1; -; mRNA.
DR   EMBL; AB451301; BAG70115.1; -; mRNA.
DR   EMBL; BC035492; AAH35492.1; -; mRNA.
DR   CCDS; CCDS10147.1; -.
DR   PIR; A56352; A56352.
DR   RefSeq; NP_002739.1; NM_002748.3.
DR   RefSeq; XP_005254594.1; XM_005254537.2.
DR   RefSeq; XP_005254595.1; XM_005254538.2.
DR   RefSeq; XP_005254596.1; XM_005254539.3.
DR   RefSeq; XP_011520084.1; XM_011521782.1.
DR   UniGene; Hs.411847; -.
DR   PDB; 2I6L; X-ray; 2.25 A; A/B=9-327.
DR   PDBsum; 2I6L; -.
DR   ProteinModelPortal; Q16659; -.
DR   SMR; Q16659; -.
DR   BioGrid; 111583; 445.
DR   CORUM; Q16659; -.
DR   IntAct; Q16659; 381.
DR   MINT; Q16659; -.
DR   STRING; 9606.ENSP00000261845; -.
DR   BindingDB; Q16659; -.
DR   ChEMBL; CHEMBL5121; -.
DR   MoonDB; Q16659; Predicted.
DR   iPTMnet; Q16659; -.
DR   PhosphoSitePlus; Q16659; -.
DR   BioMuta; MAPK6; -.
DR   DMDM; 2499596; -.
DR   EPD; Q16659; -.
DR   jPOST; Q16659; -.
DR   MaxQB; Q16659; -.
DR   PaxDb; Q16659; -.
DR   PeptideAtlas; Q16659; -.
DR   PRIDE; Q16659; -.
DR   ProteomicsDB; 61018; -.
DR   DNASU; 5597; -.
DR   Ensembl; ENST00000261845; ENSP00000261845; ENSG00000069956.
DR   GeneID; 5597; -.
DR   KEGG; hsa:5597; -.
DR   UCSC; uc002abp.4; human.
DR   CTD; 5597; -.
DR   DisGeNET; 5597; -.
DR   EuPathDB; HostDB:ENSG00000069956.11; -.
DR   GeneCards; MAPK6; -.
DR   HGNC; HGNC:6879; MAPK6.
DR   HPA; CAB005184; -.
DR   HPA; HPA030262; -.
DR   MIM; 602904; gene.
DR   neXtProt; NX_Q16659; -.
DR   OpenTargets; ENSG00000069956; -.
DR   PharmGKB; PA30624; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   eggNOG; ENOG410XNY0; LUCA.
DR   GeneTree; ENSGT00940000154351; -.
DR   HOGENOM; HOG000233020; -.
DR   HOVERGEN; HBG104376; -.
DR   InParanoid; Q16659; -.
DR   KO; K06855; -.
DR   OMA; RDSEVNH; -.
DR   OrthoDB; 741207at2759; -.
DR   PhylomeDB; Q16659; -.
DR   TreeFam; TF105098; -.
DR   BRENDA; 2.7.11.24; 2681.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   SignaLink; Q16659; -.
DR   SIGNOR; Q16659; -.
DR   ChiTaRS; MAPK6; human.
DR   EvolutionaryTrace; Q16659; -.
DR   GeneWiki; MAPK6; -.
DR   GenomeRNAi; 5597; -.
DR   PRO; PR:Q16659; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; ENSG00000069956; Expressed in 240 organ(s), highest expression level in cerebellar vermis.
DR   Genevisible; Q16659; HS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0032156; C:septin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR008350; MAPK_ERK3/4.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01771; ERK3ERK4MAPK.
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; Cell cycle; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    721       Mitogen-activated protein kinase 6.
FT                                /FTId=PRO_0000186257.
FT   DOMAIN       20    316       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      26     34       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       189    191       SEG motif.
FT   MOTIF       332    337       FRIEDE motif.
FT   ACT_SITE    152    152       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      49     49       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     189    189       Phosphoserine; by PAK1, PAK2 and PAK3.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000269|PubMed:21177870}.
FT   MOD_RES     386    386       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     452    452       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     556    556       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     558    558       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     665    665       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     684    684       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK      1      1       Peptide (Met-Gly) (interchain with G-Cter
FT                                in ubiquitin).
FT                                {ECO:0000269|PubMed:15226418}.
FT   VARIANT     290    290       L -> V (in dbSNP:rs35697691).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042256.
FT   CONFLICT    229    229       K -> R (in Ref. 4; BAG36392).
FT                                {ECO:0000305}.
FT   CONFLICT    527    527       F -> L (in Ref. 4; BAG70115).
FT                                {ECO:0000305}.
FT   STRAND       14     16       {ECO:0000244|PDB:2I6L}.
FT   TURN         17     19       {ECO:0000244|PDB:2I6L}.
FT   STRAND       20     25       {ECO:0000244|PDB:2I6L}.
FT   STRAND       34     39       {ECO:0000244|PDB:2I6L}.
FT   TURN         40     42       {ECO:0000244|PDB:2I6L}.
FT   STRAND       45     52       {ECO:0000244|PDB:2I6L}.
FT   HELIX        56     70       {ECO:0000244|PDB:2I6L}.
FT   STRAND       80     84       {ECO:0000244|PDB:2I6L}.
FT   STRAND      102    109       {ECO:0000244|PDB:2I6L}.
FT   STRAND      112    114       {ECO:0000244|PDB:2I6L}.
FT   HELIX       115    119       {ECO:0000244|PDB:2I6L}.
FT   HELIX       126    145       {ECO:0000244|PDB:2I6L}.
FT   HELIX       155    157       {ECO:0000244|PDB:2I6L}.
FT   STRAND      158    161       {ECO:0000244|PDB:2I6L}.
FT   TURN        162    165       {ECO:0000244|PDB:2I6L}.
FT   STRAND      166    169       {ECO:0000244|PDB:2I6L}.
FT   HELIX       190    192       {ECO:0000244|PDB:2I6L}.
FT   HELIX       200    204       {ECO:0000244|PDB:2I6L}.
FT   HELIX       211    227       {ECO:0000244|PDB:2I6L}.
FT   HELIX       237    247       {ECO:0000244|PDB:2I6L}.
FT   HELIX       253    260       {ECO:0000244|PDB:2I6L}.
FT   HELIX       265    270       {ECO:0000244|PDB:2I6L}.
FT   HELIX       278    281       {ECO:0000244|PDB:2I6L}.
FT   HELIX       287    294       {ECO:0000244|PDB:2I6L}.
FT   HELIX       301    303       {ECO:0000244|PDB:2I6L}.
FT   HELIX       307    311       {ECO:0000244|PDB:2I6L}.
FT   HELIX       314    317       {ECO:0000244|PDB:2I6L}.
SQ   SEQUENCE   721 AA;  82681 MW;  DAA3AAA9B98BB31F CRC64;
     MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK IVLTDPQSVK
     HALREIKIIR RLDHDNIVKV FEILGPSGSQ LTDDVGSLTE LNSVYIVQEY METDLANVLE
     QGPLLEEHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP
     HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ
     MQLILESIPV VHEEDRQELL SVIPVYIRND MTEPHKPLTQ LLPGISREAL DFLEQILTFS
     PMDRLTAEEA LSHPYMSIYS FPMDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC
     QFSEHDWPVH NNFDIDEVQL DPRALSDVTD EEEVQVDPRK YLDGDREKYL EDPAFDTNYS
     TEPCWQYSDH HENKYCDLEC SHTCNYKTRS SSYLDNLVWR ESEVNHYYEP KLIIDLSNWK
     EQSKEKSDKK GKSKCERNGL VKAQIALEEA SQQLAGKERE KNQGFDFDSF IAGTIQLSSQ
     HEPTDVVDKL NDLNSSVSQL ELKSLISKSV SQEKQEKGMA NLAQLEALYQ SSWDSQFVSG
     GEDCFFINQF CEVRKDEQVE KENTYTSYLD KFFSRKEDTE MLETEPVEDG KLGERGHEEG
     FLNNSGEFLF NKQLESIGIP QFHSPVGSPL KSIQATLTPS AMKSSPQIPH QTYSSILKHL
     N
//
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