ID D3ZG83_RAT Unreviewed; 940 AA. AC D3ZG83; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 3. DT 28-MAR-2018, entry version 69. DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|PIRNR:PIRNR000556}; DE EC=2.7.11.25 {ECO:0000256|PIRNR:PIRNR000556}; GN Name=Map3k10 {ECO:0000313|Ensembl:ENSRNOP00000031328, GN ECO:0000313|RGD:1308381}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000031328, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000031328, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031328, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000031328} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031328}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000213|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000256|PIRNR:PIRNR000556}. CC -!- ENZYME REGULATION: Homodimerization via the leucine zipper domains CC is required for autophosphorylation. CC {ECO:0000256|PIRNR:PIRNR000556}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000556}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. MAP kinase kinase kinase subfamily. CC {ECO:0000256|PIRNR:PIRNR000556}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC120811; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006228638.1; XM_006228576.3. DR UniGene; Rn.130504; -. DR STRING; 10116.ENSRNOP00000031328; -. DR iPTMnet; D3ZG83; -. DR PhosphoSitePlus; D3ZG83; -. DR PaxDb; D3ZG83; -. DR Ensembl; ENSRNOT00000034609; ENSRNOP00000031328; ENSRNOG00000023521. DR GeneID; 308463; -. DR CTD; 4294; -. DR RGD; 1308381; Map3k10. DR eggNOG; KOG0192; Eukaryota. DR eggNOG; COG0515; LUCA. DR GeneTree; ENSGT00900000140790; -. DR InParanoid; D3ZG83; -. DR OMA; ARAPWEP; -. DR OrthoDB; EOG091G0JNI; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000023521; -. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD. DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IBA:GO_Central. DR GO; GO:0004672; F:protein kinase activity; ISO:RGD. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD. DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD. DR GO; GO:0007257; P:activation of JUN kinase activity; IBA:GO_Central. DR GO; GO:0008219; P:cell death; IMP:RGD. DR GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; ISO:RGD. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD. DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD. DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD. DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD. DR GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD. DR CDD; cd12059; SH3_MLK1-3; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR015785; MAP3K10. DR InterPro; IPR035779; MLK1-3_SH3. DR InterPro; IPR016231; MLK1-4. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR43997:SF5; PTHR43997:SF5; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF14604; SH3_9; 1. DR PIRSF; PIRSF000556; MAPKKK9_11; 1. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SSF50044; 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. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000556, KW ECO:0000256|PIRSR:PIRSR000556-2}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Kinase {ECO:0000256|PIRNR:PIRNR000556}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000556, KW ECO:0000256|PIRSR:PIRSR000556-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000556}; KW SH3 domain {ECO:0000256|PROSITE-ProRule:PRU00192}; KW Transferase {ECO:0000256|PIRNR:PIRNR000556}. FT DOMAIN 16 81 SH3. {ECO:0000259|PROSITE:PS50002}. FT DOMAIN 98 360 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT NP_BIND 104 112 ATP. {ECO:0000256|PIRSR:PIRSR000556-2}. FT COILED 391 412 {ECO:0000256|SAM:Coils}. FT COILED 424 444 {ECO:0000256|SAM:Coils}. FT ACT_SITE 222 222 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000556-1}. FT BINDING 125 125 ATP. {ECO:0000256|PIRSR:PIRSR000556-2}. SQ SEQUENCE 940 AA; 103060 MW; B39EDB486730A42D CRC64; MEEEEGAAAR EWGATPAGPV WTAVFDYEAV GDEELTLRRG DRVQVLSQDC AVSGDEGWWT GQLPSGRVGV FPSNYVAPAA PAAPTDLQLP QEIPFHELQL EEIIGVGGFG KVYRALWRGE EVAVKAARLD PERDPAVTAE QVRQEARLFG ALQHPNIIAL RGACLSPPNL CLVMEYARGG ALSRVLAGRR VPPHVLVNWA VQVARGMNYL HNDAPVPIIH RDLKSINILI LEAIENHNLA DTVLKITDFG LAREWHKTTK MSAAGTYAWM APEVIRLSLF SKSSDVWSFG VLLWELLTGE VPYREIDALA VAYGVAMNKL TLPIPSTCPE PFARLLEECW DPDPHGRPDF GSILKQLEVI EQSALFQMPL ESFHSLQEDW KLEIQHMFDD LRTKEKELRS REEELLRAAQ EQRFQEEQLR RREQELAERE MDIVERELHL LMSQLSQEKP RVRKRKGNFK RSRLLKLREG SSHISLPSGF EHKITVQASP TLDKRKGSDG ASPPASPSII PRLRAIRLTP VDCGSSGGSG TWSRSGPPKK EELVGGKKKG RTWGPSSTLQ KERAGGEERL KALGEGSKQW SSSAPNLGKS PKHTPMAPGF ASLNEMEEFA EADEGNNVPP SPYSTPSYLK VPLPAEASPC AQPPWEPPAA TPSRPGHGAR RRCDLALLGC ATLLSAVGLG ADVAEARAGD GEEQRGWLDG LFFPRPGRFP RGLSPTGRPG GRREETAPGF GLAPSATLVS LSSVSDCNST RSLLRSDSDE AAPTAPSPPP SLLPPSPSTN PLVDVELESF KKDPRQSLTP THVTAAHAVS RGHRRTPSDG ALRQREPPEL TNHGPRDPLD FPRLPDPQAL FPTRRRPLEF PGRPTTLTFA PRPRPAASRP RLDPWKLVSF GRTLSISPPS RPDTPESPGP LSVQPTLLDM DMEGQSQDNT VPLCGAYGSH //