ID MK10_HUMAN Reviewed; 464 AA. AC P53779; A6NFS3; A6NG28; B3KQ94; Q15707; Q49AP1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 236. DE RecName: Full=Mitogen-activated protein kinase 10; DE Short=MAP kinase 10; DE Short=MAPK 10; DE EC=2.7.11.24; DE AltName: Full=MAP kinase p49 3F12; DE AltName: Full=Stress-activated protein kinase 1b; DE Short=SAPK1b; DE AltName: Full=Stress-activated protein kinase JNK3; DE AltName: Full=c-Jun N-terminal kinase 3; GN Name=MAPK10; Synonyms=JNK3, JNK3A, PRKM10, SAPK1B; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1). RC TISSUE=Hippocampus; RX PubMed=7826642; DOI=10.1016/0896-6273(95)90241-4; RA Mohit A.A., Martin J.H., Miller C.A.; RT "p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the RT human nervous system."; RL Neuron 14:67-78(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2). RC TISSUE=Brain; RX PubMed=8654373; DOI=10.1002/j.1460-2075.1996.tb00636.x; RA Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K., Derijard B., RA Davis R.J.; RT "Selective interaction of JNK protein kinase isoforms with transcription RT factors."; RL EMBO J. 15:2760-2770(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 143-464 (ISOFORM ALPHA-1). RC TISSUE=Caudate nucleus; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2). RC TISSUE=Brain; 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 [7] RP PARTIAL PROTEIN SEQUENCE, REGULATION BY MAP2K4 AND MAP2K7, PHOSPHORYLATION RP AT THR-221 AND TYR-223, COFACTOR, AND MASS SPECTROMETRY. RX PubMed=10715136; DOI=10.1021/bi992410+; RA Lisnock J., Griffin P., Calaycay J., Frantz B., Parsons J., O'Keefe S.J., RA LoGrasso P.; RT "Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic RT characterization of in vitro phosphorylated JNK3 alpha 1."; RL Biochemistry 39:3141-3148(2000). RN [8] RP ACTIVITY REGULATION. RX PubMed=11062067; DOI=10.1042/bj3520145; RA Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M., Cohen P.; RT "Synergistic activation of stress-activated protein kinase 1/c-Jun N- RT terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase RT kinase 4 (MKK4) and MKK7."; RL Biochem. J. 352:145-154(2000). RN [9] RP FUNCTION IN PHOSPHORYLATION OF STMN2. RX PubMed=11718727; DOI=10.1016/s0014-5793(01)03090-3; RA Neidhart S., Antonsson B., Gillieron C., Vilbois F., Grenningloh G., RA Arkinstall S.; RT "c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta RT (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator RT SCG10."; RL FEBS Lett. 508:259-264(2001). RN [10] RP INTERACTION WITH SPAG9. RX PubMed=15693750; DOI=10.1042/bj20041577; RA Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., RA Okumura K., Hasegawa A., Koyama K., Suri A.; RT "Characterization of a novel human sperm-associated antigen 9 (SPAG9) RT having structural homology with c-Jun N-terminal kinase-interacting RT protein."; RL Biochem. J. 389:73-82(2005). RN [11] RP CHROMOSOMAL REARRANGEMENT, AND DISEASE. RX PubMed=16249883; DOI=10.1007/s00439-005-0084-y; RA Shoichet S.A., Duprez L., Hagens O., Waetzig V., Menzel C., Herdegen T., RA Schweiger S., Dan B., Vamos E., Ropers H.-H., Kalscheuer V.M.; RT "Truncation of the CNS-expressed JNK3 in a patient with a severe RT developmental epileptic encephalopathy."; RL Hum. Genet. 118:559-567(2006). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=16737965; DOI=10.1074/jbc.m603659200; RA Song X., Raman D., Gurevich E.V., Vishnivetskiy S.A., Gurevich V.V.; RT "Visual and both non-visual arrestins in their 'inactive' conformation bind RT JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm."; RL J. Biol. Chem. 281:21491-21499(2006). RN [13] RP INTERACTION WITH HDAC9, AND ACTIVITY REGULATION. RX PubMed=16611996; DOI=10.1128/mcb.26.9.3550-3564.2006; RA Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., RA Olson E.N., D'Mello S.R.; RT "Neuroprotection by histone deacetylase-related protein."; RL Mol. Cell. Biol. 26:3550-3564(2006). RN [14] RP INTERACTION WITH ARRB2. RX PubMed=18435604; DOI=10.1042/bj20080685; RA Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R., RA Kolch W., Houslay M.D., Milligan G.; RT "Mutations of beta-arrestin 2 that limit self-association also interfere RT with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs: RT implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs."; RL Biochem. J. 413:51-60(2008). RN [15] RP PALMITOYLATION AT CYS-462 AND CYS-463, AND MUTAGENESIS OF CYS-462 AND RP CYS-463. RX PubMed=21941371; DOI=10.1038/cdd.2011.124; RA Yang G., Liu Y., Yang K., Liu R., Zhu S., Coquinco A., Wen W., Kojic L., RA Jia W., Cynader M.; RT "Isoform-specific palmitoylation of JNK regulates axonal development."; RL Cell Death Differ. 19:553-561(2012). RN [16] RP FUNCTION. RX PubMed=22441692; DOI=10.1038/embor.2012.37; RA Yoshitane H., Honma S., Imamura K., Nakajima H., Nishide S.Y., Ono D., RA Kiyota H., Shinozaki N., Matsuki H., Wada N., Doi H., Hamada T., Honma K., RA Fukada Y.; RT "JNK regulates the photic response of the mammalian circadian clock."; RL EMBO Rep. 13:455-461(2012). RN [17] RP FUNCTION, AND INTERACTION WITH JUND. RX PubMed=22327296; DOI=10.1038/nature10806; RA Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K., RA Merchant J.L., Hua X., Lei M.; RT "The same pocket in menin binds both MLL and JUND but has opposite effects RT on transcription."; RL Nature 482:542-546(2012). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-402. RX PubMed=9739089; DOI=10.1016/s0969-2126(98)00100-2; RA Xie X., Gu Y., Fox T., Coll J.T., Fleming M.A., Markland W., Caron P.R., RA Wilson K.P., Su M.S.-S.; RT "Crystal structure of JNK3: a kinase implicated in neuronal apoptosis."; RL Structure 6:983-991(1998). CC -!- FUNCTION: Serine/threonine-protein kinase involved in various processes CC such as neuronal proliferation, differentiation, migration and CC programmed cell death. Extracellular stimuli such as pro-inflammatory CC cytokines or physical stress stimulate the stress-activated protein CC kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this CC cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 CC phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 CC phosphorylates a number of transcription factors, primarily components CC of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional CC activity. Plays regulatory roles in the signaling pathways during CC neuronal apoptosis. Phosphorylates the neuronal microtubule regulator CC STMN2. Acts in the regulation of the amyloid-beta precursor protein/APP CC signaling during neuronal differentiation by phosphorylating APP. CC Participates also in neurite growth in spiral ganglion neurons. CC Phosphorylates the CLOCK-BMAL1 heterodimer and plays a role in the CC photic regulation of the circadian clock (PubMed:22441692). CC Phosphorylates JUND and this phosphorylation is inhibited in the CC presence of MEN1 (PubMed:22327296). {ECO:0000269|PubMed:11718727, CC ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:22441692}. 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=2.7.11.24; 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; CC Evidence={ECO:0000269|PubMed:10715136}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation by two dual specificity kinases, MAP2K4 and MAP2K7. CC MAP2K7 phosphorylates MAPK10 on Thr-221 causing a conformational change CC and a large increase in Vmax. MAP2K4 then phosphorylates Tyr-223 CC resulting in a further increase in Vmax. Inhibited by dual specificity CC phosphatases, such as DUSP1. Inhibited by HDAC9. CC {ECO:0000269|PubMed:11062067, ECO:0000269|PubMed:16611996}. CC -!- SUBUNIT: Interacts with MAPKBP1 (By similarity). Interacts with CC MAPK8IP1/JIP-1 and MAPK8IP3/JIP-3/JSAP1 (By similarity). Interacts with CC SPAG9/MAPK8IP4/JIP4 (PubMed:15693750). Interacts with HDAC9 CC (PubMed:16611996). Interacts with ARRB2; the interaction enhances CC MAPK10 activation by MAP3K5 (PubMed:18435604). Interacts with SARM1 (By CC similarity). Interacts with JUND; interaction is inhibited in the CC presence of MEN1 (PubMed:22327296). {ECO:0000250|UniProtKB:P49187, CC ECO:0000250|UniProtKB:Q61831, ECO:0000269|PubMed:15693750, CC ECO:0000269|PubMed:16611996, ECO:0000269|PubMed:18435604, CC ECO:0000269|PubMed:22327296}. CC -!- INTERACTION: CC P53779; P49407: ARRB1; NbExp=2; IntAct=EBI-713543, EBI-743313; CC P53779; P05412: JUN; NbExp=4; IntAct=EBI-713543, EBI-852823; CC P53779; P17535: JUND; NbExp=2; IntAct=EBI-713543, EBI-2682803; CC P53779; Q04206: RELA; NbExp=2; IntAct=EBI-713543, EBI-73886; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16737965}. Membrane CC {ECO:0000269|PubMed:16737965}; Lipid-anchor CC {ECO:0000269|PubMed:16737965}. Nucleus {ECO:0000269|PubMed:16737965}. CC Mitochondrion {ECO:0000269|PubMed:16737965}. Note=Palmitoylation CC regulates MAPK10 trafficking to cytoskeleton. Recruited to the CC mitochondria in the presence of SARM1 (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=A similar low level of binding to substrates is observed for CC isoform alpha-1 and isoform alpha-2. However, there is no correlation CC between binding and phosphorylation, which is achieved about at the CC same efficiency by all isoforms.; CC Name=Alpha-2; CC IsoId=P53779-1; Sequence=Displayed; CC Name=Alpha-1; CC IsoId=P53779-2; Sequence=VSP_004839; CC Name=3; CC IsoId=P53779-3; Sequence=VSP_041911; CC -!- TISSUE SPECIFICITY: Specific to a subset of neurons in the nervous CC system. Present in the hippocampus and areas, cerebellum, striatum, CC brain stem, and weakly in the spinal cord. Very weak expression in CC testis and kidney. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and MAP2K7, CC which activates the enzyme. MAP2K7 shows a strong preference for Thr- CC 221 while MAP2K4 phosphorylates Tyr-223 preferentially. Weakly CC autophosphorylated on threonine and tyrosine residues in vitro. CC {ECO:0000269|PubMed:10715136}. CC -!- PTM: Palmitoylation regulates subcellular location and axonal CC development. {ECO:0000269|PubMed:21941371}. CC -!- MASS SPECTROMETRY: Mass=44070; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:10715136}; CC -!- DISEASE: Note=A chromosomal aberration involving MAPK10 has been found CC in a single patient with pharmacoresistant epileptic encephalopathy. CC Translocation t(Y;4)(q11.2;q21) which causes MAPK10 truncation. CC {ECO:0000269|PubMed:16249883}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG51956.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/427/JNK3"; 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; U07620; AAC50101.1; -; mRNA. DR EMBL; U34819; AAC50604.1; -; mRNA. DR EMBL; U34820; AAC50605.1; -; mRNA. DR EMBL; AK057723; BAG51956.1; ALT_INIT; mRNA. DR EMBL; AK124791; BAG54096.1; -; mRNA. DR EMBL; AC096953; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104059; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108054; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110076; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX05963.1; -; Genomic_DNA. DR EMBL; BC035057; AAH35057.1; -; mRNA. DR CCDS; CCDS34026.1; -. [P53779-1] DR CCDS; CCDS3612.1; -. [P53779-3] DR CCDS; CCDS43247.1; -. [P53779-2] DR PIR; S71104; S71104. DR RefSeq; NP_001304996.1; NM_001318067.1. DR RefSeq; NP_001304997.1; NM_001318068.1. DR RefSeq; NP_001304998.1; NM_001318069.1. DR RefSeq; NP_002744.1; NM_002753.4. [P53779-2] DR RefSeq; NP_620446.1; NM_138980.3. [P53779-3] DR RefSeq; NP_620448.1; NM_138982.3. [P53779-1] DR RefSeq; XP_005263186.1; XM_005263129.2. DR RefSeq; XP_005263187.1; XM_005263130.2. DR RefSeq; XP_005263192.1; XM_005263135.3. DR RefSeq; XP_006714331.1; XM_006714268.2. DR RefSeq; XP_011530419.1; XM_011532117.2. DR RefSeq; XP_011530420.1; XM_011532118.2. DR RefSeq; XP_011530422.1; XM_011532120.2. DR RefSeq; XP_011530423.1; XM_011532121.2. DR RefSeq; XP_016863908.1; XM_017008419.1. DR RefSeq; XP_016863909.1; XM_017008420.1. DR RefSeq; XP_016863910.1; XM_017008421.1. DR RefSeq; XP_016863912.1; XM_017008423.1. DR RefSeq; XP_016863913.1; XM_017008424.1. DR RefSeq; XP_016863914.1; XM_017008425.1. DR RefSeq; XP_016863915.1; XM_017008426.1. DR RefSeq; XP_016863918.1; XM_017008429.1. DR RefSeq; XP_016863919.1; XM_017008430.1. DR RefSeq; XP_016863920.1; XM_017008431.1. DR RefSeq; XP_016863921.1; XM_017008432.1. DR PDB; 1JNK; X-ray; 2.30 A; A=1-423. DR PDB; 1PMN; X-ray; 2.20 A; A=40-401. DR PDB; 1PMU; X-ray; 2.70 A; A=40-401. DR PDB; 1PMV; X-ray; 2.50 A; A=40-401. DR PDB; 2B1P; X-ray; 1.90 A; A=46-400. DR PDB; 2EXC; X-ray; 2.75 A; X=45-400. DR PDB; 2O0U; X-ray; 2.10 A; A=39-402. DR PDB; 2O2U; X-ray; 2.45 A; A=39-402. DR PDB; 2OK1; X-ray; 2.40 A; A=40-402. DR PDB; 2P33; X-ray; 2.40 A; A=40-402. DR PDB; 2R9S; X-ray; 2.40 A; A/B=46-401. DR PDB; 2WAJ; X-ray; 2.40 A; A=39-402. DR PDB; 2ZDT; X-ray; 2.00 A; A=39-402. DR PDB; 2ZDU; X-ray; 2.50 A; A=39-402. DR PDB; 3CGF; X-ray; 3.00 A; A=40-402. DR PDB; 3CGO; X-ray; 3.00 A; A=40-402. DR PDB; 3DA6; X-ray; 2.00 A; A=39-402. DR PDB; 3FI2; X-ray; 2.28 A; A=39-402. DR PDB; 3FI3; X-ray; 2.20 A; A=39-402. DR PDB; 3FV8; X-ray; 2.28 A; A=39-402. DR PDB; 3G90; X-ray; 2.40 A; X=40-402. DR PDB; 3G9L; X-ray; 2.20 A; X=40-402. DR PDB; 3G9N; X-ray; 2.80 A; A=40-402. DR PDB; 3KVX; X-ray; 2.40 A; A=39-402. DR PDB; 3OXI; X-ray; 2.20 A; A=40-401. DR PDB; 3OY1; X-ray; 1.70 A; A=40-401. DR PDB; 3PTG; X-ray; 2.43 A; A=40-401. DR PDB; 3RTP; X-ray; 2.40 A; A=40-401. DR PDB; 3TTI; X-ray; 2.20 A; A=1-464. DR PDB; 3TTJ; X-ray; 2.10 A; A=1-464. DR PDB; 3V6R; X-ray; 2.60 A; A/B=39-402. DR PDB; 3V6S; X-ray; 2.97 A; A/B=39-402. DR PDB; 4H36; X-ray; 3.00 A; A=45-400. DR PDB; 4H39; X-ray; 1.99 A; A=45-400. DR PDB; 4H3B; X-ray; 2.08 A; A/C=45-400. DR PDB; 4KKE; X-ray; 2.20 A; A=40-402. DR PDB; 4KKG; X-ray; 2.40 A; A=40-402. DR PDB; 4KKH; X-ray; 2.00 A; A=40-402. DR PDB; 4U79; X-ray; 2.23 A; A=39-402. DR PDB; 4W4V; X-ray; 2.01 A; A=39-402. DR PDB; 4W4W; X-ray; 1.90 A; A=39-402. DR PDB; 4W4X; X-ray; 2.65 A; A=39-402. DR PDB; 4W4Y; X-ray; 2.30 A; A=39-402. DR PDB; 4WHZ; X-ray; 1.79 A; A=39-423. DR PDB; 4X21; X-ray; 1.95 A; A/B=39-402. DR PDB; 4Y46; X-ray; 2.04 A; A=39-402. DR PDB; 4Y5H; X-ray; 2.06 A; A=39-402. DR PDB; 4Z9L; X-ray; 2.10 A; A=40-401. DR PDB; 6EKD; X-ray; 2.10 A; A=39-402. DR PDB; 6EMH; X-ray; 1.76 A; A/B/C/D=39-402. DR PDB; 6EQ9; X-ray; 1.83 A; A/B=39-402. DR PDB; 7KSI; X-ray; 1.73 A; A=1-464. DR PDB; 7KSJ; X-ray; 2.06 A; A=1-464. DR PDB; 7KSK; X-ray; 1.84 A; A=1-464. DR PDB; 7ORE; X-ray; 2.18 A; A=39-402. DR PDB; 7ORF; X-ray; 1.70 A; A=39-402. DR PDB; 7S1N; X-ray; 2.11 A; A=1-464. DR PDB; 7YL1; X-ray; 2.48 A; A=1-464. DR PDB; 8BZP; X-ray; 1.86 A; A/B=39-402. DR PDB; 8ENJ; X-ray; 2.81 A; A=1-464. DR PDB; 8WGF; X-ray; 1.85 A; A=39-402. DR PDBsum; 1JNK; -. DR PDBsum; 1PMN; -. DR PDBsum; 1PMU; -. DR PDBsum; 1PMV; -. DR PDBsum; 2B1P; -. DR PDBsum; 2EXC; -. DR PDBsum; 2O0U; -. DR PDBsum; 2O2U; -. DR PDBsum; 2OK1; -. DR PDBsum; 2P33; -. DR PDBsum; 2R9S; -. DR PDBsum; 2WAJ; -. DR PDBsum; 2ZDT; -. DR PDBsum; 2ZDU; -. DR PDBsum; 3CGF; -. DR PDBsum; 3CGO; -. DR PDBsum; 3DA6; -. DR PDBsum; 3FI2; -. DR PDBsum; 3FI3; -. DR PDBsum; 3FV8; -. DR PDBsum; 3G90; -. DR PDBsum; 3G9L; -. DR PDBsum; 3G9N; -. DR PDBsum; 3KVX; -. DR PDBsum; 3OXI; -. DR PDBsum; 3OY1; -. DR PDBsum; 3PTG; -. DR PDBsum; 3RTP; -. DR PDBsum; 3TTI; -. DR PDBsum; 3TTJ; -. DR PDBsum; 3V6R; -. DR PDBsum; 3V6S; -. DR PDBsum; 4H36; -. DR PDBsum; 4H39; -. DR PDBsum; 4H3B; -. DR PDBsum; 4KKE; -. DR PDBsum; 4KKG; -. DR PDBsum; 4KKH; -. DR PDBsum; 4U79; -. DR PDBsum; 4W4V; -. DR PDBsum; 4W4W; -. DR PDBsum; 4W4X; -. DR PDBsum; 4W4Y; -. DR PDBsum; 4WHZ; -. DR PDBsum; 4X21; -. DR PDBsum; 4Y46; -. DR PDBsum; 4Y5H; -. DR PDBsum; 4Z9L; -. DR PDBsum; 6EKD; -. DR PDBsum; 6EMH; -. DR PDBsum; 6EQ9; -. DR PDBsum; 7KSI; -. DR PDBsum; 7KSJ; -. DR PDBsum; 7KSK; -. DR PDBsum; 7ORE; -. DR PDBsum; 7ORF; -. DR PDBsum; 7S1N; -. DR PDBsum; 7YL1; -. DR PDBsum; 8BZP; -. DR PDBsum; 8ENJ; -. DR PDBsum; 8WGF; -. DR AlphaFoldDB; P53779; -. DR SMR; P53779; -. DR BioGRID; 111588; 57. DR CORUM; P53779; -. DR DIP; DIP-1015N; -. DR ELM; P53779; -. DR IntAct; P53779; 27. DR MINT; P53779; -. DR BindingDB; P53779; -. DR ChEMBL; CHEMBL2637; -. DR DrugBank; DB08011; (3E)-5-fluoro-1-[(6-fluoro-4H-1,3-benzodioxin-8-yl)methyl]-1H-indole-2,3-dione 3-oxime. DR DrugBank; DB08010; (3Z)-1-[(6-fluoro-4H-1,3-benzodioxin-8-yl)methyl]-4-[(E)-2-phenylethenyl]-1H-indole-2,3-dione 3-oxime. DR DrugBank; DB08015; (3Z)-1-[(6-fluoro-4H-1,3-benzodioxin-8-yl)methyl]-4-phenyl-1H-indole-2,3-dione 3-oxime. DR DrugBank; DB08555; 1-(3-bromophenyl)-7-chloro-6-methoxy-3,4-dihydroisoquinoline. DR DrugBank; DB08026; 2-{4-[(4-imidazo[1,2-a]pyridin-3-ylpyrimidin-2-yl)amino]piperidin-1-yl}-N-methylacetamide. DR DrugBank; DB08005; 4-{[5-chloro-4-(1H-indol-3-yl)pyrimidin-2-yl]amino}-N-ethylpiperidine-1-carboxamide. DR DrugBank; DB08021; 5-bromo-N-(3-chloro-2-(4-(prop-2-ynyl)piperazin-1-yl)phenyl)furan-2-carboxamide. DR DrugBank; DB03623; 9-(4-Hydroxyphenyl)-2,7-Phenanthroline. DR DrugBank; DB02388; Cyclohexyl-{4-[5-(3,4-Dichlorophenyl)-2-Piperidin-4-Yl-3-Propyl-3h-Imidazol-4-Yl]-Pyrimidin-2-Yl}Amine. DR DrugBank; DB03084; Cyclopropyl-{4-[5-(3,4-Dichlorophenyl)-2-[(1-Methyl)-Piperidin]-4-Yl-3-Propyl-3h-Imidazol-4-Yl]-Pyrimidin-2-Yl}Amine. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB15624; Halicin. DR DrugBank; DB01017; Minocycline. DR DrugBank; DB07217; N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)-2-fluorobenzamide. DR DrugBank; DB06933; N-(tert-butyl)-4-[5-(pyridin-2-ylamino)quinolin-3-yl]benzenesulfonamide. DR DrugBank; DB07010; N-BENZYL-4-[4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL]-1H-PYRROLE-2-CARBOXAMIDE. DR DrugBank; DB08023; N-cyclohexyl-4-imidazo[1,2-a]pyridin-3-yl-N-methylpyrimidin-2-amine. DR DrugBank; DB08025; N-{2'-[(4-FLUOROPHENYL)AMINO]-4,4'-BIPYRIDIN-2-YL}-4-METHOXYCYCLOHEXANECARBOXAMIDE. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR DrugBank; DB01782; Pyrazolanthrone. DR DrugCentral; P53779; -. DR GuidetoPHARMACOLOGY; 1498; -. DR iPTMnet; P53779; -. DR PhosphoSitePlus; P53779; -. DR SwissPalm; P53779; -. DR BioMuta; MAPK10; -. DR DMDM; 2507196; -. DR CPTAC; CPTAC-2915; -. DR CPTAC; CPTAC-2916; -. DR EPD; P53779; -. DR jPOST; P53779; -. DR MassIVE; P53779; -. DR MaxQB; P53779; -. DR PaxDb; 9606-ENSP00000352157; -. DR PeptideAtlas; P53779; -. DR ProteomicsDB; 56616; -. [P53779-1] DR ProteomicsDB; 56617; -. [P53779-2] DR ProteomicsDB; 56618; -. [P53779-3] DR Pumba; P53779; -. DR Antibodypedia; 14345; 656 antibodies from 38 providers. DR DNASU; 5602; -. DR Ensembl; ENST00000395157.9; ENSP00000378586.4; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000395166.6; ENSP00000378595.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000515400.3; ENSP00000424154.3; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000515650.2; ENSP00000492204.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000638225.1; ENSP00000491866.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000638313.1; ENSP00000492292.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000639175.1; ENSP00000491160.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000639234.1; ENSP00000491306.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000639242.1; ENSP00000491089.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000640858.1; ENSP00000491122.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000640970.1; ENSP00000492231.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000641050.1; ENSP00000493270.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000641051.1; ENSP00000493275.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641066.1; ENSP00000493072.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641110.1; ENSP00000493163.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641157.1; ENSP00000493363.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641170.1; ENSP00000493237.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000641207.1; ENSP00000493450.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641274.1; ENSP00000492929.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000641283.1; ENSP00000493444.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641287.1; ENSP00000493100.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641297.1; ENSP00000493092.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641341.1; ENSP00000493290.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641391.1; ENSP00000493008.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641410.1; ENSP00000493208.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000641462.2; ENSP00000493435.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641647.1; ENSP00000493375.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641657.1; ENSP00000493105.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641724.1; ENSP00000493038.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641737.1; ENSP00000493177.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641803.1; ENSP00000493049.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641823.1; ENSP00000493408.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641862.1; ENSP00000493396.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000641902.1; ENSP00000492903.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641911.1; ENSP00000493374.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641943.1; ENSP00000492941.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000641952.1; ENSP00000493013.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000641983.1; ENSP00000493045.1; ENSG00000109339.24. [P53779-1] DR Ensembl; ENST00000642009.1; ENSP00000493168.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000642015.1; ENSP00000493040.1; ENSG00000109339.24. [P53779-3] DR Ensembl; ENST00000642038.1; ENSP00000492942.1; ENSG00000109339.24. [P53779-2] DR Ensembl; ENST00000642103.1; ENSP00000493001.1; ENSG00000109339.24. [P53779-3] DR GeneID; 5602; -. DR KEGG; hsa:5602; -. DR MANE-Select; ENST00000641462.2; ENSP00000493435.1; NM_138982.4; NP_620448.1. DR UCSC; uc003hpp.4; human. [P53779-1] DR AGR; HGNC:6872; -. DR CTD; 5602; -. DR DisGeNET; 5602; -. DR GeneCards; MAPK10; -. DR HGNC; HGNC:6872; MAPK10. DR HPA; ENSG00000109339; Tissue enhanced (brain). DR MalaCards; MAPK10; -. DR MIM; 602897; gene. DR neXtProt; NX_P53779; -. DR OpenTargets; ENSG00000109339; -. DR Orphanet; 2382; Lennox-Gastaut syndrome. DR PharmGKB; PA30617; -. DR VEuPathDB; HostDB:ENSG00000109339; -. DR eggNOG; KOG0665; Eukaryota. DR GeneTree; ENSGT00940000153692; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; P53779; -. DR OrthoDB; 158564at2759; -. DR PhylomeDB; P53779; -. DR TreeFam; TF105100; -. DR BRENDA; 2.7.11.24; 2681. DR PathwayCommons; P53779; -. DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation. DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1. DR Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors. DR SignaLink; P53779; -. DR SIGNOR; P53779; -. DR BioGRID-ORCS; 5602; 12 hits in 1186 CRISPR screens. DR ChiTaRS; MAPK10; human. DR EvolutionaryTrace; P53779; -. DR GeneWiki; MAPK10; -. DR GenomeRNAi; 5602; -. DR Pharos; P53779; Tchem. DR PRO; PR:P53779; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P53779; Protein. DR Bgee; ENSG00000109339; Expressed in adrenal tissue and 134 other cell types or tissues. DR ExpressionAtlas; P53779; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB. DR GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0090398; P:cellular senescence; TAS:Reactome. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0007254; P:JNK cascade; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0009416; P:response to light stimulus; ISS:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd07850; STKc_JNK; 1. DR DisProt; DP02328; -. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00456; -. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008351; MAPK_JNK. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF162; MITOGEN-ACTIVATED PROTEIN KINASE 10; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01772; JNKMAPKINASE. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS01351; MAPK; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P53779; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Biological rhythms; KW Chromosomal rearrangement; Cytoplasm; Direct protein sequencing; Epilepsy; KW Intellectual disability; Kinase; Lipoprotein; Membrane; Mitochondrion; KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..464 FT /note="Mitogen-activated protein kinase 10" FT /id="PRO_0000186277" FT DOMAIN 64..359 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 405..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 221..223 FT /note="TXY" FT COMPBIAS 406..454 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 189 FT /note="Proton acceptor" FT BINDING 70..78 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 221 FT /note="Phosphothreonine; by MAP2K7" FT /evidence="ECO:0000269|PubMed:10715136" FT MOD_RES 223 FT /note="Phosphotyrosine; by MAP2K4" FT /evidence="ECO:0000269|PubMed:10715136" FT LIPID 462 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:21941371" FT LIPID 463 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:21941371" FT VAR_SEQ 1..38 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041911" FT VAR_SEQ 418..464 FT /note="GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR -> A FT QVQQ (in isoform Alpha-1)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:7826642, ECO:0000303|PubMed:8654373" FT /id="VSP_004839" FT MUTAGEN 462 FT /note="C->S: Loss of palmitoylation." FT /evidence="ECO:0000269|PubMed:21941371" FT MUTAGEN 463 FT /note="C->S: Loss of palmitoylation." FT /evidence="ECO:0000269|PubMed:21941371" FT CONFLICT 162 FT /note="D -> G (in Ref. 3; BAG51956)" FT /evidence="ECO:0000305" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:7ORE" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:3OY1" FT TURN 84..87 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 88..97 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 102..114 FT /evidence="ECO:0007829|PDB:3OY1" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:3KVX" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:3OY1" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 153..157 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 163..182 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:3RTP" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:3OY1" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:3PTG" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:7ORF" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:4H3B" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:4H3B" FT HELIX 227..229 FT /evidence="ECO:0007829|PDB:4H3B" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 244..258 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 268..279 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 284..287 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 292..299 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 323..339 FT /evidence="ECO:0007829|PDB:3OY1" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 350..355 FT /evidence="ECO:0007829|PDB:3OY1" FT TURN 357..361 FT /evidence="ECO:0007829|PDB:3OY1" FT HELIX 365..368 FT /evidence="ECO:0007829|PDB:3OY1" FT TURN 378..382 FT /evidence="ECO:0007829|PDB:6EMH" FT HELIX 387..399 FT /evidence="ECO:0007829|PDB:3OY1" SQ SEQUENCE 464 AA; 52585 MW; 2E20C05EB89CDA66 CRC64; MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCR //