MK10_HUMAN
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 03-AUG-2022, entry version 227.
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-ARNTL/BMAL1 heterodimer and plays a role in
CC the 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="http://atlasgeneticsoncology.org/Genes/JNK3ID427.html";
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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. [P53779-1]
DR RefSeq; XP_005263187.1; XM_005263130.2. [P53779-1]
DR RefSeq; XP_005263192.1; XM_005263135.3. [P53779-2]
DR RefSeq; XP_006714331.1; XM_006714268.2. [P53779-3]
DR RefSeq; XP_011530419.1; XM_011532117.2. [P53779-1]
DR RefSeq; XP_011530420.1; XM_011532118.2. [P53779-1]
DR RefSeq; XP_011530422.1; XM_011532120.2. [P53779-3]
DR RefSeq; XP_011530423.1; XM_011532121.2. [P53779-3]
DR RefSeq; XP_016863908.1; XM_017008419.1.
DR RefSeq; XP_016863909.1; XM_017008420.1. [P53779-1]
DR RefSeq; XP_016863910.1; XM_017008421.1.
DR RefSeq; XP_016863912.1; XM_017008423.1. [P53779-3]
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. [P53779-2]
DR RefSeq; XP_016863919.1; XM_017008430.1. [P53779-2]
DR RefSeq; XP_016863920.1; XM_017008431.1.
DR RefSeq; XP_016863921.1; XM_017008432.1. [P53779-2]
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 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 AlphaFoldDB; P53779; -.
DR SMR; P53779; -.
DR BioGRID; 111588; 54.
DR CORUM; P53779; -.
DR DIP; DIP-1015N; -.
DR ELM; P53779; -.
DR IntAct; P53779; 27.
DR MINT; P53779; -.
DR STRING; 9606.ENSP00000352157; -.
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 EPD; P53779; -.
DR jPOST; P53779; -.
DR MassIVE; P53779; -.
DR MaxQB; P53779; -.
DR PaxDb; P53779; -.
DR PeptideAtlas; P53779; -.
DR PRIDE; P53779; -.
DR ProteomicsDB; 56616; -. [P53779-1]
DR ProteomicsDB; 56617; -. [P53779-2]
DR ProteomicsDB; 56618; -. [P53779-3]
DR Antibodypedia; 14345; 584 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 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; 741207at2759; -.
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; 11 hits in 1108 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 132 other tissues.
DR ExpressionAtlas; P53779; baseline and differential.
DR Genevisible; P53779; HS.
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; TAS:Reactome.
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:0004707; F:MAP kinase activity; IBA:GO_Central.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; TAS:Reactome.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:0051090; P:regulation of DNA-binding transcription factor activity; TAS:Reactome.
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 DisProt; DP02328; -.
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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
