JKAMP_MOUSE
ID JKAMP_MOUSE Reviewed; 311 AA.
AC Q8BI36; B8JJ79; B8JJ80; Q99LT2; Q9CUZ1;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=JNK1/MAPK8-associated membrane protein;
DE Short=JKAMP;
DE AltName: Full=JNK1-associated membrane protein;
DE Short=JAMP;
DE AltName: Full=Medulloblastoma antigen MU-MB-50.4 homolog;
GN Name=Jkamp; Synonyms=Jamp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH RNF5 AND MAPK8, MUTAGENESIS OF SER-24,
RP AND GLYCOSYLATION AT ASN-22.
RX PubMed=16166642; DOI=10.1128/mcb.25.19.8619-8630.2005;
RA Kadoya T., Khurana A., Tcherpakov M., Bromberg K.D., Didier C., Broday L.,
RA Asahara T., Bhoumik A., Ronai Z.;
RT "JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein,
RT regulates duration of JNK activity.";
RL Mol. Cell. Biol. 25:8619-8630(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH AMFR; CANX; PSMC1; PSMC2; PSMC3; PSMC5; PSMC6; PSMC8;
RP RNF5; SEC61-ALPHA AND UFD1, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18784250; DOI=10.1091/mbc.e08-08-0839;
RA Tcherpakov M., Broday L., Delaunay A., Kadoya T., Khurana A.,
RA Erdjument-Bromage H., Tempst P., Qiu X.-B., DeMartino G.N., Ronai Z.;
RT "JAMP optimizes ERAD to protect cells from unfolded proteins.";
RL Mol. Biol. Cell 19:5019-5028(2008).
RN [5]
RP INTERACTION WITH RNF5, AND UBIQUITINATION.
RX PubMed=19269966; DOI=10.1074/jbc.m808222200;
RA Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.;
RT "Regulation of endoplasmic reticulum-associated degradation by RNF5-
RT dependent ubiquitination of JNK-associated membrane protein (JAMP).";
RL J. Biol. Chem. 284:12099-12109(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II;
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).
CC -!- FUNCTION: May be a regulator of the duration of MAPK8 activity in
CC response to various stress stimuli. Facilitates degradation of
CC misfolded endoplasmic reticulum (ER) luminal proteins through the
CC recruitment of components of the proteasome and endoplasmic reticulum-
CC associated degradation (ERAD) system. {ECO:0000269|PubMed:16166642}.
CC -!- SUBUNIT: Interacts with RNF5 and MAPK8, but not with MAPK9. Binding to
CC MAPK8 occurs before and after exposure to stress, such as UV
CC irradiation. After exposure to stress, interacts with phosphorylated
CC MAPK8. Competes with DUSP10 for MAPK8 binding. Associates with multiple
CC components of the proteasome and with ERAD regulatory proteins,
CC including AMFR/GP78, CANX, PSMC1, PSMC2, PSMC3/TBP1, PSMC5, PSMC6,
CC PSMD8, SEC61-ALPHA and UFD1. {ECO:0000269|PubMed:16166642,
CC ECO:0000269|PubMed:18784250, ECO:0000269|PubMed:19269966}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:18784250}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16166642,
CC ECO:0000269|PubMed:18784250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BI36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BI36-2; Sequence=VSP_008813;
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues, including brain,
CC spleen, thymus, liver, kidney and testis. Elevated expression in
CC medulloblastoma. {ECO:0000269|PubMed:16166642}.
CC -!- INDUCTION: By ER stress. {ECO:0000269|PubMed:18784250}.
CC -!- PTM: Ubiquitinated by RNF5 via 'Lys-63'-linked ubiquitin linkage in a
CC UBE2N-dependent manner. Ubiquitination decreases association with
CC components of the proteasome and ERAD. {ECO:0000269|PubMed:19269966}.
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DR EMBL; AK013502; BAB28884.1; -; mRNA.
DR EMBL; AK004555; BAC25088.1; -; mRNA.
DR EMBL; CR974486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002238; AAH02238.1; -; mRNA.
DR CCDS; CCDS25967.1; -. [Q8BI36-1]
DR CCDS; CCDS56844.1; -. [Q8BI36-2]
DR RefSeq; NP_001191996.1; NM_001205067.1. [Q8BI36-2]
DR RefSeq; NP_077167.1; NM_024205.2. [Q8BI36-1]
DR AlphaFoldDB; Q8BI36; -.
DR STRING; 10090.ENSMUSP00000061370; -.
DR GlyGen; Q8BI36; 1 site.
DR iPTMnet; Q8BI36; -.
DR PhosphoSitePlus; Q8BI36; -.
DR MaxQB; Q8BI36; -.
DR PaxDb; Q8BI36; -.
DR PRIDE; Q8BI36; -.
DR ProteomicsDB; 269119; -. [Q8BI36-1]
DR ProteomicsDB; 269120; -. [Q8BI36-2]
DR Ensembl; ENSMUST00000057257; ENSMUSP00000061370; ENSMUSG00000005078. [Q8BI36-1]
DR Ensembl; ENSMUST00000117449; ENSMUSP00000113744; ENSMUSG00000005078. [Q8BI36-2]
DR GeneID; 104771; -.
DR KEGG; mmu:104771; -.
DR UCSC; uc007nvf.2; mouse. [Q8BI36-1]
DR UCSC; uc007nvg.2; mouse. [Q8BI36-2]
DR CTD; 51528; -.
DR MGI; MGI:1915057; Jkamp.
DR VEuPathDB; HostDB:ENSMUSG00000005078; -.
DR eggNOG; KOG3744; Eukaryota.
DR GeneTree; ENSGT00390000018097; -.
DR HOGENOM; CLU_062918_1_0_1; -.
DR InParanoid; Q8BI36; -.
DR OMA; GPTLFYI; -.
DR OrthoDB; 1289136at2759; -.
DR PhylomeDB; Q8BI36; -.
DR TreeFam; TF314201; -.
DR BioGRID-ORCS; 104771; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Jkamp; mouse.
DR PRO; PR:Q8BI36; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BI36; protein.
DR Bgee; ENSMUSG00000005078; Expressed in facial nucleus and 259 other tissues.
DR ExpressionAtlas; Q8BI36; baseline and differential.
DR Genevisible; Q8BI36; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR008485; JAMP.
DR PANTHER; PTHR12740; PTHR12740; 1.
DR Pfam; PF05571; JAMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Unfolded protein response.
FT CHAIN 1..311
FT /note="JNK1/MAPK8-associated membrane protein"
FT /id="PRO_0000089904"
FT TOPO_DOM 1..57
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..149
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..277
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16166642"
FT VAR_SEQ 1..7
FT /note="MAVDIQP -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008813"
FT MUTAGEN 24
FT /note="S->A: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:16166642"
FT CONFLICT 261
FT /note="H -> R (in Ref. 2; BAC25088)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="I -> M (in Ref. 2; BAC25088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 35248 MW; 7C167E3ABCD8D814 CRC64;
MAVDIQPACL GLYCGKTLLF KNGSSEIYGE CGVCPRGQRT NAQKYCQPCT ESPELYDWLY
LGFMAMLPLV LHWFFIEWYS GKKSSSALFQ HITALFECTM AAIITLLVSD PVGVLYIRSC
RVLMLSDWYT MLYNPSPDYV TTVHCTHEAV YPLYTIVFVY YAFCLVLMML LRPLLVKKIA
CGLGKSDRFK SIYAALYFFP ILTVLQAVGG GLLYYAFPYI ILVLSLVTLA VYMSASEIEN
CYDLLVRKKR LIVLFSHWLL HAYGIVSISR VDRLEHDLPL LALVPTPALF YLFTAKFTEP
SRILSEGANG H
