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   27-MAR-2024, entry version 126.
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   FUNCTION, INTERACTION WITH AMFR; CANX; PSMC1; PSMC2; PSMC3; PSMC5; PSMC6;
RP   PSMC8; RNF5; SEC61-ALPHA AND UFD1, AND SUBCELLULAR LOCATION.
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: Regulates the duration of MAPK8 activity in response to
CC       various stress stimuli (PubMed:16166642). Facilitates degradation of
CC       misfolded endoplasmic reticulum (ER) proteins through the recruitment
CC       of components of the proteasome and endoplasmic reticulum-associated
CC       degradation (ERAD) system (PubMed:18784250).
CC       {ECO:0000269|PubMed:16166642, ECO:0000269|PubMed:18784250}.
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 (PubMed:16166642,
CC       PubMed:19269966). Associates with multiple components of the proteasome
CC       and with ERAD regulatory proteins, including AMFR/GP78, CANX, PSMC1,
CC       PSMC2, PSMC3/TBP1, PSMC5, PSMC6, PSMD8, SEC61-ALPHA and UFD1
CC       (PubMed:18784250). {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.
CC       {ECO:0000269|PubMed:16166642}.
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   GlyCosmos; Q8BI36; 1 site, No reported glycans.
DR   GlyGen; Q8BI36; 1 site.
DR   iPTMnet; Q8BI36; -.
DR   PhosphoSitePlus; Q8BI36; -.
DR   MaxQB; Q8BI36; -.
DR   PaxDb; 10090-ENSMUSP00000061370; -.
DR   ProteomicsDB; 269119; -. [Q8BI36-1]
DR   ProteomicsDB; 269120; -. [Q8BI36-2]
DR   Ensembl; ENSMUST00000057257.10; ENSMUSP00000061370.9; ENSMUSG00000005078.17. [Q8BI36-1]
DR   Ensembl; ENSMUST00000117449.8; ENSMUSP00000113744.2; ENSMUSG00000005078.17. [Q8BI36-2]
DR   GeneID; 104771; -.
DR   KEGG; mmu:104771; -.
DR   UCSC; uc007nvf.2; mouse. [Q8BI36-1]
DR   UCSC; uc007nvg.2; mouse. [Q8BI36-2]
DR   AGR; MGI:1915057; -.
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; WLLHGYG; -.
DR   OrthoDB; 2912838at2759; -.
DR   PhylomeDB; Q8BI36; -.
DR   TreeFam; TF314201; -.
DR   BioGRID-ORCS; 104771; 3 hits in 75 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 263 other cell types or tissues.
DR   ExpressionAtlas; Q8BI36; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; JNK1/MAPK8-ASSOCIATED MEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR12740:SF3; JNK1_MAPK8-ASSOCIATED MEMBRANE PROTEIN; 1.
DR   Pfam; PF05571; JAMP; 1.
DR   Genevisible; Q8BI36; MM.
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
//