ID   JKAMP_HUMAN             Reviewed;         311 AA.
AC   Q9P055; B4DP67; Q6FIB6; Q6IAJ2; Q7Z5D4; Q86SY6; Q9H0Q6; Q9H2W0; Q9HAH5;
AC   Q9P0R3;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 4.
DT   27-MAR-2024, entry version 169.
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;
GN   Name=JKAMP; Synonyms=C14orf100, JAMP;
GN   ORFNames=CDA06, HSPC213, HSPC327;
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 2).
RC   TISSUE=Medulloblastoma;
RX   PubMed=12800201; DOI=10.1002/ijc.11208;
RA   Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A.,
RA   Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S.,
RA   Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F.,
RA   Asmuss H.-P., Bise K., Mautner J.;
RT   "Novel tumor antigens identified by autologous antibody screening of
RT   childhood medulloblastoma cDNA libraries.";
RL   Int. J. Cancer 106:244-251(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Embryo, and Teratocarcinoma;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Pheochromocytoma;
RA   Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT   "A novel gene expressed in human pheochromocytoma.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Cervix carcinoma;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Bone marrow;
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   [10] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH DERL1.
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).
CC   -!- FUNCTION: Regulates the duration of MAPK8 activity in response to
CC       various stress stimuli (By similarity). 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:0000250|UniProtKB:Q8BI36, 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. 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 (By similarity). Interacts with DERL1 (in
CC       the presence of misfolded protein CFTR(F508del)) (PubMed:18784250).
CC       {ECO:0000250|UniProtKB:Q8BI36, ECO:0000269|PubMed:18784250}.
CC   -!- INTERACTION:
CC       Q9P055-4; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-13310605, EBI-751210;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:18784250}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9P055-4; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P055-2; Sequence=VSP_060708;
CC       Name=3;
CC         IsoId=Q9P055-3; Sequence=VSP_060710;
CC       Name=4;
CC         IsoId=Q9P055-5; Sequence=VSP_060709;
CC   -!- INDUCTION: Basal expression under nonstress conditions; expression
CC       increases transiently after endoplasmic reticulum (ER) stress.
CC       {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:0000250|UniProtKB:Q8BI36}.
CC   -!- MISCELLANEOUS: Elevated expression in medulloblastomas
CC       (PubMed:12800201). Patients with cancer had 2 to 12-fold higher
CC       frequencies of antibodies against this antigen (PubMed:12800201).
CC       {ECO:0000269|PubMed:12800201}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF29005.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAF36133.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF529304; AAP85636.1; -; mRNA.
DR   EMBL; AF151047; AAF36133.1; ALT_FRAME; mRNA.
DR   EMBL; AF161445; AAF29005.1; ALT_SEQ; mRNA.
DR   EMBL; AL136696; CAB66631.1; -; mRNA.
DR   EMBL; AK021683; BAB13874.1; -; mRNA.
DR   EMBL; AK027591; BAB55216.1; -; mRNA.
DR   EMBL; AK298209; BAG60479.1; -; mRNA.
DR   EMBL; AF212245; AAG41781.1; -; mRNA.
DR   EMBL; BX161501; CAD61945.1; -; mRNA.
DR   EMBL; CR457163; CAG33444.1; -; mRNA.
DR   EMBL; CR533510; CAG38541.1; -; mRNA.
DR   EMBL; CH471061; EAW80753.1; -; Genomic_DNA.
DR   EMBL; BC005198; AAH05198.1; -; mRNA.
DR   EMBL; BC010359; AAH10359.1; -; mRNA.
DR   CCDS; CCDS45116.1; -. [Q9P055-4]
DR   CCDS; CCDS45117.1; -. [Q9P055-3]
DR   CCDS; CCDS61463.1; -. [Q9P055-5]
DR   RefSeq; NP_001092095.1; NM_001098625.2. [Q9P055-3]
DR   RefSeq; NP_001271130.1; NM_001284201.1.
DR   RefSeq; NP_001271131.1; NM_001284202.1. [Q9P055-5]
DR   RefSeq; NP_001271132.1; NM_001284203.1. [Q9P055-2]
DR   RefSeq; NP_001271133.1; NM_001284204.1.
DR   RefSeq; NP_057559.2; NM_016475.4. [Q9P055-4]
DR   AlphaFoldDB; Q9P055; -.
DR   BioGRID; 119590; 13.
DR   IntAct; Q9P055; 4.
DR   MINT; Q9P055; -.
DR   STRING; 9606.ENSP00000450749; -.
DR   GlyGen; Q9P055; 1 site.
DR   iPTMnet; Q9P055; -.
DR   PhosphoSitePlus; Q9P055; -.
DR   BioMuta; JKAMP; -.
DR   DMDM; 38257782; -.
DR   MassIVE; Q9P055; -.
DR   PaxDb; 9606-ENSP00000450749; -.
DR   PeptideAtlas; Q9P055; -.
DR   ProteomicsDB; 83542; -. [Q9P055-2]
DR   ProteomicsDB; 83543; -. [Q9P055-3]
DR   ProteomicsDB; 83544; -. [Q9P055-4]
DR   ProteomicsDB; 83545; -. [Q9P055-5]
DR   Antibodypedia; 51808; 56 antibodies from 9 providers.
DR   DNASU; 51528; -.
DR   Ensembl; ENST00000356057.9; ENSP00000348351.5; ENSG00000050130.18. [Q9P055-5]
DR   Ensembl; ENST00000425728.6; ENSP00000389699.2; ENSG00000050130.18. [Q9P055-3]
DR   Ensembl; ENST00000616435.5; ENSP00000479775.2; ENSG00000050130.18. [Q9P055-4]
DR   GeneID; 51528; -.
DR   KEGG; hsa:51528; -.
DR   MANE-Select; ENST00000616435.5; ENSP00000479775.2; NM_016475.5; NP_057559.2.
DR   UCSC; uc001xef.6; human. [Q9P055-4]
DR   AGR; HGNC:20184; -.
DR   GeneCards; JKAMP; -.
DR   HGNC; HGNC:20184; JKAMP.
DR   HPA; ENSG00000050130; Low tissue specificity.
DR   MIM; 611176; gene.
DR   neXtProt; NX_Q9P055; -.
DR   OpenTargets; ENSG00000050130; -.
DR   PharmGKB; PA165479069; -.
DR   VEuPathDB; HostDB:ENSG00000050130; -.
DR   eggNOG; KOG3744; Eukaryota.
DR   GeneTree; ENSGT00390000018097; -.
DR   HOGENOM; CLU_062918_1_0_1; -.
DR   InParanoid; Q9P055; -.
DR   OMA; WLLHGYG; -.
DR   OrthoDB; 2912838at2759; -.
DR   PhylomeDB; Q9P055; -.
DR   TreeFam; TF314201; -.
DR   PathwayCommons; Q9P055; -.
DR   SignaLink; Q9P055; -.
DR   SIGNOR; Q9P055; -.
DR   BioGRID-ORCS; 51528; 20 hits in 1153 CRISPR screens.
DR   ChiTaRS; JKAMP; human.
DR   GeneWiki; JKAMP; -.
DR   GenomeRNAi; 51528; -.
DR   Pharos; Q9P055; Tbio.
DR   PRO; PR:Q9P055; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9P055; Protein.
DR   Bgee; ENSG00000050130; Expressed in islet of Langerhans and 186 other cell types or tissues.
DR   ExpressionAtlas; Q9P055; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR   InterPro; IPR008485; JAMP.
DR   PANTHER; PTHR12740; JNK1/MAPK8-ASSOCIATED MEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR12740:SF4; JNK1_MAPK8-ASSOCIATED MEMBRANE PROTEIN; 1.
DR   Pfam; PF05571; JAMP; 1.
DR   Genevisible; Q9P055; HS.
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_0000089903"
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:0000255"
FT   VAR_SEQ         1..63
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305|PubMed:12800201"
FT                   /id="VSP_060708"
FT   VAR_SEQ         1..8
FT                   /note="MAVDIQPA -> MKGEIQQSLGAWVLLT (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060709"
FT   VAR_SEQ         1..7
FT                   /note="MAVDIQP -> M (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060710"
FT   CONFLICT        70
FT                   /note="V -> A (in Ref. 4; BAB13874)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="S -> P (in Ref. 2; AAF36133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="N -> S (in Ref. 2; AAF36133)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  35239 MW;  F294B4CAFDDCECE4 CRC64;
     MAVDIQPACL GLYCGKTLLF KNGSTEIYGE CGVCPRGQRT NAQKYCQPCT ESPELYDWLY
     LGFMAMLPLV LHWFFIEWYS GKKSSSALFQ HITALFECSM AAIITLLVSD PVGVLYIRSC
     RVLMLSDWYT MLYNPSPDYV TTVHCTHEAV YPLYTIVFIY YAFCLVLMML LRPLLVKKIA
     CGLGKSDRFK SIYAALYFFP ILTVLQAVGG GLLYYAFPYI ILVLSLVTLA VYMSASEIEN
     CYDLLVRKKR LIVLFSHWLL HAYGIISISR VDKLEQDLPL LALVPTPALF YLFTAKFTEP
     SRILSEGANG H
//