JKAMP_HUMAN
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 03-AUG-2022, entry version 160.
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; 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).
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 (By similarity). {ECO:0000250}.
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). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P055-4; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-13310605, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Patients with cancer had 2 to 12-fold higher frequencies
CC of antibodies against this antigen.
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; 12.
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; Q9P055; -.
DR PeptideAtlas; Q9P055; -.
DR PRIDE; Q9P055; -.
DR ProteomicsDB; 83542; -. [Q9P055-2]
DR ProteomicsDB; 83543; -. [Q9P055-3]
DR ProteomicsDB; 83544; -. [Q9P055-4]
DR ProteomicsDB; 83545; -. [Q9P055-5]
DR Antibodypedia; 51808; 52 antibodies from 7 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 CTD; 51528; -.
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; GPTLFYI; -.
DR PhylomeDB; Q9P055; -.
DR TreeFam; TF314201; -.
DR PathwayCommons; Q9P055; -.
DR SignaLink; Q9P055; -.
DR BioGRID-ORCS; 51528; 20 hits in 1076 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 184 other tissues.
DR ExpressionAtlas; Q9P055; baseline and differential.
DR Genevisible; Q9P055; HS.
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; 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; PTHR12740; 1.
DR Pfam; PF05571; JAMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW 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 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
