Full text data of IGJ
IGJ
(IGCJ)
[Confidence: low (only semi-automatic identification from reviews)]
Immunoglobulin J chain; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Immunoglobulin J chain; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P01591
ID IGJ_HUMAN Reviewed; 159 AA.
AC P01591;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-OCT-2009, sequence version 4.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Immunoglobulin J chain;
DE Flags: Precursor;
GN Name=IGJ; Synonyms=IGCJ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 23-159.
RX PubMed=407930; DOI=10.1021/bi00635a002;
RA Mole J.E., Bhown A.S., Bennett J.C.;
RT "Primary structure of human J chain: alignment of peptides from
RT chemical and enzymatic hydrolyses.";
RL Biochemistry 16:3507-3513(1977).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-159.
RX PubMed=2984306; DOI=10.1084/jem.161.4.832;
RA Max E.E., Korsmeyer S.J.;
RT "Human J chain gene. Structure and expression in B lymphoid cells.";
RL J. Exp. Med. 161:832-849(1985).
RN [4]
RP DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1472500; DOI=10.1021/bi00165a014;
RA Frutiger S., Hughes G.J., Paquet N., Luethy R., Jaton J.-C.;
RT "Disulfide bond assignment in human J chain and its covalent pairing
RT with immunoglobulin M.";
RL Biochemistry 31:12643-12647(1992).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP GLYCOSYLATION AT ASN-71.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Serves to link two monomer units of either IgM or IgA.
CC In the case of IgM, the J chain-joined dimer is a nucleating unit
CC for the IgM pentamer, and in the case of IgA it induces larger
CC polymers. It also help to bind these immunoglobulins to secretory
CC component.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK312014; BAG34952.1; -; mRNA.
DR EMBL; M12759; AAA58902.1; -; Genomic_DNA.
DR EMBL; M12378; AAA58902.1; JOINED; Genomic_DNA.
DR PIR; A01859; JIHU.
DR RefSeq; NP_653247.1; NM_144646.3.
DR UniGene; Hs.643431; -.
DR ProteinModelPortal; P01591; -.
DR IntAct; P01591; 2.
DR STRING; 9606.ENSP00000254801; -.
DR PhosphoSite; P01591; -.
DR UniCarbKB; P01591; -.
DR SWISS-2DPAGE; P01591; -.
DR PaxDb; P01591; -.
DR PRIDE; P01591; -.
DR Ensembl; ENST00000254801; ENSP00000254801; ENSG00000132465.
DR Ensembl; ENST00000510437; ENSP00000426687; ENSG00000132465.
DR GeneID; 3512; -.
DR KEGG; hsa:3512; -.
DR UCSC; uc003hfn.4; human.
DR CTD; 3512; -.
DR GeneCards; GC04M071478; -.
DR HGNC; HGNC:5713; IGJ.
DR HPA; CAB034436; -.
DR MIM; 147790; gene.
DR neXtProt; NX_P01591; -.
DR PharmGKB; PA29733; -.
DR eggNOG; NOG43056; -.
DR HOGENOM; HOG000113012; -.
DR HOVERGEN; HBG006138; -.
DR InParanoid; P01591; -.
DR OrthoDB; EOG7G1V7R; -.
DR PhylomeDB; P01591; -.
DR ChiTaRS; IGJ; human.
DR GeneWiki; IGJ; -.
DR GenomeRNAi; 3512; -.
DR NextBio; 13774; -.
DR PRO; PR:P01591; -.
DR ArrayExpress; P01591; -.
DR Bgee; P01591; -.
DR CleanEx; HS_IGJ; -.
DR Genevestigator; P01591; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR InterPro; IPR024110; Ig_J.
DR PANTHER; PTHR10070; PTHR10070; 1.
DR Pfam; PF15097; Ig_J_chain; 1.
DR ProDom; PD021296; PD021296; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 22
FT CHAIN 23 159 Immunoglobulin J chain.
FT /FTId=PRO_0000084174.
FT MOD_RES 23 23 Pyrrolidone carboxylic acid.
FT CARBOHYD 71 71 N-linked (GlcNAc...) (complex).
FT /FTId=CAR_000167.
FT DISULFID 35 123
FT DISULFID 37 37 Interchain (with heavy chain).
FT DISULFID 91 91 Interchain (with heavy chain).
FT DISULFID 94 114
FT DISULFID 131 156
SQ SEQUENCE 159 AA; 18099 MW; B7835C02CCC0CB05 CRC64;
MKNHLLFWGV LAVFIKAVHV KAQEDERIVL VDNKCKCARI TSRIIRSSED PNEDIVERNI
RIIVPLNNRE NISDPTSPLR TRFVYHLSDL CKKCDPTEVE LDNQIVTATQ SNICDEDSAT
ETCYTYDRNK CYTAVVPLVY GGETKMVETA LTPDACYPD
//
ID IGJ_HUMAN Reviewed; 159 AA.
AC P01591;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-OCT-2009, sequence version 4.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Immunoglobulin J chain;
DE Flags: Precursor;
GN Name=IGJ; Synonyms=IGCJ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 23-159.
RX PubMed=407930; DOI=10.1021/bi00635a002;
RA Mole J.E., Bhown A.S., Bennett J.C.;
RT "Primary structure of human J chain: alignment of peptides from
RT chemical and enzymatic hydrolyses.";
RL Biochemistry 16:3507-3513(1977).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-159.
RX PubMed=2984306; DOI=10.1084/jem.161.4.832;
RA Max E.E., Korsmeyer S.J.;
RT "Human J chain gene. Structure and expression in B lymphoid cells.";
RL J. Exp. Med. 161:832-849(1985).
RN [4]
RP DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1472500; DOI=10.1021/bi00165a014;
RA Frutiger S., Hughes G.J., Paquet N., Luethy R., Jaton J.-C.;
RT "Disulfide bond assignment in human J chain and its covalent pairing
RT with immunoglobulin M.";
RL Biochemistry 31:12643-12647(1992).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
RA Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by
RT glycoprotein capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP GLYCOSYLATION AT ASN-71.
RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core
RT fucosylated glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Serves to link two monomer units of either IgM or IgA.
CC In the case of IgM, the J chain-joined dimer is a nucleating unit
CC for the IgM pentamer, and in the case of IgA it induces larger
CC polymers. It also help to bind these immunoglobulins to secretory
CC component.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK312014; BAG34952.1; -; mRNA.
DR EMBL; M12759; AAA58902.1; -; Genomic_DNA.
DR EMBL; M12378; AAA58902.1; JOINED; Genomic_DNA.
DR PIR; A01859; JIHU.
DR RefSeq; NP_653247.1; NM_144646.3.
DR UniGene; Hs.643431; -.
DR ProteinModelPortal; P01591; -.
DR IntAct; P01591; 2.
DR STRING; 9606.ENSP00000254801; -.
DR PhosphoSite; P01591; -.
DR UniCarbKB; P01591; -.
DR SWISS-2DPAGE; P01591; -.
DR PaxDb; P01591; -.
DR PRIDE; P01591; -.
DR Ensembl; ENST00000254801; ENSP00000254801; ENSG00000132465.
DR Ensembl; ENST00000510437; ENSP00000426687; ENSG00000132465.
DR GeneID; 3512; -.
DR KEGG; hsa:3512; -.
DR UCSC; uc003hfn.4; human.
DR CTD; 3512; -.
DR GeneCards; GC04M071478; -.
DR HGNC; HGNC:5713; IGJ.
DR HPA; CAB034436; -.
DR MIM; 147790; gene.
DR neXtProt; NX_P01591; -.
DR PharmGKB; PA29733; -.
DR eggNOG; NOG43056; -.
DR HOGENOM; HOG000113012; -.
DR HOVERGEN; HBG006138; -.
DR InParanoid; P01591; -.
DR OrthoDB; EOG7G1V7R; -.
DR PhylomeDB; P01591; -.
DR ChiTaRS; IGJ; human.
DR GeneWiki; IGJ; -.
DR GenomeRNAi; 3512; -.
DR NextBio; 13774; -.
DR PRO; PR:P01591; -.
DR ArrayExpress; P01591; -.
DR Bgee; P01591; -.
DR CleanEx; HS_IGJ; -.
DR Genevestigator; P01591; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR InterPro; IPR024110; Ig_J.
DR PANTHER; PTHR10070; PTHR10070; 1.
DR Pfam; PF15097; Ig_J_chain; 1.
DR ProDom; PD021296; PD021296; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 22
FT CHAIN 23 159 Immunoglobulin J chain.
FT /FTId=PRO_0000084174.
FT MOD_RES 23 23 Pyrrolidone carboxylic acid.
FT CARBOHYD 71 71 N-linked (GlcNAc...) (complex).
FT /FTId=CAR_000167.
FT DISULFID 35 123
FT DISULFID 37 37 Interchain (with heavy chain).
FT DISULFID 91 91 Interchain (with heavy chain).
FT DISULFID 94 114
FT DISULFID 131 156
SQ SEQUENCE 159 AA; 18099 MW; B7835C02CCC0CB05 CRC64;
MKNHLLFWGV LAVFIKAVHV KAQEDERIVL VDNKCKCARI TSRIIRSSED PNEDIVERNI
RIIVPLNNRE NISDPTSPLR TRFVYHLSDL CKKCDPTEVE LDNQIVTATQ SNICDEDSAT
ETCYTYDRNK CYTAVVPLVY GGETKMVETA LTPDACYPD
//
MIM
147790
*RECORD*
*FIELD* NO
147790
*FIELD* TI
*147790 IMMUNOGLOBULIN J POLYPEPTIDE, LINKER PROTEIN FOR IMMUNOGLOBULIN ALPHA
AND MU POLYPEPTIDES; IGJ
read more;;IGCJ;;
J CHAIN; JCH
*FIELD* TX
J chain is a 137-amino acid protein that is synthesized in B lymphocytes
and serves 2 known functions: linking immunoglobulin monomers (IgM to
pentamers, IgA to dimers) and binding these immunoglobulins to secretory
component (Koshland, 1985). Using probes from J chain clones, Max et al.
(1986) assigned the J chain gene to 4q21 by Southern analysis of somatic
cell hybrids and by in situ hybridization. This band is the site of
translocations with chromosome 11 in some acute lymphocytic leukemias.
In the mouse, JCH maps to chromosome 5 which carries 4 other genes that
are also on human no. 4 (PGM2, PEPS, ALB, and AFP). Max et al. (1986)
also discovered genetic variation in the number of repeats of a 27-bp
sequence that is tandemly reduplicated 5-prime of the human J chain
gene. They suggested that this polymorphism may be 'useful in genetic
linkage studies in a region of chromosome 4 heretofore relatively barren
of markers definitively localized to a particular subband.' (The J chain
gene is not to be confused with the J region gene of immunoglobulins;
see 146970, 147010, and 147230 for the J region genes of kappa, heavy,
and lambda chains, respectively.)
Lim et al. (2006) showed that the CRLZ1 (UTP3; 611614) and IgJ genes are
adjacent but divergently transcribed in human and mouse. By chromatin
immunoprecipitation and FACS analysis of sorted mouse pre-B cells and
plasma cells, they found that IgJ was expressed in the plasma cell
stage, whereas Crlz1 was expressed in the pre-B cell stage. The
stage-specific expression of IgJ and Crlz1 was regulated by chromatin
accessibility and acetylation. DNase I hypersensitive site 1 on the IgJ
promoter was opened in plasma cells, but hypersensitive sites 9 and 10
on the Crlz1 promoter were opened in pre-B cells. H3 (see 602810) and H4
(see 602822) histones were hyperacetylated in the chromatin of Crlz1 in
pre-B cells, whereas those in the chromatin of IgJ were hyperacetylated
in plasma cells. Lim et al. (2006) concluded that the CRLZ1-IgJ locus
shows stage-specific gene expression regulation, and they proposed that
additional regulatory elements may exist between the genes to coordinate
chromatin accessibility and histone acetylation over the locus.
*FIELD* RF
1. Koshland, M. E.: The coming of age of the immunoglobulin J chain. Annu.
Rev. Immun. 3: 425-453, 1985.
2. Lim, J.-H.; Cho, S.-J.; Park, S.-K.; Kim, J.; Cho, D.; Lee, W.
J.; Kang, C.-J.: Stage-specific expression of two neighboring Crlz1
and IgJ genes during B cell development is regulated by their chromatin
accessibility and histone acetylation. J. Immun. 177: 5420-5429,
2006.
3. Max, E. E.; McBride, O. W.; Morton, C. C.; Robinson, M. A.: Human
J chain gene: chromosomal localization and associated restriction
fragment length polymorphisms. Proc. Nat. Acad. Sci. 83: 5592-5596,
1986.
*FIELD* CN
Paul J. Converse - updated: 11/15/2007
*FIELD* CD
Victor A. McKusick: 10/16/1986
*FIELD* ED
mgross: 02/05/2013
mgross: 11/26/2007
terry: 11/15/2007
carol: 11/16/1998
alopez: 7/16/1997
carol: 3/26/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 3/6/1989
root: 2/13/1989
*RECORD*
*FIELD* NO
147790
*FIELD* TI
*147790 IMMUNOGLOBULIN J POLYPEPTIDE, LINKER PROTEIN FOR IMMUNOGLOBULIN ALPHA
AND MU POLYPEPTIDES; IGJ
read more;;IGCJ;;
J CHAIN; JCH
*FIELD* TX
J chain is a 137-amino acid protein that is synthesized in B lymphocytes
and serves 2 known functions: linking immunoglobulin monomers (IgM to
pentamers, IgA to dimers) and binding these immunoglobulins to secretory
component (Koshland, 1985). Using probes from J chain clones, Max et al.
(1986) assigned the J chain gene to 4q21 by Southern analysis of somatic
cell hybrids and by in situ hybridization. This band is the site of
translocations with chromosome 11 in some acute lymphocytic leukemias.
In the mouse, JCH maps to chromosome 5 which carries 4 other genes that
are also on human no. 4 (PGM2, PEPS, ALB, and AFP). Max et al. (1986)
also discovered genetic variation in the number of repeats of a 27-bp
sequence that is tandemly reduplicated 5-prime of the human J chain
gene. They suggested that this polymorphism may be 'useful in genetic
linkage studies in a region of chromosome 4 heretofore relatively barren
of markers definitively localized to a particular subband.' (The J chain
gene is not to be confused with the J region gene of immunoglobulins;
see 146970, 147010, and 147230 for the J region genes of kappa, heavy,
and lambda chains, respectively.)
Lim et al. (2006) showed that the CRLZ1 (UTP3; 611614) and IgJ genes are
adjacent but divergently transcribed in human and mouse. By chromatin
immunoprecipitation and FACS analysis of sorted mouse pre-B cells and
plasma cells, they found that IgJ was expressed in the plasma cell
stage, whereas Crlz1 was expressed in the pre-B cell stage. The
stage-specific expression of IgJ and Crlz1 was regulated by chromatin
accessibility and acetylation. DNase I hypersensitive site 1 on the IgJ
promoter was opened in plasma cells, but hypersensitive sites 9 and 10
on the Crlz1 promoter were opened in pre-B cells. H3 (see 602810) and H4
(see 602822) histones were hyperacetylated in the chromatin of Crlz1 in
pre-B cells, whereas those in the chromatin of IgJ were hyperacetylated
in plasma cells. Lim et al. (2006) concluded that the CRLZ1-IgJ locus
shows stage-specific gene expression regulation, and they proposed that
additional regulatory elements may exist between the genes to coordinate
chromatin accessibility and histone acetylation over the locus.
*FIELD* RF
1. Koshland, M. E.: The coming of age of the immunoglobulin J chain. Annu.
Rev. Immun. 3: 425-453, 1985.
2. Lim, J.-H.; Cho, S.-J.; Park, S.-K.; Kim, J.; Cho, D.; Lee, W.
J.; Kang, C.-J.: Stage-specific expression of two neighboring Crlz1
and IgJ genes during B cell development is regulated by their chromatin
accessibility and histone acetylation. J. Immun. 177: 5420-5429,
2006.
3. Max, E. E.; McBride, O. W.; Morton, C. C.; Robinson, M. A.: Human
J chain gene: chromosomal localization and associated restriction
fragment length polymorphisms. Proc. Nat. Acad. Sci. 83: 5592-5596,
1986.
*FIELD* CN
Paul J. Converse - updated: 11/15/2007
*FIELD* CD
Victor A. McKusick: 10/16/1986
*FIELD* ED
mgross: 02/05/2013
mgross: 11/26/2007
terry: 11/15/2007
carol: 11/16/1998
alopez: 7/16/1997
carol: 3/26/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 3/6/1989
root: 2/13/1989