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HLA class II histocompatibility antigen gamma chain (HLA-DR antigens-associated invariant chain) (Ia antigen-associated invariant chain) (Ii) (p33) (CD antigen CD74)

 HG2A_HUMAN              Reviewed;         296 AA.
P04233; A8K7R1; B4DNE8; D3DQG3; D3DQG4; Q14597; Q29832; Q5U0J8;
Q8SNA0; Q8WLP6;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 3.
25-OCT-2017, entry version 200.
RecName: Full=HLA class II histocompatibility antigen gamma chain;
AltName: Full=HLA-DR antigens-associated invariant chain;
AltName: Full=Ia antigen-associated invariant chain;
Short=Ii;
AltName: Full=p33;
AltName: CD_antigen=CD74;
Name=CD74; Synonyms=DHLAG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=6324166; DOI=10.1073/pnas.80.24.7395;
Claesson L., Larhammar D., Rask L., Peterson P.A.;
"cDNA clone for the human invariant gamma chain of class II
histocompatibility antigens and its implications for the protein
structure.";
Proc. Natl. Acad. Sci. U.S.A. 80:7395-7399(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=6586420;
Strubin M., Mach B., Long E.O.;
"The complete sequence of the mRNA for the HLA-DR-associated invariant
chain reveals a polypeptide with an unusual transmembrane polarity.";
EMBO J. 3:869-872(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
2).
PubMed=3001652; DOI=10.1093/nar/13.24.8827;
Kudo J., Chao L.-Y., Narni F., Saunders G.F.;
"Structure of the human gene encoding the invariant gamma-chain of
class II histocompatibility antigens.";
Nucleic Acids Res. 13:8827-8841(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
TISSUE=Liver;
PubMed=3459184; DOI=10.1073/pnas.83.12.4484;
O'Sullivan D.M., Larhammar D., Wilson M.C., Peterson P.A.,
Quaranta V.;
"Structure of the human Ia-associated invariant (gamma)-chain gene:
identification of 5' sequences shared with major histocompatibility
complex class II genes.";
Proc. Natl. Acad. Sci. U.S.A. 83:4484-4488(1986).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Heart, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=B-cell, and Tonsil;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 22-35; 81-94; 171-179 AND 273-288, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 97-120.
PubMed=1448172; DOI=10.1038/360474a0;
Riberdy J.M., Newcomb J.R., Surman M.J., Barbosa J.A., Cresswell P.;
"HLA-DR molecules from an antigen-processing mutant cell line are
associated with invariant chain peptides.";
Nature 360:474-477(1992).
[12]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1.
PubMed=12661006; DOI=10.1002/gcc.10207;
Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H.,
Housman D.;
"Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma
with an interstitial del(6)(q21q21).";
Genes Chromosomes Cancer 37:58-71(2003).
[13]
INTERACTION WITH MIF.
PubMed=12782713; DOI=10.1084/jem.20030286;
Leng L., Metz C.N., Fang Y., Xu J., Donnelly S., Baugh J.,
Delohery T., Chen Y., Mitchell R.A., Bucala R.;
"MIF signal transduction initiated by binding to CD74.";
J. Exp. Med. 197:1467-1476(2003).
[14]
REVIEW.
PubMed=19092054; DOI=10.1242/jcs.035089;
Berger A.C., Roche P.A.;
"MHC class II transport at a glance.";
J. Cell Sci. 122:1-4(2009).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
GLYCOSYLATION AT THR-203, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[18]
GLYCOSYLATION AT THR-203 AND SER-281, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 103-117 (CLIP) IN COMPLEX
WITH HLA-DRA/HLA-DRB1 HETERODIMER.
PubMed=7477400; DOI=10.1038/378457a0;
Ghosh P., Amaya M., Mellins E., Wiley D.C.;
"The structure of an intermediate in class II MHC maturation: CLIP
bound to HLA-DR3.";
Nature 378:457-462(1995).
[21]
STRUCTURE BY NMR OF 134-208.
PubMed=9843486; DOI=10.1093/emboj/17.23.6812;
Jasanoff A., Wagner G., Wiley D.C.;
"Structure of a trimeric domain of the MHC class II-associated
chaperonin and targeting protein Ii.";
EMBO J. 17:6812-6818(1998).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 210-274, GLYCOSYLATION AT
ASN-256, AND DISULFIDE BONDS.
PubMed=10022822; DOI=10.1093/emboj/18.4.793;
Guncar G., Pungercic G., Klemencic I., Turk V., Turk D.;
"Crystal structure of MHC class II-associated p41 Ii fragment bound to
cathepsin L reveals the structural basis for differentiation between
cathepsins L and S.";
EMBO J. 18:793-803(1999).
-!- FUNCTION: Plays a critical role in MHC class II antigen processing
by stabilizing peptide-free class II alpha/beta heterodimers in a
complex soon after their synthesis and directing transport of the
complex from the endoplasmic reticulum to the endosomal/lysosomal
system where the antigen processing and binding of antigenic
peptides to MHC class II takes place. Serves as cell surface
receptor for the cytokine MIF.
-!- SUBUNIT: Homotrimer. In the endoplasmic reticulum (ER) it forms a
heterononameric MHC II-Ii complex: 3 MHC class II molecules
(heterodimers of an alpha and a beta subunit) bind to the CD74
homotrimer (also known as invariant chain or HLA class II
histocompatibility antigen gamma chain). In the
endosomal/lysosomal system, the CD74 component undergoes
sequential degradation by various proteases, including CTSS and
CTSL, leaving a small fragment termed CLIP (class-II-associated
invariant chain peptide) attached to the MHC class II molecule
(alpha-beta-CLIP complex). This processed complex interacts with
HLA_DM and HLA_DO heterodimers in order to release CLIP and
facilitate the binding of antigenic peptides to the MHC class II
molecules. {ECO:0000269|PubMed:12782713,
ECO:0000269|PubMed:7477400}.
-!- INTERACTION:
P61073:CXCR4; NbExp=4; IntAct=EBI-2622890, EBI-489411;
P0A6Y8:dnaK (xeno); NbExp=8; IntAct=EBI-2622890, EBI-542092;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type II membrane protein {ECO:0000305}. Endoplasmic reticulum
membrane. Golgi apparatus, trans-Golgi network. Endosome.
Lysosome. Note=Transits through a number of intracellular
compartments in the endocytic pathway. It can either undergo
proteolysis or reach the cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=P04233-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P04233-2; Sequence=VSP_005331;
Name=3;
IsoId=P04233-3; Sequence=VSP_037869, VSP_037870;
-!- PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly
core 8 glycans. {ECO:0000269|PubMed:10022822,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360}.
-!- DISEASE: Note=A chromosomal aberration involving CD74 is found in
a non-small cell lung tumor. Results in the formation of a CD74-
ROS1 chimeric protein. {ECO:0000269|PubMed:12661006}.
-!- SEQUENCE CAUTION:
Sequence=AAA36304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; K01144; AAA36304.1; ALT_INIT; mRNA.
EMBL; X00497; CAA25192.1; -; mRNA.
EMBL; X00497; CAA25193.1; -; mRNA.
EMBL; X03339; CAA27046.1; -; Genomic_DNA.
EMBL; X03340; CAA27047.1; -; Genomic_DNA.
EMBL; M13560; AAA36033.1; -; Genomic_DNA.
EMBL; M13555; AAA36033.1; JOINED; Genomic_DNA.
EMBL; M13556; AAA36033.1; JOINED; Genomic_DNA.
EMBL; M13558; AAA36033.1; JOINED; Genomic_DNA.
EMBL; M13559; AAA36033.1; JOINED; Genomic_DNA.
EMBL; BT019505; AAV38312.1; -; mRNA.
EMBL; AK292076; BAF84765.1; -; mRNA.
EMBL; AK297889; BAG60210.1; -; mRNA.
EMBL; AC011372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61727.1; -; Genomic_DNA.
EMBL; CH471062; EAW61728.1; -; Genomic_DNA.
EMBL; CH471062; EAW61729.1; -; Genomic_DNA.
EMBL; CH471062; EAW61730.1; -; Genomic_DNA.
EMBL; CH471062; EAW61731.1; -; Genomic_DNA.
EMBL; BC018726; AAH18726.1; -; mRNA.
EMBL; BC024272; AAH24272.1; -; mRNA.
CCDS; CCDS34276.1; -. [P04233-3]
CCDS; CCDS47308.1; -. [P04233-2]
CCDS; CCDS47309.1; -. [P04233-1]
PIR; A93981; HLHUG.
RefSeq; NP_001020329.1; NM_001025158.2. [P04233-3]
RefSeq; NP_001020330.1; NM_001025159.2. [P04233-1]
RefSeq; NP_004346.1; NM_004355.3. [P04233-2]
UniGene; Hs.436568; -.
PDB; 1A6A; X-ray; 2.75 A; C=103-117.
PDB; 1ICF; X-ray; 2.00 A; I/J=210-274.
PDB; 1IIE; NMR; -; A/B/C=134-208.
PDB; 1L3H; NMR; -; A=210-274.
PDB; 1MUJ; X-ray; 2.15 A; C=97-121.
PDB; 3PDO; X-ray; 1.95 A; C=102-120.
PDB; 3PGC; X-ray; 2.66 A; C/F=106-120.
PDB; 3PGD; X-ray; 2.72 A; C/F=106-120.
PDB; 3QXA; X-ray; 2.71 A; C/F=103-117.
PDB; 3QXD; X-ray; 2.30 A; C/F=103-117.
PDB; 4AEN; X-ray; 2.20 A; C=106-120.
PDB; 4AH2; X-ray; 2.36 A; B=106-120.
PDB; 4X5W; X-ray; 1.34 A; C=102-120.
PDB; 5KSU; X-ray; 2.73 A; C/F=103-117.
PDB; 5KSV; X-ray; 2.19 A; C=109-123.
PDBsum; 1A6A; -.
PDBsum; 1ICF; -.
PDBsum; 1IIE; -.
PDBsum; 1L3H; -.
PDBsum; 1MUJ; -.
PDBsum; 3PDO; -.
PDBsum; 3PGC; -.
PDBsum; 3PGD; -.
PDBsum; 3QXA; -.
PDBsum; 3QXD; -.
PDBsum; 4AEN; -.
PDBsum; 4AH2; -.
PDBsum; 4X5W; -.
PDBsum; 5KSU; -.
PDBsum; 5KSV; -.
ProteinModelPortal; P04233; -.
SMR; P04233; -.
BioGrid; 107410; 12.
ELM; P04233; -.
IntAct; P04233; 89.
MINT; MINT-1488574; -.
STRING; 9606.ENSP00000009530; -.
BindingDB; P04233; -.
ChEMBL; CHEMBL4692; -.
GuidetoPHARMACOLOGY; 2840; -.
MEROPS; I31.002; -.
iPTMnet; P04233; -.
PhosphoSitePlus; P04233; -.
SwissPalm; P04233; -.
UniCarbKB; P04233; -.
BioMuta; CD74; -.
DMDM; 20178292; -.
EPD; P04233; -.
MaxQB; P04233; -.
PaxDb; P04233; -.
PeptideAtlas; P04233; -.
PRIDE; P04233; -.
DNASU; 972; -.
Ensembl; ENST00000009530; ENSP00000009530; ENSG00000019582. [P04233-1]
Ensembl; ENST00000353334; ENSP00000230685; ENSG00000019582. [P04233-2]
Ensembl; ENST00000377795; ENSP00000367026; ENSG00000019582. [P04233-3]
GeneID; 972; -.
KEGG; hsa:972; -.
UCSC; uc003lsc.4; human. [P04233-1]
CTD; 972; -.
DisGeNET; 972; -.
EuPathDB; HostDB:ENSG00000019582.14; -.
GeneCards; CD74; -.
HGNC; HGNC:1697; CD74.
HPA; CAB002506; -.
HPA; HPA010592; -.
MIM; 142790; gene.
neXtProt; NX_P04233; -.
OpenTargets; ENSG00000019582; -.
PharmGKB; PA26236; -.
eggNOG; ENOG410IMYW; Eukaryota.
eggNOG; ENOG410Z4PR; LUCA.
GeneTree; ENSGT00390000008961; -.
HOVERGEN; HBG004444; -.
InParanoid; P04233; -.
KO; K06505; -.
PhylomeDB; P04233; -.
TreeFam; TF317779; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
SIGNOR; P04233; -.
ChiTaRS; CD74; human.
EvolutionaryTrace; P04233; -.
GeneWiki; CD74; -.
GenomeRNAi; 972; -.
PMAP-CutDB; P04233; -.
PRO; PR:P04233; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000019582; -.
CleanEx; HS_CD74; -.
ExpressionAtlas; P04233; baseline and differential.
Genevisible; P04233; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
GO; GO:0005622; C:intracellular; TAS:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042613; C:MHC class II protein complex; IEA:Ensembl.
GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
GO; GO:0035693; C:NOS2-CD74 complex; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0005773; C:vacuole; IDA:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; IPI:BHF-UCL.
GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA.
GO; GO:0019955; F:cytokine binding; IPI:UniProtKB.
GO; GO:0004896; F:cytokine receptor activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; TAS:UniProtKB.
GO; GO:0035718; F:macrophage migration inhibitory factor binding; IPI:BHF-UCL.
GO; GO:0042289; F:MHC class II protein binding; ISS:BHF-UCL.
GO; GO:0042658; F:MHC class II protein binding, via antigen binding groove; IDA:UniProtKB.
GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0044183; F:protein binding involved in protein folding; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; NAS:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:Ensembl.
GO; GO:0006952; P:defense response; IEA:Ensembl.
GO; GO:0016064; P:immunoglobulin mediated immune response; ISS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0035691; P:macrophage migration inhibitory factor signaling pathway; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IEA:Ensembl.
GO; GO:0002792; P:negative regulation of peptide secretion; IDA:BHF-UCL.
GO; GO:0045581; P:negative regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:BHF-UCL.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISS:BHF-UCL.
GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA.
GO; GO:0033674; P:positive regulation of kinase activity; IDA:CAFA.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:CAFA.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA.
GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:0002830; P:positive regulation of type 2 immune response; IEA:Ensembl.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:CAFA.
GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA.
GO; GO:0070206; P:protein trimerization; IEA:InterPro.
GO; GO:0043030; P:regulation of macrophage activation; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0045058; P:T cell selection; NAS:UniProtKB.
Gene3D; 1.10.870.10; -; 1.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR015386; MHC_II-assoc_invar/CLIP_MHC-bd.
InterPro; IPR022339; MHC_II-assoc_invar_chain.
InterPro; IPR011988; MHC_II-assoc_invariant_trimer.
InterPro; IPR036613; MHCII_invariant_trimer_sf.
InterPro; IPR000716; Thyroglobulin_1.
InterPro; IPR036857; Thyroglobulin_1_sf.
Pfam; PF09307; MHC2-interact; 1.
Pfam; PF08831; MHCassoc_trimer; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
PRINTS; PR01990; CD74ANTIGEN.
SMART; SM00211; TY; 1.
SUPFAM; SSF48305; SSF48305; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
Chaperone; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
Golgi apparatus; Immunity; Lysosome; Membrane; Phosphoprotein;
Proteoglycan; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 296 HLA class II histocompatibility antigen
gamma chain.
/FTId=PRO_0000067954.
TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.
TRANSMEM 47 72 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 73 296 Extracellular. {ECO:0000255}.
DOMAIN 210 271 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
REGION 103 117 CLIP.
SITE 208 209 Breakpoint for translocation to form a
CD74-ROS1 fusion protein.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:P04441}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 203 203 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10022822}.
CARBOHYD 281 281 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:23234360}.
DISULFID 213 232 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:10022822}.
DISULFID 243 250 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:10022822}.
DISULFID 252 271 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:10022822}.
VAR_SEQ 148 160 NADPLKVYPPLKG -> SHWNWRTRLLGWV (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037869.
VAR_SEQ 161 296 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037870.
VAR_SEQ 209 272 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:6324166,
ECO:0000303|PubMed:6586420,
ECO:0000303|Ref.5}.
/FTId=VSP_005331.
CONFLICT 167 167 R -> T (in Ref. 3; CAA27047).
{ECO:0000305}.
HELIX 139 149 {ECO:0000244|PDB:1IIE}.
HELIX 162 172 {ECO:0000244|PDB:1IIE}.
HELIX 175 194 {ECO:0000244|PDB:1IIE}.
HELIX 212 217 {ECO:0000244|PDB:1ICF}.
STRAND 236 238 {ECO:0000244|PDB:1L3H}.
STRAND 240 244 {ECO:0000244|PDB:1ICF}.
TURN 245 248 {ECO:0000244|PDB:1ICF}.
STRAND 249 253 {ECO:0000244|PDB:1ICF}.
STRAND 265 267 {ECO:0000244|PDB:1ICF}.
SEQUENCE 296 AA; 33516 MW; 27A13F252D5FB91D CRC64;
MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY TGFSILVTLL
LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP PKPVSKMRMA TPLLMQALPM
GALPQGPMQN ATKYGNMTED HVMHLLQNAD PLKVYPPLKG SFPENLRHLK NTMETIDWKV
FESWMHHWLL FEMSRHSLEQ KPTDAPPKVL TKCQEEVSHI PAVHPGSFRP KCDENGNYLP
LQCYGSIGYC WCVFPNGTEV PNTRSRGHHN CSESLELEDP SSGLGVTKQD LGPVPM


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