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HLA class II histocompatibility antigen gamma chain (HLA-DR antigens-associated invariant chain) (Ia antigen-associated invariant chain) (Ii) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)]

 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.
07-APR-2021, entry version 226.
RecName: Full=HLA class II histocompatibility antigen gamma chain {ECO:0000305};
AltName: Full=HLA-DR antigens-associated invariant chain;
AltName: Full=Ia antigen-associated invariant chain;
Short=Ii;
AltName: CD_antigen=CD74;
Contains:
RecName: Full=Class-II-associated invariant chain peptide {ECO:0000303|PubMed:1448172};
Short=CLIP {ECO:0000303|PubMed:1448172};
Name=CD74 {ECO:0000312|HGNC:HGNC:1697}; 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 P35).
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 P35).
PubMed=6586420; DOI=10.1002/j.1460-2075.1984.tb01898.x;
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 P35).
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 P45
AND P35).
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 P35).
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 P45 AND P35).
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 P35 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, AND FUNCTION.
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]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=3104027; DOI=10.1002/j.1460-2075.1986.tb04673.x;
Strubin M., Berte C., Mach B.;
"Alternative splicing and alternative initiation of translation explain the
four forms of the Ia antigen-associated invariant chain.";
EMBO J. 5:3483-3488(1986).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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 11:1-17(2012).
[19]
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).
[20]
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).
[21]
FUNCTION (ISOFORM P41), ALTERNATIVE SPLICING, AND MUTAGENESIS OF
225-PRO-GLY-226.
PubMed=32855215; DOI=10.1126/science.abb3753;
Bruchez A., Sha K., Johnson J., Chen L., Stefani C., McConnell H.,
Gaucherand L., Prins R., Matreyek K.A., Hume A.J., Muehlberger E.,
Schmidt E.V., Olinger G.G., Stuart L.M., Lacy-Hulbert A.;
"MHC class II transactivator CIITA induces cell resistance to Ebola virus
and SARS-like coronaviruses.";
Science 370:241-247(2020).
[22]
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).
[23]
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 210-274, GLYCOSYLATION AT ASN-256,
DISULFIDE BONDS, AND INTERACTION WITH CTSL.
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.
-!- FUNCTION: [Class-II-associated invariant chain peptide]: Binds to the
peptide-binding site of MHC class II alpha/beta heterodimers forming an
alpha-beta-CLIP complex, thereby preventing the loading of antigenic
peptides to the MHC class II complex until its release by HLA-DM in the
endosome. {ECO:0000269|PubMed:1448172}.
-!- FUNCTION: [Isoform p41]: Stabilizes the conformation of mature CTSL by
binding to its active site and serving as a chaperone to help maintain
a pool of mature enzyme in endocytic compartments and extracellular
space of antigen-presenting cells (APCs). Has antiviral activity by
stymieing the endosomal entry of Ebola virus and coronaviruses,
including SARS-CoV-2 (PubMed:32855215). Disrupts cathepsin-mediated
Ebola virus glycoprotein processing, which prevents viral fusion and
entry. This antiviral activity is specific to p41 isoform
(PubMed:32855215). {ECO:0000250|UniProtKB:P04441,
ECO:0000269|PubMed:32855215}.
-!- 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. Interacts with CD44; this complex is essential for the MIF-
induced signaling cascade that results in B cell survival.
{ECO:0000250|UniProtKB:P04441, ECO:0000269|PubMed:12782713,
ECO:0000269|PubMed:7477400}.
-!- SUBUNIT: [Isoform p41]: Interacts with the mature form of CTSL; the
complex survive in neutral pH environment.
{ECO:0000269|PubMed:10022822}.
-!- INTERACTION:
P04233; P16070: CD44; NbExp=9; IntAct=EBI-2622890, EBI-490245;
P04233; P25025: CXCR2; NbExp=2; IntAct=EBI-2622890, EBI-2835281;
P04233; P61073: CXCR4; NbExp=4; IntAct=EBI-2622890, EBI-489411;
P04233; P60228: EIF3E; NbExp=2; IntAct=EBI-2622890, EBI-347740;
P04233; P0DMV8: HSPA1A; NbExp=4; IntAct=EBI-2622890, EBI-11052499;
P04233; Q14974: KPNB1; NbExp=2; IntAct=EBI-2622890, EBI-286758;
P04233; P0A6Y8: dnaK; Xeno; NbExp=8; IntAct=EBI-2622890, EBI-542092;
P04233-2; O15155: BET1; NbExp=3; IntAct=EBI-12222807, EBI-749204;
P04233-2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-12222807, EBI-12256978;
P04233-2; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-12222807, EBI-11989440;
P04233-2; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-12222807, EBI-2807956;
P04233-2; P56851: EDDM3B; NbExp=3; IntAct=EBI-12222807, EBI-10215665;
P04233-2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12222807, EBI-711490;
P04233-2; P37268: FDFT1; NbExp=3; IntAct=EBI-12222807, EBI-714550;
P04233-2; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-12222807, EBI-713304;
P04233-2; Q9UBY5: LPAR3; NbExp=4; IntAct=EBI-12222807, EBI-12033434;
P04233-2; Q8N912: NRAC; NbExp=4; IntAct=EBI-12222807, EBI-12051377;
P04233-2; P0DJD7: PGA4; NbExp=3; IntAct=EBI-12222807, EBI-12957629;
P04233-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-12222807, EBI-12188331;
P04233-2; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-12222807, EBI-10485931;
P04233-2; Q8WZA1: POMGNT1; NbExp=3; IntAct=EBI-12222807, EBI-3912424;
P04233-2; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-12222807, EBI-14199621;
P04233-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-12222807, EBI-10244780;
P04233-2; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-12222807, EBI-8652744;
P04233-2; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-12222807, EBI-10329948;
P04233-2; P78383: SLC35B1; NbExp=3; IntAct=EBI-12222807, EBI-12147661;
P04233-2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12222807, EBI-12188413;
P04233-2; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-12222807, EBI-11523345;
P04233-2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-12222807, EBI-10171534;
P04233-2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-12222807, EBI-12887458;
P04233-2; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-12222807, EBI-11956809;
P04233-2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12222807, EBI-2852148;
P04233-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12222807, EBI-12111910;
P04233-2; O00526: UPK2; NbExp=4; IntAct=EBI-12222807, EBI-10179682;
-!- 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.
-!- SUBCELLULAR LOCATION: [Isoform p41]: Late endosome
{ECO:0000250|UniProtKB:P04441}. Lysosome
{ECO:0000250|UniProtKB:P04441}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=5;
Name=p45 {ECO:0000303|PubMed:3104027}; Synonyms=Long;
IsoId=P04233-1; Sequence=Displayed;
Name=p35 {ECO:0000303|PubMed:3104027}; Synonyms=Short;
IsoId=P04233-2; Sequence=VSP_005331;
Name=3;
IsoId=P04233-3; Sequence=VSP_037869, VSP_037870;
Name=p41 {ECO:0000303|PubMed:3104027};
IsoId=P04233-4; Sequence=VSP_060904;
Name=p33 {ECO:0000303|PubMed:3104027};
IsoId=P04233-5; Sequence=VSP_060904, VSP_005331;
-!- TISSUE SPECIFICITY: [Isoform p41]: In B cells, represents 10% of total
CD74 expression. {ECO:0000269|PubMed:3104027}.
-!- TISSUE SPECIFICITY: [Isoform p33]: In B cells, represents 70% of total
CD74 expression. {ECO:0000269|PubMed:3104027}.
-!- DOMAIN: Antiviral activity requires delivery of the thyroglobulin
domain to the endosomal membrane. {ECO:0000269|PubMed:32855215}.
-!- 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; Note=Truncated N-terminus.; 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]
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; -.
BMRB; P04233; -.
SMR; P04233; -.
BioGRID; 107410; 139.
ELM; P04233; -.
IntAct; P04233; 200.
MINT; P04233; -.
STRING; 9606.ENSP00000009530; -.
BindingDB; P04233; -.
ChEMBL; CHEMBL4692; -.
GuidetoPHARMACOLOGY; 2840; -.
MEROPS; I31.002; -.
TCDB; 9.A.75.1.1; the mhc ii receptor (mhc2r) family.
GlyConnect; 659; 11 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site).
GlyGen; P04233; 9 sites, 1 O-linked glycan (4 sites).
iPTMnet; P04233; -.
PhosphoSitePlus; P04233; -.
SwissPalm; P04233; -.
BioMuta; CD74; -.
DMDM; 20178292; -.
jPOST; P04233; -.
MassIVE; P04233; -.
MaxQB; P04233; -.
PaxDb; P04233; -.
PeptideAtlas; P04233; -.
PRIDE; P04233; -.
ProteomicsDB; 51689; -. [P04233-1]
ProteomicsDB; 51690; -. [P04233-2]
ProteomicsDB; 51691; -. [P04233-3]
ABCD; P04233; 19 sequenced antibodies.
Antibodypedia; 2245; 2329 antibodies.
CPTC; P04233; 1 antibody.
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; -.
GeneCards; CD74; -.
HGNC; HGNC:1697; CD74.
HPA; ENSG00000019582; Tissue enhanced (blood).
MIM; 142790; gene.
neXtProt; NX_P04233; -.
OpenTargets; ENSG00000019582; -.
PharmGKB; PA26236; -.
VEuPathDB; HostDB:ENSG00000019582.14; -.
eggNOG; KOG1214; Eukaryota.
GeneTree; ENSGT00390000008961; -.
InParanoid; P04233; -.
OMA; GTFRPQC; -.
OrthoDB; 1190626at2759; -.
PhylomeDB; P04233; -.
TreeFam; TF317779; -.
PathwayCommons; P04233; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
SIGNOR; P04233; -.
BioGRID-ORCS; 972; 3 hits in 989 CRISPR screens.
ChiTaRS; CD74; human.
EvolutionaryTrace; P04233; -.
GeneWiki; CD74; -.
GenomeRNAi; 972; -.
Pharos; P04233; Tchem.
PRO; PR:P04233; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P04233; protein.
Bgee; ENSG00000019582; Expressed in spleen and 246 other tissues.
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:0005737; C:cytoplasm; IDA:ARUK-UCL.
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; HDA: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:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; HDA: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:0005634; C:nucleus; IDA:ARUK-UCL.
GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
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:BHF-UCL.
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 folding chaperone; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0019882; P:antigen processing and presentation; IBA:GO_Central.
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 population proliferation; IEA:Ensembl.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; 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:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
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:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
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:0032722; P:positive regulation of chemokine production; IMP:ARUK-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:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:ARUK-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:ARUK-UCL.
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:2000448; P:positive regulation of macrophage migration inhibitory factor signaling pathway; IMP:ARUK-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:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:ARUK-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; IBA:GO_Central.
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:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0070206; P:protein trimerization; IEA:InterPro.
GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
GO; GO:0043030; P:regulation of macrophage activation; NAS:UniProtKB.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
GO; GO:0045058; P:T cell selection; NAS:UniProtKB.
CDD; cd00191; TY; 1.
Gene3D; 1.10.870.10; -; 1.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR043530; CD74_antigen.
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.
PIRSF; PIRSF001992; CD74_antigen; 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 initiation;
Alternative splicing; Cell membrane; Chaperone; 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
/note="HLA class II histocompatibility antigen gamma chain"
/id="PRO_0000067954"
PEPTIDE 97..120
/note="Class-II-associated invariant chain peptide"
/evidence="ECO:0000269|PubMed:1448172"
/id="PRO_0000448886"
TOPO_DOM 1..46
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 47..72
/note="Helical; Signal-anchor for type II membrane protein"
/evidence="ECO:0000255"
TOPO_DOM 73..296
/note="Extracellular"
/evidence="ECO:0000255"
DOMAIN 210..271
/note="Thyroglobulin type-1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
REGION 225..226
/note="Required for interaction with CTSL"
/evidence="ECO:0000305|PubMed:10022822,
ECO:0000305|PubMed:32855215"
SITE 208..209
/note="Breakpoint for translocation to form a CD74-ROS1
fusion protein"
MOD_RES 25
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P04441"
CARBOHYD 130
/note="N-linked (GlcNAc...) asparagine"
CARBOHYD 136
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 203
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360"
CARBOHYD 256
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:10022822"
CARBOHYD 281
/note="O-linked (GalNAc...) serine"
/evidence="ECO:0000269|PubMed:23234360"
DISULFID 213..232
/evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:10022822"
DISULFID 243..250
/evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:10022822"
DISULFID 252..271
/evidence="ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:10022822"
VAR_SEQ 1..16
/note="Missing (in isoform p41 and isoform p33)"
/evidence="ECO:0000303|PubMed:3104027"
/id="VSP_060904"
VAR_SEQ 148..160
/note="NADPLKVYPPLKG -> SHWNWRTRLLGWV (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_037869"
VAR_SEQ 161..296
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_037870"
VAR_SEQ 209..272
/note="Missing (in isoform p35 and isoform p33)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:6324166,
ECO:0000303|PubMed:6586420, ECO:0000303|Ref.5"
/id="VSP_005331"
MUTAGEN 225..226
/note="PG->RR,DD: Decreases inhibition of Ebola virus
infection."
/evidence="ECO:0000269|PubMed:32855215"
MUTAGEN 225..226
/note="PG->TT: No effect on inhibition of Ebola virus
infection."
/evidence="ECO:0000269|PubMed:32855215"
CONFLICT 167
/note="R -> T (in Ref. 3; CAA27047)"
/evidence="ECO:0000305"
HELIX 139..149
/evidence="ECO:0007744|PDB:1IIE"
HELIX 162..172
/evidence="ECO:0007744|PDB:1IIE"
HELIX 175..194
/evidence="ECO:0007744|PDB:1IIE"
HELIX 212..217
/evidence="ECO:0007744|PDB:1ICF"
STRAND 236..238
/evidence="ECO:0007744|PDB:1L3H"
STRAND 240..244
/evidence="ECO:0007744|PDB:1ICF"
TURN 245..248
/evidence="ECO:0007744|PDB:1ICF"
STRAND 249..253
/evidence="ECO:0007744|PDB:1ICF"
STRAND 265..267
/evidence="ECO:0007744|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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Related Genes :
[CD74 DHLAG] HLA class II histocompatibility antigen gamma chain (HLA-DR antigens-associated invariant chain) (Ia antigen-associated invariant chain) (Ii) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)]
[Cd74 Ii] H-2 class II histocompatibility antigen gamma chain (Ia antigen-associated invariant chain) (Ii) (Ii chain) (MHC class II-associated invariant chain) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)]
[Cd74] H-2 class II histocompatibility antigen gamma chain (Ia antigen-associated invariant chain) (Ii) (MHC class II-associated invariant chain) (CD antigen CD74) [Cleaved into: Class-II-associated invariant chain peptide (CLIP)]
[HLA-DRB5] HLA class II histocompatibility antigen, DR beta 5 chain (DR beta-5) (DR2-beta-2) (Dw2) (MHC class II antigen DRB5)
[HLA-DRA HLA-DRA1] HLA class II histocompatibility antigen, DR alpha chain (MHC class II antigen DRA)
[HLA-DRB3] HLA class II histocompatibility antigen, DR beta 3 chain (MHC class II antigen DRB3)
[HLA-DPB1 HLA-DP1B] HLA class II histocompatibility antigen, DP beta 1 chain (HLA class II histocompatibility antigen, DP(W4) beta chain) (MHC class II antigen DPB1)
[HLA-DRB4] HLA class II histocompatibility antigen, DR beta 4 chain (MHC class II antigen DRB4)
[HLA-DQA2 HLA-DXA] HLA class II histocompatibility antigen, DQ alpha 2 chain (DX alpha chain) (HLA class II histocompatibility antigen, DQ(6) alpha chain) (HLA-DQA1) (MHC class II DQA2)
[HLA-DQB2 HLA-DXB] HLA class II histocompatibility antigen, DQ beta 2 chain (HLA class II histocompatibility antigen, DX beta chain) (MHC class II antigen DQB2)
[HLA-DQB1 HLA-DQB] HLA class II histocompatibility antigen, DQ beta 1 chain (MHC class II antigen DQB1)
[HLA-DPA1 HLA-DP1A HLASB] HLA class II histocompatibility antigen, DP alpha 1 chain (DP(W3)) (DP(W4)) (HLA-SB alpha chain) (MHC class II DP3-alpha) (MHC class II DPA1)
[HLA-DQA1] HLA class II histocompatibility antigen, DQ alpha 1 chain (DC-1 alpha chain) (DC-alpha) (HLA-DCA) (MHC class II DQA1)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1 beta chain (Human leukocyte antigen DRB1) (HLA-DRB1)
[HLA-E HLA-6.2 HLAE] HLA class I histocompatibility antigen, alpha chain E (MHC class I antigen E) [Cleaved into: Soluble HLA class I histocompatibility antigen, alpha chain E (sHLA-E)]
[HLA-B HLAB] HLA class I histocompatibility antigen, B alpha chain (Human leukocyte antigen B) (HLA-B)
[HLA-A HLAA] HLA class I histocompatibility antigen, A alpha chain (Human leukocyte antigen A) (HLA-A)
[HLA-F HLA-5.4 HLAF] HLA class I histocompatibility antigen, alpha chain F (CDA12) (HLA F antigen) (Leukocyte antigen F) (MHC class I antigen F)
[HLA-C HLAC] HLA class I histocompatibility antigen, C alpha chain (HLA-C) (HLA-Cw) (Human leukocyte antigen C)
[MR1] Major histocompatibility complex class I-related gene protein (MHC class I-related gene protein) (Class I histocompatibility antigen-like protein)
[Mr1 Mr1a] Major histocompatibility complex class I-related gene protein (MHC class I-related gene protein) (Class I histocompatibility antigen-like protein)
[H2-D1] H-2 class I histocompatibility antigen, D-B alpha chain (H-2D(B))
[MR1] Major histocompatibility complex class I-related gene protein (MHC class I-related gene protein) (Class I histocompatibility antigen-like protein)
[H2-L] H-2 class I histocompatibility antigen, L-D alpha chain
[Cd44 Ly-24] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[CD1A] T-cell surface glycoprotein CD1a (T-cell surface antigen T6/Leu-6) (hTa1 thymocyte antigen) (CD antigen CD1a)
[CD8A MAL] T-cell surface glycoprotein CD8 alpha chain (T-lymphocyte differentiation antigen T8/Leu-2) (CD antigen CD8a)
[Cd1d1 Cd1.1] Antigen-presenting glycoprotein CD1d1 (CD antigen CD1d.1)
[MYO1G HA2] Unconventional myosin-Ig [Cleaved into: Minor histocompatibility antigen HA-2 (mHag HA-2)]
[TAP2 ABCB3 PSF2 RING11 Y1] Antigen peptide transporter 2 (APT2) (EC 7.4.2.-) (ATP-binding cassette sub-family B member 3) (Peptide supply factor 2) (Peptide transporter PSF2) (PSF-2) (Peptide transporter TAP2) (Peptide transporter involved in antigen processing 2) (Really interesting new gene 11 protein) (RING11)

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