P04233 (HG2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
HLA class II histocompatibility antigen gamma chain

Alternative name(s):
HLA-DR antigens-associated invariant chain
Ia antigen-associated invariant chain
Short name=Ii
p33
CD_antigen=CD74

Gene names

Name:	CD74
Synonyms:	DHLAG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	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. Ref.13
Subcellular location	Cell membrane; Single-pass type II membrane protein Potential. 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.
Post-translational modification	N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. Ref.17 Ref.18 Ref.21
Involvement in disease	A chromosomal aberration involving CD74 is found in a non-small cell lung tumor. Results in the formation of a CD74-ROS1 chimeric protein. Ref.12
Sequence similarities	Contains 1 thyroglobulin type-1 domain.
Sequence caution	The sequence AAA36304.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Chaperone
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell selection Non-traceable author statement PubMed 10981873. Source: UniProtKB activation of MAPK activity Inferred from electronic annotation. Source: Compara antigen processing and presentation of endogenous antigen Non-traceable author statement PubMed 10981873. Source: UniProtKB antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome cell proliferation Inferred from direct assay Ref.13. Source: UniProtKB chaperone mediated protein folding requiring cofactor Inferred from electronic annotation. Source: Compara defense response Inferred from electronic annotation. Source: Compara immunoglobulin mediated immune response Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein transport Inferred from sequence or structural similarity. Source: UniProtKB macrophage migration inhibitory factor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of DNA damage response, signal transduction by p53 class mediator Inferred from direct assay PubMed 17045821. Source: BHF-UCL negative regulation of T cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay Ref.13. Source: UniProtKB negative regulation of mature B cell apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of peptide secretion Inferred from direct assay PubMed 19849849. Source: BHF-UCL negative thymic T cell selection Inferred from electronic annotation. Source: Compara positive regulation of B cell proliferation Inferred from mutant phenotype Ref.13. Source: BHF-UCL positive regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 17045821. Source: BHF-UCL positive regulation of T cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of chemokine (C-X-C motif) ligand 2 production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cytokine-mediated signaling pathway Inferred from mutant phenotype Ref.13. Source: BHF-UCL positive regulation of dendritic cell antigen processing and presentation Inferred from electronic annotation. Source: Compara positive regulation of fibroblast proliferation Inferred from mutant phenotype Ref.13. Source: BHF-UCL positive regulation of macrophage cytokine production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of neutrophil chemotaxis Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 17045821. Source: BHF-UCL positive regulation of type 2 immune response Inferred from electronic annotation. Source: Compara positive thymic T cell selection Inferred from electronic annotation. Source: Compara prostaglandin biosynthetic process Inferred from direct assay Ref.13. Source: UniProtKB protein complex assembly Inferred from sequence or structural similarity. Source: UniProtKB regulation of macrophage activation Non-traceable author statement Ref.13. Source: UniProtKB
Cellular_component	ER to Golgi transport vesicle membrane Traceable author statement. Source: Reactome Golgi membrane Traceable author statement. Source: Reactome MHC class II protein complex Inferred from electronic annotation. Source: Compara NOS2-CD74 complex Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay PubMed 17045821. Source: BHF-UCL clathrin-coated endocytic vesicle membrane Traceable author statement. Source: Reactome external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to lumenal side of endoplasmic reticulum membrane Traceable author statement. Source: Reactome lysosomal lumen Traceable author statement. Source: Reactome lysosomal membrane Traceable author statement. Source: Reactome macrophage migration inhibitory factor receptor complex Inferred from direct assay PubMed 17045821. Source: BHF-UCL multivesicular body Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome trans-Golgi network membrane Traceable author statement. Source: Reactome
Molecular_function	MHC class II protein binding Non-traceable author statement PubMed 10981873. Source: UniProtKB beta-amyloid binding Inferred from physical interaction PubMed 19849849. Source: BHF-UCL cytokine receptor activity Inferred from direct assay PubMed 17045821. Source: BHF-UCL identical protein binding Traceable author statement Ref.13. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P04233-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P04233-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     209-272: Missing.

Isoform 3 (identifier: P04233-3)

The sequence of this isoform differs from the canonical sequence as follows:
     148-160: NADPLKVYPPLKG → SHWNWRTRLLGWV
     161-296: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

HLA class II histocompatibility antigen gamma chain

PRO_0000067954

Regions

Topological domain

1 – 46

46

Cytoplasmic Potential

Transmembrane

47 – 72

26

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

73 – 296

224

Extracellular Potential

Domain

210 – 271

62

Thyroglobulin type-1

Region

103 – 117

15

CLIP

Sites

Site

208 – 209

2

Breakpoint for translocation to form a CD74-ROS1 fusion protein

Amino acid modifications

Modified residue

25

1

Phosphoserine By similarity

Glycosylation

130

1

N-linked (GlcNAc...)

Glycosylation

136

1

N-linked (GlcNAc...) Ref.15

Glycosylation

203

1

O-linked (GalNAc...) Ref.17 Ref.18

Glycosylation

256

1

N-linked (GlcNAc...) Ref.21

Glycosylation

281

1

O-linked (GalNAc...) Ref.18

Disulfide bond

213 ↔ 232

Ref.21

Disulfide bond

243 ↔ 250

Ref.21

Disulfide bond

252 ↔ 271

Ref.21

Natural variations

Alternative sequence

148 – 160

13

NADPL…PPLKG → SHWNWRTRLLGWV in isoform 3.

VSP_037869

Alternative sequence

161 – 296

136

Missing in isoform 3.

VSP_037870

Alternative sequence

209 – 272

64

Missing in isoform 2.

VSP_005331

Experimental info

Sequence conflict

167

1

R → T in CAA27047. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

296

Helix Strand Turn

Details...

Helix

139 – 149

11

Helix

162 – 172

11

Helix

175 – 194

20

Helix

212 – 217

6

Beta strand

236 – 238

3

Beta strand

240 – 244

5

Turn

245 – 248

4

Beta strand

249 – 253

5

Beta strand

265 – 267

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified April 16, 2002. Version 3. Checksum: 27A13F252D5FB91D	FASTA	296	33,516
	10 20 30 40 50 60 MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY TGFSILVTLL 70 80 90 100 110 120 LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP PKPVSKMRMA TPLLMQALPM 130 140 150 160 170 180 GALPQGPMQN ATKYGNMTED HVMHLLQNAD PLKVYPPLKG SFPENLRHLK NTMETIDWKV 190 200 210 220 230 240 FESWMHHWLL FEMSRHSLEQ KPTDAPPKVL TKCQEEVSHI PAVHPGSFRP KCDENGNYLP 250 260 270 280 290 LQCYGSIGYC WCVFPNGTEV PNTRSRGHHN CSESLELEDP SSGLGVTKQD LGPVPM
	Isoform 2 (Short) [UniParc]. Checksum: 5144439D0FD27C99	FASTA	232	26,399
	10 20 30 40 50 60 MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY TGFSILVTLL 70 80 90 100 110 120 LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP PKPVSKMRMA TPLLMQALPM 130 140 150 160 170 180 GALPQGPMQN ATKYGNMTED HVMHLLQNAD PLKVYPPLKG SFPENLRHLK NTMETIDWKV 190 200 210 220 230 FESWMHHWLL FEMSRHSLEQ KPTDAPPKES LELEDPSSGL GVTKQDLGPV PM
	Isoform 3 [UniParc]. Checksum: 95CB3D7226497DE8	FASTA	160	18,328
	10 20 30 40 50 60 MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY TGFSILVTLL 70 80 90 100 110 120 LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP PKPVSKMRMA TPLLMQALPM 130 140 150 160 GALPQGPMQN ATKYGNMTED HVMHLLQSHW NWRTRLLGWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA clone for the human invariant gamma chain of class II histocompatibility antigens and its implications for the protein structure." Claesson L., Larhammar D., Rask L., Peterson P.A. Proc. Natl. Acad. Sci. U.S.A. 80:7395-7399(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"The complete sequence of the mRNA for the HLA-DR-associated invariant chain reveals a polypeptide with an unusual transmembrane polarity." Strubin M., Mach B., Long E.O. EMBO J. 3:869-872(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Structure of the human gene encoding the invariant gamma-chain of class II histocompatibility antigens." Kudo J., Chao L.-Y., Narni F., Saunders G.F. Nucleic Acids Res. 13:8827-8841(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
[4]	"Structure of the human Ia-associated invariant (gamma)-chain gene: identification of 5' sequences shared with major histocompatibility complex class II genes." O'Sullivan D.M., Larhammar D., Wilson M.C., Peterson P.A., Quaranta V. Proc. Natl. Acad. Sci. U.S.A. 83:4484-4488(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2). Tissue: Liver.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Heart and Synovium.
[7]	"The DNA sequence and comparative analysis of human chromosome 5." 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. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: B-cell and Tonsil.
[10]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 22-35; 81-94; 171-179 AND 273-288, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[11]	"HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides." Riberdy J.M., Newcomb J.R., Surman M.J., Barbosa J.A., Cresswell P. Nature 360:474-477(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 97-120.
[12]	"Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with an interstitial del(6)(q21q21)." Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H., Housman D. Genes Chromosomes Cancer 37:58-71(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH ROS1.
[13]	"MIF signal transduction initiated by binding to CD74." Leng L., Metz C.N., Fang Y., Xu J., Donnelly S., Baugh J., Delohery T., Chen Y., Mitchell R.A., Bucala R. J. Exp. Med. 197:1467-1476(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MIF.
[14]	"MHC class II transport at a glance." Berger A.C., Roche P.A. J. Cell Sci. 122:1-4(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[15]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD." Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-203, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[18]	"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins." Halim A., Ruetschi U., Larson G., Nilsson J. J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-203 AND SER-281, MASS SPECTROMETRY.
[19]	"The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3." Ghosh P., Amaya M., Mellins E., Wiley D.C. Nature 378:457-462(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 103-117 (CLIP) IN COMPLEX WITH HLA-DRA/HLA-DRB1 HETERODIMER.
[20]	"Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii." Jasanoff A., Wagner G., Wiley D.C. EMBO J. 17:6812-6818(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 134-208.
[21]	"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." Guncar G., Pungercic G., Klemencic I., Turk V., Turk D. EMBO J. 18:793-803(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 210-274, GLYCOSYLATION AT ASN-256, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K01144 mRNA. Translation: AAA36304.1. Different initiation.
X00497 mRNA. Translation: CAA25192.1.
X00497 mRNA. Translation: CAA25193.1.
X03339 Genomic DNA. Translation: CAA27046.1.
X03340 Genomic DNA. Translation: CAA27047.1.
M13560 , M13555, M13556, M13558, M13559 Genomic DNA. Translation: AAA36033.1.
BT019505 mRNA. Translation: AAV38312.1.
AK292076 mRNA. Translation: BAF84765.1.
AK297889 mRNA. Translation: BAG60210.1.
AC011372 Genomic DNA. No translation available.
AC011388 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61727.1.
CH471062 Genomic DNA. Translation: EAW61728.1.
CH471062 Genomic DNA. Translation: EAW61729.1.
CH471062 Genomic DNA. Translation: EAW61730.1.
CH471062 Genomic DNA. Translation: EAW61731.1.
BC018726 mRNA. Translation: AAH18726.1.
BC024272 mRNA. Translation: AAH24272.1.

IPI

IPI00022933.
IPI00217775.
IPI00607573.

PIR

HLHUG. A93981.

RefSeq

NP_001020329.1. NM_001025158.2.
NP_001020330.1. NM_001025159.2.
NP_004346.1. NM_004355.3.

UniGene

Hs.436568.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A6A	X-ray	2.75	C	103-117	[»]
1ICF	X-ray	2.00	I/J	210-274	[»]
1IIE	NMR	-	A/B/C	134-208	[»]
1L3H	NMR	-	A	210-274	[»]
1MUJ	X-ray	2.15	C	97-121	[»]
3PDO	X-ray	1.95	C	102-120	[»]
3PGC	X-ray	2.66	C/F	106-120	[»]
3PGD	X-ray	2.72	C/F	106-120	[»]
3QXA	X-ray	2.71	C/F	103-117	[»]
3QXD	X-ray	2.30	C/F	103-117	[»]
4AEN	X-ray	2.20	C	106-120	[»]
4AH2	X-ray	2.36	B	106-121	[»]

ProteinModelPortal

P04233.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04233. 53 interactions.

MINT

MINT-1488574.

STRING

9606.ENSP00000009530.

Protein family/group databases

MEROPS

I31.002.

PTM databases

PhosphoSite

P04233.

Polymorphism databases

DMDM

20178292.

Proteomic databases

PaxDb

P04233.

PRIDE

P04233.

Protocols and materials databases

DNASU

972.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000009530; ENSP00000009530; ENSG00000019582.
ENST00000353334; ENSP00000230685; ENSG00000019582.
ENST00000377795; ENSP00000367026; ENSG00000019582.

GeneID

972.

KEGG

hsa:972.

UCSC

uc003lsc.3. human.
uc003lsd.3. human.
uc003lse.3. human.

Organism-specific databases

CTD

972.

GeneCards

GC05M149753.

HGNC

HGNC:1697. CD74.

HPA

CAB002506.
HPA010592.

MIM

142790. gene.

neXtProt

NX_P04233.

PharmGKB

PA26236.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG248215.

HOVERGEN

HBG004444.

InParanoid

P04233.

KO

K06505.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P04233.

Bgee

P04233.

CleanEx

HS_CD74.

Genevestigator

P04233.

GermOnline

ENSG00000019582. Homo sapiens.

Family and domain databases

Gene3D

1.10.870.10. 1 hit.
4.10.800.10. 1 hit.

InterPro

IPR015386. MHC_II-assoc_invar/CLIP_MHC-bd.
IPR022339. MHC_II-assoc_invar_chain.
IPR011988. MHC_II-assoc_invariant_trimer.
IPR000716. Thyroglobulin_1.
[Graphical view]

PANTHER

PTHR14093. PTHR14093. 1 hit.

Pfam

PF09307. MHC2-interact. 1 hit.
PF08831. MHCassoc_trimer. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001992. CD74_antigen. 1 hit.

PRINTS

PR01990. CD74ANTIGEN.

SMART

SM00211. TY. 1 hit.
[Graphical view]

SUPFAM

SSF48305. MHC_II-assoc_invariant_trimer. 1 hit.
SSF57610. Thyroglobulin_1. 1 hit.

PROSITE

PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04233.

ChEMBL

CHEMBL4692.

ChiTaRS

CD74. human.

EvolutionaryTrace

P04233.

GenomeRNAi

972.

NextBio

4068.

PMAP-CutDB

P04233.

SOURCE

Search...

Entry information

Entry name

HG2A_HUMAN

Accession

Primary (citable) accession number: P04233
Secondary accession number(s): A8K7R1 , B4DNE8, D3DQG3, D3DQG4, Q14597, Q29832, Q5U0J8, Q8SNA0, Q8WLP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	April 16, 2002
Last modified:	May 1, 2013
This is version 157 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.