Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04233 (HG2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence 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 apparatustrans-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 processAdaptive immunity
Immunity
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionChaperone
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell selection

Non-traceable author statement PubMed 10981873. Source: UniProtKB

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

defense response

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

negative regulation of apoptotic process

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype PubMed 17045821. Source: BHF-UCL

negative regulation of mature B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptide secretion

Inferred from direct assay PubMed 19849849. Source: BHF-UCL

negative thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

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: Ensembl

positive thymic T cell selection

Inferred from electronic annotation. Source: Ensembl

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

signal transduction

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentER 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: Ensembl

NOS2-CD74 complex

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from direct assay Ref.13. Source: BHF-UCL

intracellular

Traceable author statement Ref.13. Source: UniProtKB

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: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

trans-Golgi network membrane

Traceable author statement. Source: Reactome

transport vesicle membrane

Traceable author statement. Source: Reactome

vacuole

Inferred from direct assay PubMed 19849849. Source: BHF-UCL

   Molecular_functionMHC 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 binding

Inferred from physical interaction Ref.13. Source: UniProtKB

cytokine receptor activity

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

identical protein binding

Traceable author statement Ref.13. Source: UniProtKB

macrophage migration inhibitory factor binding

Inferred from physical interaction PubMed 17045821. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CXCR4P610734EBI-2622890,EBI-489411

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296HLA class II histocompatibility antigen gamma chain
PRO_0000067954

Regions

Topological domain1 – 4646Cytoplasmic Potential
Transmembrane47 – 7226Helical; Signal-anchor for type II membrane protein; Potential
Topological domain73 – 296224Extracellular Potential
Domain210 – 27162Thyroglobulin type-1
Region103 – 11715CLIP

Sites

Site208 – 2092Breakpoint for translocation to form a CD74-ROS1 fusion protein

Amino acid modifications

Modified residue251Phosphoserine By similarity
Glycosylation1301N-linked (GlcNAc...)
Glycosylation1361N-linked (GlcNAc...) Ref.15
Glycosylation2031O-linked (GalNAc...) Ref.17 Ref.18
Glycosylation2561N-linked (GlcNAc...) Ref.21
Glycosylation2811O-linked (GalNAc...) Ref.18
Disulfide bond213 ↔ 232 Ref.21
Disulfide bond243 ↔ 250 Ref.21
Disulfide bond252 ↔ 271 Ref.21

Natural variations

Alternative sequence148 – 16013NADPL…PPLKG → SHWNWRTRLLGWV in isoform 3.
VSP_037869
Alternative sequence161 – 296136Missing in isoform 3.
VSP_037870
Alternative sequence209 – 27264Missing in isoform 2.
VSP_005331

Experimental info

Sequence conflict1671R → T in CAA27047. Ref.3

Secondary structure

................. 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified April 16, 2002. Version 3.
Checksum: 27A13F252D5FB91D

FASTA29633,516
        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 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 5144439D0FD27C99
Show »

FASTA23226,399
Isoform 3 [UniParc].

Checksum: 95CB3D7226497DE8
Show »

FASTA16018,328

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.
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, IDENTIFICATION BY 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, IDENTIFICATION BY 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 expand/collapse EMBL AC list , 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.
PIRHLHUG. A93981.
RefSeqNP_001020329.1. NM_001025158.2.
NP_001020330.1. NM_001025159.2.
NP_004346.1. NM_004355.3.
UniGeneHs.436568.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6AX-ray2.75C103-117[»]
1ICFX-ray2.00I/J210-274[»]
1IIENMR-A/B/C134-208[»]
1L3HNMR-A210-274[»]
1MUJX-ray2.15C97-121[»]
3PDOX-ray1.95C102-120[»]
3PGCX-ray2.66C/F106-120[»]
3PGDX-ray2.72C/F106-120[»]
3QXAX-ray2.71C/F103-117[»]
3QXDX-ray2.30C/F103-117[»]
4AENX-ray2.20C106-120[»]
4AH2X-ray2.36B106-121[»]
ProteinModelPortalP04233.
SMRP04233. Positions 134-208, 210-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107410. 5 interactions.
IntActP04233. 54 interactions.
MINTMINT-1488574.
STRING9606.ENSP00000009530.

Chemistry

BindingDBP04233.
ChEMBLCHEMBL4692.

Protein family/group databases

MEROPSI31.002.

PTM databases

PhosphoSiteP04233.

Polymorphism databases

DMDM20178292.

Proteomic databases

PaxDbP04233.
PRIDEP04233.

Protocols and materials databases

DNASU972.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000009530; ENSP00000009530; ENSG00000019582. [P04233-1]
ENST00000353334; ENSP00000230685; ENSG00000019582. [P04233-2]
ENST00000377795; ENSP00000367026; ENSG00000019582. [P04233-3]
GeneID972.
KEGGhsa:972.
UCSCuc003lsc.3. human. [P04233-1]
uc003lsd.3. human. [P04233-2]
uc003lse.3. human. [P04233-3]

Organism-specific databases

CTD972.
GeneCardsGC05M149753.
HGNCHGNC:1697. CD74.
HPACAB002506.
HPA010592.
MIM142790. gene.
neXtProtNX_P04233.
PharmGKBPA26236.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248215.
HOVERGENHBG004444.
InParanoidP04233.
KOK06505.
OrthoDBEOG793B8J.
PhylomeDBP04233.
TreeFamTF317779.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP04233.
BgeeP04233.
CleanExHS_CD74.
GenevestigatorP04233.

Family and domain databases

Gene3D1.10.870.10. 1 hit.
4.10.800.10. 1 hit.
InterProIPR015386. MHC_II-assoc_invar/CLIP_MHC-bd.
IPR022339. MHC_II-assoc_invar_chain.
IPR011988. MHC_II-assoc_invariant_trimer.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERPTHR14093. PTHR14093. 1 hit.
PfamPF09307. MHC2-interact. 1 hit.
PF08831. MHCassoc_trimer. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PIRSFPIRSF001992. CD74_antigen. 1 hit.
PRINTSPR01990. CD74ANTIGEN.
SMARTSM00211. TY. 1 hit.
[Graphical view]
SUPFAMSSF48305. SSF48305. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEPS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD74. human.
EvolutionaryTraceP04233.
GeneWikiCD74.
GenomeRNAi972.
NextBio4068.
PMAP-CutDBP04233.
PROP04233.
SOURCESearch...

Entry information

Entry nameHG2A_HUMAN
AccessionPrimary (citable) accession number: P04233
Secondary accession number(s): A8K7R1 expand/collapse secondary AC list , 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: April 16, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries