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P04233

- HG2A_HUMAN

UniProt

P04233 - HG2A_HUMAN

Protein

HLA class II histocompatibility antigen gamma chain

Gene

CD74

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei208 – 2092Breakpoint for translocation to form a CD74-ROS1 fusion protein

    GO - Molecular functioni

    1. beta-amyloid binding Source: BHF-UCL
    2. cytokine binding Source: UniProtKB
    3. cytokine receptor activity Source: BHF-UCL
    4. identical protein binding Source: UniProtKB
    5. macrophage migration inhibitory factor binding Source: BHF-UCL
    6. MHC class II protein binding Source: UniProtKB
    7. MHC class II protein binding, via antigen binding groove Source: UniProt
    8. MHC class II protein complex binding Source: UniProt
    9. protein binding Source: IntAct
    10. protein binding involved in protein folding Source: UniProt

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. antigen processing and presentation of endogenous antigen Source: UniProtKB
    3. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    4. cell proliferation Source: UniProtKB
    5. chaperone mediated protein folding requiring cofactor Source: Ensembl
    6. defense response Source: Ensembl
    7. immunoglobulin mediated immune response Source: UniProtKB
    8. intracellular protein transport Source: UniProtKB
    9. macrophage migration inhibitory factor signaling pathway Source: Ensembl
    10. negative regulation of apoptotic process Source: UniProtKB
    11. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    12. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    13. negative regulation of mature B cell apoptotic process Source: Ensembl
    14. negative regulation of peptide secretion Source: BHF-UCL
    15. negative regulation of T cell differentiation Source: Ensembl
    16. negative thymic T cell selection Source: Ensembl
    17. positive regulation of B cell proliferation Source: BHF-UCL
    18. positive regulation of chemokine (C-X-C motif) ligand 2 production Source: BHF-UCL
    19. positive regulation of cytokine-mediated signaling pathway Source: BHF-UCL
    20. positive regulation of dendritic cell antigen processing and presentation Source: Ensembl
    21. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    22. positive regulation of fibroblast proliferation Source: BHF-UCL
    23. positive regulation of macrophage cytokine production Source: BHF-UCL
    24. positive regulation of neutrophil chemotaxis Source: BHF-UCL
    25. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    26. positive regulation of T cell differentiation Source: Ensembl
    27. positive regulation of type 2 immune response Source: Ensembl
    28. positive thymic T cell selection Source: Ensembl
    29. prostaglandin biosynthetic process Source: UniProtKB
    30. protein complex assembly Source: UniProtKB
    31. regulation of macrophage activation Source: UniProtKB
    32. signal transduction Source: UniProtKB
    33. T cell selection Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.

    Protein family/group databases

    MEROPSiI31.002.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:CD74
    Synonyms:DHLAG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1697. CD74.

    Subcellular locationi

    Cell membrane Curated; Single-pass type II membrane protein Curated. 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.

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. clathrin-coated endocytic vesicle membrane Source: Reactome
    3. endocytic vesicle membrane Source: Reactome
    4. ER to Golgi transport vesicle membrane Source: Reactome
    5. external side of plasma membrane Source: Ensembl
    6. extracellular vesicular exosome Source: UniProt
    7. Golgi membrane Source: Reactome
    8. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    9. integral component of membrane Source: BHF-UCL
    10. intracellular Source: UniProtKB
    11. lysosomal lumen Source: Reactome
    12. lysosomal membrane Source: Reactome
    13. macrophage migration inhibitory factor receptor complex Source: BHF-UCL
    14. membrane Source: UniProtKB
    15. MHC class II protein complex Source: Ensembl
    16. multivesicular body Source: Ensembl
    17. NOS2-CD74 complex Source: Ensembl
    18. plasma membrane Source: Reactome
    19. trans-Golgi network membrane Source: Reactome
    20. transport vesicle membrane Source: Reactome
    21. vacuole Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving CD74 is found in a non-small cell lung tumor. Results in the formation of a CD74-ROS1 chimeric protein.1 Publication

    Organism-specific databases

    PharmGKBiPA26236.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296HLA class II histocompatibility antigen gamma chainPRO_0000067954Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251PhosphoserineBy similarity
    Glycosylationi130 – 1301N-linked (GlcNAc...)
    Glycosylationi136 – 1361N-linked (GlcNAc...)1 Publication
    Glycosylationi203 – 2031O-linked (GalNAc...)2 Publications
    Disulfide bondi213 ↔ 2321 PublicationPROSITE-ProRule annotation
    Disulfide bondi243 ↔ 2501 PublicationPROSITE-ProRule annotation
    Disulfide bondi252 ↔ 2711 PublicationPROSITE-ProRule annotation
    Glycosylationi256 – 2561N-linked (GlcNAc...)1 Publication
    Glycosylationi281 – 2811O-linked (GalNAc...)1 Publication

    Post-translational modificationi

    N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

    Proteomic databases

    MaxQBiP04233.
    PaxDbiP04233.
    PRIDEiP04233.

    PTM databases

    PhosphoSiteiP04233.

    Miscellaneous databases

    PMAP-CutDBP04233.

    Expressioni

    Gene expression databases

    ArrayExpressiP04233.
    BgeeiP04233.
    CleanExiHS_CD74.
    GenevestigatoriP04233.

    Organism-specific databases

    HPAiCAB002506.
    HPA010592.

    Interactioni

    Subunit structurei

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CXCR4P610734EBI-2622890,EBI-489411

    Protein-protein interaction databases

    BioGridi107410. 5 interactions.
    IntActiP04233. 55 interactions.
    MINTiMINT-1488574.
    STRINGi9606.ENSP00000009530.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi139 – 14911
    Helixi162 – 17211
    Helixi175 – 19420
    Helixi212 – 2176
    Beta strandi236 – 2383
    Beta strandi240 – 2445
    Turni245 – 2484
    Beta strandi249 – 2535
    Beta strandi265 – 2673

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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-ray2.36B106-120[»]
    ProteinModelPortaliP04233.
    SMRiP04233. Positions 134-208, 210-274.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04233.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4646CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini73 – 296224ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei47 – 7226Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini210 – 27162Thyroglobulin type-1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni103 – 11715CLIPAdd
    BLAST

    Sequence similaritiesi

    Contains 1 thyroglobulin type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG248215.
    HOVERGENiHBG004444.
    InParanoidiP04233.
    KOiK06505.
    OrthoDBiEOG793B8J.
    PhylomeDBiP04233.
    TreeFamiTF317779.

    Family and domain databases

    Gene3Di1.10.870.10. 1 hit.
    4.10.800.10. 1 hit.
    InterProiIPR015386. MHC_II-assoc_invar/CLIP_MHC-bd.
    IPR022339. MHC_II-assoc_invar_chain.
    IPR011988. MHC_II-assoc_invariant_trimer.
    IPR000716. Thyroglobulin_1.
    [Graphical view]
    PANTHERiPTHR14093. PTHR14093. 1 hit.
    PfamiPF09307. MHC2-interact. 1 hit.
    PF08831. MHCassoc_trimer. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001992. CD74_antigen. 1 hit.
    PRINTSiPR01990. CD74ANTIGEN.
    SMARTiSM00211. TY. 1 hit.
    [Graphical view]
    SUPFAMiSSF48305. SSF48305. 1 hit.
    SSF57610. SSF57610. 1 hit.
    PROSITEiPS00484. THYROGLOBULIN_1_1. 1 hit.
    PS51162. THYROGLOBULIN_1_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04233-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MHRRRSRSCR EDQKPVMDDQ RDLISNNEQL PMLGRRPGAP ESKCSRGALY    50
    TGFSILVTLL LAGQATTAYF LYQQQGRLDK LTVTSQNLQL ENLRMKLPKP 100
    PKPVSKMRMA TPLLMQALPM GALPQGPMQN ATKYGNMTED HVMHLLQNAD 150
    PLKVYPPLKG SFPENLRHLK NTMETIDWKV FESWMHHWLL FEMSRHSLEQ 200
    KPTDAPPKVL TKCQEEVSHI PAVHPGSFRP KCDENGNYLP LQCYGSIGYC 250
    WCVFPNGTEV PNTRSRGHHN CSESLELEDP SSGLGVTKQD LGPVPM 296
    Length:296
    Mass (Da):33,516
    Last modified:April 16, 2002 - v3
    Checksum:i27A13F252D5FB91D
    GO
    Isoform 2 (identifier: P04233-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

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

    Show »
    Length:232
    Mass (Da):26,399
    Checksum:i5144439D0FD27C99
    GO
    Isoform 3 (identifier: P04233-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:160
    Mass (Da):18,328
    Checksum:i95CB3D7226497DE8
    GO

    Sequence cautioni

    The sequence AAA36304.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671R → T in CAA27047. (PubMed:3001652)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei148 – 16013NADPL…PPLKG → SHWNWRTRLLGWV in isoform 3. 1 PublicationVSP_037869Add
    BLAST
    Alternative sequencei161 – 296136Missing in isoform 3. 1 PublicationVSP_037870Add
    BLAST
    Alternative sequencei209 – 27264Missing in isoform 2. 5 PublicationsVSP_005331Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS34276.1. [P04233-3]
    CCDS47308.1. [P04233-2]
    CCDS47309.1. [P04233-1]
    PIRiA93981. HLHUG.
    RefSeqiNP_001020329.1. NM_001025158.2. [P04233-3]
    NP_001020330.1. NM_001025159.2. [P04233-1]
    NP_004346.1. NM_004355.3. [P04233-2]
    UniGeneiHs.436568.

    Genome annotation databases

    EnsembliENST00000009530; ENSP00000009530; ENSG00000019582. [P04233-1]
    ENST00000353334; ENSP00000230685; ENSG00000019582. [P04233-2]
    ENST00000377795; ENSP00000367026; ENSG00000019582. [P04233-3]
    GeneIDi972.
    KEGGihsa:972.
    UCSCiuc003lsc.3. human. [P04233-1]
    uc003lsd.3. human. [P04233-2]
    uc003lse.3. human. [P04233-3]

    Polymorphism databases

    DMDMi20178292.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS34276.1. [P04233-3 ]
    CCDS47308.1. [P04233-2 ]
    CCDS47309.1. [P04233-1 ]
    PIRi A93981. HLHUG.
    RefSeqi NP_001020329.1. NM_001025158.2. [P04233-3 ]
    NP_001020330.1. NM_001025159.2. [P04233-1 ]
    NP_004346.1. NM_004355.3. [P04233-2 ]
    UniGenei Hs.436568.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 106-120 [» ]
    ProteinModelPortali P04233.
    SMRi P04233. Positions 134-208, 210-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107410. 5 interactions.
    IntActi P04233. 55 interactions.
    MINTi MINT-1488574.
    STRINGi 9606.ENSP00000009530.

    Chemistry

    BindingDBi P04233.
    ChEMBLi CHEMBL2111430.

    Protein family/group databases

    MEROPSi I31.002.

    PTM databases

    PhosphoSitei P04233.

    Polymorphism databases

    DMDMi 20178292.

    Proteomic databases

    MaxQBi P04233.
    PaxDbi P04233.
    PRIDEi P04233.

    Protocols and materials databases

    DNASUi 972.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000009530 ; ENSP00000009530 ; ENSG00000019582 . [P04233-1 ]
    ENST00000353334 ; ENSP00000230685 ; ENSG00000019582 . [P04233-2 ]
    ENST00000377795 ; ENSP00000367026 ; ENSG00000019582 . [P04233-3 ]
    GeneIDi 972.
    KEGGi hsa:972.
    UCSCi uc003lsc.3. human. [P04233-1 ]
    uc003lsd.3. human. [P04233-2 ]
    uc003lse.3. human. [P04233-3 ]

    Organism-specific databases

    CTDi 972.
    GeneCardsi GC05M149753.
    HGNCi HGNC:1697. CD74.
    HPAi CAB002506.
    HPA010592.
    MIMi 142790. gene.
    neXtProti NX_P04233.
    PharmGKBi PA26236.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248215.
    HOVERGENi HBG004444.
    InParanoidi P04233.
    KOi K06505.
    OrthoDBi EOG793B8J.
    PhylomeDBi P04233.
    TreeFami TF317779.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.

    Miscellaneous databases

    ChiTaRSi CD74. human.
    EvolutionaryTracei P04233.
    GeneWikii CD74.
    GenomeRNAii 972.
    NextBioi 4068.
    PMAP-CutDB P04233.
    PROi P04233.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04233.
    Bgeei P04233.
    CleanExi HS_CD74.
    Genevestigatori P04233.

    Family and domain databases

    Gene3Di 1.10.870.10. 1 hit.
    4.10.800.10. 1 hit.
    InterProi 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 ]
    PANTHERi PTHR14093. PTHR14093. 1 hit.
    Pfami PF09307. MHC2-interact. 1 hit.
    PF08831. MHCassoc_trimer. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001992. CD74_antigen. 1 hit.
    PRINTSi PR01990. CD74ANTIGEN.
    SMARTi SM00211. TY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48305. SSF48305. 1 hit.
    SSF57610. SSF57610. 1 hit.
    PROSITEi PS00484. THYROGLOBULIN_1_1. 1 hit.
    PS51162. THYROGLOBULIN_1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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.

    Entry informationi

    Entry nameiHG2A_HUMAN
    AccessioniPrimary (citable) accession number: P04233
    Secondary accession number(s): A8K7R1
    , B4DNE8, D3DQG3, D3DQG4, Q14597, Q29832, Q5U0J8, Q8SNA0, Q8WLP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 171 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3