DnaJ homolog subfamily A member 3, mitochondrial

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATP binding Source: InterPro
• GTPase regulator activity Source: Ensembl
• Hsp70 protein binding Source: Ensembl
• IkappaB kinase complex binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• interferon-gamma receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
    Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
    J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
• metal ion binding Source: UniProtKB-KW
• NF-kappaB binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex binding Source: UniProtKBInferred from direct assayⁱ
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.2

    "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
    Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
    J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• transcription factor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate."
    Lu B., Garrido N., Spelbrink J.N., Suzuki C.K.
    J Biol Chem 281:13150-13158(2006) [PubMed] [Europe PMC] [Abstract]
  • "The tumor suppressor hTid1 inhibits STAT5b activity via functional interaction."
    Dhennin-Duthille I., Nyga R., Yahiaoui S., Gouilleux-Gruart V., Regnier A., Lassoued K., Gouilleux F.
    J Biol Chem 286:5034-5042(2011) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: Ensembl

GO - Biological processⁱ

• activation-induced cell death of T cells Source: Ensembl
• activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions."
    Syken J., De-Medina T., Muenger K.
    Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-121.
• cell aging Source: Ensembl
• mitochondrial DNA replication Source: Ensembl
• mitochondrion organization Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions."
    Syken J., De-Medina T., Muenger K.
    Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-121.
• negative regulation of cell population proliferation Source: UniProtKBInferred from direct assayⁱ
  • "Human T cell leukemia virus type 1 Tax associates with a molecular chaperone complex containing hTid-1 and Hsp70."
    Cheng H., Cenciarelli C., Shao Z., Vidal M., Parks W.P., Pagano M., Cheng-Mayer C.
    Curr Biol 11:1771-1775(2001) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions."
    Syken J., De-Medina T., Muenger K.
    Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-121.
• negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKBInferred from direct assayⁱ
  • "HTLV-1 Tax-associated hTid-1, a human DnaJ protein, is a repressor of Ikappa B kinase beta subunit."
    Cheng H., Cenciarelli C., Tao M., Parks W.P., Cheng-Mayer C.
    J Biol Chem 277:20605-20610(2002) [PubMed] [Europe PMC] [Abstract]
• negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
    Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
    J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
• negative regulation of NF-kappaB transcription factor activity Source: UniProtKBInferred from direct assayⁱ
  • "HTLV-1 Tax-associated hTid-1, a human DnaJ protein, is a repressor of Ikappa B kinase beta subunit."
    Cheng H., Cenciarelli C., Tao M., Parks W.P., Cheng-Mayer C.
    J Biol Chem 277:20605-20610(2002) [PubMed] [Europe PMC] [Abstract]
• negative regulation of programmed cell death Source: Ensembl
• negative regulation of protein kinase activity Source: UniProtKBInferred from direct assayⁱ
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • "The tumor suppressor hTid1 inhibits STAT5b activity via functional interaction."
    Dhennin-Duthille I., Nyga R., Yahiaoui S., Gouilleux-Gruart V., Regnier A., Lassoued K., Gouilleux F.
    J Biol Chem 286:5034-5042(2011) [PubMed] [Europe PMC] [Abstract]
• neuromuscular junction development Source: UniProtKBInferred from direct assayⁱ
  • "A mammalian homolog of Drosophila tumorous imaginal discs, Tid1, mediates agrin signaling at the neuromuscular junction."
    Linnoila J., Wang Y., Yao Y., Wang Z.Z.
    Neuron 60:625-641(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of apoptotic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions."
    Syken J., De-Medina T., Muenger K.
    Proc. Natl. Acad. Sci. U.S.A. 96:8499-8504(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-121.
• positive regulation of protein ubiquitination Source: UniProtKBInferred from direct assayⁱ
  • "Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells."
    Kim S.W., Chao T.H., Xiang R., Lo J.F., Campbell M.J., Fearns C., Lee J.D.
    Cancer Res 64:7732-7739(2004) [PubMed] [Europe PMC] [Abstract]
• positive regulation of T cell proliferation Source: Ensembl
• protein folding Source: UniProtKBInferred from direct assayⁱ
  • "Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate."
    Lu B., Garrido N., Spelbrink J.N., Suzuki C.K.
    J Biol Chem 281:13150-13158(2006) [PubMed] [Europe PMC] [Abstract]
• protein stabilization Source: UniProtKBInferred from direct assayⁱ
  • "HTLV-1 Tax-associated hTid-1, a human DnaJ protein, is a repressor of Ikappa B kinase beta subunit."
    Cheng H., Cenciarelli C., Tao M., Parks W.P., Cheng-Mayer C.
    J Biol Chem 277:20605-20610(2002) [PubMed] [Europe PMC] [Abstract]
• regulation of apoptotic process Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to heat Source: InterPro
• response to interferon-gamma Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
    Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
    J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
• skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
• small GTPase mediated signal transduction Source: Ensembl
• T cell differentiation in thymus Source: Ensembl

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• Hsp70 protein binding Source: Ensembl
• interferon-gamma receptor binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
    Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
    J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
• NF-kappaB binding Source: UniProtKBInferred from physical interactionⁱ
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.2

    "hTid-1, a human DnaJ protein, modulates the interferon signaling pathway."
    Sarkar S., Pollack B.P., Lin K.-T., Kotenko S.V., Cook J.R., Lewis A., Pestka S.
    J. Biol. Chem. 276:49034-49042(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH JAK2; HSP70 AND IFN-GAMMAR2, VARIANT TYR-75.
  • "Molecular mechanism of hTid-1, the human homolog of Drosophila tumor suppressor l(2)Tid, in the regulation of NF-kappaB activity and suppression of tumor growth."
    Cheng H., Cenciarelli C., Nelkin G., Tsan R., Fan D., Cheng-Mayer C., Fidler I.J.
    Mol Cell Biol 25:44-59(2005) [PubMed] [Europe PMC] [Abstract]
• transcription factor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate."
    Lu B., Garrido N., Spelbrink J.N., Suzuki C.K.
    J Biol Chem 281:13150-13158(2006) [PubMed] [Europe PMC] [Abstract]
  • "The tumor suppressor hTid1 inhibits STAT5b activity via functional interaction."
    Dhennin-Duthille I., Nyga R., Yahiaoui S., Gouilleux-Gruart V., Regnier A., Lassoued K., Gouilleux F.
    J Biol Chem 286:5034-5042(2011) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: Ensembl

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

Zinc finger

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS 
        60         70         80         90        100
SLTSCGPRAL LTLRPGVSLT GTKHNPFICT ASFHTSAPLA KEDYYQILGV 
       110        120        130        140        150
PRNASQKEIK KAYYQLAKKY HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK 
       160        170        180        190        200
RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV DPEELFRKIF GEFSSSSFGD 
       210        220        230        240        250
FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN GKGNEPGTKV 
       260        270        280        290        300
QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ 
       310        320        330        340        350
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL 
       360        370        380        390        400
FISIAQALLG GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG 
       410        420        430        440        450
YGDHYIHIKI RVPKRLTSRQ QSLILSYAED ETDVEGTVNG VTLTSSGGST 
       460        470        480
MDSSAGSKAR REAGEDEEGF LSKLKKMFTS                       

        10         20         30         40         50
MAARCSTRWL LVVVGTPRLP AISGRGARPP REGVVGAWLS RKLSVPAFAS 
        60         70         80         90        100
SLTSCGPRAL LTLRPGVSLT GTKHNPFICT ASFHTSAPLA KEDYYQILGV 
       110        120        130        140        150
PRNASQKEIK KAYYQLAKKY HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK 
       160        170        180        190        200
RKQYDAYGSA GFDPGASGSQ HSYWKGGPTV DPEELFRKIF GEFSSSSFGD 
       210        220        230        240        250
FQTVFDQPQE YFMELTFNQA AKGVNKEFTV NIMDTCERCN GKGNEPGTKV 
       260        270        280        290        300
QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIIISPCV VCRGAGQAKQ 
       310        320        330        340        350
KKRVMIPVPA GVEDGQTVRM PVGKREIFIT FRVQKSPVFR RDGADIHSDL 
       360        370        380        390        400
FISIAQALLG GTARAQGLYE TINVTIPPGT QTDQKIRMGG KGIPRINSYG 
       410        420        430        440        450
YGDHYIHIKI RVPKRLTSRQ QSLILSYAED ETDVEGTVNG VTLTSSGKRS 

TGN                                                    

        10         20         30         40         50
MAEPQAERPR LCVFPDLLRP PSAADIETWC QPYRKIFGEF SSSSFGDFQT 
        60         70         80         90        100
VFDQPQEYFM ELTFNQAAKG VNKEFTVNIM DTCERCNGKG NEPGTKVQHC 
       110        120        130        140        150
HYCGGSGMET INTGPFVMRS TCRRCGGRGS IIISPCVVCR GAGQAKQKKR 
       160        170        180        190        200
VMIPVPAGVE DGQTVRMPVG KREIFITFRV QKSPVFRRDG ADIHSDLFIS 
       210        220        230        240        250
IAQALLGGTA RAQGLYETIN VTIPPGTQTD QKIRMGGKGI PRINSYGYGD 
       260        270        280        290        300
HYIHIKIRVP KRLTSRQQSL ILSYAEDETD VEGTVNGVTL TSSGKRSTGN 

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Human chromosome 16
   Human chromosome 16: entries, gene names and cross-references to MIM
2. Human entries with genetic variants
   List of human entries with genetic variants
3. Human variants curated from literature reports
   Index of human variants curated from literature reports
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references