E3 ubiquitin-protein ligase ARIH2

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.5

    "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
    Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
    Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
  • Ref.6

    "Gfi1 ubiquitination and proteasomal degradation is inhibited by the ubiquitin ligase Triad1."
    Marteijn J.A., van der Meer L.T., van Emst L., van Reijmersdal S., Wissink W., de Witte T., Jansen J.H., Van der Reijden B.A.
    Blood 110:3128-3135(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GFI1 AND GFI1B.
  • Ref.8

    "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
    Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
    Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.

  EC:2.3.2.31

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

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

• ubiquitin conjugating enzyme 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
  • Ref.10

    "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes."
    Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A., Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.
    EMBO J. 32:2848-2860(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND CUL5, INTERACTION WITH ECS COMPLEX, ACTIVITY REGULATION, MUTAGENESIS OF 84-LEU--VAL-86; TRP-100; HIS-158; CYS-257; CYS-300 AND CYS-310.
• ubiquitin protein ligase activity 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-protein transferase activity 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
  • Ref.5

    "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
    Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
    Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
  • Ref.10

    "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes."
    Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A., Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.
    EMBO J. 32:2848-2860(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND CUL5, INTERACTION WITH ECS COMPLEX, ACTIVITY REGULATION, MUTAGENESIS OF 84-LEU--VAL-86; TRP-100; HIS-158; CYS-257; CYS-300 AND CYS-310.
• zinc ion binding Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "TRIADs: a new class of proteins with a novel cysteine-rich signature."
    van der Reijden B.A., Erpelinck-Verschueren C.A.J., Loewenberg B., Jansen J.H.
    Protein Sci. 8:1557-1561(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

GO - Biological processⁱ

• developmental cell growth Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
    Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
    Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
• hematopoietic stem cell proliferation Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
    Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
    Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
  • Ref.8

    "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
    Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
    Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
• multicellular organism development Source: ProtIncTraceable author statementⁱ
  • Ref.1

    "TRIADs: a new class of proteins with a novel cysteine-rich signature."
    van der Reijden B.A., Erpelinck-Verschueren C.A.J., Loewenberg B., Jansen J.H.
    Protein Sci. 8:1557-1561(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• positive regulation of proteasomal ubiquitin-dependent protein catabolic 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCLInferred from high throughput mutant phenotypeⁱ
  • "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
    Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
    Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
• protein K48-linked ubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
    Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
    Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
  • Ref.8

    "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
    Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
    Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
• protein K63-linked ubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
    Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
    Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
• protein polyubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
    Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
    Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
  • Ref.8

    "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
    Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
    Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
• protein ubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes."
    Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A., Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.
    EMBO J. 32:2848-2860(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND CUL5, INTERACTION WITH ECS COMPLEX, ACTIVITY REGULATION, MUTAGENESIS OF 84-LEU--VAL-86; TRP-100; HIS-158; CYS-257; CYS-300 AND CYS-310.
• ubiquitin-dependent protein catabolic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.5

    "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
    Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
    Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.

<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

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

Polymorphism and mutation 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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

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%27">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

• ubiquitin conjugating enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.10

    "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes."
    Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A., Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.
    EMBO J. 32:2848-2860(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND CUL5, INTERACTION WITH ECS COMPLEX, ACTIVITY REGULATION, MUTAGENESIS OF 84-LEU--VAL-86; TRP-100; HIS-158; CYS-257; CYS-300 AND CYS-310.

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

3D structure 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

Region

<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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

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>Sequence (1+)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.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG 
        60         70         80         90        100
ADAFDPEEYQ FTCLTYKESE GALNEHMTSL ASVLKVSHSV AKLILVNFHW 
       110        120        130        140        150
QVSEILDRYK SNSAQLLVEA RVQPNPSKHV PTSHPPHHCA VCMQFVRKEN 
       160        170        180        190        200
LLSLACQHQF CRSCWEQHCS VLVKDGVGVG VSCMAQDCPL RTPEDFVFPL 
       210        220        230        240        250
LPNEELREKY RRYLFRDYVE SHYQLQLCPG ADCPMVIRVQ EPRARRVQCN 
       260        270        280        290        300
RCNEVFCFKC RQMYHAPTDC ATIRKWLTKC ADDSETANYI SAHTKDCPKC 
       310        320        330        340        350
NICIEKNGGC NHMQCSKCKH DFCWMCLGDW KTHGSEYYEC SRYKENPDIV 
       360        370        380        390        400
NQSQQAQARE ALKKYLFYFE RWENHNKSLQ LEAQTYQRIH EKIQERVMNN 
       410        420        430        440        450
LGTWIDWQYL QNAAKLLAKC RYTLQYTYPY AYYMESGPRK KLFEYQQAQL 
       460        470        480        490 
EAEIENLSWK VERADSYDRG DLENQMHIAE QRRRTLLKDF HDT        

<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

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

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation 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. SIMILARITY comments
   Index of protein domains and families
2. PATHWAY comments
   Index of metabolic and biosynthesis pathways
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
6. Human chromosome 3
   Human chromosome 3: entries, gene names and cross-references to MIM