Trafficking kinesin-binding protein 2

<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>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

• enzyme binding Source: RGD <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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.
• GABA receptor binding Source: MGI <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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.1

    "Identification, molecular cloning, and characterization of a novel GABAA receptor-associated protein, GRIF-1."
    Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M., Chazot P.L., Pollard S., Stephenson F.A.
    J. Biol. Chem. 277:30079-30090(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH GABA-A RECEPTOR.
• kinesin binding Source: RGDInferred from direct assayⁱ
  • "GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin."
    Brickley K., Smith M.J., Beck M., Stephenson F.A.
    J. Biol. Chem. 280:14723-14732(2005) [PubMed] [Europe PMC] [Abstract]
• myosin binding 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-go-evidence-codes#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]
• signaling receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Identification, molecular cloning, and characterization of a novel GABAA receptor-associated protein, GRIF-1."
    Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M., Chazot P.L., Pollard S., Stephenson F.A.
    J. Biol. Chem. 277:30079-30090(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH GABA-A RECEPTOR.
• TPR domain binding Source: RGDInferred from direct assayⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.

GO - Biological processⁱ

• anterograde axonal transport 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]
• anterograde axonal transport of mitochondrion 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]
• anterograde dendritic transport of mitochondrion Source: RGDInferred from sequence orthologyⁱ
  • "TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites."
    van Spronsen M., Mikhaylova M., Lipka J., Schlager M.A., van den Heuvel D.J., Kuijpers M., Wulf P.S., Keijzer N., Demmers J., Kapitein L.C., Jaarsma D., Gerritsen H.C., Akhmanova A., Hoogenraad C.C.
    Neuron 77:485-502(2013) [PubMed] [Europe PMC] [Abstract]
• dendrite morphogenesis Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites."
    van Spronsen M., Mikhaylova M., Lipka J., Schlager M.A., van den Heuvel D.J., Kuijpers M., Wulf P.S., Keijzer N., Demmers J., Kapitein L.C., Jaarsma D., Gerritsen H.C., Akhmanova A., Hoogenraad C.C.
    Neuron 77:485-502(2013) [PubMed] [Europe PMC] [Abstract]
• dendritic transport of mitochondrion Source: RGDInferred from mutant phenotypeⁱ
  • "TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites."
    van Spronsen M., Mikhaylova M., Lipka J., Schlager M.A., van den Heuvel D.J., Kuijpers M., Wulf P.S., Keijzer N., Demmers J., Kapitein L.C., Jaarsma D., Gerritsen H.C., Akhmanova A., Hoogenraad C.C.
    Neuron 77:485-502(2013) [PubMed] [Europe PMC] [Abstract]
• endosome to lysosome transport Source: RGDInferred from direct assayⁱ
  • Ref.5

    "GRIF1 binds Hrs and is a new regulator of endosomal trafficking."
    Kirk E., Chin L.S., Li L.
    J. Cell Sci. 119:4689-4701(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH HGS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
• mitochondrion distribution 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]
• negative regulation of axonogenesis Source: RGDInferred from mutant phenotypeⁱ
  • "TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites."
    van Spronsen M., Mikhaylova M., Lipka J., Schlager M.A., van den Heuvel D.J., Kuijpers M., Wulf P.S., Keijzer N., Demmers J., Kapitein L.C., Jaarsma D., Gerritsen H.C., Akhmanova A., Hoogenraad C.C.
    Neuron 77:485-502(2013) [PubMed] [Europe PMC] [Abstract]
• neurogenesis 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]
• neurotransmitter transport Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • Ref.1

    "Identification, molecular cloning, and characterization of a novel GABAA receptor-associated protein, GRIF-1."
    Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M., Chazot P.L., Pollard S., Stephenson F.A.
    J. Biol. Chem. 277:30079-30090(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH GABA-A RECEPTOR.
• protein localization 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]
• protein O-linked glycosylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.
• protein targeting Source: UniProtKBInferred from direct assayⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.
• regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.
• vesicle transport along microtubule 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]

<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

<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 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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

<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_section">'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_section">'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_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• enzyme binding Source: RGDInferred from physical interactionⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.
• GABA receptor binding Source: MGIInferred from direct assayⁱ
  • Ref.1

    "Identification, molecular cloning, and characterization of a novel GABAA receptor-associated protein, GRIF-1."
    Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M., Chazot P.L., Pollard S., Stephenson F.A.
    J. Biol. Chem. 277:30079-30090(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH GABA-A RECEPTOR.
• kinesin binding Source: RGDInferred from direct assayⁱ
  • "GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin."
    Brickley K., Smith M.J., Beck M., Stephenson F.A.
    J. Biol. Chem. 280:14723-14732(2005) [PubMed] [Europe PMC] [Abstract]
• myosin binding 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]
• signaling receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Identification, molecular cloning, and characterization of a novel GABAA receptor-associated protein, GRIF-1."
    Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M., Chazot P.L., Pollard S., Stephenson F.A.
    J. Biol. Chem. 277:30079-30090(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH GABA-A RECEPTOR.
• TPR domain binding Source: RGDInferred from direct assayⁱ
  • Ref.3

    "Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
    Iyer S.P.N., Akimoto Y., Hart G.W.
    J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.

Protein-protein interaction 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

Domains and Repeats

Region

Coiled coil

<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

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_length">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 (2+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MSLSQNAIFK SQTGEENLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ 
        60         70         80         90        100
LPQYKLRVDS LFLYENQDWS QSSHQQQDAS ETLSPVLAEE TFRYMILGTD 
       110        120        130        140        150
RVEQMTKTYN DIDMVTHLLA ERDRDLELAA RIGQALLKRN HVLSEQNESL 
       160        170        180        190        200
EEQLGQAFDQ VNQLQHELSK KEELLRIVSI ASEESETDSS CSTPLRFNES 
       210        220        230        240        250
FSLSQGLLQL DMMHEKLKEL EEENMALRSK ACHIKTETFT YEEKEQKLIN 
       260        270        280        290        300
DCVNELRETN AQMSRMTEEL SGKSDELLRY QEEISSLLSQ IVDLQHKLKE 
       310        320        330        340        350
HVIEKEELRL HLQASKDAQR QLTMELHELQ DRNMECLGML HESQEEIKEL 
       360        370        380        390        400
RNKAGPSAHL CFSQAYGVFA GESLAAEIEG TMRKKLSLDE ESVFKQKAQQ 
       410        420        430        440        450
KRVFDTVKVA NDTRGRSVTF PVLLPIPGSN RSSVIMTAKP FESGVQQTED 
       460        470        480        490        500
KTLPNQGSST EVPGNSHPRD PPGLPEDSDL ATALHRLSLR RQNYLSEKQF 
       510        520        530        540        550
FAEEWERKLQ ILAEQEEEVS SCEALTENLA SFCTDQSETT ELGSAGCLRG 
       560        570        580        590        600
FMPEKLQIVK PLEGSQTLHH WQQLAQPNLG TILDPRPGVI TKGFTQMPKD 
       610        620        630        640        650
AVYHISDLEE DEEVGITFQV QQPLQLEQKP APPPPVTGIF LPPMTSAGGP 
       660        670        680        690        700
VSVATSNPGK CLSFTNSTFT FTTCRILHPS DITQVTPSSG FPSLSCGSSA 
       710        720        730        740        750
GSASNTAVNS PAASYRLSIG ESITNRRDST ITFSSTRSLA KLLQERGISA 
       760        770        780        790        800
KVYHSPASEN PLLQLRPKAL ATPSTPPNSP SQSPCSSPVP FEPRVHVSEN 
       810        820        830        840        850
FLASRPAETF LQEMYGLRPS RAPPDVGQLK MNLVDRLKRL GIARVVKTPV 
       860        870        880        890        900
PRENGKSREA EMGLQKPDSA VYLNSGGSLL GGLRRNQSLP VMMGSFGAPV 
       910 
CTTSPKMGIL KED                                         

        10         20         30         40         50
MSLSQNAIFK SQTGEENLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ 
        60         70         80         90        100
LPQYKLRVDS LFLYENQDWS QSSHQQQDAS ETLSPVLAEE TFRYMILGTD 
       110        120        130        140        150
RVEQMTKTYN DIDMVTHLLA ERDRDLELAA RIGQALLKRN HVLSEQNESL 
       160        170        180        190        200
EEQLGQAFDQ VNQLQHELSK KEELLRIVSI ASEESETDSS CSTPLRFNES 
       210        220        230        240        250
FSLSQGLLQL DMMHEKLKEL EEENMALRSK ACHIKTETFT YEEKEQKLIN 
       260        270        280        290        300
DCVNELRETN AQMSRMTEEL SGKSDELLRY QEEISSLLSQ IVDLQHKLKE 
       310        320        330        340        350
HVIEKEELRL HLQASKDAQR QLTMELHELQ DRNMECLGML HESQEEIKEL 
       360        370        380        390        400
RNKAGPSAHL CFSQAYGVFA GESLAAEIEG TMRKKLSLDE ESVFKQKAQQ 
       410        420        430        440        450
KRVFDTVKVA NDTRGRSVTF PVLLPIPGSN RSSVIMTAKP FESGVQQTED 
       460        470        480        490        500
KTLPNQGSST EVPGNSHPRD PPGLPEDSDL ATALHRLSLR RQNYLSEKQF 
       510        520        530        540        550
FAEEWERKLQ ILAEQEEEVS SCEALTENLA SFCTDQSETT ELGSAGCLRG 
       560        570        580        590        600
FMPEKLQIVK PLEGSQTLHH WQQLAQPNLG TILDPRPGVI TKGFTQMPKD 
       610        620        630        640        650
AVYHISDLEE DEEVGITFQV QQPLQLEQKP APPPPVTGIF LPPMTSAGGP 
       660        670 
VSALVSHHCP VEAVRAVHPT RL                               

<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

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

• 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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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