Gremlin-1

<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

• BMP 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
  • Ref.10

    "Structure of Gremlin-1 and analysis of its interaction with BMP-2."
    Kisonaite M., Wang X., Hyvonen M.
    Biochem. J. 473:1593-1604(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-184, FUNCTION, SUBUNIT, INTERACTION WITH BMP2, DISULFIDE BONDS.
• cytokine activity Source: UniProtKB-KW
• morphogen activity Source: BHF-UCL <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• protein homodimerization activity 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

    "Structure of Gremlin-1 and analysis of its interaction with BMP-2."
    Kisonaite M., Wang X., Hyvonen M.
    Biochem. J. 473:1593-1604(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-184, FUNCTION, SUBUNIT, INTERACTION WITH BMP2, DISULFIDE BONDS.
• receptor ligand activity Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• transmembrane receptor protein tyrosine kinase activator activity Source: BHF-UCL
• vascular endothelial growth factor receptor 2 binding Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).

GO - Biological processⁱ

• apoptotic process Source: Ensembl
• cell-cell signaling Source: Ensembl
• cell migration involved in sprouting angiogenesis Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• cell morphogenesis Source: BHF-UCLInferred from direct assayⁱ
  • "The bone morphogenetic protein antagonist gremlin 1 is overexpressed in human cancers and interacts with YWHAH protein."
    Namkoong H., Shin S.M., Kim H.K., Ha S.A., Cho G.W., Hur S.Y., Kim T.E., Kim J.W.
    BMC Cancer 6:74-74(2006) [PubMed] [Europe PMC] [Abstract]
• collagen fibril organization Source: BHF-UCL <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• determination of dorsal identity Source: BHF-UCLInferred from mutant phenotypeⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• embryonic limb morphogenesis Source: Ensembl
• limb development Source: AgBaseInferred from mutant phenotypeⁱ
  • "The BMP antagonist Gremlin regulates outgrowth, chondrogenesis and programmed cell death in the developing limb."
    Merino R., Rodriguez-Leon J., Macias D., Ganan Y., Economides A.N., Hurle J.M.
    Development 126:5515-5522(1999) [PubMed] [Europe PMC] [Abstract]
• mesenchymal to epithelial transition involved in metanephros morphogenesis Source: Ensembl
• negative regulation of apoptotic process Source: AgBaseInferred from mutant phenotypeⁱ
  • "The BMP antagonist Gremlin regulates outgrowth, chondrogenesis and programmed cell death in the developing limb."
    Merino R., Rodriguez-Leon J., Macias D., Ganan Y., Economides A.N., Hurle J.M.
    Development 126:5515-5522(1999) [PubMed] [Europe PMC] [Abstract]
• negative regulation of BMP signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of bone mineralization Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of bone mineralization involved in bone maturation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of bone remodeling Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of bone trabecula formation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of canonical Wnt signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell growth Source: Ensembl
• negative regulation of chondrocyte differentiation Source: AgBaseInferred from mutant phenotypeⁱ
  • "The BMP antagonist Gremlin regulates outgrowth, chondrogenesis and programmed cell death in the developing limb."
    Merino R., Rodriguez-Leon J., Macias D., Ganan Y., Economides A.N., Hurle J.M.
    Development 126:5515-5522(1999) [PubMed] [Europe PMC] [Abstract]
• negative regulation of monocyte chemotaxis Source: BHF-UCL
• negative regulation of osteoblast differentiation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.10

    "Structure of Gremlin-1 and analysis of its interaction with BMP-2."
    Kisonaite M., Wang X., Hyvonen M.
    Biochem. J. 473:1593-1604(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-184, FUNCTION, SUBUNIT, INTERACTION WITH BMP2, DISULFIDE BONDS.
• negative regulation of osteoblast proliferation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of osteoclast proliferation Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCLInferred from direct assayⁱ
  • "Skeletal overexpression of gremlin impairs bone formation and causes osteopenia."
    Gazzerro E., Pereira R.C., Jorgetti V., Olson S., Economides A.N., Canalis E.
    Endocrinology 146:655-665(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transcription, DNA-templated Source: Ensembl
• positive regulation of angiogenesis Source: Ensembl
• positive regulation of branching involved in ureteric bud morphogenesis Source: Ensembl
• positive regulation of cardiac muscle cell differentiation Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• positive regulation of cell population proliferation Source: BHF-UCLInferred from direct assayⁱ
  • "The bone morphogenetic protein antagonist gremlin 1 is overexpressed in human cancers and interacts with YWHAH protein."
    Namkoong H., Shin S.M., Kim H.K., Ha S.A., Cho G.W., Hur S.Y., Kim T.E., Kim J.W.
    BMC Cancer 6:74-74(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of NF-kappaB transcription factor activity Source: Ensembl
• positive regulation of NIK/NF-kappaB signaling Source: Ensembl
• positive regulation of peptidyl-tyrosine autophosphorylation Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• positive regulation of receptor internalization Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• positive regulation of signaling receptor activity Source: BHF-UCL
• positive regulation of telomerase activity Source: BHF-UCLInferred from direct assayⁱ
  • "The bone morphogenetic protein antagonist gremlin 1 is overexpressed in human cancers and interacts with YWHAH protein."
    Namkoong H., Shin S.M., Kim H.K., Ha S.A., Cho G.W., Hur S.Y., Kim T.E., Kim J.W.
    BMC Cancer 6:74-74(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of transcription by RNA polymerase II Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• proximal/distal pattern formation Source: Ensembl
• regulation of epithelial to mesenchymal transition Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Bone morphogenetic protein-4 inhibitor gremlin is overexpressed in idiopathic pulmonary fibrosis."
    Koli K., Myllarniemi M., Vuorinen K., Salmenkivi K., Ryynanen M.J., Kinnula V.L., Keski-Oja J.
    Am. J. Pathol. 169:61-71(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of focal adhesion assembly Source: Ensembl
• signal transduction Source: BHF-UCL
• ureteric bud formation 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

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

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

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="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

• BMP binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Structure of Gremlin-1 and analysis of its interaction with BMP-2."
    Kisonaite M., Wang X., Hyvonen M.
    Biochem. J. 473:1593-1604(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-184, FUNCTION, SUBUNIT, INTERACTION WITH BMP2, DISULFIDE BONDS.
• cytokine activity Source: UniProtKB-KW
• morphogen activity Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.10

    "Structure of Gremlin-1 and analysis of its interaction with BMP-2."
    Kisonaite M., Wang X., Hyvonen M.
    Biochem. J. 473:1593-1604(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 72-184, FUNCTION, SUBUNIT, INTERACTION WITH BMP2, DISULFIDE BONDS.
• receptor ligand activity Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• vascular endothelial growth factor receptor 2 binding Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "The Xenopus dorsalizing factor Gremlin identifies a novel family of secreted proteins that antagonize BMP activities."
    Hsu D.R., Economides A.N., Wang X., Eimon P.M., Harland R.M.
    Mol. Cell 1:673-683(1998) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).

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

<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 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%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 (2+)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 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MSRTAYTVGA LLLLLGTLLP AAEGKKKGSQ GAIPPPDKAQ HNDSEQTQSP 
        60         70         80         90        100
QQPGSRNRGR GQGRGTAMPG EEVLESSQEA LHVTERKYLK RDWCKTQPLK 
       110        120        130        140        150
QTIHEEGCNS RTIINRFCYG QCNSFYIPRH IRKEEGSFQS CSFCKPKKFT 
       160        170        180 
TMMVTLNCPE LQPPTKKKRV TRVKQCRCIS IDLD                  

        10         20         30         40         50
MSRTAYTVGA LLLLLGTLLP AAEGKKKGSQ GAIPPPDKAL HVTERKYLKR 
        60         70         80         90        100
DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC 
       110        120        130        140 
SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD        

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

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

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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Human chromosome 15
   Human chromosome 15: entries, gene names and cross-references to MIM
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot