Histone H4 transcription factor

<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

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

• chromatin binding Source: Ensembl
• DNA 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.13

    "The histone gene cell cycle regulator HiNF-P is a unique zinc finger transcription factor with a novel conserved auxiliary DNA-binding motif."
    Medina R., Buck T., Zaidi S.K., Miele-Chamberland A., Lian J.B., Stein J.L., van Wijnen A.J., Stein G.S.
    Biochemistry 47:11415-11423(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, REGION, MUTAGENESIS OF TYR-381.
  • "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
    Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
    Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription factor activity Source: UniProtKB <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
  • "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
    Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
    Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]
• DNA-binding transcription repressor activity, RNA polymerase II-specific Source: Ensembl
• 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.6

    "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2."
    Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.
    J. Biol. Chem. 276:42632-42638(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MBD2.
• histone binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.7

    "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
    Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
    Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  • "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
    Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
    Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: Ensembl
• transcription coactivator activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.13

    "The histone gene cell cycle regulator HiNF-P is a unique zinc finger transcription factor with a novel conserved auxiliary DNA-binding motif."
    Medina R., Buck T., Zaidi S.K., Miele-Chamberland A., Lian J.B., Stein J.L., van Wijnen A.J., Stein G.S.
    Biochemistry 47:11415-11423(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, REGION, MUTAGENESIS OF TYR-381.
  • "CDK inhibitors selectively diminish cell cycle controlled activation of the histone H4 gene promoter by p220NPAT and HiNF-P."
    Mitra P., Ghule P.N., van der Deen M., Medina R., Xie R.L., Holmes W.F., Ye X., Nakayama K.I., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.
    J. Cell. Physiol. 219:438-448(2009) [PubMed] [Europe PMC] [Abstract]
• transcription regulatory region DNA binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Sequence-specific transcriptional repression by an MBD2-interacting zinc finger protein MIZF."
    Sekimata M., Homma Y.
    Nucleic Acids Res. 32:590-597(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
  • "Regulation of Rb gene expression by an MBD2-interacting zinc finger protein MIZF during myogenic differentiation."
    Sekimata M., Homma Y.
    Biochem. Biophys. Res. Commun. 325:653-659(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.9

    "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition."
    Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., Stein G.S.
    Mol. Cell. Biol. 25:6140-6153(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH NPAT, SUBCELLULAR LOCATION.
  • Ref.11

    "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.

GO - Biological processⁱ

• DNA damage checkpoint Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• DNA repair Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• establishment of protein localization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.9

    "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition."
    Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., Stein G.S.
    Mol. Cell. Biol. 25:6140-6153(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH NPAT, SUBCELLULAR LOCATION.
• G1/S transition of mitotic cell cycle Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.7

    "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
    Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
    Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
• in utero embryonic development Source: UniProtKB
• myoblast differentiation Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Regulation of Rb gene expression by an MBD2-interacting zinc finger protein MIZF during myogenic differentiation."
    Sekimata M., Homma Y.
    Biochem. Biophys. Res. Commun. 325:653-659(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of gene expression Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Regulation of Rb gene expression by an MBD2-interacting zinc finger protein MIZF during myogenic differentiation."
    Sekimata M., Homma Y.
    Biochem. Biophys. Res. Commun. 325:653-659(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.11

    "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• negative regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.6

    "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2."
    Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.
    J. Biol. Chem. 276:42632-42638(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MBD2.
  • Ref.8

    "Sequence-specific transcriptional repression by an MBD2-interacting zinc finger protein MIZF."
    Sekimata M., Homma Y.
    Nucleic Acids Res. 32:590-597(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
  • "Regulation of Rb gene expression by an MBD2-interacting zinc finger protein MIZF during myogenic differentiation."
    Sekimata M., Homma Y.
    Biochem. Biophys. Res. Commun. 325:653-659(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.12

    "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4 gene transcription."
    Mitra P., Xie R.-L., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.
    J. Cell. Biochem. 101:181-191(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• positive regulation of gene expression Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.7

    "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
    Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
    Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  • Ref.11

    "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• positive regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
    Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
    Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  • Ref.12

    "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4 gene transcription."
    Mitra P., Xie R.-L., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.
    J. Cell. Biochem. 101:181-191(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
  • Ref.11

    "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
    Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
    Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• regulation of gene expression Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.9

    "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition."
    Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., Stein G.S.
    Mol. Cell. Biol. 25:6140-6153(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH NPAT, SUBCELLULAR LOCATION.
• regulation of transcription, DNA-templated Source: UniProtKBInferred from mutant phenotypeⁱ
  • "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
    Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
    Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription involved in G1/S transition of mitotic cell cycle Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.9

    "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition."
    Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., Stein G.S.
    Mol. Cell. Biol. 25:6140-6153(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH NPAT, SUBCELLULAR LOCATION.
• transcription, DNA-templated 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

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

<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

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_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

GO - Molecular functionⁱ

• enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.6

    "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2."
    Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.
    J. Biol. Chem. 276:42632-42638(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MBD2.
• histone binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.7

    "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
    Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
    Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  • "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 gene: mechanistic differences between distinct H4 genes."
    Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., Soprano K.J., Stein J.L., Stein G.S.
    Mol. Biol. Rep. 25:1-12(1998) [PubMed] [Europe PMC] [Abstract]

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

Compositional bias

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_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 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MPPPGKVPRK ENLWLQCEWG SCSFVCSTME KFFEHVTQHL QQHLHGSGEE 
        60         70         80         90        100
EEEEEEDDPL EEEFSCLWQE CGFCSLDSSA DLIRHVYFHC YHTKLKQWGL 
       110        120        130        140        150
QALQSQADLG PCILDFQSRN VIPDIPDHFL CLWEHCENSF DNPEWFYRHV 
       160        170        180        190        200
EAHSLCCEYE AVGKDNPVVL CGWKGCTCTF KDRSKLREHL RSHTQEKVVA 
       210        220        230        240        250
CPTCGGMFAN NTKFLDHIRR QTSLDQQHFQ CSHCSKRFAT ERLLRDHMRN 
       260        270        280        290        300
HVNHYKCPLC DMTCPLPSSL RNHMRFRHSE DRPFKCDCCD YSCKNLIDLQ 
       310        320        330        340        350
KHLDTHSEEP AYRCDFENCT FSARSLCSIK SHYRKVHEGD SEPRYKCHVC 
       360        370        380        390        400
DKCFTRGNNL TVHLRKKHQF KWPSGHPRFR YKEHEDGYMR LQLVRYESVE 
       410        420        430        440        450
LTQQLLRQPQ EGSGLGTSLN ESSLQGIILE TVPGEPGRKE EEEEGKGSEG 
       460        470        480        490        500
TALSASQDNP SSVIHVVNQT NAQGQQEIVY YVLSEAPGEP PPAPEPPSGG 
       510 
IMEKLQGIAE EPEIQMV                                     

        10         20         30         40         50
MPPPGKVPRK ENLWLQCEWG SCSFVCSTME KFFEHVTQHL QQHLHGSGEE 
        60         70         80         90        100
EEEEEEDDPL EEEFSCLWQE CGFCSLDSSA DLIRHVYFHC YHTKLKQWGL 
       110        120        130        140        150
QALQSQADLG PCILDFQSRN VIPDIPDHFL CLWEHCENSF DNPEWFYRHV 
       160        170        180        190        200
EAHSLCCEYE AVGKDNPVVL CGWKGCTCTF KDRSKLREHL RSHTQEKVVA 
       210        220        230        240        250
CPTCGGMFAN NTKFLDHIRR QTSLDQQHFQ CSHCSKRFAT ERLLRDHMRN 
       260        270        280        290        300
HVNHYKCPLC DMTCPLPSSL RNHMRFRHSE DRPFKCDCCD YSCKNLIDLQ 
       310        320        330        340        350
KHLDTHSEEP AYRCDFENCT FSARSLCSIK SHYRKVHEGD SEPRYKCHVC 
       360        370        380        390        400
DKCFTRGNNL TVHLRKKHQF KWPSGHPRFR LGHFCIPLPG FAALYAPTSP 
       410 
GTRNMKMAIC GCSWFATRV                                   

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

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. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
2. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
4. Human chromosome 11
   Human chromosome 11: entries, gene names and cross-references to MIM