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

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each <span class="caps">DNA</span>-binding domain present within the protein.</p><p><a href='../manual/dna_bind' target='_top'>More...</a></p>DNA bindingi	641 – 653	13	A.T hook 1			Add BLAST
<p>Specifies the position and type of each <span class="caps">DNA</span>-binding domain present within the protein.</p><p><a href='../manual/dna_bind' target='_top'>More...</a></p>DNA bindingi	662 – 674	13	A.T hook 2			Add BLAST
<p>Specifies the position and type of each <span class="caps">DNA</span>-binding domain present within the protein.</p><p><a href='../manual/dna_bind' target='_top'>More...</a></p>DNA bindingi	1176 – 1188	13	A.T hook 3			Add BLAST
<p>Specifies the position and type of each <span class="caps">DNA</span>-binding domain present within the protein.</p><p><a href='../manual/dna_bind' target='_top'>More...</a></p>DNA bindingi	1390 – 1402	13	A.T hook 4			Add BLAST
<p>Specifies the position(s) and type(s) of zinc fingers within the protein.</p><p><a href='../manual/zn_fing' target='_top'>More...</a></p>Zinc fingeri	1662 – 1712	51	PHD-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00146			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. DNA 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

   • 11532953

2. lysine-acetylated histone 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

   • 16085498
   • 19578370

3. RNA 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

   • 18600236
   • 19578370

4. zinc ion binding Source: InterPro

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. chromatin remodeling Source: MGI

   <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ

   • 11532953

2. chromatin silencing at rDNA 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

   • 12198165
   • 16085498
   • 19578370

3. DNA methylation 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

   • 16085498
   • 19578370

4. heterochromatin assembly involved in chromatin silencing 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

   • 16678107

5. histone deacetylation 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

   • 12198165

6. histone H3-K9 methylation 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

   • 16678107

7. histone H4 deacetylation 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

   • 16678107

8. histone H4-K20 methylation 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

   • 16678107

9. transcription, DNA-templated Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Ligandⁱ

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. chromatin silencing complex 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

   • 16085498
   • 19578370

2. nucleolus 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

   • 16085498
   • 18600236
   • 19578370

3. rDNA heterochromatin 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

   • 12198165
   • 19578370

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Cellular componentⁱ

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	570 – 571	2	WY → GA: Impairs interaction with pRNA and heterochromatin formation but retains ability to trigger DNA methylation and silence rDNA transcription. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "Intergenic transcripts regulate the epigenetic state of rRNA genes." Mayer C., Schmitz K.-M., Li J., Grummt I., Santoro R. Mol. Cell 22:351-361(2006) [PubMed] [Europe PMC] [Abstract] Cited for: RNA-BINDING, DOMAIN MBD, MUTAGENESIS OF 570-TRP-TYR-571. Ref.10 "Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing." Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I. Nat. Cell Biol. 11:1010-1016(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 570-TRP-TYR-571 AND LYS-672.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	672 – 672	1	K → R: Abolishes acetylation by KAT8/MOF, leading to increase interaction with TTF1 and association with pRNA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.10 "Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing." Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I. Nat. Cell Biol. 11:1010-1016(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 570-TRP-TYR-571 AND LYS-672.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	1814 – 1814	1	Y → F: Impairs binding to chromatin. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.4 "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription." Zhou Y., Santoro R., Grummt I. EMBO J. 21:4632-4640(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1 AND SIN3A, MUTAGENESIS OF TYR-1814.

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 1889	1889	Bromodomain adjacent to zinc finger domain protein 2A		PRO_0000211173	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	134 – 134	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	501 – 501	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	672 – 672	1	N6-acetyllysine; by KAT81 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.10 "Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing." Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I. Nat. Cell Biol. 11:1010-1016(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 570-TRP-TYR-571 AND LYS-672.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	790 – 790	1	N6-acetyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.11 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1383 – 1383	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1545 – 1545	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1733 – 1733	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1755 – 1755	1	PhosphoserineBy similarity
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1767 – 1767	1	PhosphoserineBy similarity

<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - PTMⁱ

Proteomic databases

PTM databases

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

Gene expression databases

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

<p>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 ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

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

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	538 – 609	72	MBDPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00338			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	839 – 904	66	DDTPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00063			Add BLAST
<p>Describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.</p><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	1794 – 1864	71	BromoPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00035			Add BLAST

Coiled coil

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Denotes the positions of regions of coiled coil within the protein.</p><p><a href='../manual/coiled' target='_top'>More...</a></p>Coiled coili	686 – 813	128	Sequence Analysis			Add BLAST

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	652 – 777	126	Lys-rich			Add BLAST
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	1045 – 1051	7	Poly-Glu

<p>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><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Zinc finger

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position(s) and type(s) of zinc fingers within the protein.</p><p><a href='../manual/zn_fing' target='_top'>More...</a></p>Zinc fingeri	1662 – 1712	51	PHD-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00146			Add BLAST

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)ⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry describes 3<p>Lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.</p><p><a href='../manual/alternative_products' target='_top'>More...</a></p> isoformsⁱ produced by alternative splicing. Align

        10         20         30         40         50
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN 
        60         70         80         90        100
GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS 
       110        120        130        140        150
ANPGNNLKDP PLLSQFPGGQ YPLNGILGGN RQPSSPSHNT NLRAGSQEFW 
       160        170        180        190        200
ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI 
       210        220        230        240        250
QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL EEEQPELKMC 
       260        270        280        290        300
GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 
       310        320        330        340        350
PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA 
       360        370        380        390        400
FSLLADDSQT SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ 
       410        420        430        440        450
SSNFQRPLTE PAPDQPPSTQ LHPAVSPTAS PAASLTASAE ISPAVSPVAS 
       460        470        480        490        500
SPVPPEVFVA VSPASSPALP AISLEASMTT PVTSPQGSPE PSPAAAFQTV 
       510        520        530        540        550
SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT PEEVRLPLQH 
       560        570        580        590        600
GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE 
       610        620        630        640        650
HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN 
       660        670        680        690        700
EKAKNKEVPK VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA 
       710        720        730        740        750
KMTKNKKKMR QKVQRGESQT PVQGQARNKR KQDTKSLKQK DTKKKLKAEK 
       760        770        780        790        800
EKMKTKQEKL KEKVKREKKE KVKAKGKEGP RARPSCRADK TLATQKRLEE 
       810        820        830        840        850
QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR AFSDCLTIVE 
       860        870        880        890        900
FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH 
       910        920        930        940        950
DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR 
       960        970        980        990       1000
TQPFQAQPPQ QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV 
      1010       1020       1030       1040       1050
EGRLRRLKTA LAKRTGRPEV MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE 
      1060       1070       1080       1090       1100
ENTTAVHGRR GRKEGEIDVA ASSIPELERH IEKLSKRQLF FRKKLLHSSQ 
      1110       1120       1130       1140       1150
MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI KQETESLMEV 
      1160       1170       1180       1190       1200
VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR 
      1210       1220       1230       1240       1250
ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL 
      1260       1270       1280       1290       1300
SQSAFLSWLS QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ 
      1310       1320       1330       1340       1350
SCPGPQGPWF NFSAQIPCDA APTPPPAVSE DQPTPSLQLL ASSKPMNTPG 
      1360       1370       1380       1390       1400
AANPCSPVQL SSTHLPGGTP KRLSGDSEEM SQSPTGLGQP KRRGRPPSKF 
      1410       1420       1430       1440       1450
FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA LHPRGIREKA 
      1460       1470       1480       1490       1500
LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD 
      1510       1520       1530       1540       1550
LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP 
      1560       1570       1580       1590       1600
WRGRGREGTV PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV 
      1610       1620       1630       1640       1650
EKALLSTPNG APDGTSTEIS YEITPRVRVW RQTLERCRSA AQVCLCMGQL 
      1660       1670       1680       1690       1700
ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC DGCDRGCHIY CHRPKMEAVP 
      1710       1720       1730       1740       1750
EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP EGDSRRRMLS 
      1760       1770       1780       1790       1800
RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW 
      1810       1820       1830       1840       1850
PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF 
      1860       1870       1880 
DNCQTFNEDD SEVGKAGHVM RRFFESRWEE FYQGKQANL            

        10         20         30         40         50
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN 
        60         70         80         90        100
GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS 
       110        120        130        140        150
ANPGNNLKDP PLLSQFPGGQ YPLNGILGGN RQPSSPSHNT NLRAGSQEFW 
       160        170        180        190        200
ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI 
       210        220        230        240        250
QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL EEEQPELKMC 
       260        270        280        290        300
GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 
       310        320        330        340        350
PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA 
       360        370        380        390        400
FSLLADDSQT SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ 
       410        420        430        440        450
SSNFQRPLTE PAPDQPPSTQ LHPAVSPTAS PAASLTASAE ISPAVSPVAS 
       460        470        480        490        500
SPVPPEVFVA VSPASSPALP AISLEASMTT PVTSPQGSPE PSPAAAFQTV 
       510        520        530        540        550
SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT PEEVRLPLQH 
       560        570        580        590        600
GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE 
       610        620        630        640        650
HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN 
       660        670        680        690        700
EKAKNKEVPK VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA 
       710        720        730        740        750
KMTKNKKKMR QKVQRGESQT PVQGQARNKR KQDTKSLKQK DTKKKLKAEK 
       760        770        780        790        800
EKMKTKQEKL KEKVKREKKE KVKAKGKEGP RARPSCRADK TLATQKRLEE 
       810        820        830        840        850
QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR AFSDCLTIVE 
       860        870        880        890        900
FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH 
       910        920        930        940        950
DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR 
       960        970        980        990       1000
TQPFQAQPPQ QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV 
      1010       1020       1030       1040       1050
EGRLRRLKTA LAKRTGRPEV MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE 
      1060       1070       1080       1090       1100
ENTTAVHGRR GRKEGEIDVA ASSIPELERH IEKLSKRQLF FRKKLLHSSQ 
      1110       1120       1130       1140       1150
MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI KQETESLMEV 
      1160       1170       1180       1190       1200
VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR 
      1210       1220       1230       1240       1250
ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL 
      1260       1270       1280       1290       1300
SQSAFLSWLS QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ 
      1310       1320       1330       1340       1350
SCPGPQGPWF NFSAQIPCDA APTPPPAVSE DQPTPSLQLL ASSKPMNTPG 
      1360       1370       1380       1390       1400
AANPCSPVQL SSTHLPGGTP KRLSGDSEEM SQSPTGLGQP KRRGRPPSKF 
      1410       1420       1430       1440       1450
FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA LHPRGIREKA 
      1460       1470       1480       1490       1500
LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD 
      1510       1520       1530       1540       1550
LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP 
      1560       1570       1580       1590       1600
WRGRGREGTV PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV 
      1610       1620       1630       1640       1650
EKALLSTPNG APDGTSTEIS YEITPRVRVW RQTLERCRSA AQVCLCMGQL 
      1660       1670       1680       1690       1700
ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC DGCDRGCHIY CHRPKMEAVP 
      1710       1720       1730       1740       1750
EGDWFCAVCL SQVEEEYTQR PGFPKRGQKR KSSFPLTFPE GDSRRRMLSR 
      1760       1770       1780       1790       1800
SRDSPAVPRY PEDGLSPPKR RRHSMRSHHS DLTFCEIILM EMESHDAAWP 
      1810       1820       1830       1840       1850
FLEPVNPRLV SGYRRVIKNP MDFSTMRERL LRGGYTSSEE FAADALLVFD 
      1860       1870       1880 
NCQTFNEDDS EVGKAGHVMR RFFESRWEEF YQGKQANL            

        10         20         30         40         50
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN 
        60         70         80         90        100
GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS 
       110        120        130        140        150
ANPGNNLKDP PLLSQFPGGQ YPLNGILGGN RQPSSPSHNT NLRAGSQEFW 
       160        170        180        190        200
ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI 
       210        220        230        240        250
QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL EEEQPELKMC 
       260        270        280        290        300
GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE 
       310        320        330        340        350
PFDSLAAAEP VSGSLYGIDD AELMGAEDKL PLEGNPVISA LDCPALSNAN 
       360        370        380        390        400
AFSLLADDSQ TSASIFVSPT SPPVLGESVL QDNSFGLNSC SDSEQEEIET 
       410        420        430        440        450
QSSNFQRPLT EPAPDQPPST QLHPAVSPTA SPAASLTASA EISPAVSPVA 
       460        470        480        490        500
SSPVPPEVFV AVSPASSPAL PAISLEASMT TPVTSPQGSP EPSPAAAFQT 
       510        520        530        540        550
VSPARKNVSS APKARADREE TTGGAVAVSG SGDVLKRRIA TPEEVRLPLQ 
       560        570        580        590        600
HGWRREVRIK KGSHRWQGET WYYGPCGKRM KQFPEVIKYL SRNVVHSVRR 
       610        620        630        640        650
EHFSFSPRMP VGDFFEERDT PEGLQWVQLS AEEIPSRIQA ITGKRGRPRN 
       660        670        680        690        700
NEKAKNKEVP KVKRGRGRPP KIKMPELLNK TDNRLPKKLE TQEILSEDDK 
       710        720        730        740        750
AKMTKNKKKM RQKVQRGESQ TPVQGQARNK RKQDTKSLKQ KDTKKKLKAE 
       760        770        780        790        800
KEKMKTKQEK LKEKVKREKK EKVKAKGKEG PRARPSCRAD KTLATQKRLE 
       810        820        830        840        850
EQQRQQAILE EMKKPTEGMC LSDHQPLPDF TRIPGLTLSS RAFSDCLTIV 
       860        870        880        890        900
EFLHSFGKVL GFDLTKDVPS LGVLQEGLLC QGDSLDKVQD LLVRLLKAAL 
       910        920        930        940        950
HDPGLPPYCQ SLKILGEKMS EIPLTRDNVS EILRCFLMAY RVEPPFCDSL 
       960        970        980        990       1000
RTQPFQAQPP QQKAAILAFL VHELNSSTII INEIDKTLES VSSCRKNKWI 
      1010       1020       1030       1040       1050
VEGRLRRLKT ALAKRTGRPE VMMEGAEDGL GRRRSSRIME ETSGIEEEEE 
      1060       1070       1080       1090       1100
EENTTAVHGR RGRKEGEIDV AASSIPELER HIEKLSKRQL FFRKKLLHSS 
      1110       1120       1130       1140       1150
QMLRAVSLGQ DRYRRHYWVL PYLAGIFVEG SEGSTVTEDE IKQETESLME 
      1160       1170       1180       1190       1200
VVTSTPSSAR ASVKRELTGS NASTSPARSR GRPRKPKPGS LQPQHLQSTI 
      1210       1220       1230       1240       1250
RECDSEQAQT QVHPEPQPQL QAPTQPHLQP SSGFLEPEGS PFSLGQSQHD 
      1260       1270       1280       1290       1300
LSQSAFLSWL SQTQSHNSLL SSSVLTPDSS PGKLDSAPSQ SLEEPEPDEA 
      1310       1320       1330       1340       1350
QSCPGPQGPW FNFSAQIPCD AAPTPPPAVS EDQPTPSLQL LASSKPMNTP 
      1360       1370       1380       1390       1400
GAANPCSPVQ LSSTHLPGGT PKRLSGDSEE MSQSPTGLGQ PKRRGRPPSK 
      1410       1420       1430       1440       1450
FFKQVEQHYL TQLTAQPIPP EMCSGWWWIR DPETLDVLLK ALHPRGIREK 
      1460       1470       1480       1490       1500
ALHKHLSKHK DFLQEVCLQP LTDPIFEPNE LPALEEGVMS WSPKEKTYET 
      1510       1520       1530       1540       1550
DLAVLQWVEE LEQRVVLSDL QIRGWTCPTP DSTREDLTYC EHLPDSPEDI 
      1560       1570       1580       1590       1600
PWRGRGREGT VPQRQNNNPL DLAVMRLAVL EQNVERRYLR EPLWAAHEVV 
      1610       1620       1630       1640       1650
VEKALLSTPN GAPDGTSTEI SYEITPRVRV WRQTLERCRS AAQVCLCMGQ 
      1660       1670       1680       1690       1700
LERSIAWEKS VNKVTCLVCR KGDNDEFLLL CDGCDRGCHI YCHRPKMEAV 
      1710       1720       1730       1740       1750
PEGDWFCAVC LSQQVEEEYT QRPGFPKRGQ KRKSSFPLTF PEGDSRRRML 
      1760       1770       1780       1790       1800
SRSRDSPAVP RYPEDGLSPP KRRRHSMRSH HSDLTFCEII LMEMESHDAA 
      1810       1820       1830       1840       1850
WPFLEPVNPR LVSGYRRVIK NPMDFSTMRE RLLRGGYTSS EEFAADALLV 
      1860       1870       1880       1890
FDNCQTFNED DSEVGKAGHV MRRFFESRWE EFYQGKQANL            

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	41 – 42	2	NF → SL in CAC69992. (PubMed:16141072)Curated

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	305 – 305	1	L → LA in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.1 "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-703 (ISOFORM 3).		VSP_037962
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	1712 – 1712	1	Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.3 "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H. DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1003-1889 (ISOFORM 2).		VSP_037963

Sequence databases

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Coding sequence diversityⁱ

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

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "The transcriptional landscape of the mammalian genome."
   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.

   , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
   Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-703 (ISOFORM 3).
   Strain: NOD.
   
2. "NoRC -- a novel member of mammalian ISWI-containing chromatin remodeling machines."
   Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R., Laengst G., Grummt I.
   EMBO J. 20:4892-4900(2001) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-1889 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA5 AND TTF1.
3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
   DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1003-1889 (ISOFORM 2).
   Tissue: Brain.
   
4. "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription."
   Zhou Y., Santoro R., Grummt I.
   EMBO J. 21:4632-4640(2002) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1 AND SIN3A, MUTAGENESIS OF TYR-1814.
5. "The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo."
   Nemeth A., Strohner R., Grummt I., Laengst G.
   Nucleic Acids Res. 32:4091-4099(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: INTERACTION WITH TTF1.
6. "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing."
   Zhou Y., Grummt I.
   Curr. Biol. 15:1434-1438(2005) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BROMO AND PHD-TYPE ZINC-FINGER, INTERACTION WITH DNMT1; DNM3B; HDAC1 AND SMARCA5.
7. "Intergenic transcripts regulate the epigenetic state of rRNA genes."
   Mayer C., Schmitz K.-M., Li J., Grummt I., Santoro R.
   Mol. Cell 22:351-361(2006) [PubMed] [Europe PMC] [Abstract]
   Cited for: RNA-BINDING, DOMAIN MBD, MUTAGENESIS OF 570-TRP-TYR-571.
8. "Large-scale phosphorylation analysis of mouse liver."
   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
   Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
   Tissue: Liver.
   
9. "The structure of NoRC-associated RNA is crucial for targeting the chromatin remodelling complex NoRC to the nucleolus."
   Mayer C., Neubert M., Grummt I.
   EMBO Rep. 9:774-780(2008) [PubMed] [Europe PMC] [Abstract]
   Cited for: SUBCELLULAR LOCATION, RNA-BINDING.
10. "Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing."
    Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.
    Nat. Cell Biol. 11:1010-1016(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 570-TRP-TYR-571 AND LYS-672.
11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
    

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Documents

1. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ