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Protein

Host cell factor 1

Gene

HCFC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Involved in control of the cell cycle (PubMed:10629049, PubMed:10779346, PubMed:15190068, PubMed:16624878, PubMed:23629655). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (PubMed:10675337, PubMed:12244100). Coactivator for EGR2 and GABP2 (PubMed:12244100, PubMed:14532282). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together (PubMed:12670868). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed:20200153). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition (PubMed:23629655).11 Publications
(Microbial infection) In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes.2 Publications

Caution

Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203).2 Publications

<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

  • activating transcription factor binding Source: CAFA
  • cadherin binding Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • distal enhancer DNA-binding transcription activator activity, RNA polymerase II-specific Source: Ensembl
  • DNA-binding transcription factor activity Source: ProtInc
  • identical protein binding Source: IntAct
  • protein binding, bridging Source: UniProtKB
  • sequence-specific double-stranded DNA binding Source: Ensembl
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

<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

Molecular functionChromatin regulator
Biological processCell cycle, Host-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-3214847 HATs acetylate histones
R-HSA-5689603 UCH proteinases

SIGNOR Signaling Network Open Resource

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SIGNORi
P51610

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HCFC1
Synonyms:HCF1, HFC1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000172534.13

Human Gene Nomenclature Database

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HGNCi
HGNC:4839 HCFC1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300019 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P51610

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

Mental retardation, X-linked 3 (MRX3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
See also OMIM:309541
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_069098225S → N in MRX3. 1 PublicationCorresponds to variant dbSNP:rs318240758EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi30P → S: Severely reduces VP16-induced complex (VIC) formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Abolishes interaction with CREB3. 1 Publication1
Mutagenesisi79P → S: Severely reduces VIC formation, but retains association with VP16. Severely reduces association with CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi82C → D: Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi105K → D: Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi134P → S: Eliminates VIC formation and association with VP16. Weak association with POU2F1. Unable to associate with CREBZF and BAP1. Unable to rescue proliferation in temperature-sensitive arrested cells. 3 Publications1
Mutagenesisi137R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi197P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi200R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi228R → D: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi252P → S: Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi255R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi289 – 291EWK → AAA: Minor reduction in VIC formation and association with VP16. Weak association with POU2F1. Severely reduces association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 1 Publication3
Mutagenesisi319P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi322R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi338S → A: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 1 Publication1
Mutagenesisi344 – 345RK → AA: Eliminates VIC formation, but only minor reduction in association with VP16. Unable to associate with POU2F1, but only minor reduction in association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. 1 Publication2
Mutagenesisi1017 – 1021PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat. 1 Publication5
Mutagenesisi1072V → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1073R → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1074V → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1075C → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1076S → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1077N → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1078P → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1079 – 1083PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat. 5
Mutagenesisi1079P → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1080C → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1081E → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1081E → D: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1082T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1082T → F: Reduces cleavage at HCF repeat. 1
Mutagenesisi1082T → S: Reduces cleavage at HCF repeat. 1
Mutagenesisi1083H → A: Reduces cleavage at HCF repeat. 1
Mutagenesisi1084E → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1085T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1086G → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1087T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1088T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1089N → A: Reduces cleavage at HCF repeat. 1
Mutagenesisi1090T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1092T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1093T → A: Inactivates cleavage at HCF repeat. 1
Mutagenesisi1095T → A: Reduces cleavage at HCF repeat. 1
Mutagenesisi1096S → A: No effect on cleavage at HCF repeat. 1
Mutagenesisi1097N → A: No effect on cleavage at HCF repeat. 1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
3054

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
HCFC1

MalaCards human disease database

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MalaCardsi
HCFC1
MIMi309541 phenotype

Open Targets

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OpenTargetsi
ENSG00000172534

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
369962 Methylmalonic acidemia with homocystinuria, type cblX
777 X-linked non-syndromic intellectual disability

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29215

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HCFC1

Domain mapping of disease mutations (DMDM)

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DMDMi
160332311

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000166112 – 1423HCF N-terminal chain 6Add BLAST1422
ChainiPRO_00000166122 – 1323HCF N-terminal chain 5Add BLAST1322
ChainiPRO_00000166132 – 1295HCF N-terminal chain 4Add BLAST1294
ChainiPRO_00000166142 – 1110HCF N-terminal chain 3Add BLAST1109
ChainiPRO_00000166152 – 1081HCF N-terminal chain 2Add BLAST1080
ChainiPRO_00000166162 – 1019HCF N-terminal chain 1Add BLAST1018
ChainiPRO_00000166171020 – 2035HCF C-terminal chain 1Add BLAST1016
ChainiPRO_00000166181082 – 2035HCF C-terminal chain 2Add BLAST954
ChainiPRO_00000166191111 – 2035HCF C-terminal chain 3Add BLAST925
ChainiPRO_00000166201296 – 2035HCF C-terminal chain 4Add BLAST740
ChainiPRO_00000166211324 – 2035HCF C-terminal chain 5Add BLAST712
ChainiPRO_00000166221424 – 2035HCF C-terminal chain 6Add BLAST612

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei6PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei288N6-acetyllysineCombined sources1
Cross-linki363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei411PhosphoserineCombined sources1
Modified residuei504Omega-N-methylarginineCombined sources1
Modified residuei524Omega-N-methylarginineCombined sources1
Modified residuei598PhosphoserineCombined sources1
Modified residuei666PhosphoserineCombined sources1
Modified residuei669PhosphoserineCombined sources1
Modified residuei813N6-acetyllysineCombined sources1
Modified residuei1205PhosphoserineCombined sources1
Modified residuei1219Omega-N-methylarginineCombined sources1
Modified residuei1224PhosphoserineCombined sources1
Modified residuei1491PhosphothreonineCombined sources1
Modified residuei1497PhosphoserineCombined sources1
Modified residuei1507PhosphoserineCombined sources1
Modified residuei1771PhosphoserineCombined sources1
Cross-linki1807Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1808Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1838PhosphoserineBy similarity1
Modified residuei2005N6-acetyllysineCombined sources1
Cross-linki2024Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<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

Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Further cleavage of the primary N- and C-terminal chains results in a 'trimming' and accumulation of the smaller chains. Cleavage is promoted by O-glycosylation.1 Publication
O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing.3 Publications
Ubiquitinated. Lys-1807 and Lys-1808 are ubiquitinated both via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by BAP1 does not seem to stabilize the protein.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1019 – 1020Cleavage; by autolysis2
Sitei1081 – 1082Cleavage; by autolysis2
Sitei1110 – 1111Cleavage; by autolysis2
Sitei1295 – 1296Cleavage; by autolysis2
Sitei1323 – 1324Cleavage; by autolysis2
Sitei1423 – 1424Cleavage; by autolysis2

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P51610

MaxQB - The MaxQuant DataBase

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MaxQBi
P51610

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P51610

PeptideAtlas

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PeptideAtlasi
P51610

PRoteomics IDEntifications database

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PRIDEi
P51610

ProteomicsDB human proteome resource

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ProteomicsDBi
56346
56347 [P51610-2]
56348 [P51610-3]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P51610-2 [P51610-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P51610

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P51610

<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

Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000172534 Expressed in 224 organ(s), highest expression level in adenohypophysis

CleanEx database of gene expression profiles

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CleanExi
HS_HCFC1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P51610 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51610 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA018312

<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

Composed predominantly of six polypeptides ranging from 110 to 150 kDa and a minor 300 kDa polypeptide (PubMed:10920196). The majority of N- and C-terminal cleavage products remain tightly, albeit non-covalently, associated (PubMed:10920196). Interacts with POU2F1, CREB3, ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2 (PubMed:9271389, PubMed:9389645, PubMed:10675337, PubMed:10976766, PubMed:10629049, PubMed:10871379, PubMed:10984507, PubMed:12244100, PubMed:14532282, PubMed:12670868, PubMed:15705566, PubMed:16624878). Component of a MLL1 complex, composed of at least the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15199122, PubMed:15960975). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed:20200153). Interacts directly with THAP3 (via its HBM) (PubMed:20200153). Interacts (via the Kelch-repeat domain) with THAP1 (via the HBM); the interaction recruits HCHC1 to the RRM1 (PubMed:20200153). Interacts directly with OGT; the interaction, which requires the HCFC1 cleavage site domain, glycosylates and promotes the proteolytic processing of HCFC1, retains OGT in the nucleus and impacts the expression of herpes simplex virus immediate early viral genes (PubMed:12670868, PubMed:21285374, PubMed:23353889). Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30 (PubMed:17998332, PubMed:18838538). Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (PubMed:19131338). Interacts with TET2 and TET3 (PubMed:23353889). Interacts with HCFC1R1 (PubMed:12235138). Interacts with THAP11 (By similarity). Interacts (via Kelch domain) with KMT2E/MLL5 isoform 3 (via HBM motif) (PubMed:23629655). Interacts with E2F1 (PubMed:23629655).By similarity24 Publications
(Microbial infection) Associates with the VP16-induced complex; binding to HCFC1 activates the viral transcriptional activator VP16 for association with POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the viral immediate early genes (PubMed:10629049). Interacts with the viral transactivator protein VP16 (PubMed:9271389, PubMed:9389645, PubMed:10629049).3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
109304, 112 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-809 NSL histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P51610

Database of interacting proteins

More...
DIPi
DIP-32955N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P51610

Protein interaction database and analysis system

More...
IntActi
P51610, 64 interactors

Molecular INTeraction database

More...
MINTi
P51610

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000309555

<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

12035
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P51610

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P51610

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati44 – 89Kelch 1Add BLAST46
Repeati93 – 140Kelch 2Add BLAST48
Repeati148 – 194Kelch 3Add BLAST47
Repeati217 – 265Kelch 4Add BLAST49
Repeati266 – 313Kelch 5Add BLAST48
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section 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><a href='/help/domain' target='_top'>More...</a></p>Domaini366 – 466Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST101
Repeati1010 – 1035HCF repeat 1Add BLAST26
Repeati1072 – 1097HCF repeat 2Add BLAST26
Repeati1101 – 1126HCF repeat 3Add BLAST26
Repeati1158 – 1183HCF repeat 4; degenerateAdd BLAST26
Repeati1286 – 1311HCF repeat 5Add BLAST26
Repeati1314 – 1339HCF repeat 6Add BLAST26
Repeati1349 – 1374HCF repeat 7; degenerateAdd BLAST26
Repeati1414 – 1439HCF repeat 8Add BLAST26
Domaini1797 – 1888Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST92
Domaini1890 – 2006Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni500 – 550Required for interaction with OGTAdd BLAST51
Regioni610 – 722Interaction with SIN3A1 PublicationAdd BLAST113
Regioni750 – 902Interaction with ZBTB171 PublicationAdd BLAST153
Regioni813 – 912Interaction with GABP21 PublicationAdd BLAST100

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The HCF repeat is a highly specific proteolytic cleavage signal.1 Publication
The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1.1 Publication

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4152 Eukaryota
ENOG410Y5AC LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000161383

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000293192

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG051888

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P51610

KEGG Orthology (KO)

More...
KOi
K14966

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P51610

TreeFam database of animal gene trees

More...
TreeFami
TF314757

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063 FN3, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.120.10.80, 2 hits
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR037854 HCFC1
IPR013783 Ig-like_fold
IPR015915 Kelch-typ_b-propeller
IPR006652 Kelch_1

The PANTHER Classification System

More...
PANTHERi
PTHR23244:SF339 PTHR23244:SF339, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01344 Kelch_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00060 FN3, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF117281 SSF117281, 2 hits
SSF49265 SSF49265, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 3 hits

<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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)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.

<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 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 describes 4 <p>This subsection of the ‘Sequence’ section 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><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P51610-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG
60 70 80 90 100
GNEGIVDELH VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM
110 120 130 140 150
VEYGKYSNDL YELQASRWEW KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY
160 170 180 190 200
LFGGLANDSE DPKNNIPRYL NDLYILELRP GSGVVAWDIP ITYGVLPPPR
210 220 230 240 250
ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL TWNKPSLSGV
260 270 280 290 300
APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
310 320 330 340 350
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ
360 370 380 390 400
VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY
410 420 430 440 450
DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLLPQ
460 470 480 490 500
AAPAPPTTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL
510 520 530 540 550
VTMRPASQAG KAPVTVTSLP AGVRMVVPTQ SAQGTVIGSS PQMSGMAALA
560 570 580 590 600
AAAAATQKIP PSSAPTVLSV PAGTTIVKTM AVTPGTTTLP ATVKVASSPV
610 620 630 640 650
MVSNPATRML KTAAAQVGTS VSSATNTSTR PIITVHKSGT VTVAQQAQVV
660 670 680 690 700
TTVVGGVTKT ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ
710 720 730 740 750
ASTGPVTQII QTKGPLPAGT ILKLVTSADG KPTTIITTTQ ASGAGTKPTI
760 770 780 790 800
LGISSVSPST TKPGTTTIIK TIPMSAIITQ AGATGVTSSP GIKSPITIIT
810 820 830 840 850
TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG QPGTILRTVP
860 870 880 890 900
MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGGH
910 920 930 940 950
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT
960 970 980 990 1000
MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG
1010 1020 1030 1040 1050
QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC
1060 1070 1080 1090 1100
DRQEAAASLV TSTVGQQNGS VVRVCSNPPC ETHETGTTNT ATTATSNMAG
1110 1120 1130 1140 1150
QHGCSNPPCE THETGTTNTA TTAMSSVGAN HQRDARRACA AGTPAVIRIS
1160 1170 1180 1190 1200
VATGALEAAQ GSKSQCQTRQ TSATSTTMTV MATGAPCSAG PLLGPSMARE
1210 1220 1230 1240 1250
PGGRSPAFVQ LAPLSSKVRL SSPSIKDLPA GRHSHAVSTA AMTRSSVGAG
1260 1270 1280 1290 1300
EPRMAPVCES LQGGSPSTTV TVTALEALLC PSATVTQVCS NPPCETHETG
1310 1320 1330 1340 1350
TTNTATTSNA GSAQRVCSNP PCETHETGTT HTATTATSNG GTGQPEGGQQ
1360 1370 1380 1390 1400
PPAGRPCETH QTTSTGTTMS VSVGALLPDA TSSHRTVESG LEVAAAPSVT
1410 1420 1430 1440 1450
PQAGTALLAP FPTQRVCSNP PCETHETGTT HTATTVTSNM SSNQDPPPAA
1460 1470 1480 1490 1500
SDQGEVESTQ GDSVNITSSS AITTTVSSTL TRAVTTVTQS TPVPGPSVPP
1510 1520 1530 1540 1550
PEELQVSPGP RQQLPPRQLL QSASTALMGE SAEVLSASQT PELPAAVDLS
1560 1570 1580 1590 1600
STGEPSSGQE SAGSAVVATV VVQPPPPTQS EVDQLSLPQE LMAEAQAGTT
1610 1620 1630 1640 1650
TLMVTGLTPE ELAVTAAAEA AAQAAATEEA QALAIQAVLQ AAQQAVMGTG
1660 1670 1680 1690 1700
EPMDTSEAAA TVTQAELGHL SAEGQEGQAT TIPIVLTQQE LAALVQQQQL
1710 1720 1730 1740 1750
QEAQAQQQHH HLPTEALAPA DSLNDPAIES NCLNELAGTV PSTVALLPST
1760 1770 1780 1790 1800
ATESLAPSNT FVAPQPVVVA SPAKLQAAAT LTEVANGIES LGVKPDLPPP
1810 1820 1830 1840 1850
PSKAPMKKEN QWFDVGVIKG TNVMVTHYFL PPDDAVPSDD DLGTVPDYNQ
1860 1870 1880 1890 1900
LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS
1910 1920 1930 1940 1950
KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQAGGELKS STPAQLAFMR
1960 1970 1980 1990 2000
VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG YGPATQVRWL
2010 2020 2030
QETSKDSSGT KPANKRPMSS PEMKSAPKKS KADGQ
Length:2,035
Mass (Da):208,732
Last modified:November 13, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0B0C581E2454631E
GO
Isoform 2 (identifier: P51610-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     382-450: Missing.

Note: The N- and the C-terminal fragments fail to associate. No experimental confirmation available.
Show »
Length:1,966
Mass (Da):201,850
Checksum:iA20A8EA295A5D9B5
GO
Isoform 3 (identifier: P51610-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     428-428: P → L
     429-2035: Missing.

Note: No experimental confirmation available.
Show »
Length:428
Mass (Da):47,189
Checksum:iF8514EA1A9FD8D49
GO
Isoform 4 (identifier: P51610-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1499-1499: P → PKISSMTETAPRALTTEVPIPAKITVTIANTETSDMPFSAVDILQ

Note: No experimental confirmation available.
Show »
Length:2,079
Mass (Da):213,405
Checksum:iF4C85542EA495848
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A6NEM2A6NEM2_HUMAN
Host cell factor 1
HCFC1
2,080Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C1C4H7C1C4_HUMAN
Host cell factor 1
HCFC1
611Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA55790 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section 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><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti564A → R in CAA55790 (PubMed:7829097).Curated1
Sequence conflicti603S → SVS in CAA55790 (PubMed:7829097).Curated1
Sequence conflicti665K → T no nucleotide entry (PubMed:7876203).Curated1
Sequence conflicti1638V → E no nucleotide entry (PubMed:7876203).Curated1
Sequence conflicti1685V → A no nucleotide entry (PubMed:7876203).Curated1
Sequence conflicti1735E → Q no nucleotide entry (PubMed:7876203).Curated1
Sequence conflicti1873G → A in CAA55790 (PubMed:7829097).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069098225S → N in MRX3. 1 PublicationCorresponds to variant dbSNP:rs318240758EnsemblClinVar.1
Natural variantiVAR_0198131164S → P1 PublicationCorresponds to variant dbSNP:rs1051152EnsemblClinVar.1
Natural variantiVAR_0500432004S → I. Corresponds to variant dbSNP:rs6643651Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section 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><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_002815382 – 450Missing in isoform 2. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_012984428P → L in isoform 3. 1 Publication1
Alternative sequenceiVSP_012985429 – 2035Missing in isoform 3. 1 PublicationAdd BLAST1607
Alternative sequenceiVSP_0471381499P → PKISSMTETAPRALTTEVPI PAKITVTIANTETSDMPFSA VDILQ in isoform 4. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L20010 mRNA No translation available.
U52112 Genomic DNA No translation available.
BC063435 mRNA Translation: AAH63435.1
X79198 Genomic DNA Translation: CAA55790.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS44020.1 [P51610-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40718

NCBI Reference Sequences

More...
RefSeqi
NP_005325.2, NM_005334.2 [P51610-1]
XP_006724879.1, XM_006724816.2 [P51610-4]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.83634

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000310441; ENSP00000309555; ENSG00000172534 [P51610-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3054

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3054

UCSC genome browser

More...
UCSCi
uc004fjp.4 human [P51610-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20010 mRNA No translation available.
U52112 Genomic DNA No translation available.
BC063435 mRNA Translation: AAH63435.1
X79198 Genomic DNA Translation: CAA55790.1 Different initiation.
CCDSiCCDS44020.1 [P51610-1]
PIRiA40718
RefSeqiNP_005325.2, NM_005334.2 [P51610-1]
XP_006724879.1, XM_006724816.2 [P51610-4]
UniGeneiHs.83634

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GO6X-ray2.70A/C360-402[»]
B/D1806-2035[»]
4N39X-ray1.76B1082-1097[»]
4N3AX-ray1.88B1072-1097[»]
4N3BX-ray2.17B1072-1097[»]
4N3CX-ray2.55B1072-1097[»]
5LWVX-ray1.90A1078-1095[»]
ProteinModelPortaliP51610
SMRiP51610
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109304, 112 interactors
ComplexPortaliCPX-809 NSL histone acetyltransferase complex
CORUMiP51610
DIPiDIP-32955N
ELMiP51610
IntActiP51610, 64 interactors
MINTiP51610
STRINGi9606.ENSP00000309555

PTM databases

iPTMnetiP51610
PhosphoSitePlusiP51610

Polymorphism and mutation databases

BioMutaiHCFC1
DMDMi160332311

Proteomic databases

EPDiP51610
MaxQBiP51610
PaxDbiP51610
PeptideAtlasiP51610
PRIDEiP51610
ProteomicsDBi56346
56347 [P51610-2]
56348 [P51610-3]
TopDownProteomicsiP51610-2 [P51610-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310441; ENSP00000309555; ENSG00000172534 [P51610-1]
GeneIDi3054
KEGGihsa:3054
UCSCiuc004fjp.4 human [P51610-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3054
DisGeNETi3054
EuPathDBiHostDB:ENSG00000172534.13

GeneCards: human genes, protein and diseases

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GeneCardsi
HCFC1
GeneReviewsiHCFC1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0056221
HGNCiHGNC:4839 HCFC1
HPAiHPA018312
MalaCardsiHCFC1
MIMi300019 gene
309541 phenotype
neXtProtiNX_P51610
OpenTargetsiENSG00000172534
Orphaneti369962 Methylmalonic acidemia with homocystinuria, type cblX
777 X-linked non-syndromic intellectual disability
PharmGKBiPA29215

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4152 Eukaryota
ENOG410Y5AC LUCA
GeneTreeiENSGT00940000161383
HOGENOMiHOG000293192
HOVERGENiHBG051888
InParanoidiP51610
KOiK14966
PhylomeDBiP51610
TreeFamiTF314757

Enzyme and pathway databases

ReactomeiR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-3214847 HATs acetylate histones
R-HSA-5689603 UCH proteinases
SIGNORiP51610

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
HCFC1 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Host_cell_factor_C1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
3054

Protein Ontology

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PROi
PR:P51610

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000172534 Expressed in 224 organ(s), highest expression level in adenohypophysis
CleanExiHS_HCFC1
ExpressionAtlasiP51610 baseline and differential
GenevisibleiP51610 HS

Family and domain databases

CDDicd00063 FN3, 2 hits
Gene3Di2.120.10.80, 2 hits
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR037854 HCFC1
IPR013783 Ig-like_fold
IPR015915 Kelch-typ_b-propeller
IPR006652 Kelch_1
PANTHERiPTHR23244:SF339 PTHR23244:SF339, 1 hit
PfamiView protein in Pfam
PF01344 Kelch_1, 1 hit
SMARTiView protein in SMART
SM00060 FN3, 3 hits
SUPFAMiSSF117281 SSF117281, 2 hits
SSF49265 SSF49265, 1 hit
PROSITEiView protein in PROSITE
PS50853 FN3, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHCFC1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P51610
Secondary accession number(s): Q6P4G5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: December 5, 2018
This is version 208 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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