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Entry version 178 (22 Apr 2020)
Sequence version 2 (05 Sep 2006)
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Protein

ATPase MORC2

Gene

MORC2

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

Essential for epigenetic silencing by the HUSH (human silencing hub) complex. Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing (PubMed:28581500, PubMed:29440755). Represses germ cell-related genes and L1 retrotransposons in collaboration with SETDB1 and the HUSH complex, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). During DNA damage response, regulates chromatin remodeling through ATP hydrolysis. Upon DNA damage, is phosphorylated by PAK1, both colocalize to chromatin and induce H2AX expression. ATPase activity is required and dependent of phosphorylation by PAK1 and presence of DNA (PubMed:23260667). Recruits histone deacetylases, such as HDAC4, to promoter regions, causing local histone H3 deacetylation and transcriptional repression of genes such as CA9 (PubMed:20225202, PubMed:20110259). Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation (PubMed:24286864).7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ATPase activity is dependent of phosphorylation by PAK1 and presence of DNA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi39Magnesium1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei39ATP1 Publication1
Binding sitei427ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi87 – 89ATP1 Publication3
Nucleotide bindingi99 – 105ATP1 Publication7
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri490 – 544CW-typePROSITE-ProRule annotation1 PublicationAdd BLAST55

<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

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 functionHydrolase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-75105 Fatty acyl-CoA biosynthesis

<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%5Fand%5Ftaxonomy%5Fsection">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
Recommended name:
ATPase MORC2Curated (EC:3.6.1.33 Publications)
Alternative name(s):
MORC family CW-type zinc finger protein 2Curated
Zinc finger CW-type coiled-coil domain protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:MORC2Imported
Synonyms:KIAA0852, ZCWCC1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 22

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:23573 MORC2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
616661 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9Y6X9

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, 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

Charcot-Marie-Tooth disease 2Z (CMT2Z)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant, axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
Related information in OMIM
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_07645487S → L in CMT2Z; decreased ATPase activity; ATP-independent homodimerization; slightly increases HUSH-dependent gene silencing. 1 PublicationCorresponds to variant dbSNP:rs864309504EnsemblClinVar.1
Natural variantiVAR_07645596Q → E in CMT2Z; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs749060708EnsemblClinVar.1
Natural variantiVAR_076456236E → G in CMT2Z. 1 PublicationCorresponds to variant dbSNP:rs886037934EnsemblClinVar.1
Natural variantiVAR_076458252R → W in CMT2Z; slightly decreased ATPase activity; increased HUSH-dependent gene silencing in neuronal cells. 4 PublicationsCorresponds to variant dbSNP:rs864309503EnsemblClinVar.1
Natural variantiVAR_076460444G → R in CMT2Z; unknown pathological significance. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi18Y → A: Abolishes homodimerization. No effect on ATPase activity. Loss of HUSH-dependent gene silencing. 1 Publication1
Mutagenesisi39N → A: Loss of ATP-binding and ATPase activity. Does not homodimerizes. Seems to abolish chromatin compaction. 2 Publications1
Mutagenesisi68D → A: Loss of ATP-binding and ATPase activity. Loss of binding to ATP and ATPase activity; when associated with A-69. Unables chromatin remodeling. 2 Publications1
Mutagenesisi69D → A: No effect on binding to ATP and ATPase activity; when associated with A-68. 1 Publication1
Mutagenesisi266R → A: Increases HUSH-dependent gene silencing. 1 Publication1
Mutagenesisi319R → E: No effect on HUSH-dependent gene silencing. 1 Publication1
Mutagenesisi326R → E: Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-329 and E-333. 1 Publication1
Mutagenesisi329R → E: Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-326 and E-333. 1 Publication1
Mutagenesisi333R → E: Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-326 and E-329. 1 Publication1
Mutagenesisi344R → E: No effect on HUSH-dependent gene silencing. 1 Publication1
Mutagenesisi351R → E: No effect on HUSH-dependent gene silencing. 1 Publication1
Mutagenesisi358R → E: No effect on HUSH-dependent gene silencing. 1 Publication1
Mutagenesisi725S → A: No effect on phosphorylation by PAK1. 1 Publication1
Mutagenesisi730S → A: No effect on phosphorylation by PAK1. 1 Publication1
Mutagenesisi739S → A: Abolishes phosphorylation by PAK1. Not recruited on damaged chromatin. Loss of ATPase activity. Unables chromatin remodeling. Upon irradiation, increases levels of damaged DNA. 1 Publication1
Mutagenesisi773S → A: No effect on phosphorylation by PAK1. 1 Publication1

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

DisGeNET

More...
DisGeNETi
22880

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

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GeneReviewsi
MORC2

MalaCards human disease database

More...
MalaCardsi
MORC2
MIMi616688 phenotype

Open Targets

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OpenTargetsi
ENSG00000133422

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

More...
Orphaneti
466768 Autosomal dominant Charcot-Marie-Tooth disease type 2Z

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134986990

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9Y6X9 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MORC2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
114152840

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000965372 – 1032ATPase MORC2Add BLAST1031

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 residuei582PhosphothreonineCombined sources1
Modified residuei602PhosphoserineCombined sources1
Modified residuei615PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki652Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei696PhosphoserineCombined sources1
Cross-linki704Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei705PhosphoserineCombined sources1
Cross-linki716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei725PhosphoserineCombined sources1
Modified residuei730PhosphoserineCombined sources1
Modified residuei733PhosphothreonineCombined sources1
Modified residuei739Phosphoserine; by PAK1Combined sources1 Publication1
Modified residuei743PhosphoserineCombined sources1
Cross-linki767Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei777PhosphoserineCombined sources1
Modified residuei779PhosphoserineCombined sources1
Cross-linki819Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki932Glycyl 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%5Fprocessing%5Fsection">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

Phosphorylated by PAK1 at Ser-739 upon DNA damage. Phosphorylation is required for ATPase activity and recruitment to damaged chromatin.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9Y6X9

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Y6X9

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9Y6X9

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

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PaxDbi
Q9Y6X9

PeptideAtlas

More...
PeptideAtlasi
Q9Y6X9

PRoteomics IDEntifications database

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PRIDEi
Q9Y6X9

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
86822 [Q9Y6X9-1]
86823 [Q9Y6X9-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Y6X9

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

More...
PhosphoSitePlusi
Q9Y6X9

<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 smooth muscle, pancreas and testis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000133422 Expressed in testis and 231 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Y6X9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y6X9 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000133422 Tissue enhanced (testis)

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimerizes upon ATP-binding and dissociate upon ATP hydrolysis; homodimerization is required for gene silencing (PubMed:29440755).

Interacts with HDAC4 (PubMed:20110259).

Interacts with ACLY (PubMed:24286864).

Interacts with TASOR and MPHOSPH8; the interactions associate MORC2 with the HUSH complex which recruits MORC2 to heterochromatic loci (PubMed:28581500).

4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
116547, 21 interactors

Protein interaction database and analysis system

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IntActi
Q9Y6X9, 14 interactors

Molecular INTeraction database

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MINTi
Q9Y6X9

STRING: functional protein association networks

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STRINGi
9606.ENSP00000215862

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q9Y6X9 protein

<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

11032
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q9Y6X9

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili282 – 362Sequence analysisAdd BLAST81
Coiled coili547 – 584Sequence analysisAdd BLAST38
Coiled coili741 – 761Sequence analysisAdd BLAST21
Coiled coili966 – 1016Sequence analysisAdd BLAST51

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri490 – 544CW-typePROSITE-ProRule annotation1 PublicationAdd BLAST55

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1845 Eukaryota
ENOG411033B LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153998

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_011516_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Y6X9

Identification of Orthologs from Complete Genome Data

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OMAi
KEWFTGR

Database of Orthologous Groups

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OrthoDBi
193855at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9Y6X9

TreeFam database of animal gene trees

More...
TreeFami
TF329118

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.565.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036890 HATPase_C_sf
IPR041006 Morc_S5
IPR011124 Znf_CW

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17942 Morc6_S5, 1 hit
PF07496 zf-CW, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55874 SSF55874, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51050 ZF_CW, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: Q9Y6X9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI
60 70 80 90 100
YAERREDLRG GFMLCFLDDG AGMDPSDAAS VIQFGKSAKR TPESTQIGQY
110 120 130 140 150
GNGLKSGSMR IGKDFILFTK KEDTMTCLFL SRTFHEEEGI DEVIVPLPTW
160 170 180 190 200
NARTREPVTD NVEKFAIETE LIYKYSPFRT EEEVMTQFMK IPGDSGTLVI
210 220 230 240 250
IFNLKLMDNG EPELDIISNP RDIQMAETSP EGTKPERRSF RAYAAVLYID
260 270 280 290 300
PRMRIFIHGH KVQTKRLSCC LYKPRMYKYT SSRFKTRAEQ EVKKAEHVAR
310 320 330 340 350
IAEEKAREAE SKARTLEVRL GGDLTRDSRV MLRQVQNRAI TLRREADVKK
360 370 380 390 400
RIKEAKQRAL KEPKELNFVF GVNIEHRDLD GMFIYNCSRL IKMYEKVGPQ
410 420 430 440 450
LEGGMACGGV VGVVDVPYLV LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY
460 470 480 490 500
WKDIAIAQRG IIKFWDEFGY LSANWNQPPS SELRYKRRRA MEIPTTIQCD
510 520 530 540 550
LCLKWRTLPF QLSSVEKDYP DTWVCSMNPD PEQDRCEASE QKQKVPLGTF
560 570 580 590 600
RKDMKTQEEK QKQLTEKIRQ QQEKLEALQK TTPIRSQADL KKLPLEVTTR
610 620 630 640 650
PSTEEPVRRP QRPRSPPLPA VIRNAPSRPP SLPTPRPASQ PRKAPVISST
660 670 680 690 700
PKLPALAARE EASTSRLLQP PEAPRKPANT LVKTASRPAP LVQQLSPSLL
710 720 730 740 750
PNSKSPREVP SPKVIKTPVV KKTESPIKLS PATPSRKRSV AVSDEEEVEE
760 770 780 790 800
EAERRKERCK RGRFVVKEEK KDSNELSDSA GEEDSADLKR AQKDKGLHVE
810 820 830 840 850
VRVNREWYTG RVTAVEVGKH VVRWKVKFDY VPTDTTPRDR WVEKGSEDVR
860 870 880 890 900
LMKPPSPEHQ SLDTQQEGGE EEVGPVAQQA IAVAEPSTSE CLRIEPDTTA
910 920 930 940 950
LSTNHETIDL LVQILRNCLR YFLPPSFPIS KKQLSAMNSD ELISFPLKEY
960 970 980 990 1000
FKQYEVGLQN LCNSYQSRAD SRAKASEESL RTSERKLRET EEKLQKLRTN
1010 1020 1030
IVALLQKVQE DIDINTDDEL DAYIEDLITK GD
Length:1,032
Mass (Da):117,823
Last modified:September 5, 2006 - 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:i7BEFA46E4150ABF5
GO
Isoform 2 (identifier: Q9Y6X9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.

Show »
Length:970
Mass (Da):110,724
Checksum:i459161807B8B53F6
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
H7C1V1H7C1V1_HUMAN
ATPase MORC2
MORC2
191Annotation score:

Annotation score:2 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>
H7C3M1H7C3M1_HUMAN
ATPase MORC2
MORC2
89Annotation 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 AAC12954 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAA74875 differs from that shown. Intron retention.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07645487S → L in CMT2Z; decreased ATPase activity; ATP-independent homodimerization; slightly increases HUSH-dependent gene silencing. 1 PublicationCorresponds to variant dbSNP:rs864309504EnsemblClinVar.1
Natural variantiVAR_07645596Q → E in CMT2Z; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs749060708EnsemblClinVar.1
Natural variantiVAR_076456236E → G in CMT2Z. 1 PublicationCorresponds to variant dbSNP:rs886037934EnsemblClinVar.1
Natural variantiVAR_076457248Y → C1 PublicationCorresponds to variant dbSNP:rs1355363942Ensembl.1
Natural variantiVAR_076458252R → W in CMT2Z; slightly decreased ATPase activity; increased HUSH-dependent gene silencing in neuronal cells. 4 PublicationsCorresponds to variant dbSNP:rs864309503EnsemblClinVar.1
Natural variantiVAR_076459283R → H1 PublicationCorresponds to variant dbSNP:rs1482880426Ensembl.1
Natural variantiVAR_081260424T → R Probable disease-associated mutation found in a child with spinal atrophy-phenotype, cerebellar atrophy and diaphragmatic paralysis as well a second child with early onset cerebbellar ataxia, axonal polyneuropathy and nocturanl hypoventilation; increased ATPase activity; increased rate of dimer assembly and disassembly; decreased HUSH-dependent gene silencing. 3 Publications1
Natural variantiVAR_076460444G → R in CMT2Z; unknown pathological significance. 1 Publication1
Natural variantiVAR_076461466D → H1 Publication1
Natural variantiVAR_076462585R → C1 PublicationCorresponds to variant dbSNP:rs548292999EnsemblClinVar.1
Natural variantiVAR_076463757E → G1 PublicationCorresponds to variant dbSNP:rs774444542Ensembl.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0417591 – 62Missing in isoform 2. 2 PublicationsAdd BLAST62

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
AB020659 mRNA Translation: BAA74875.2 Sequence problems.
CR456469 mRNA Translation: CAG30355.1
AC004542 Genomic DNA Translation: AAC12954.1 Sequence problems.
AL133637 mRNA Translation: CAB63760.1
CH471095 Genomic DNA Translation: EAW59921.1
BC019257 mRNA Translation: AAH19257.3
BC136782 mRNA Translation: AAI36783.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS33636.1 [Q9Y6X9-2]
CCDS77668.1 [Q9Y6X9-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
T02436
T43455

NCBI Reference Sequences

More...
RefSeqi
NP_001290185.1, NM_001303256.2 [Q9Y6X9-1]
NP_001290186.1, NM_001303257.2
NP_055756.1, NM_014941.3 [Q9Y6X9-2]
XP_016884157.1, XM_017028668.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000215862; ENSP00000215862; ENSG00000133422 [Q9Y6X9-2]
ENST00000397641; ENSP00000380763; ENSG00000133422 [Q9Y6X9-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
22880

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:22880

UCSC genome browser

More...
UCSCi
uc003aje.2 human [Q9Y6X9-1]

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
AB020659 mRNA Translation: BAA74875.2 Sequence problems.
CR456469 mRNA Translation: CAG30355.1
AC004542 Genomic DNA Translation: AAC12954.1 Sequence problems.
AL133637 mRNA Translation: CAB63760.1
CH471095 Genomic DNA Translation: EAW59921.1
BC019257 mRNA Translation: AAH19257.3
BC136782 mRNA Translation: AAI36783.1
CCDSiCCDS33636.1 [Q9Y6X9-2]
CCDS77668.1 [Q9Y6X9-1]
PIRiT02436
T43455
RefSeqiNP_001290185.1, NM_001303256.2 [Q9Y6X9-1]
NP_001290186.1, NM_001303257.2
NP_055756.1, NM_014941.3 [Q9Y6X9-2]
XP_016884157.1, XM_017028668.1

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
5OF9X-ray1.81A/B1-603[»]
5OFAX-ray2.57A/B1-603[»]
5OFBX-ray2.02A/B1-603[»]
SMRiQ9Y6X9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi116547, 21 interactors
IntActiQ9Y6X9, 14 interactors
MINTiQ9Y6X9
STRINGi9606.ENSP00000215862

PTM databases

iPTMnetiQ9Y6X9
PhosphoSitePlusiQ9Y6X9

Polymorphism and mutation databases

BioMutaiMORC2
DMDMi114152840

Proteomic databases

EPDiQ9Y6X9
jPOSTiQ9Y6X9
MassIVEiQ9Y6X9
PaxDbiQ9Y6X9
PeptideAtlasiQ9Y6X9
PRIDEiQ9Y6X9
ProteomicsDBi86822 [Q9Y6X9-1]
86823 [Q9Y6X9-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
235 130 antibodies

The DNASU plasmid repository

More...
DNASUi
22880

Genome annotation databases

EnsembliENST00000215862; ENSP00000215862; ENSG00000133422 [Q9Y6X9-2]
ENST00000397641; ENSP00000380763; ENSG00000133422 [Q9Y6X9-1]
GeneIDi22880
KEGGihsa:22880
UCSCiuc003aje.2 human [Q9Y6X9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
22880
DisGeNETi22880

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MORC2
GeneReviewsiMORC2
HGNCiHGNC:23573 MORC2
HPAiENSG00000133422 Tissue enhanced (testis)
MalaCardsiMORC2
MIMi616661 gene
616688 phenotype
neXtProtiNX_Q9Y6X9
OpenTargetsiENSG00000133422
Orphaneti466768 Autosomal dominant Charcot-Marie-Tooth disease type 2Z
PharmGKBiPA134986990

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1845 Eukaryota
ENOG411033B LUCA
GeneTreeiENSGT00940000153998
HOGENOMiCLU_011516_0_0_1
InParanoidiQ9Y6X9
OMAiKEWFTGR
OrthoDBi193855at2759
PhylomeDBiQ9Y6X9
TreeFamiTF329118

Enzyme and pathway databases

ReactomeiR-HSA-75105 Fatty acyl-CoA biosynthesis

Miscellaneous databases

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

More...
ChiTaRSi
MORC2 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MORC2

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

More...
GenomeRNAii
22880
PharosiQ9Y6X9 Tbio

Protein Ontology

More...
PROi
PR:Q9Y6X9
RNActiQ9Y6X9 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000133422 Expressed in testis and 231 other tissues
ExpressionAtlasiQ9Y6X9 baseline and differential
GenevisibleiQ9Y6X9 HS

Family and domain databases

Gene3Di3.30.565.10, 1 hit
InterProiView protein in InterPro
IPR036890 HATPase_C_sf
IPR041006 Morc_S5
IPR011124 Znf_CW
PfamiView protein in Pfam
PF17942 Morc6_S5, 1 hit
PF07496 zf-CW, 1 hit
SUPFAMiSSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS51050 ZF_CW, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiMORC2_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: Q9Y6X9
Secondary accession number(s): B2RNB1, Q9UF28, Q9Y6V2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: September 5, 2006
Last modified: April 22, 2020
This is version 178 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, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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