MORC2
entrez
22880
canonical
uniprot
Q9Y6X9
canonical
ensembl
ENSG00000133422
resolver
ensp
ENSP00000215862
resolver
ensp
ENSP00000380763
resolver
ensp
ENSP00000681514
resolver
genesymbol
MORC2
resolver
genesymbol_syn
KIAA0852
resolver
genesymbol_syn
ZCWCC1
resolver
hgnc
HGNC:23573
resolver
uniprot
B2RNB1
resolver
uniprot
Q9UF28
resolver
uniprot
Q9Y6V2
resolver
uniprot_entry
MORC2_HUMAN
resolver
uniprot_sec
B2RNB1
resolver
uniprot_sec
Q9UF28
resolver
uniprot_sec
Q9Y6V2
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity depends on phosphorylation by PAK1 and the presence of DNA (PubMed:23260667, PubMed:40593625). {ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:40593625}.
uniprot
proteins
amino_acid_sequence
MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQFGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDTMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVEKFAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFNLKLMDNGEPELDIISNPRDIQMAETSPEGTKPERRSFRAYAAVLYIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRAEQEVKKAEHVARIAEEKAREAESKARTLEVRLGGDLTRDSRVMLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNFVFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGVVGVVDVPYLVLEPTHNKQDFADAKEYRHLLRAMGEHLAQYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRRRAMEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNPDPEQDRCEASEQKQKVPLGTFRKDMKTQEEKQKQLTEKIRQQQEKLEALQKTTPIRSQADLKKLPLEVTTRPSTEEPVRRPQRPRSPPLPAVIRNAPSRPPSLPTPRPASQPRKAPVISSTPKLPALAAREEASTSRLLQPPEAPRKPANTLVKTASRPAPLVQQLSPSLLPNSKSPREVPSPKVIKTPVVKKTESPIKLSPATPSRKRSVAVSDEEEVEEEAERRKERCKRGRFVVKEEKKDSNELSDSAGEEDSADLKRAQKDKGLHVEVRVNREWYTGRVTAVEVGKHVVRWKVKFDYVPTDTTPRDRWVEKGSEDVRLMKPPSPEHQSLDTQQEGGEEEVGPVAQQAIAVAEPSTSECLRIEPDTTALSTNHETIDLLVQILRNCLRYFLPPSFPISKKQLSAMNSDELISFPLKEYFKQYEVGLQNLCNSYQSRADSRAKASEESLRTSERKLRETEEKLQKLRTNIVALLQKVQEDIDINTDDELDAYIEDLITKGD
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, axonal, type 2Z (CMT2Z) [MIM:616688]: An 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. {ECO:0000269|PubMed:26497905, ECO:0000269|PubMed:26659848, ECO:0000269|PubMed:27329773, ECO:0000269|PubMed:28581500, ECO:0000269|PubMed:28771897, ECO:0000269|PubMed:29440755, ECO:0000269|PubMed:32693025}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental delay, impaired growth, dysmorphic facies, and axonal neuropathy (DIGFAN) [MIM:619090]: An autosomal dominant disease characterized by developmental delay, intellectual disability, hypotonia, poor growth, short stature, microcephaly, and variable craniofacial dysmorphism. Patients often present weakness, hyporeflexia, and electrophysiologic abnormalities consistent with an axonal sensorimotor peripheral neuropathy. Additional features may include hearing loss, pigmentary retinopathy, and abnormalities on brain imaging, including cerebral or cerebellar atrophy, hypomyelination, and lesions in the basal ganglia or brainstem. Disease severity is highly variable. {ECO:0000269|PubMed:32693025}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
function
FUNCTION: ATP-dependent chromatin remodeler essential for epigenetic silencing by the HUSH (human silencing hub) complex (PubMed:28581500, PubMed:29440755, PubMed:32693025, PubMed:40593625). Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing (PubMed:28581500, PubMed:29440755, PubMed:32693025). 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:20110259, PubMed:20225202). Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation (PubMed:24286864). Together with MPHOSPH8, mediates silencing of protocadherin genes in the nervous system (By similarity). {ECO:0000250|UniProtKB:Q69ZX6, ECO:0000269|PubMed:20110259, ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:24286864, ECO:0000269|PubMed:28581500, ECO:0000269|PubMed:29211708, ECO:0000269|PubMed:29440755, ECO:0000269|PubMed:32693025, ECO:0000269|PubMed:40593625}.
uniprot
proteins
mass_dalton
117823
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="Y->A: Abolishes homodimerization. No effect on ATPase activity. Loss of HUSH-dependent gene silencing."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 39; /note="N->A: Loss of ATP-binding and ATPase activity. Does not homodimerizes. Seems to abolish chromatin compaction."; /evidence="ECO:0000269|PubMed:28581500, ECO:0000269|PubMed:29440755"; MUTAGEN 68; /note="D->A: Loss of ATP-binding and ATPase activity. Loss of binding to ATP and ATPase activity; when associated with A-69. Prevents chromatin remodeling."; /evidence="ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:28581500"; MUTAGEN 69; /note="D->A: No effect on binding to ATP and ATPase activity; when associated with A-68."; /evidence="ECO:0000269|PubMed:23260667"; MUTAGEN 266; /note="R->A: Increases HUSH-dependent gene silencing."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 319; /note="R->E: No effect on HUSH-dependent gene silencing."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 326; /note="R->E: Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-329 and E-333."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 329; /note="R->E: Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-326 and E-333."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 333; /note="R->E: Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-326 and E-329."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 344; /note="R->E: No effect on HUSH-dependent gene silencing."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 351; /note="R->E: No effect on HUSH-dependent gene silencing."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 358; /note="R->E: No effect on HUSH-dependent gene silencing."; /evidence="ECO:0000269|PubMed:29440755"; MUTAGEN 725; /note="S->A: No effect on phosphorylation by PAK1."; /evidence="ECO:0000269|PubMed:23260667"; MUTAGEN 730; /note="S->A: No effect on phosphorylation by PAK1."; /evidence="ECO:0000269|PubMed:23260667"; MUTAGEN 739; /note="S->A: Abolishes phosphorylation by PAK1. Not recruited on damaged chromatin. Loss of ATPase activity. Prevents chromatin remodeling. Upon irradiation, increases levels of damaged DNA."; /evidence="ECO:0000269|PubMed:23260667"; MUTAGEN 773; /note="S->A: No effect on phosphorylation by PAK1."; /evidence="ECO:0000269|PubMed:23260667
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Ubiquitinated by herpes simplex virus 1/HHV-1 protein ICP0, leading to proteasomal degradation. {ECO:0000269|PubMed:39589886}.; PTM: Phosphorylated by PAK1 at Ser-739 upon DNA damage (PubMed:23260667). Phosphorylation is required for ATPase activity and recruitment to damaged chromatin (PubMed:23260667, PubMed:40593625). {ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:40593625}.
uniprot
proteins
pubmed
10048485
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20110259
uniprot
proteins
pubmed
20225202
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23260667
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24286864
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
26497905
uniprot
proteins
pubmed
26659848
uniprot
proteins
pubmed
27329773
uniprot
proteins
pubmed
27794525
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28402445
uniprot
proteins
pubmed
28581500
uniprot
proteins
pubmed
28771897
uniprot
proteins
pubmed
29211708
uniprot
proteins
pubmed
29440755
uniprot
proteins
pubmed
32693025
uniprot
proteins
pubmed
39589886
uniprot
proteins
pubmed
40593625
uniprot
proteins
sequence_length
1032
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:28581500}. Cytoplasm, cytosol {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:24286864}. Chromosome {ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:28581500}. Nucleus matrix {ECO:0000269|PubMed:23260667}. Note=Mainly located in the nucleus (PubMed:20225202). Upon phosphorylation at Ser-739, recruited to damaged chromatin (PubMed:23260667). {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:23260667}.
uniprot
proteins