RC3H2
entrez
54542
canonical
uniprot
Q9HBD1
canonical
ensembl
ENSG00000056586
resolver
ensp
ENSP00000335150
resolver
ensp
ENSP00000349783
resolver
ensp
ENSP00000411767
resolver
ensp
ENSP00000555863
resolver
ensp
ENSP00000585963
resolver
ensp
ENSP00000709607
resolver
enst
ENST00000335387
resolver
genesymbol
RC3H2
resolver
genesymbol_syn
MNAB
resolver
genesymbol_syn
RNF164
resolver
hgnc
HGNC:21461
resolver
uniprot
A6NHN2
resolver
uniprot
Q4VXB1
resolver
uniprot
Q5JPD7
resolver
uniprot
Q86ST6
resolver
uniprot
Q8N3D6
resolver
uniprot
Q96F27
resolver
uniprot
Q9H5J2
resolver
uniprot
Q9HBD2
resolver
uniprot
Q9NWN9
resolver
uniprot
Q9NXE1
resolver
uniprot_entry
A6NHN2_HUMAN
resolver
uniprot_entry
RC3H2_HUMAN
resolver
uniprot_sec
Q4VXB1
resolver
uniprot_sec
Q5JPD7
resolver
uniprot_sec
Q86ST6
resolver
uniprot_sec
Q8N3D6
resolver
uniprot_sec
Q96F27
resolver
uniprot_sec
Q9H5J2
resolver
uniprot_sec
Q9HBD2
resolver
uniprot_sec
Q9NWN9
resolver
uniprot_sec
Q9NXE1
resolver
activity_regulation
ACTIVITY REGULATION: Binding to dsRNA, but not CDE RNA, crosstalks with the E3 ubiquitin ligase activity and may inhibit ubiquitination. {ECO:0000269|PubMed:26489670}.
uniprot
proteins
amino_acid_sequence
MPVQAAQWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQTAINTDIDVLPVNFALLQLVGAQVPDHQSIKLSNLGENKHYEVAKKCVEDLALYLKPLSGGKGVASLNQSALSRPMQRKLVTLVNCQLVEEEGRVRAMRAARSLGERTVTELILQHQNPQQLSANLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRSYEALRREHDAQIVHIAMEAGLRISPEQWSSLLYGDLAHKSHMQSIIDKLQSPESFAKSVQELTIVLQRTGDPANLNRLRPHLELLANIDPNPDAVSPTWEQLENAMVAVKTVVHGLVDFIQNYSRKGHETPQPQPNSKYKTSMCRDLRQQGGCPRGTNCTFAHSQEELEKYRLRNKKINATVRTFPLLNKVGVNNTVTTTAGNVISVIGSTETTGKIVPSTNGISNAENSVSQLISRSTDSTLRALETVKKVGKVGANGQNAAGPSADSVTENKIGSPPKTPVSNVAATSAGPSNVGTELNSVPQKSSPFLTRVPVYPPHSENIQYFQDPRTQIPFEVPQYPQTGYYPPPPTVPAGVAPCVPRFVRSNNVPESSLPPASMPYADHYSTFSPRDRMNSSPYQPPPPQPYGPVPPVPSGMYAPVYDSRRIWRPPMYQRDDIIRSNSLPPMDVMHSSVYQTSLRERYNSLDGYYSVACQPPSEPRTTVPLPREPCGHLKTSCEEQIRRKPDQWAQYHTQKAPLVSSTLPVATQSPTPPSPLFSVDFRADFSESVSGTKFEEDHLSHYSPWSCGTIGSCINAIDSEPKDVIANSNAVLMDLDSGDVKRRVHLFETQRRTKEEDPIIPFSDGPIISKWGAISRSSRTGYHTTDPVQATASQGSATKPISVSDYVPYVNAVDSRWSSYGNEATSSAHYVERDRFIVTDLSGHRKHSSTGDLLSLELQQAKSNSLLLQREANALAMQQKWNSLDEGRHLTLNLLSKEIELRNGELQSDYTEDATDTKPDRDIELELSALDTDEPDGQSEPIEEILDIQLGISSQNDQLLNGMAVENGHPVQQHQKEPPKQKKQSLGEDHVILEEQKTILPVTSCFSQPLPVSISNASCLPITTSVSAGNLILKTHVMSEDKNDFLKPVANGKMVNS
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression. Also recognizes CDE in its own mRNA and in that of paralogous RC3H1, possibly leading to feedback loop regulation (By similarity). miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression (PubMed:25697406). Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2B, UBE2D2, UBE2E2, UBE2E3, UBE2G2, UBE2K and UBE2Q2 and produces polyubiquitin chains (PubMed:26489670). Shows the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains (PubMed:26489670). Involved in the ubiquitination of MAP3K5 (PubMed:24448648, PubMed:26489670, PubMed:29186683). Able to interact with double-stranded RNA (dsRNA) (PubMed:26489670). {ECO:0000250|UniProtKB:P0C090, ECO:0000269|PubMed:24448648, ECO:0000269|PubMed:26489670, ECO:0000269|PubMed:29186683}.
uniprot
proteins
mass_dalton
131669
uniprot
proteins
mutagenesis
MUTAGEN 33; /note="C->S: Loss of activity. Loss of MAP3K5 ubiquitination."; /evidence="ECO:0000269|PubMed:24448648"; MUTAGEN 244..248; /note="QLLYR->ALLAA: Abolishes binding to CDERNA but not dsRNA."; /evidence="ECO:0000269|PubMed:26489670"; MUTAGEN 323; /note="S->E: Decreases dsRNA-binding."; /evidence="ECO:0000269|PubMed:26489670"; MUTAGEN 691; /note="Y->F: Impaired ability to interact with KLHL6."; /evidence="ECO:0000269|PubMed:29695787
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:24448648, ECO:0000269|PubMed:26489670}.
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved after Arg-509 and Arg-585 by MALT1 in activated CD4(+) T cells; cleavage at Arg-509 and Arg-585 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation. {ECO:0000250|UniProtKB:P0C090}.; PTM: Ubiquitinated by the BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex composed of at least CUL3, KLHL6 and RBX1; leading to proteasomal degradation. {ECO:0000269|PubMed:29695787}.
uniprot
proteins
pubmed
10938276
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20412057
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23550652
uniprot
proteins
pubmed
24448648
uniprot
proteins
pubmed
25697406
uniprot
proteins
pubmed
26249698
uniprot
proteins
pubmed
26489670
uniprot
proteins
pubmed
29186683
uniprot
proteins
pubmed
29695787
uniprot
proteins
sequence_length
1191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=During stress, such as that induced by arsenite, localizes to cytosolic stress granules. Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger. {ECO:0000269|PubMed:20412057}.
uniprot
proteins