Hcfc1
entrez
15161
canonical
uniprot
Q61191
canonical
ensembl
ENSMUSG00000031386
resolver
ensp
ENSMUSP00000033761
resolver
ensp
ENSMUSP00000110012
resolver
ensp
ENSMUSP00000160322
resolver
enst
ENSMUST00000033761
resolver
enst
ENSMUST00000114372
resolver
genesymbol
Hcfc1
resolver
uniprot
B1AUX1
resolver
uniprot
B1AUX2
resolver
uniprot
Q684R1
resolver
uniprot
Q7TSB0
resolver
uniprot
Q8C2D0
resolver
uniprot
Q9QWH2
resolver
uniprot_entry
B1AUX2_MOUSE
resolver
uniprot_entry
HCFC1_MOUSE
resolver
uniprot_sec
B1AUX1
resolver
uniprot_sec
Q684R1
resolver
uniprot_sec
Q7TSB0
resolver
uniprot_sec
Q8C2D0
resolver
uniprot_sec
Q9QWH2
resolver
amino_acid_sequence
MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIETLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPRARAGHCAVAINTRLYIWSGRDGYRKAWNNQVCCKDLWYLETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDIPATAATATSPTPNPVPSVPANPPKSPAPAAAAPAVQPLTQVGITLVPQAATAPPSTTTIQVLPTVPGSSISVPTAARTQGVPAVLKVTGPQATTGTPLVTMRPASQAGKAPVTVTSLPASVRMVVPTQSAQGTVIGSNPQMSGMAALAAAAAATQKIPPSSAPTVLSVPAGTTIVKTVAVTPGTTTLPATVKVASSPVMVSNPATRMLKTAAAQVGTSVSSAANTSTRPIITVHKSGTVTVAQQAQVVTTVVGGVTKTITLVKSPISVPGGSALISNLGKVMSVVQTKPVQTSAVTGQASTGPVTQIIQTKGPLPAGTILKLVTSADGKPTTIITTTQASGAGTKPTILGISSVSPSTTKPGTTTIIKTIPMSAIITQAGATGVTSSPGIKSPITIITTKVMTSGTGAPAKIITAVPKIATGHGQQGVTQVVLKGAPGQPGTILRTVPMGGVRLVTPVTVSAVKPAVTTLVVKGTTGVTTLGTVTGTVSTSLAGAGAHSTSASLATPITTLGTIATLSSQVINPTAITVSAAQTTLTAAGGLTTPTITMQPVSQPTQVTLITAPSGVEAQPVHDLPVSILASPTTEQPTATVTIADSGQGDVQPGTVTLVCSNPPCETHETGTTNTATTTVVANLGGHPQPTQVQFVCDRQETAASLVTSAVGQQNGNVVRVCSNPPCETHETGTTNTATTATSNMAGQHGCSNPPCETHETGTTSTATTAMSSMGTGQQRDTRRTTNTPTVVRITVAPGALERVQGTVKPQCQTQQTNMTTTTMTVQATGAPCSAGPLLRPSVALESGSHSPAFVQLALPSVRVGLSGPSSKDMPTGRQPETYHTYTTNTPTTTRSIMVAGELGAARVVPTSTYESLQASSPSSTMTMTALEALLCPSATVTQVCSNPPCETHETGTTNTATTSNAGSAQRVCSNPPCETHETGTTHTATTATSNGGAGQPEGGQQPASGHPCETHQTTSTGTTMSVSVGTLIPDATSSHGTLESGLEVVAVPTVTSQAGSTLLASFPTQRVCSNPPCETHETGTTHTATTVTSNMSSNQDPPPAASDQGEVASTQGDSTNITSASAITTSVSSTLPRAVTTVTQSTPVPGPSVPPPEELQVSPGPRQQLPPRQLLQSASTPLMGESTEVLSASQTPELQAAVDLSSTGDPSSGQEPTTSAVVATVVVQPPPPTQSEVDQLSLPQELMAEAQAGTTTLMVTGLTPEELAVTAAAEAAAQAAATEEAQALAIQAVLQAAQQAVMGTGEPMDTSEAAAAVTQAELGHLSAEGQEGQATTIPIVLTQQELAALVQQQQQLQEAQAQAQQQHHLPTEALAPADSLNDPSIESNCLNELASAVPSTVALLPSTATESLAPSNTFVAPQPVVASPAKMQAAATLTEVANGIESLGVKPDLPPPPSKAPVKKENQWFDVGVIKGTSVMVTHYFLPPDDAVQSDDDSGTVPDYNQLKKQELQPGTAYKFRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQASGEPKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIAARNEKGYGPATQVRWLQETSKDSSGTKPASKRPMSSPEMKSAPKKSKADGQ
uniprot
proteins
function
FUNCTION: Transcriptional coregulator (By similarity). Serves as a scaffold protein, bridging interactions between transcription factors, including THAP11 and ZNF143, and transcriptional coregulators (By similarity). Involved in control of the cell cycle (PubMed:9334261, PubMed:9990006). Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By similarity). 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 (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). Recruits KMT2E to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition (By similarity). Modulates expression of homeobox protein PDX1, perhaps acting in concert with transcription factor E2F1, thereby regulating pancreatic beta-cell growth and glucose-stimulated insulin secretion (By similarity). May negatively modulate transcriptional activity of FOXO3 (By similarity). {ECO:0000250|UniProtKB:D3ZN95, ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:9334261, ECO:0000269|PubMed:9990006}.
uniprot
proteins
mass_dalton
210437
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:P51610}.; PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing. {ECO:0000250|UniProtKB:P51610}.; PTM: Ubiquitinated. Lys-1817 and Lys-1818 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. {ECO:0000250|UniProtKB:P51610}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16452088
uniprot
proteins
pubmed
18585351
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
9334261
uniprot
proteins
pubmed
9990006
uniprot
proteins
sequence_length
2045
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51610}. Cytoplasm {ECO:0000269|PubMed:9990006}. Note=HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm (By similarity). Localizes to cytoplasm in trigeminal ganglia (PubMed:9990006). Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER. {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:9990006}.; SUBCELLULAR LOCATION: Note=(Microbial infection) In trigeminal ganglia, becoming nuclear upon HSV reactivation from the latent state. {ECO:0000269|PubMed:9990006}.
uniprot
proteins