HCFC1
entrez
3054
canonical
uniprot
P51610
canonical
ensembl
ENSG00000172534
resolver
ensp
ENSP00000309555
resolver
ensp
ENSP00000359001
resolver
ensp
ENSP00000595256
resolver
ensp
ENSP00000595257
resolver
ensp
ENSP00000595258
resolver
ensp
ENSP00000595260
resolver
ensp
ENSP00000595261
resolver
ensp
ENSP00000595262
resolver
enst
ENST00000369984
resolver
genesymbol
HCFC1
resolver
genesymbol_syn
HCF1
resolver
genesymbol_syn
HFC1
resolver
hgnc
HGNC:4839
resolver
uniprot
A6NEM2
resolver
uniprot
Q6P4G5
resolver
uniprot_entry
A6NEM2_HUMAN
resolver
uniprot_entry
HCFC1_HUMAN
resolver
uniprot_sec
Q6P4G5
resolver
amino_acid_sequence
MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIDTLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPRARAGHCAVAINTRLYIWSGRDGYRKAWNNQVCCKDLWYLETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDIPATAATATSPTPNPVPSVPANPPKSPAPAAAAPAVQPLTQVGITLLPQAAPAPPTTTTIQVLPTVPGSSISVPTAARTQGVPAVLKVTGPQATTGTPLVTMRPASQAGKAPVTVTSLPAGVRMVVPTQSAQGTVIGSSPQMSGMAALAAAAAATQKIPPSSAPTVLSVPAGTTIVKTMAVTPGTTTLPATVKVASSPVMVSNPATRMLKTAAAQVGTSVSSATNTSTRPIITVHKSGTVTVAQQAQVVTTVVGGVTKTITLVKSPISVPGGSALISNLGKVMSVVQTKPVQTSAVTGQASTGPVTQIIQTKGPLPAGTILKLVTSADGKPTTIITTTQASGAGTKPTILGISSVSPSTTKPGTTTIIKTIPMSAIITQAGATGVTSSPGIKSPITIITTKVMTSGTGAPAKIITAVPKIATGHGQQGVTQVVLKGAPGQPGTILRTVPMGGVRLVTPVTVSAVKPAVTTLVVKGTTGVTTLGTVTGTVSTSLAGAGGHSTSASLATPITTLGTIATLSSQVINPTAITVSAAQTTLTAAGGLTTPTITMQPVSQPTQVTLITAPSGVEAQPVHDLPVSILASPTTEQPTATVTIADSGQGDVQPGTVTLVCSNPPCETHETGTTNTATTTVVANLGGHPQPTQVQFVCDRQEAAASLVTSTVGQQNGSVVRVCSNPPCETHETGTTNTATTATSNMAGQHGCSNPPCETHETGTTNTATTAMSSVGANHQRDARRACAAGTPAVIRISVATGALEAAQGSKSQCQTRQTSATSTTMTVMATGAPCSAGPLLGPSMAREPGGRSPAFVQLAPLSSKVRLSSPSIKDLPAGRHSHAVSTAAMTRSSVGAGEPRMAPVCESLQGGSPSTTVTVTALEALLCPSATVTQVCSNPPCETHETGTTNTATTSNAGSAQRVCSNPPCETHETGTTHTATTATSNGGTGQPEGGQQPPAGRPCETHQTTSTGTTMSVSVGALLPDATSSHRTVESGLEVAAAPSVTPQAGTALLAPFPTQRVCSNPPCETHETGTTHTATTVTSNMSSNQDPPPAASDQGEVESTQGDSVNITSSSAITTTVSSTLTRAVTTVTQSTPVPGPSVPPPEELQVSPGPRQQLPPRQLLQSASTALMGESAEVLSASQTPELPAAVDLSSTGEPSSGQESAGSAVVATVVVQPPPPTQSEVDQLSLPQELMAEAQAGTTTLMVTGLTPEELAVTAAAEAAAQAAATEEAQALAIQAVLQAAQQAVMGTGEPMDTSEAAATVTQAELGHLSAEGQEGQATTIPIVLTQQELAALVQQQQLQEAQAQQQHHHLPTEALAPADSLNDPAIESNCLNELAGTVPSTVALLPSTATESLAPSNTFVAPQPVVVASPAKLQAAATLTEVANGIESLGVKPDLPPPPSKAPMKKENQWFDVGVIKGTNVMVTHYFLPPDDAVPSDDDLGTVPDYNQLKKQELQPGTAYKFRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQAGGELKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIAARNEKGYGPATQVRWLQETSKDSSGTKPANKRPMSSPEMKSAPKKSKADGQ
uniprot
proteins
disease_involvement
DISEASE: Methylmalonic aciduria and homocystinuria, cblX type (MAHCX) [MIM:309541]: An X-linked recessive metabolic disorder characterized by severely delayed psychomotor development apparent in infancy, failure to thrive, impaired intellectual development, and intractable epilepsy. Additional features may include microcephaly and choreoathetosis. {ECO:0000269|PubMed:23000143}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:26416877). 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). 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:0000269|PubMed:10629049, ECO:0000269|PubMed:10675337, ECO:0000269|PubMed:10779346, ECO:0000269|PubMed:12244100, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:15190068, ECO:0000269|PubMed:16624878, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:23629655, ECO:0000269|PubMed:26416877}.; FUNCTION: (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. {ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:17578910}.
uniprot
proteins
mass_dalton
208732
uniprot
proteins
mutagenesis
MUTAGEN 30; /note="P->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."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 79; /note="P->S: Severely reduces VIC formation, but retains association with VP16. Severely reduces association with CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 82; /note="C->D: Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 105; /note="K->D: Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 134; /note="P->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."; /evidence="ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:19815555, ECO:0000269|PubMed:9271389"; MUTAGEN 137; /note="R->D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 197; /note="P->S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 200; /note="R->D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 228; /note="R->D: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 252; /note="P->S: Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 255; /note="R->D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 289..291; /note="EWK->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."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 319; /note="P->S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 322; /note="R->D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 338; /note="S->A: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 344..345; /note="RK->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."; /evidence="ECO:0000269|PubMed:10629049"; MUTAGEN 1017..1021; /note="PCETH->AAAAA: Reduces and disrupts cleavage at HCF repeat."; /evidence="ECO:0000269|PubMed:7590226"; MUTAGEN 1072; /note="V->A: No effect on cleavage at HCF repeat."; MUTAGEN 1073; /note="R->A: No effect on cleavage at HCF repeat."; MUTAGEN 1074; /note="V->A: No effect on cleavage at HCF repeat."; MUTAGEN 1075; /note="C->A: No effect on cleavage at HCF repeat."; MUTAGEN 1076; /note="S->A: No effect on cleavage at HCF repeat."; MUTAGEN 1077; /note="N->A: No effect on cleavage at HCF repeat."; MUTAGEN 1078; /note="P->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1079..1083; /note="PCETH->AAAAA: Reduces and disrupts cleavage at HCF repeat."; MUTAGEN 1079; /note="P->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1080; /note="C->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1081; /note="E->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1081; /note="E->D: Inactivates cleavage at HCF repeat."; MUTAGEN 1082; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1082; /note="T->F: Reduces cleavage at HCF repeat."; MUTAGEN 1082; /note="T->S: Reduces cleavage at HCF repeat."; MUTAGEN 1083; /note="H->A: Reduces cleavage at HCF repeat."; MUTAGEN 1084; /note="E->A: No effect on cleavage at HCF repeat."; MUTAGEN 1085; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1086; /note="G->A: No effect on cleavage at HCF repeat."; MUTAGEN 1087; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1088; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1089; /note="N->A: Reduces cleavage at HCF repeat."; MUTAGEN 1090; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1092; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1093; /note="T->A: Inactivates cleavage at HCF repeat."; MUTAGEN 1095; /note="T->A: Reduces cleavage at HCF repeat."; MUTAGEN 1096; /note="S->A: No effect on cleavage at HCF repeat."; MUTAGEN 1097; /note="N->A: No effect on cleavage at HCF repeat.
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats (PubMed:10920196, PubMed:21285374, PubMed:7590226). 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 (PubMed:21285374, PubMed:28302723, PubMed:28584052). {ECO:0000269|PubMed:10920196, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:28302723, ECO:0000269|PubMed:28584052, ECO:0000269|PubMed:7590226}.; PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing. {ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:28302723, ECO:0000269|PubMed:28584052}.; PTM: 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. {ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:19815555}.
uniprot
proteins
pubmed
10623756
uniprot
proteins
pubmed
10629049
uniprot
proteins
pubmed
10675337
uniprot
proteins
pubmed
10779346
uniprot
proteins
pubmed
10871379
uniprot
proteins
pubmed
10920196
uniprot
proteins
pubmed
10976766
uniprot
proteins
pubmed
10984507
uniprot
proteins
pubmed
12235138
uniprot
proteins
pubmed
12244100
uniprot
proteins
pubmed
12670868
uniprot
proteins
pubmed
14532282
uniprot
proteins
pubmed
15190068
uniprot
proteins
pubmed
15199122
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15705566
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
16624878
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17578910
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17998332
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18838538
uniprot
proteins
pubmed
19131338
uniprot
proteins
pubmed
19188440
uniprot
proteins
pubmed
19377461
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19815555
uniprot
proteins
pubmed
20018852
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20200153
uniprot
proteins
pubmed
20805357
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21285374
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23000143
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23353889
uniprot
proteins
pubmed
23629655
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24336203
uniprot
proteins
pubmed
26416877
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28302723
uniprot
proteins
pubmed
28584052
uniprot
proteins
pubmed
30664650
uniprot
proteins
pubmed
31905202
uniprot
proteins
pubmed
7590226
uniprot
proteins
pubmed
7829097
uniprot
proteins
pubmed
7876203
uniprot
proteins
pubmed
8392914
uniprot
proteins
pubmed
9271389
uniprot
proteins
pubmed
9389645
uniprot
proteins
pubmed
9990006
uniprot
proteins
sequence_length
2035
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12235138}. Nucleus {ECO:0000269|PubMed:10623756, ECO:0000269|PubMed:12235138, ECO:0000269|PubMed:19188440, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23629655}. Note=HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm (PubMed:12235138). Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER. {ECO:0000269|PubMed:12235138}.
uniprot
proteins