P51610 (HCFC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Host cell factor 1
Short name=HCF
Short name=HCF-1

Alternative name(s):
C1 factor
CFF
VCAF
VP16 accessory protein

Cleaved into the following 12 chains:

1. HCF N-terminal chain 1
2. HCF N-terminal chain 2
3. HCF N-terminal chain 3
4. HCF N-terminal chain 4
5. HCF N-terminal chain 5
6. HCF N-terminal chain 6
7. HCF C-terminal chain 1
8. HCF C-terminal chain 2
9. HCF C-terminal chain 3
10. HCF C-terminal chain 4
11. HCF C-terminal chain 5
12. HCF C-terminal chain 6

Gene names

Name:	HCFC1
Synonyms:	HCF1, HFC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2035 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. 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. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. 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. Ref.6 Ref.10 Ref.11 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21 Ref.22 Ref.27 Ref.29 Ref.38 Ref.39
Subunit structure	Composed predominantly of six polypeptides ranging from 110 to 150 kDa and a minor 300 kDa polypeptide. The majority of N- and C-terminal cleavage products remain tightly, albeit non-covalently, associated. Interacts with POU2F1, CREB3, ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2. Component of a MLL1 complex, composed of at least the core components MLL, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8, PELP1, PHF20,. PRP31, RING2, RUVBL1, RUVBL2, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the MLL5-L complex, composed of at least MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Interacts directly with OGT; the interaction, which requires the HCFC1 cleavage site domain, glycosylates and promotes the proteolytic processing of HCFC1, retains OGT in the nucleus and impacts the expression of herpes simplex virus immediate early viral genes. Interacts with TET2 and TET3. Interacts directly with THAP3 (via its HBM). Interacts (via the Kelch-repeat domain) with THAP1 (via the HBM); the interaction recruits HCHC1 to the RRM1. Interacts with HCFC1R1 and THAP11. Associates with the VP16-induced complex; binding to HCFC1 activates the viral transcriptional activator VP16 for association with POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the viral immediate early genes. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with the viral transactivator protein VP16. Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.27 Ref.30 Ref.31 Ref.35 Ref.38 Ref.39 Ref.42 Ref.44
Subcellular location	Cytoplasm. Nucleus. Note: HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. Nuclear in general, but uniquely cytoplasmic in trigeminal ganglia, becoming nuclear upon HSV reactivation from the latent state. Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER. Ref.10 Ref.12 Ref.18 Ref.34 Ref.38 Ref.42
Tissue specificity	Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested. Ref.9
Domain	The HCF repeat is a highly specific proteolytic cleavage signal. Ref.18 The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1. Ref.18
Post-translational modification	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. Ref.6 Ref.7 Ref.27 Ref.42 O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing. Ref.39 Ref.42 Ref.44 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. Ref.33 Ref.34
Involvement in disease	Mental retardation, X-linked 3 (MRX3) [MIM:309541]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.45
Sequence similarities	Contains 5 Kelch repeats.
Sequence caution	The sequence CAA55790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Domain	Kelch repeat Repeat
Molecular function	Chromatin regulator
PTM	Acetylation Autocatalytic cleavage Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW histone H4-K16 acetylation Inferred from direct assay Ref.38. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.38. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.38. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell cycle Traceable author statement Ref.12. Source: UniProtKB positive regulation of gene expression Inferred from direct assay Ref.42. Source: UniProtKB protein stabilization Inferred from direct assay Ref.42. Source: UniProtKB regulation of protein complex assembly Inferred from direct assay Ref.11. Source: UniProtKB release from viral latency Non-traceable author statement Ref.11. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	MLL1 complex Inferred from direct assay Ref.24. Source: UniProtKB MLL5-L complex Inferred from direct assay Ref.35. Source: UniProtKB Set1C/COMPASS complex Inferred from direct assay Ref.30Ref.31. Source: UniProtKB histone acetyltransferase complex Inferred from direct assay Ref.38. Source: UniProtKB mitochondrion Inferred from direct assay. Source: HPA neuronal cell body Inferred from direct assay PubMed 20091349. Source: UniProtKB
Molecular_function	chromatin binding Inferred from direct assay Ref.42. Source: UniProtKB sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.1. Source: ProtInc transcription coactivator activity Inferred from mutant phenotype Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-396176,EBI-396176
ASH2L	Q9UBL3	4	EBI-396176,EBI-540797
CREB3	O43889	5	EBI-396176,EBI-625002
CREB3	O43889-2	4	EBI-396176,EBI-625022
CREBZF	Q9NS37	8	EBI-396176,EBI-632965
FOXO3	O43524	2	EBI-396176,EBI-1644164
GABPA	Q06546	2	EBI-396176,EBI-638925
GABPB1	Q06547	3	EBI-396176,EBI-618165
GABPB1	Q06547-2	6	EBI-396176,EBI-618189
HDAC1	Q13547	2	EBI-396176,EBI-301834
HDAC2	Q92769	2	EBI-396176,EBI-301821
OGT	O15294	9	EBI-396176,EBI-539828
SETD1A	O15047	2	EBI-396176,EBI-540779
SIN3A	Q96ST3	6	EBI-396176,EBI-347218
SIRT1	Q96EB6	2	EBI-396176,EBI-1802965
SP1	P08047	4	EBI-396176,EBI-298336
SUDS3	Q9H7L9	2	EBI-396176,EBI-540496
THAP11	Q96EK4	2	EBI-396176,EBI-1790529
WDR5	P61964	4	EBI-396176,EBI-540834
ZBTB17	Q13105	9	EBI-396176,EBI-372156

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P51610-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P51610-2)

The sequence of this isoform differs from the canonical sequence as follows:
     382-450: Missing.

Note: The N- and the C-terminal fragments fail to associate. No experimental confirmation available.

Isoform 3 (identifier: P51610-3)

The sequence of this isoform differs from the canonical sequence as follows:
     428-428: P → L
     429-2035: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.40
	Chain	2 – 1423	1422	HCF N-terminal chain 6		PRO_0000016611
	Chain	2 – 1323	1322	HCF N-terminal chain 5		PRO_0000016612
	Chain	2 – 1295	1294	HCF N-terminal chain 4		PRO_0000016613
	Chain	2 – 1110	1109	HCF N-terminal chain 3		PRO_0000016614
	Chain	2 – 1081	1080	HCF N-terminal chain 2		PRO_0000016615
	Chain	2 – 1019	1018	HCF N-terminal chain 1		PRO_0000016616
	Chain	1020 – 2035	1016	HCF C-terminal chain 1		PRO_0000016617
	Chain	1082 – 2035	954	HCF C-terminal chain 2		PRO_0000016618
	Chain	1111 – 2035	925	HCF C-terminal chain 3		PRO_0000016619
	Chain	1296 – 2035	740	HCF C-terminal chain 4		PRO_0000016620
	Chain	1324 – 2035	712	HCF C-terminal chain 5		PRO_0000016621
	Chain	1424 – 2035	612	HCF C-terminal chain 6		PRO_0000016622
Regions
	Repeat	44 – 89	46	Kelch 1
	Repeat	93 – 140	48	Kelch 2
	Repeat	148 – 194	47	Kelch 3
	Repeat	217 – 265	49	Kelch 4
	Repeat	266 – 313	48	Kelch 5
	Repeat	1010 – 1035	26	HCF repeat 1
	Repeat	1072 – 1097	26	HCF repeat 2
	Repeat	1101 – 1126	26	HCF repeat 3
	Repeat	1158 – 1183	26	HCF repeat 4; degenerate
	Repeat	1286 – 1311	26	HCF repeat 5
	Repeat	1314 – 1339	26	HCF repeat 6
	Repeat	1349 – 1374	26	HCF repeat 7; degenerate
	Repeat	1414 – 1439	26	HCF repeat 8
	Region	500 – 550	51	Required for interaction with OGT
	Region	610 – 722	113	Interaction with SIN3A
	Region	750 – 902	153	Interaction with ZBTB17
	Region	813 – 912	100	Interaction with GABP2
Sites
	Site	1019 – 1020	2	Cleavage; by autolysis
	Site	1081 – 1082	2	Cleavage; by autolysis
	Site	1110 – 1111	2	Cleavage; by autolysis
	Site	1295 – 1296	2	Cleavage; by autolysis
	Site	1323 – 1324	2	Cleavage; by autolysis
	Site	1423 – 1424	2	Cleavage; by autolysis
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.40 Ref.43
	Modified residue	6	1	Phosphoserine Ref.40 Ref.43
	Modified residue	288	1	N6-acetyllysine Ref.37
	Modified residue	411	1	Phosphoserine Ref.36
	Modified residue	666	1	Phosphoserine Ref.26 Ref.28 Ref.32 Ref.40 Ref.43
	Modified residue	669	1	Phosphoserine Ref.40
	Modified residue	813	1	N6-acetyllysine Ref.37
	Modified residue	1205	1	Phosphoserine Ref.32
	Modified residue	1491	1	Phosphothreonine Ref.26
	Modified residue	1507	1	Phosphoserine Ref.26 Ref.32 Ref.36 Ref.40 Ref.43
	Modified residue	2005	1	N6-acetyllysine Ref.37
	Cross-link	105		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33
	Cross-link	163		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33
	Cross-link	244		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33
	Cross-link	363		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33
	Cross-link	1807		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.34
	Cross-link	1808		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.34
Natural variations
	Alternative sequence	382 – 450	69	Missing in isoform 2.		VSP_002815
	Alternative sequence	428	1	P → L in isoform 3.		VSP_012984
	Alternative sequence	429 – 2035	1607	Missing in isoform 3.		VSP_012985
	Natural variant	225	1	S → N in MRX3. Ref.45		VAR_069098
	Natural variant	1164	1	S → P. Ref.5 Corresponds to variant rs1051152 [ dbSNP | Ensembl ].		VAR_019813
	Natural variant	2004	1	S → I. Corresponds to variant rs6643651 [ dbSNP | Ensembl ].		VAR_050043
Experimental info
	Mutagenesis	30	1	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. Ref.14
	Mutagenesis	79	1	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. Ref.14
	Mutagenesis	82	1	C → D: Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	105	1	K → D: Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	134	1	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. Ref.8 Ref.14 Ref.33
	Mutagenesis	137	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	197	1	P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	200	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	228	1	R → D: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	252	1	P → S: Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	255	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	289 – 291	3	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. Ref.14
	Mutagenesis	319	1	P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	322	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	338	1	S → A: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. Ref.14
	Mutagenesis	344 – 345	2	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.
	Mutagenesis	1017 – 1021	5	PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat. Ref.7
	Mutagenesis	1072	1	V → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1073	1	R → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1074	1	V → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1075	1	C → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1076	1	S → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1077	1	N → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1078	1	P → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1079 – 1083	5	PCETH → AAAAA: Reduces and disrupts cleavage at HCF repeat.
	Mutagenesis	1079	1	P → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1080	1	C → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1081	1	E → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1081	1	E → D: Inactivates cleavage at HCF repeat.
	Mutagenesis	1082	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1082	1	T → F: Reduces cleavage at HCF repeat.
	Mutagenesis	1082	1	T → S: Reduces cleavage at HCF repeat.
	Mutagenesis	1083	1	H → A: Reduces cleavage at HCF repeat.
	Mutagenesis	1084	1	E → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1085	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1086	1	G → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1087	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1088	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1089	1	N → A: Reduces cleavage at HCF repeat.
	Mutagenesis	1090	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1092	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1093	1	T → A: Inactivates cleavage at HCF repeat.
	Mutagenesis	1095	1	T → A: Reduces cleavage at HCF repeat.
	Mutagenesis	1096	1	S → A: No effect on cleavage at HCF repeat.
	Mutagenesis	1097	1	N → A: No effect on cleavage at HCF repeat.
	Sequence conflict	564	1	A → R in CAA55790. Ref.5
	Sequence conflict	603	1	S → SVS in CAA55790. Ref.5
	Sequence conflict	665	1	K → T no nucleotide entry Ref.2
	Sequence conflict	1638	1	V → E no nucleotide entry Ref.2
	Sequence conflict	1685	1	V → A no nucleotide entry Ref.2
	Sequence conflict	1735	1	E → Q no nucleotide entry Ref.2
	Sequence conflict	1873	1	G → A in CAA55790. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 0B0C581E2454631E	FASTA	2,035	208,732
	10 20 30 40 50 60 MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH 70 80 90 100 110 120 VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW 130 140 150 160 170 180 KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP 190 200 210 220 230 240 GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL 250 260 270 280 290 300 TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 310 320 330 340 350 360 LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE 370 380 390 400 410 420 TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV 430 440 450 460 470 480 PANPPKSPAP AAAAPAVQPL TQVGITLLPQ AAPAPPTTTT IQVLPTVPGS SISVPTAART 490 500 510 520 530 540 QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP AGVRMVVPTQ SAQGTVIGSS 550 560 570 580 590 600 PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTM AVTPGTTTLP ATVKVASSPV 610 620 630 640 650 660 MVSNPATRML KTAAAQVGTS VSSATNTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT 670 680 690 700 710 720 ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT 730 740 750 760 770 780 ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ 790 800 810 820 830 840 AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG 850 860 870 880 890 900 QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGGH 910 920 930 940 950 960 STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV 970 980 990 1000 1010 1020 TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET 1030 1040 1050 1060 1070 1080 HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQEAAASLV TSTVGQQNGS VVRVCSNPPC 1090 1100 1110 1120 1130 1140 ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTNTA TTAMSSVGAN HQRDARRACA 1150 1160 1170 1180 1190 1200 AGTPAVIRIS VATGALEAAQ GSKSQCQTRQ TSATSTTMTV MATGAPCSAG PLLGPSMARE 1210 1220 1230 1240 1250 1260 PGGRSPAFVQ LAPLSSKVRL SSPSIKDLPA GRHSHAVSTA AMTRSSVGAG EPRMAPVCES 1270 1280 1290 1300 1310 1320 LQGGSPSTTV TVTALEALLC PSATVTQVCS NPPCETHETG TTNTATTSNA GSAQRVCSNP 1330 1340 1350 1360 1370 1380 PCETHETGTT HTATTATSNG GTGQPEGGQQ PPAGRPCETH QTTSTGTTMS VSVGALLPDA 1390 1400 1410 1420 1430 1440 TSSHRTVESG LEVAAAPSVT PQAGTALLAP FPTQRVCSNP PCETHETGTT HTATTVTSNM 1450 1460 1470 1480 1490 1500 SSNQDPPPAA SDQGEVESTQ GDSVNITSSS AITTTVSSTL TRAVTTVTQS TPVPGPSVPP 1510 1520 1530 1540 1550 1560 PEELQVSPGP RQQLPPRQLL QSASTALMGE SAEVLSASQT PELPAAVDLS STGEPSSGQE 1570 1580 1590 1600 1610 1620 SAGSAVVATV VVQPPPPTQS EVDQLSLPQE LMAEAQAGTT TLMVTGLTPE ELAVTAAAEA 1630 1640 1650 1660 1670 1680 AAQAAATEEA QALAIQAVLQ AAQQAVMGTG EPMDTSEAAA TVTQAELGHL SAEGQEGQAT 1690 1700 1710 1720 1730 1740 TIPIVLTQQE LAALVQQQQL QEAQAQQQHH HLPTEALAPA DSLNDPAIES NCLNELAGTV 1750 1760 1770 1780 1790 1800 PSTVALLPST ATESLAPSNT FVAPQPVVVA SPAKLQAAAT LTEVANGIES LGVKPDLPPP 1810 1820 1830 1840 1850 1860 PSKAPMKKEN QWFDVGVIKG TNVMVTHYFL PPDDAVPSDD DLGTVPDYNQ LKKQELQPGT 1870 1880 1890 1900 1910 1920 AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI 1930 1940 1950 1960 1970 1980 IEYSVYLAIQ SSQAGGELKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII 1990 2000 2010 2020 2030 FRIAARNEKG YGPATQVRWL QETSKDSSGT KPANKRPMSS PEMKSAPKKS KADGQ
	Isoform 2 [UniParc]. Checksum: A20A8EA295A5D9B5	FASTA	1,966	201,850
	10 20 30 40 50 60 MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH 70 80 90 100 110 120 VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW 130 140 150 160 170 180 KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP 190 200 210 220 230 240 GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL 250 260 270 280 290 300 TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 310 320 330 340 350 360 LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE 370 380 390 400 410 420 TEKPPPPARV QLVRANTNSL EAAPAPPTTT TIQVLPTVPG SSISVPTAAR TQGVPAVLKV 430 440 450 460 470 480 TGPQATTGTP LVTMRPASQA GKAPVTVTSL PAGVRMVVPT QSAQGTVIGS SPQMSGMAAL 490 500 510 520 530 540 AAAAAATQKI PPSSAPTVLS VPAGTTIVKT MAVTPGTTTL PATVKVASSP VMVSNPATRM 550 560 570 580 590 600 LKTAAAQVGT SVSSATNTST RPIITVHKSG TVTVAQQAQV VTTVVGGVTK TITLVKSPIS 610 620 630 640 650 660 VPGGSALISN LGKVMSVVQT KPVQTSAVTG QASTGPVTQI IQTKGPLPAG TILKLVTSAD 670 680 690 700 710 720 GKPTTIITTT QASGAGTKPT ILGISSVSPS TTKPGTTTII KTIPMSAIIT QAGATGVTSS 730 740 750 760 770 780 PGIKSPITII TTKVMTSGTG APAKIITAVP KIATGHGQQG VTQVVLKGAP GQPGTILRTV 790 800 810 820 830 840 PMGGVRLVTP VTVSAVKPAV TTLVVKGTTG VTTLGTVTGT VSTSLAGAGG HSTSASLATP 850 860 870 880 890 900 ITTLGTIATL SSQVINPTAI TVSAAQTTLT AAGGLTTPTI TMQPVSQPTQ VTLITAPSGV 910 920 930 940 950 960 EAQPVHDLPV SILASPTTEQ PTATVTIADS GQGDVQPGTV TLVCSNPPCE THETGTTNTA 970 980 990 1000 1010 1020 TTTVVANLGG HPQPTQVQFV CDRQEAAASL VTSTVGQQNG SVVRVCSNPP CETHETGTTN 1030 1040 1050 1060 1070 1080 TATTATSNMA GQHGCSNPPC ETHETGTTNT ATTAMSSVGA NHQRDARRAC AAGTPAVIRI 1090 1100 1110 1120 1130 1140 SVATGALEAA QGSKSQCQTR QTSATSTTMT VMATGAPCSA GPLLGPSMAR EPGGRSPAFV 1150 1160 1170 1180 1190 1200 QLAPLSSKVR LSSPSIKDLP AGRHSHAVST AAMTRSSVGA GEPRMAPVCE SLQGGSPSTT 1210 1220 1230 1240 1250 1260 VTVTALEALL CPSATVTQVC SNPPCETHET GTTNTATTSN AGSAQRVCSN PPCETHETGT 1270 1280 1290 1300 1310 1320 THTATTATSN GGTGQPEGGQ QPPAGRPCET HQTTSTGTTM SVSVGALLPD ATSSHRTVES 1330 1340 1350 1360 1370 1380 GLEVAAAPSV TPQAGTALLA PFPTQRVCSN PPCETHETGT THTATTVTSN MSSNQDPPPA 1390 1400 1410 1420 1430 1440 ASDQGEVEST QGDSVNITSS SAITTTVSST LTRAVTTVTQ STPVPGPSVP PPEELQVSPG 1450 1460 1470 1480 1490 1500 PRQQLPPRQL LQSASTALMG ESAEVLSASQ TPELPAAVDL SSTGEPSSGQ ESAGSAVVAT 1510 1520 1530 1540 1550 1560 VVVQPPPPTQ SEVDQLSLPQ ELMAEAQAGT TTLMVTGLTP EELAVTAAAE AAAQAAATEE 1570 1580 1590 1600 1610 1620 AQALAIQAVL QAAQQAVMGT GEPMDTSEAA ATVTQAELGH LSAEGQEGQA TTIPIVLTQQ 1630 1640 1650 1660 1670 1680 ELAALVQQQQ LQEAQAQQQH HHLPTEALAP ADSLNDPAIE SNCLNELAGT VPSTVALLPS 1690 1700 1710 1720 1730 1740 TATESLAPSN TFVAPQPVVV ASPAKLQAAA TLTEVANGIE SLGVKPDLPP PPSKAPMKKE 1750 1760 1770 1780 1790 1800 NQWFDVGVIK GTNVMVTHYF LPPDDAVPSD DDLGTVPDYN QLKKQELQPG TAYKFRVAGI 1810 1820 1830 1840 1850 1860 NACGRGPFSE ISAFKTCLPG FPGAPCAIKI SKSPDGAHLT WEPPSVTSGK IIEYSVYLAI 1870 1880 1890 1900 1910 1920 QSSQAGGELK SSTPAQLAFM RVYCGPSPSC LVQSSSLSNA HIDYTTKPAI IFRIAARNEK 1930 1940 1950 1960 GYGPATQVRW LQETSKDSSG TKPANKRPMS SPEMKSAPKK SKADGQ
	Isoform 3 [UniParc]. Checksum: F8514EA1A9FD8D49	FASTA	428	47,189
	10 20 30 40 50 60 MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH 70 80 90 100 110 120 VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW 130 140 150 160 170 180 KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP 190 200 210 220 230 240 GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIDTL 250 260 270 280 290 300 TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 310 320 330 340 350 360 LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE 370 380 390 400 410 420 TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV PANPPKSL

References

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[1]	"The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein." Wilson A.C., Lamarco K., Peterson M.G., Herr W. Cell 74:115-125(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE. Tissue: Hepatoma.
[2]	"The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides." Kristie T.M., Pomerantz J.L., Twomey T.C., Parent S.A., Sharp P.A. J. Biol. Chem. 270:4387-4394(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Mammary gland.
[5]	"Genomic organization of the human VP16 accessory protein, a housekeeping gene (HCFC1) mapping to Xq28." Frattini A., Faranda S., Redolfi E., Zucchi I., Villa A., Patrosso M.C., Strina D., Susani L., Vezzoni P. Genomics 23:30-35(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-2035, VARIANT PRO-1164. Tissue: Fetal brain.
[6]	"Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): a potential role for proteolytic regulation of coactivator function." Vogel J.L., Kristie T.M. Proc. Natl. Acad. Sci. U.S.A. 97:9425-9430(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1324-1336; 1424-1436 AND 1446-1457, FUNCTION, AUTOCATALYTIC CLEAVAGE.
[7]	"The HCF repeat is an unusual proteolytic cleavage signal." Wilson A.C., Peterson M.G., Herr W. Genes Dev. 9:2445-2458(1995) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF 1017-PRO--HIS-1021 AND 1072-VAL--ASN-1097.
[8]	"Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor." Lu R., Yang P., O'Hare P., Misra V. Mol. Cell. Biol. 17:5117-5126(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CREB3 AND VP16, MUTAGENESIS OF PRO-134.
[9]	"Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP." Freiman R.N., Herr W. Genes Dev. 11:3122-3127(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CREB3 AND VP16, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[10]	"Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency." Kristie T.M., Vogel J.L., Sears A.E. Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation and mediates transcription activation by GABP." Vogel J.L., Kristie T.M. EMBO J. 19:683-690(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GABP2.
[12]	"Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency." Lu R., Misra V. J. Virol. 74:934-943(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening." Gunther M., Laithier M., Brison O. Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SP1.
[14]	"Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP." Mahajan S.S., Wilson A.C. Mol. Cell. Biol. 20:919-928(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH POU2F1; VP16 AND CREB3, MUTAGENESIS OF PRO-30; PRO-79; CYS-82; LYS-105; PRO-134; ARG-137; PRO-197; ARG-200; ARG-228; PRO-252; ARG-255; 289-GLU--LYS-291; PRO-319; ARG-322; SER-338 AND 344-ARG-LYS-345.
[15]	"A novel 50-kilodalton fragment of host cell factor 1 (C1) in G(0) cells." Scarr R.B., Smith M.R., Beddall M., Sharp P.A. Mol. Cell. Biol. 20:3568-3575(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Zhangfei: a second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16." Lu R., Misra V. Nucleic Acids Res. 28:2446-2454(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CREBZF.
[17]	"N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif." Luciano R.L., Wilson A.C. Proc. Natl. Acad. Sci. U.S.A. 97:10757-10762(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CREB3.
[18]	"Interaction of HCF-1 with a cellular nuclear export factor." Mahajan S.S., Little M.M., Vazquez R., Wilson A.C. J. Biol. Chem. 277:44292-44299(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH HCFC1R1. Tissue: Brain.
[19]	"Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1." Piluso D., Bilan P., Capone J.P. J. Biol. Chem. 277:46799-46808(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZBTB17.
[20]	"HCF-1 functions as a coactivator for the zinc finger protein Krox20." Luciano R.L., Wilson A.C. J. Biol. Chem. 278:51116-51124(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EGR2 AND E2F4.
[21]	"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SIN3A; HDAC1; HDAC2; SUDS3; SAP30; SIN3B; OGT; SET1; ASH2 AND WDR5.
[22]	"A protein sequestering system reveals control of cellular programs by the transcriptional coactivator HCF-1." Khurana B., Kristie T.M. J. Biol. Chem. 279:33673-33683(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression." Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L. Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1 COMPLEX.
[24]	"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF." Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G. Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1 COMPLEX.
[25]	"Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman." Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P. J. Biol. Chem. 280:15257-15266(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CREBZF AND CREB3.
[26]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-1491 AND SER-1507, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors." Vogel J.L., Kristie T.M. Proc. Natl. Acad. Sci. U.S.A. 103:6817-6822(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AUTOCATALYTIC CLEAVAGE, INTERACTION WITH FHL2.
[28]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesvirus immediate early promoters for initiation of infection." Narayanan A., Ruyechan W.T., Kristie T.M. Proc. Natl. Acad. Sci. U.S.A. 104:10835-10840(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes." Lee J.H., Skalnik D.G. Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A.
[31]	"Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS." Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A. Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN SET1 COMPLEX.
[32]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1205 AND SER-1507, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1." Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A. J. Biol. Chem. 284:34179-34188(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-105; LYS-163; LYS-244 AND LYS-363, DEUBIQUITINATION BY BAP1, MUTAGENESIS OF PRO-134.
[34]	"Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1." Misaghi S., Ottosen S., Izrael-Tomasevic A., Arnott D., Lamkanfi M., Lee J., Liu J., O'Rourke K., Dixit V.M., Wilson A.C. Mol. Cell. Biol. 29:2181-2192(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-1807 AND LYS-1808, DEUBIQUITINATION BY BAP1, SUBCELLULAR LOCATION.
[35]	"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis." Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S. Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
[36]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-1507, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[37]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-813 AND LYS-2005, MASS SPECTROMETRY.
[38]	"Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex." Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C. J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
[39]	"The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias." Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B., Kristie T.M., Girard J.P. J. Biol. Chem. 285:13364-13371(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX, INTERACTION WITH OGT; THAP1 AND THAP3, GLYCOSYLATION, FUNCTION.
[40]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-666; SER-669 AND SER-1507, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[41]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]	"Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway." Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G., Vogel J.L., Kristie T.M., Affar E.B. Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, INTERACTION WITH OGT.
[43]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-666 AND SER-1507, MASS SPECTROMETRY.
[44]	"TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS." Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N., Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., Levine R.L., Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., Fuks F. EMBO J. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, INTERACTION WITH OGT; TET2 AND TET3.
[45]	"A noncoding, regulatory mutation implicates HCFC1 in nonsyndromic intellectual disability." Huang L., Jolly L.A., Willis-Owen S., Gardner A., Kumar R., Douglas E., Shoubridge C., Wieczorek D., Tzschach A., Cohen M., Hackett A., Field M., Froyen G., Hu H., Haas S.A., Ropers H.H., Kalscheuer V.M., Corbett M.A., Gecz J. Am. J. Hum. Genet. 91:694-702(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRX3 ASN-225.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L20010 mRNA. No translation available.
U52112 Genomic DNA. No translation available.
BC063435 mRNA. Translation: AAH63435.1.
X79198 Genomic DNA. Translation: CAA55790.1. Different initiation.

IPI

IPI00019848.
IPI00219326.
IPI00847789.

PIR

A40718.

RefSeq

NP_005325.2. NM_005334.2.

UniGene

Hs.83634.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GO6	X-ray	2.70	A/C	360-402	[»]
			B/D	1806-2035	[»]

ProteinModelPortal

P51610.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51610. 41 interactions.

STRING

9606.ENSP00000309555.

PTM databases

PhosphoSite

P51610.

Polymorphism databases

DMDM

160332311.

Proteomic databases

PaxDb

P51610.

PRIDE

P51610.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310441; ENSP00000309555; ENSG00000172534.
ENST00000354233; ENSP00000346174; ENSG00000172534.
ENST00000596798; ENSP00000470486; ENSG00000268768.
ENST00000599201; ENSP00000470791; ENSG00000268768.

GeneID

3054.

KEGG

hsa:3054.

UCSC

uc004fjp.3. human.

Organism-specific databases

CTD

3054.

GeneCards

GC0XM153213.

H-InvDB

HIX0056221.

HGNC

HGNC:4839. HCFC1.

HPA

HPA018312.

MIM

300019. gene.
309541. phenotype.

neXtProt

NX_P51610.

PharmGKB

PA29215.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000293192.

HOVERGEN

HBG051888.

KO

K14966.

OrthoDB

EOG49GKGP.

PhylomeDB

P51610.

Gene expression databases

ArrayExpress

P51610.

Bgee

P51610.

CleanEx

HS_HCFC1.

Genevestigator

P51610.

GermOnline

ENSG00000172534. Homo sapiens.

Family and domain databases

Gene3D

2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
2.60.40.10. 2 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR015916. Gal_Oxidase_b-propeller.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view]

Pfam

PF01344. Kelch_1. 1 hit.
[Graphical view]

SMART

SM00060. FN3. 3 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.

ProtoNet

Search...

Other

ChiTaRS

HCFC1. human.

GenomeRNAi

3054.

NextBio

12089.

SOURCE

Search...

Entry information

Entry name

HCFC1_HUMAN

Accession

Primary (citable) accession number: P51610
Secondary accession number(s): Q6P4G5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.