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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. 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.8 Ref.9 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.24 Ref.37
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, SDS3), SAP30, SIN3B, OGT1 and FHL2. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, DPY30, E2F6, HCFC2, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. 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/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts (via HBM motif) with SETD1A. Interacts with OGT; this prevents degradation of OGT. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 Ref.27 Ref.37
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. Ref.8 Ref.14 Ref.32 Ref.37
Tissue specificity	Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested.
Domain	The HCF repeat is a highly specific proteolytic cleavage signal. Ref.14 The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1. Ref.14
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. Ref.6 Ref.7 Ref.22 Ref.37 O-glycosylated. 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.31 Ref.32
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
Domain	Kelch repeat Repeat
PTM	Acetylation Autocatalytic cleavage Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW 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. Source: UniProtKB positive regulation of gene expression Inferred from direct assay Ref.37. Source: UniProtKB protein stabilization Inferred from direct assay Ref.37. Source: UniProtKB reactivation of latent virus Non-traceable author statement Ref.9. Source: UniProtKB regulation of protein complex assembly Inferred from direct assay Ref.9. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	MLL1 complex Inferred from direct assay Ref.20. Source: UniProtKB MLL5-L complex Inferred from direct assay Ref.33. Source: UniProtKB Set1C/COMPASS complex Inferred from direct assay Ref.27Ref.28. Source: UniProtKB mitochondrion Inferred from direct assay. Source: HPA
Molecular function	chromatin binding Inferred from direct assay Ref.37. Source: UniProtKB identical protein binding Inferred from physical interaction Ref.17. Source: IntAct sequence-specific DNA binding transcription factor activity Non-traceable author statement. Source: ProtInc transcription coactivator activity Inferred from mutant phenotype Ref.9. 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	3	EBI-396176,EBI-625022
CREBZF	Q9NS37	7	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
	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	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.30
	Modified residue	6	1	Phosphoserine Ref.30
	Modified residue	288	1	N6-acetyllysine Ref.35
	Modified residue	411	1	Phosphoserine Ref.30 Ref.34
	Modified residue	598	1	Phosphoserine Ref.23 Ref.30 Ref.34
	Modified residue	666	1	Phosphoserine Ref.23 Ref.26 Ref.29 Ref.30 Ref.34
	Modified residue	733	1	Phosphothreonine Ref.23
	Modified residue	737	1	Phosphothreonine Ref.23
	Modified residue	738	1	Phosphothreonine Ref.23
	Modified residue	813	1	N6-acetyllysine Ref.35
	Modified residue	836	1	N6-acetyllysine Ref.35
	Modified residue	1205	1	Phosphoserine Ref.29
	Modified residue	1491	1	Phosphothreonine Ref.26
	Modified residue	1507	1	Phosphoserine Ref.26 Ref.29 Ref.30 Ref.34
	Modified residue	2005	1	N6-acetyllysine Ref.35
	Modified residue	2007	1	Phosphoserine Ref.23
	Modified residue	2008	1	Phosphoserine Ref.23
	Modified residue	2020	1	Phosphoserine Ref.23 Ref.25
	Cross-link	105		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.31
	Cross-link	163		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.31
	Cross-link	244		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.31
	Cross-link	363		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.31
	Cross-link	1807		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.32
	Cross-link	1808		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.32
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	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. Ref.11
	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.11
	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.11
	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.11
	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.11 Ref.31
	Mutagenesis	137	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	Mutagenesis	197	1	P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	Mutagenesis	200	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	Mutagenesis	228	1	R → D: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	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.11
	Mutagenesis	255	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	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.11
	Mutagenesis	319	1	P → S: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	Mutagenesis	322	1	R → D: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	Mutagenesis	338	1	S → A: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. Ref.11
	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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[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: 7876203] [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: 15772651] [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: 15489334] [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: 7829097] [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: 10920196] [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: 7590226] [Abstract] Cited for: AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF 1017-PRO--HIS-1021 AND 1072-VAL--ASN-1097.
[8]	"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: 9990006] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"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: 10675337] [Abstract] Cited for: FUNCTION, INTERACTION WITH GABP2.
[10]	"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: 10976766] [Abstract] Cited for: INTERACTION WITH SP1.
[11]	"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: 10629049] [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.
[12]	"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: 10779346] [Abstract] Cited for: FUNCTION.
[13]	"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: 10871379] [Abstract] Cited for: INTERACTION WITH CREBZF.
[14]	"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: 12235138] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH HCFC1R1. Tissue: Brain.
[15]	"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: 12244100] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZBTB17.
[16]	"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: 14532282] [Abstract] Cited for: FUNCTION, INTERACTION WITH EGR2 AND E2F4.
[17]	"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: 12670868] [Abstract] Cited for: FUNCTION, INTERACTION WITH SIN3A; HDAC1; HDAC2; SDS3; SAP30; SIN3B; OGT; SET1; ASH2 AND WDR5.
[18]	"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: 15190068] [Abstract] Cited for: FUNCTION.
[19]	"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: 15199122] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[20]	"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: 15960975] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[21]	"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: 15705566] [Abstract] Cited for: INTERACTION WITH CREBZF AND CREB3.
[22]	"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: 16624878] [Abstract] Cited for: FUNCTION, AUTOCATALYTIC CLEAVAGE, INTERACTION WITH FHL2.
[23]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598; SER-666; THR-733; THR-737; THR-738; SER-2007; SER-2008 AND SER-2020, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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: 17578910] [Abstract] Cited for: FUNCTION.
[25]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2020, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; THR-1491 AND SER-1507, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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: 17998332] [Abstract] Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A.
[28]	"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: 18838538] [Abstract] Cited for: IDENTIFICATION IN SET1 COMPLEX.
[29]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1205 AND SER-1507, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-411; SER-598; SER-666 AND SER-1507, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[31]	"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: 19815555] [Abstract] Cited for: UBIQUITINATION AT LYS-105; LYS-163; LYS-244 AND LYS-363, DEUBIQUITINATION BY BAP1, MUTAGENESIS OF PRO-134.
[32]	"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: 19188440] [Abstract] Cited for: UBIQUITINATION AT LYS-1807 AND LYS-1808, DEUBIQUITINATION BY BAP1, SUBCELLULAR LOCATION.
[33]	"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: 19377461] [Abstract] Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
[34]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-598; SER-666 AND SER-1507, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[35]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-813; LYS-836 AND LYS-2005, MASS SPECTROMETRY.
[36]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]	"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: 21285374] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, INTERACTION WITH OGT.
+	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
ProteinModelPortal	P51610.
SMR	P51610. Positions 276-302, 361-386, 1792-2008.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51610. 44 interactions.
STRING	P51610.
PTM databases
PhosphoSite	P51610.
Polymorphism databases
DMDM	160332311.
Proteomic databases
PRIDE	P51610.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000310441; ENSP00000309555; ENSG00000172534.
GeneID	3054.
KEGG	hsa:3054.
UCSC	uc004fjp.1. human.
Organism-specific databases
CTD	3054.
GeneCards	GC0XM153213.
H-InvDB	HIX0203319.
HGNC	HGNC:4839. HCFC1.
HPA	HPA018312.
MIM	300019. gene.
neXtProt	NX_P51610.
PharmGKB	PA29215.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09425.
HOVERGEN	HBG051888.
OrthoDB	EOG49GKGP.
PhylomeDB	P51610.
Gene expression databases
ArrayExpress	P51610.
Bgee	P51610.
CleanEx	HS_HCFC1.
Genevestigator	P51610.
GermOnline	ENSG00000172534. Homo sapiens.
Family and domain databases
InterPro	IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR015915. Kelch-typ_b-propeller. IPR006652. Kelch_1. IPR011498. Kelch_2. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits. G3DSA:2.120.10.80. Kelch-typ_b-propeller. 1 hit.
KO	K14966.
Pfam	PF01344. Kelch_1. 2 hits. PF07646. Kelch_2. 1 hit. [Graphical view]
SMART	SM00060. FN3. 3 hits. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits.
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 137 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.