HCFC1 Antibody - #DF6651

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Product: HCFC1 Antibody
Catalog: DF6651
Description: Rabbit polyclonal antibody to HCFC1
Application: WB IHC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Rabbit, Dog, Xenopus
Mol.Wt.: 209kDa; 209kD(Calculated).
Uniprot: P51610
RRID: AB_2838613

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MS Report
HPLC Report
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%), Dog(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
HCFC1 Antibody detects endogenous levels of total HCFC1.
RRID:
AB_2838613
Cite Format: Affinity Biosciences Cat# DF6651, RRID:AB_2838613.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

C1 factor; CFF; HCF 1; HCF; HCF C-terminal chain 6; HCF-1; HCF1; Hcfc1; HCFC1_HUMAN; HFC1; Host cell factor 1; Host cell factor; Host cell factor C1 (VP16 accessory protein); Host cell factor C1; MGC70925; MRX3; VCAF; VP16 accessory protein;

Immunogens

Immunogen:
Uniprot:

P51610(HCFC1_HUMAN) >>Visit HPA database.

Gene(ID):
HCFC1(3054)
Expression:
P51610 HCFC1_HUMAN:

Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested.

Description:
This gene is a member of the host cell factor family and encodes a protein with five Kelch repeats, a fibronectin-like motif, and six HCF repeats, each of which contains a highly specific cleavage signal. This nuclear coactivator is proteolytically cleaved at one of the six possible sites, resulting in the creation of an N-terminal chain and the corresponding C-terminal chain. The final form of this protein consists of noncovalently bound N- and C-terminal chains. The protein is involved in control of the cell cycle and transcriptional regulation during herpes simplex virus infection. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008]
Sequence:
MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIDTLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPRARAGHCAVAINTRLYIWSGRDGYRKAWNNQVCCKDLWYLETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDIPATAATATSPTPNPVPSVPANPPKSPAPAAAAPAVQPLTQVGITLLPQAAPAPPTTTTIQVLPTVPGSSISVPTAARTQGVPAVLKVTGPQATTGTPLVTMRPASQAGKAPVTVTSLPAGVRMVVPTQSAQGTVIGSSPQMSGMAALAAAAAATQKIPPSSAPTVLSVPAGTTIVKTMAVTPGTTTLPATVKVASSPVMVSNPATRMLKTAAAQVGTSVSSATNTSTRPIITVHKSGTVTVAQQAQVVTTVVGGVTKTITLVKSPISVPGGSALISNLGKVMSVVQTKPVQTSAVTGQASTGPVTQIIQTKGPLPAGTILKLVTSADGKPTTIITTTQASGAGTKPTILGISSVSPSTTKPGTTTIIKTIPMSAIITQAGATGVTSSPGIKSPITIITTKVMTSGTGAPAKIITAVPKIATGHGQQGVTQVVLKGAPGQPGTILRTVPMGGVRLVTPVTVSAVKPAVTTLVVKGTTGVTTLGTVTGTVSTSLAGAGGHSTSASLATPITTLGTIATLSSQVINPTAITVSAAQTTLTAAGGLTTPTITMQPVSQPTQVTLITAPSGVEAQPVHDLPVSILASPTTEQPTATVTIADSGQGDVQPGTVTLVCSNPPCETHETGTTNTATTTVVANLGGHPQPTQVQFVCDRQEAAASLVTSTVGQQNGSVVRVCSNPPCETHETGTTNTATTATSNMAGQHGCSNPPCETHETGTTNTATTAMSSVGANHQRDARRACAAGTPAVIRISVATGALEAAQGSKSQCQTRQTSATSTTMTVMATGAPCSAGPLLGPSMAREPGGRSPAFVQLAPLSSKVRLSSPSIKDLPAGRHSHAVSTAAMTRSSVGAGEPRMAPVCESLQGGSPSTTVTVTALEALLCPSATVTQVCSNPPCETHETGTTNTATTSNAGSAQRVCSNPPCETHETGTTHTATTATSNGGTGQPEGGQQPPAGRPCETHQTTSTGTTMSVSVGALLPDATSSHRTVESGLEVAAAPSVTPQAGTALLAPFPTQRVCSNPPCETHETGTTHTATTVTSNMSSNQDPPPAASDQGEVESTQGDSVNITSSSAITTTVSSTLTRAVTTVTQSTPVPGPSVPPPEELQVSPGPRQQLPPRQLLQSASTALMGESAEVLSASQTPELPAAVDLSSTGEPSSGQESAGSAVVATVVVQPPPPTQSEVDQLSLPQELMAEAQAGTTTLMVTGLTPEELAVTAAAEAAAQAAATEEAQALAIQAVLQAAQQAVMGTGEPMDTSEAAATVTQAELGHLSAEGQEGQATTIPIVLTQQELAALVQQQQLQEAQAQQQHHHLPTEALAPADSLNDPAIESNCLNELAGTVPSTVALLPSTATESLAPSNTFVAPQPVVVASPAKLQAAATLTEVANGIESLGVKPDLPPPPSKAPMKKENQWFDVGVIKGTNVMVTHYFLPPDDAVPSDDDLGTVPDYNQLKKQELQPGTAYKFRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQAGGELKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIAARNEKGYGPATQVRWLQETSKDSSGTKPANKRPMSSPEMKSAPKKSKADGQ

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Dog
100
Xenopus
100
Rabbit
100
Sheep
0
Zebrafish
0
Chicken
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P51610 As Substrate

Site PTM Type Enzyme
A2 Acetylation
S6 Phosphorylation
S26 Phosphorylation
K105 Ubiquitination
Y111 Phosphorylation
K129 Ubiquitination
S143 Phosphorylation
K148 Ubiquitination
K163 Ubiquitination
Y208 Phosphorylation
K244 Ubiquitination
K266 Ubiquitination
K288 Acetylation
K288 Ubiquitination
K291 Acetylation
R322 Methylation
K345 Ubiquitination
K354 Ubiquitination
K363 Ubiquitination
T377 Phosphorylation
T408 Phosphorylation
T410 Phosphorylation
S411 Phosphorylation
T413 Phosphorylation
S419 Phosphorylation
T480 Phosphorylation
K488 Ubiquitination
T490 O-Glycosylation
T495 O-Glycosylation
T496 Phosphorylation
T498 Phosphorylation
T502 Phosphorylation
R504 Methylation
S507 Phosphorylation
K511 Methylation
K511 Ubiquitination
T515 Phosphorylation
R524 Methylation
K558 Methylation
S562 O-Glycosylation
S563 O-Glycosylation
S569 O-Glycosylation
T579 O-Glycosylation
S597 Phosphorylation
S598 Phosphorylation
S603 Phosphorylation
R608 Methylation
K611 Ubiquitination
T619 Phosphorylation
S620 O-Glycosylation
S622 O-Glycosylation
S623 O-Glycosylation
T625 O-Glycosylation
T651 O-Glycosylation
T652 O-Glycosylation
T660 Phosphorylation
T662 Phosphorylation
K665 Ubiquitination
S666 Phosphorylation
S669 Phosphorylation
S674 Phosphorylation
S685 O-Glycosylation
K690 Acetylation
K690 Ubiquitination
T694 O-Glycosylation
K713 Ubiquitination
T720 Phosphorylation
T726 O-Glycosylation
T733 Phosphorylation
T737 Phosphorylation
T738 Phosphorylation
T739 O-Glycosylation
S755 Phosphorylation
S757 Phosphorylation
S759 Phosphorylation
T760 O-Glycosylation
T761 O-Glycosylation
T766 Phosphorylation
T771 Phosphorylation
T779 O-Glycosylation
S788 Phosphorylation
S789 Phosphorylation
S794 Phosphorylation
T797 Phosphorylation
T801 O-Glycosylation
S806 O-Glycosylation
T808 O-Glycosylation
K813 Acetylation
K813 Ubiquitination
K820 Ubiquitination
K836 Acetylation
K836 Ubiquitination
R847 Methylation
T848 Phosphorylation
R855 Methylation
T861 O-Glycosylation
K866 Ubiquitination
T877 O-Glycosylation
T878 O-Glycosylation
T881 O-Glycosylation
S921 O-Glycosylation
T927 O-Glycosylation
S932 O-Glycosylation
T936 O-Glycosylation
T937 O-Glycosylation
T939 O-Glycosylation
T950 O-Glycosylation
S955 O-Glycosylation
S984 Phosphorylation
T995 O-Glycosylation
T1020 O-Glycosylation
T1025 O-Glycosylation
T1030 O-Glycosylation
T1031 O-Glycosylation
S1070 Phosphorylation
T1143 O-Glycosylation
T1143 Phosphorylation
S1150 O-Glycosylation
S1150 Phosphorylation
K1163 Ubiquitination
S1164 Phosphorylation
S1188 Phosphorylation
S1196 Phosphorylation
R1204 Methylation
S1205 Phosphorylation
S1215 Phosphorylation
K1217 Ubiquitination
R1219 Methylation
S1221 Phosphorylation
S1222 Phosphorylation
S1224 Phosphorylation
K1226 Ubiquitination
T1239 O-Glycosylation
R1244 Methylation
S1246 Phosphorylation
R1253 Methylation
T1273 O-Glycosylation
T1335 O-Glycosylation
S1370 Phosphorylation
T1400 Phosphorylation
T1413 Phosphorylation
T1485 Phosphorylation
S1490 Phosphorylation
T1491 Phosphorylation
S1497 Phosphorylation
S1507 Phosphorylation
T1743 O-Glycosylation
S1771 Phosphorylation
K1803 Acetylation
K1807 Acetylation
K1807 Ubiquitination
K1808 Acetylation
K1808 Ubiquitination
S1838 Phosphorylation
K1852 Ubiquitination
K1853 Ubiquitination
K1863 Ubiquitination
S1881 Phosphorylation
K1884 Ubiquitination
C1886 S-Nitrosylation
C1895 S-Nitrosylation
K1901 Ubiquitination
S1902 Phosphorylation
Y1923 Phosphorylation
S1940 Phosphorylation
S1941 Phosphorylation
T1942 Phosphorylation
K1976 Ubiquitination
K1989 Acetylation
K1989 Ubiquitination
K2005 Acetylation
K2005 Ubiquitination
S2007 Phosphorylation
S2008 Phosphorylation
S2019 Phosphorylation
S2020 Phosphorylation

Research Backgrounds

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. Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting transcriptional activation and thereby facilitates G1 to S phase transition.

(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.

PTMs:

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.

O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing.

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.

Subcellular Location:

Cytoplasm. Nucleus.
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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Highly expressed in fetal tissues and the adult kidney. Present in all tissues tested.

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 KMT2A/MLL1, 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 a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. 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 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. 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. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with TET2 and TET3. Interacts with HCFC1R1. Interacts with THAP11 (By similarity). Interacts (via Kelch domain) with KMT2E/MLL5 isoform 3 (via HBM motif). Interacts with E2F1.

(Microbial infection) 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. Interacts with the viral transactivator protein VP16.

Family&Domains:

The HCF repeat is a highly specific proteolytic cleavage signal.

The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1.

Research Fields

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

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