ID HCFC1_MOUSE Reviewed; 2045 AA. AC Q61191; B1AUX1; Q684R1; Q7TSB0; Q8C2D0; Q9QWH2; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 202. DE RecName: Full=Host cell factor 1 {ECO:0000303|PubMed:9334261}; DE Short=HCF {ECO:0000303|PubMed:9334261}; DE Short=HCF-1 {ECO:0000250|UniProtKB:P51610}; DE AltName: Full=C1 factor {ECO:0000303|PubMed:9334261}; DE Contains: DE RecName: Full=HCF N-terminal chain 1 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF N-terminal chain 2 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF N-terminal chain 3 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF N-terminal chain 4 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF N-terminal chain 5 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF N-terminal chain 6 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF C-terminal chain 1 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF C-terminal chain 2 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF C-terminal chain 3 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF C-terminal chain 4 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF C-terminal chain 5 {ECO:0000250|UniProtKB:P51610}; DE Contains: DE RecName: Full=HCF C-terminal chain 6 {ECO:0000250|UniProtKB:P51610}; GN Name=Hcfc1 {ECO:0000312|MGI:MGI:105942}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB01163.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal liver {ECO:0000269|PubMed:9334261}; RX PubMed=9334261; DOI=10.1074/jbc.272.42.26749; RA Kristie T.M.; RT "The mouse homologue of the human transcription factor C1 (host cell RT factor). Conservation of forms and function."; RL J. Biol. Chem. 272:26749-26755(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0000305, ECO:0000312|EMBL:CAF25305.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH53742.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb mesenchyme {ECO:0000269|PubMed:15489334}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-209. RC STRAIN=NOD; TISSUE=Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] {ECO:0000305, ECO:0000312|EMBL:CAF25305.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-520. RC STRAIN=NMRI; TISSUE=Embryo; RA Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J., RA Pepperkok R., Wiemann S., Poustka A.; RT "Towards functional annotation of all Xq28 genes: expression and RT intracellular localization analyses reveal novel candidates for disease RT genes."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000305} RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=BALB/cJ {ECO:0000269|PubMed:9990006}; RX PubMed=9990006; DOI=10.1073/pnas.96.4.1229; RA Kristie T.M., Vogel J.L., Sears A.E.; RT "Nuclear localization of the C1 factor (host cell factor) in sensory RT neurons correlates with reactivation of herpes simplex virus from RT latency."; RL Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200; RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., RA Schoepfer R., Burlingame A.L.; RT "O-linked N-acetylglucosamine proteomics of postsynaptic density RT preparations using lectin weak affinity chromatography and mass RT spectrometry."; RL Mol. Cell. Proteomics 5:923-934(2006). RN [9] RP INTERACTION WITH THAP11. RX PubMed=18585351; DOI=10.1016/j.cell.2008.05.047; RA Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F., RA Songyang Z., Thomson J.A., Zwaka T.P.; RT "Ronin is essential for embryogenesis and the pluripotency of mouse RT embryonic stem cells."; RL Cell 133:1162-1174(2008). RN [10] RP ERRATUM OF PUBMED:18585351. RA Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F., RA Songyang Z., Thomson J.A., Zwaka T.P.; RL Cell 134:692-692(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1516 AND SER-1848, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [14] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-504; ARG-524 AND ARG-1216, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Transcriptional coregulator (By similarity). Involved in CC control of the cell cycle (PubMed:9334261, PubMed:9990006). Also CC antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 CC activation of the p15(INK4b) promoter and inhibits its ability to CC recruit p300 (By similarity). Coactivator for EGR2 and GABP2 (By CC similarity). Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys- CC 4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) CC complexes (involved in the activation and repression of transcription CC respectively) together (By similarity). As part of the NSL complex it CC may be involved in acetylation of nucleosomal histone H4 on several CC lysine residues (By similarity). Recruits KMT2E to E2F1 responsive CC promoters promoting transcriptional activation and thereby facilitates CC G1 to S phase transition (By similarity). Modulates expression of CC homeobox protein PDX1, perhaps acting in concert with transcription CC factor E2F1, thereby regulating pancreatic beta-cell growth and CC glucose-stimulated insulin secretion (By similarity). May negatively CC modulate transcriptional activity of FOXO3 (By similarity). CC {ECO:0000250|UniProtKB:D3ZN95, ECO:0000250|UniProtKB:P51610, CC ECO:0000269|PubMed:9334261, ECO:0000269|PubMed:9990006}. CC -!- SUBUNIT: Composed predominantly of six polypeptides ranging from 110 to CC 150 kDa and a minor 300 kDa polypeptide (PubMed:9334261). The majority CC of N- and C-terminal cleavage products remain tightly, albeit non- CC covalently, associated (By similarity). Interacts with POU2F1, CREB3, CC ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, CC HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2 (By similarity). Component CC of a MLL1 complex, composed of at least the core components KMT2A/MLL1, CC ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components CC BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, CC MCRS1, MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2, CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (By similarity). CC Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the CC regulation of the transcriptional activity of RRM1 (By similarity). CC Interacts directly with THAP3 (via its HBM) (By similarity). Interacts CC (via the Kelch-repeat domain) with THAP1 (via the HBM); the interaction CC recruits HCHC1 to the RRM1 (By similarity). Interacts directly with CC OGT; the interaction, which requires the HCFC1 cleavage site domain, CC glycosylates and promotes the proteolytic processing of HCFC1 and CC retains OGT in the nucleus (By similarity). Component of the SET1 CC complex, at least composed of the catalytic subunit (SETD1A or SETD1B), CC WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30 (By similarity). CC Component of the NSL complex at least composed of MOF/KAT8, KANSL1, CC KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity). CC Component of a complex at least composed of ZNF335, HCFC1, CCAR2, EMSY, CC MKI67, RBBP5, ASH2L and WDR5; the complex is formed as a result of CC interactions between components of a nuclear receptor-mediated CC transcription complex and a histone methylation complex (By CC similarity). Within the complex interacts with ZNF335 (By similarity). CC Interacts with TET2 and TET3 (By similarity). Interacts with HCFC1R1 CC (By similarity). Interacts with THAP11 (PubMed:18585351). Interacts CC (via Kelch domain) with KMT2E (via HBM motif) (By similarity). CC Interacts with E2F1 (By similarity). {ECO:0000250|UniProtKB:P51610, CC ECO:0000269|PubMed:18585351, ECO:0000269|PubMed:9334261}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51610}. Cytoplasm CC {ECO:0000269|PubMed:9990006}. Note=HCFC1R1 modulates its subcellular CC localization and overexpression of HCFC1R1 leads to accumulation of CC HCFC1 in the cytoplasm (By similarity). Localizes to cytoplasm in CC trigeminal ganglia (PubMed:9990006). Non-processed HCFC1 associates CC with chromatin. Colocalizes with CREB3 and CANX in the ER. CC {ECO:0000250|UniProtKB:P51610, ECO:0000269|PubMed:9990006}. CC -!- SUBCELLULAR LOCATION: Note=(Microbial infection) In trigeminal ganglia, CC becoming nuclear upon HSV reactivation from the latent state. CC {ECO:0000269|PubMed:9990006}. CC -!- TISSUE SPECIFICITY: Expressed in liver, pituitary gland, skeletal CC muscle, kidney, eye and brain (at protein level). Also observed at low CC level in heart, spleen and lung. {ECO:0000269|PubMed:9334261, CC ECO:0000269|PubMed:9990006}. CC -!- DOMAIN: The HCF repeat is a highly specific proteolytic cleavage CC signal. {ECO:0000250|UniProtKB:P51610}. CC -!- DOMAIN: The kelch repeats fold into a 6-bladed kelch beta-propeller CC called the beta-propeller domain which mediates interaction with CC HCFC1R1. {ECO:0000250|UniProtKB:P51610}. CC -!- PTM: Proteolytically cleaved at one or several PPCE--THET sites within CC the HCF repeats. Further cleavage of the primary N- and C-terminal CC chains results in a 'trimming' and accumulation of the smaller chains. CC Cleavage is promoted by O-glycosylation. CC {ECO:0000250|UniProtKB:P51610}. CC -!- PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic CC processing. {ECO:0000250|UniProtKB:P51610}. CC -!- PTM: Ubiquitinated. Lys-1817 and Lys-1818 are ubiquitinated both via CC 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated CC deubiquitination of 'Lys-48'-linked polyubiquitin chains; CC deubiquitination by BAP1 does not seem to stabilize the protein. CC {ECO:0000250|UniProtKB:P51610}. CC -!- SEQUENCE CAUTION: CC Sequence=CAF25305.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U53925; AAB01163.1; -; Genomic_DNA. DR EMBL; U80821; AAD09225.1; -; Genomic_DNA. DR EMBL; AL672002; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466650; EDL29851.1; -; Genomic_DNA. DR EMBL; BC053742; AAH53742.1; -; mRNA. DR EMBL; AK088827; BAC40597.1; -; mRNA. DR EMBL; AJ627036; CAF25305.1; ALT_FRAME; mRNA. DR CCDS; CCDS30218.1; -. DR RefSeq; NP_032250.2; NM_008224.4. DR PDB; 2M26; NMR; -; A=1896-2020. DR PDBsum; 2M26; -. DR AlphaFoldDB; Q61191; -. DR BMRB; Q61191; -. DR SMR; Q61191; -. DR BioGRID; 200248; 27. DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex. DR IntAct; Q61191; 5. DR MINT; Q61191; -. DR STRING; 10090.ENSMUSP00000033761; -. DR ChEMBL; CHEMBL4879471; -. DR GlyGen; Q61191; 102 sites, 1 O-linked glycan (102 sites). DR iPTMnet; Q61191; -. DR PhosphoSitePlus; Q61191; -. DR SwissPalm; Q61191; -. DR EPD; Q61191; -. DR jPOST; Q61191; -. DR MaxQB; Q61191; -. DR PaxDb; 10090-ENSMUSP00000033761; -. DR PeptideAtlas; Q61191; -. DR ProteomicsDB; 269817; -. DR Pumba; Q61191; -. DR Antibodypedia; 7165; 293 antibodies from 33 providers. DR DNASU; 15161; -. DR Ensembl; ENSMUST00000033761.13; ENSMUSP00000033761.7; ENSMUSG00000031386.15. DR GeneID; 15161; -. DR KEGG; mmu:15161; -. DR UCSC; uc009tnm.2; mouse. DR AGR; MGI:105942; -. DR CTD; 3054; -. DR MGI; MGI:105942; Hcfc1. DR VEuPathDB; HostDB:ENSMUSG00000031386; -. DR eggNOG; KOG4152; Eukaryota. DR GeneTree; ENSGT00940000161383; -. DR HOGENOM; CLU_002603_0_0_1; -. DR InParanoid; Q61191; -. DR OMA; PDYGQMK; -. DR OrthoDB; 4642026at2759; -. DR TreeFam; TF314757; -. DR Reactome; R-MMU-3214847; HATs acetylate histones. DR Reactome; R-MMU-5689603; UCH proteinases. DR Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes. DR BioGRID-ORCS; 15161; 28 hits in 83 CRISPR screens. DR ChiTaRS; Hcfc1; mouse. DR PRO; PR:Q61191; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q61191; Protein. DR Bgee; ENSMUSG00000031386; Expressed in undifferentiated genital tubercle and 260 other cell types or tissues. DR ExpressionAtlas; Q61191; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB. DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central. DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB. DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB. DR GO; GO:0044545; C:NSL complex; ISO:MGI. DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI. DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI. DR GO; GO:0019046; P:release from viral latency; IDA:UniProtKB. DR CDD; cd00063; FN3; 2. DR Gene3D; 6.10.250.2590; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR043536; HCF1/2. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR015915; Kelch-typ_b-propeller. DR InterPro; IPR006652; Kelch_1. DR PANTHER; PTHR46003; HOST CELL FACTOR; 1. DR PANTHER; PTHR46003:SF3; HOST CELL FACTOR 1; 1. DR Pfam; PF01344; Kelch_1; 1. DR Pfam; PF13415; Kelch_3; 1. DR Pfam; PF13854; Kelch_5; 2. DR SMART; SM00060; FN3; 2. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF117281; Kelch motif; 1. DR PROSITE; PS50853; FN3; 3. DR Genevisible; Q61191; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Autocatalytic cleavage; Cell cycle; KW Chromatin regulator; Cytoplasm; Glycoprotein; Isopeptide bond; KW Kelch repeat; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CHAIN 2..1432 FT /note="HCF N-terminal chain 6" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016635" FT CHAIN 2..1332 FT /note="HCF N-terminal chain 5" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016636" FT CHAIN 2..1304 FT /note="HCF N-terminal chain 4" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016637" FT CHAIN 2..1110 FT /note="HCF N-terminal chain 3" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016638" FT CHAIN 2..1081 FT /note="HCF N-terminal chain 2" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016639" FT CHAIN 2..1019 FT /note="HCF N-terminal chain 1" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016640" FT CHAIN 1020..2045 FT /note="HCF C-terminal chain 1" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016641" FT CHAIN 1082..2045 FT /note="HCF C-terminal chain 2" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016642" FT CHAIN 1111..2045 FT /note="HCF C-terminal chain 3" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016643" FT CHAIN 1305..2045 FT /note="HCF C-terminal chain 4" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016644" FT CHAIN 1333..2045 FT /note="HCF C-terminal chain 5" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016645" FT CHAIN 1433..2045 FT /note="HCF C-terminal chain 6" FT /evidence="ECO:0000250|UniProtKB:P51610" FT /id="PRO_0000016646" FT REPEAT 44..89 FT /note="Kelch 1" FT /evidence="ECO:0000255" FT REPEAT 93..140 FT /note="Kelch 2" FT /evidence="ECO:0000255" FT REPEAT 148..194 FT /note="Kelch 3" FT /evidence="ECO:0000255" FT REPEAT 217..265 FT /note="Kelch 4" FT /evidence="ECO:0000255" FT REPEAT 266..313 FT /note="Kelch 5" FT /evidence="ECO:0000255" FT DOMAIN 366..457 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REPEAT 1010..1035 FT /note="HCF repeat 1" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1072..1097 FT /note="HCF repeat 2" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1101..1126 FT /note="HCF repeat 3" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1157..1182 FT /note="HCF repeat 4; degenerate" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1295..1320 FT /note="HCF repeat 5" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1323..1348 FT /note="HCF repeat 6" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1358..1383 FT /note="HCF repeat 7; degenerate" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REPEAT 1423..1448 FT /note="HCF repeat 8" FT /evidence="ECO:0000250|UniProtKB:P51610" FT DOMAIN 1808..1898 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1900..2016 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 407..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 500..550 FT /note="Required for interaction with OGT" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REGION 610..722 FT /note="Interaction with SIN3A" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REGION 750..902 FT /note="Interaction with ZBTB17" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REGION 813..912 FT /note="Interaction with GABP2" FT /evidence="ECO:0000250|UniProtKB:P51610" FT REGION 1219..1242 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1302..1375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1444..1475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1494..1525 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2004..2045 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 414..432 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1225..1242 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1302..1355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2007..2025 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 1019..1020 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P51610" FT SITE 1081..1082 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P51610" FT SITE 1110..1111 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P51610" FT SITE 1304..1305 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P51610" FT SITE 1332..1333 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P51610" FT SITE 1432..1433 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 288 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 504 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 524 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 598 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 666 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 669 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 813 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 1204 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 1216 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1223 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 1500 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 1506 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 1516 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1781 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT MOD_RES 1848 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2015 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 105 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 163 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 244 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 282 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 363 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 1817 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 1818 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CROSSLNK 2034 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P51610" FT CONFLICT 483 FT /note="V -> R (in Ref. 1; AAB01163/AAD09225)" FT /evidence="ECO:0000305" FT CONFLICT 520 FT /note="P -> S (in Ref. 6; CAF25305)" FT /evidence="ECO:0000305" FT CONFLICT 567..568 FT /note="VL -> AW (in Ref. 1; AAB01163/AAD09225)" FT /evidence="ECO:0000305" FT CONFLICT 711 FT /note="Q -> H (in Ref. 1; AAD09225)" FT /evidence="ECO:0000305" FT CONFLICT 1104 FT /note="C -> S (in Ref. 1; AAB01163/AAD09225)" FT /evidence="ECO:0000305" FT CONFLICT 1230 FT /note="G -> A (in Ref. 1; AAB01163/AAD09225)" FT /evidence="ECO:0000305" FT STRAND 1897..1899 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 1905..1912 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 1915..1921 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 1924..1926 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 1930..1938 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 1965..1968 FT /evidence="ECO:0007829|PDB:2M26" FT HELIX 1973..1977 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 1984..1997 FT /evidence="ECO:0007829|PDB:2M26" FT STRAND 2005..2010 FT /evidence="ECO:0007829|PDB:2M26" SQ SEQUENCE 2045 AA; 210437 MW; AD0EC38C9DB19F22 CRC64; MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLVPQ AATAPPSTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV MVSNPATRML KTAAAQVGTS VSSAANTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGAH STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQETAASLV TSAVGQQNGN VVRVCSNPPC ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN TPTVVRITVA PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI MVAGELGAAR VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN PPCETHETGT TNTATTSNAG SAQRVCSNPP CETHETGTTH TATTATSNGG AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV SVGTLIPDAT SSHGTLESGL EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH TATTVTSNMS SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP ELQAAVDLSS TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL MAEAQAGTTT LMVTGLTPEE LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA AQQAVMGTGE PMDTSEAAAA VTQAELGHLS AEGQEGQATT IPIVLTQQEL AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE SNCLNELASA VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD DSGTVPDYNQ LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS KADGQ //