HCFC1_RAT
ID HCFC1_RAT Reviewed; 2034 AA.
AC D3ZN95;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Host cell factor 1 {ECO:0000303|PubMed:21909281};
DE Short=HCF {ECO:0000250|UniProtKB:P51610};
DE Short=HCF-1 {ECO:0000303|PubMed:21909281};
DE AltName: Full=C1 factor {ECO:0000250|UniProtKB:P51610};
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|RGD:1563804};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=21909281; DOI=10.1371/journal.pgen.1002235;
RA Rizki G., Iwata T.N., Li J., Riedel C.G., Picard C.L., Jan M., Murphy C.T.,
RA Lee S.S.;
RT "The evolutionarily conserved longevity determinants HCF-1 and SIR-
RT 2.1/SIRT1 collaborate to regulate DAF-16/FOXO.";
RL PLoS Genet. 7:E1002235-E1002235(2011).
RN [4] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=24250814; DOI=10.1371/journal.pone.0078841;
RA Iwata T.N., Cowley T.J., Sloma M., Ji Y., Kim H., Qi L., Lee S.S.;
RT "The transcriptional co-regulator HCF-1 is required for INS-1 beta-cell
RT glucose-stimulated insulin secretion.";
RL PLoS ONE 8:e78841-e78841(2013).
CC -!- FUNCTION: Transcriptional coregulator (PubMed:24250814). Involved in
CC control of the cell cycle (By similarity). Also antagonizes
CC transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the
CC p15(INK4b) promoter and inhibits its ability to recruit p300 (By
CC similarity). Coactivator for EGR2 and GABP2 (By similarity). Tethers
CC the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase
CC (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the
CC activation and repression of transcription, respectively) together (By
CC similarity). Component of a THAP1/THAP3-HCFC1-OGT complex that is
CC required for the regulation of the transcriptional activity of RRM1 (By
CC similarity). As part of the NSL complex it may be involved in
CC acetylation of nucleosomal histone H4 on several lysine residues (By
CC similarity). Recruits KMT2E/MLL5 to E2F1 responsive promoters promoting
CC transcriptional activation and thereby facilitates G1 to S phase
CC transition (By similarity). Modulates expression of homeobox protein
CC PDX1, perhaps acting in concert with transcription factor E2F1, thereby
CC regulating pancreatic beta-cell growth and glucose-stimulated insulin
CC secretion (PubMed:24250814). May negatively modulate transcriptional
CC activity of FOXO3 (PubMed:21909281). {ECO:0000250|UniProtKB:P51610,
CC ECO:0000269|PubMed:21909281, ECO:0000269|PubMed:24250814}.
CC -!- SUBUNIT: Composed predominantly of six polypeptides ranging from 110 to
CC 150 kDa and a minor 300 kDa polypeptide. The majority of N- and C-
CC terminal cleavage products remain tightly, albeit non-covalently,
CC associated. Interacts with POU2F1, CREB3, ZBTB17, EGR2, E2F4, CREBZF,
CC SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SUDS3), SAP30,
CC SIN3B and FHL2. Component of a MLL1 complex, composed of at least the
CC core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as
CC the facultative components BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70,
CC INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8, PELP1, PHF20,
CC PRP31, RING2, RUVBL1, RUVBL2, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Component of a THAP1/THAP3-HCFC1-OGT complex that is required
CC for the regulation of the transcriptional activity of RRM1. Interacts
CC directly with THAP3 (via its HBM). Interacts (via the Kelch-repeat
CC domain) with THAP1 (via the HBM); the interaction recruits HCHC1 to the
CC RRM1. Interacts directly with OGT; the interaction, which requires the
CC HCFC1 cleavage site domain, glycosylates and promotes the proteolytic
CC processing of HCFC1, retains OGT in the nucleus and impacts the
CC expression of herpes simplex virus immediate early viral genes.
CC Component of the SET1 complex, at least composed of the catalytic
CC subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and
CC DPY30. Component of the NSL complex at least composed of MOF/KAT8,
CC KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
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. Within the
CC complex interacts with ZNF335. Interacts with TET2 and TET3. Interacts
CC with HCFC1R1 (By similarity). Interacts with THAP11 (By similarity).
CC Interacts (via Kelch domain) with KMT2E/MLL5 isoform 3 (via HBM motif).
CC Interacts with E2F1 (By similarity). {ECO:0000250|UniProtKB:P51610,
CC ECO:0000250|UniProtKB:Q61191}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51610}. Nucleus
CC {ECO:0000250|UniProtKB:P51610}. Note=HCFC1R1 modulates its subcellular
CC localization and overexpression of HCFC1R1 leads to accumulation of
CC HCFC1 in the cytoplasm. Non-processed HCFC1 associates with chromatin.
CC Colocalizes with CREB3 and CANX in the ER.
CC {ECO:0000250|UniProtKB:P51610}.
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-1818 and Lys-1819 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}.
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DR EMBL; AABR07071934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001132979.1; NM_001139507.1.
DR AlphaFoldDB; D3ZN95; -.
DR SMR; D3ZN95; -.
DR STRING; 10116.ENSRNOP00000060327; -.
DR iPTMnet; D3ZN95; -.
DR PhosphoSitePlus; D3ZN95; -.
DR jPOST; D3ZN95; -.
DR PaxDb; D3ZN95; -.
DR PeptideAtlas; D3ZN95; -.
DR PRIDE; D3ZN95; -.
DR GeneID; 363519; -.
DR KEGG; rno:363519; -.
DR CTD; 3054; -.
DR RGD; 1563804; Hcfc1.
DR VEuPathDB; HostDB:ENSRNOG00000051948; -.
DR eggNOG; KOG4152; Eukaryota.
DR HOGENOM; CLU_002603_0_0_1; -.
DR InParanoid; D3ZN95; -.
DR OMA; GPCGTIH; -.
DR OrthoDB; 416932at2759; -.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000051948; Expressed in Ammon's horn and 19 other tissues.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISO:RGD.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISO:RGD.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0044545; C:NSL complex; ISO:RGD.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0001835; P:blastocyst hatching; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISO:RGD.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISO:RGD.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; ISO:RGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0019046; P:release from viral latency; ISO:RGD.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR037854; HCF1.
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; PTHR46003; 2.
DR PANTHER; PTHR46003:SF3; PTHR46003:SF3; 2.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW Acetylation; Autocatalytic cleavage; Cell cycle; Chromatin regulator;
KW Coiled coil; Cytoplasm; Glycoprotein; Host-virus interaction;
KW Isopeptide bond; Kelch repeat; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; 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_0000454328"
FT CHAIN 2..1332
FT /note="HCF N-terminal chain 5"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454329"
FT CHAIN 2..1304
FT /note="HCF N-terminal chain 4"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454330"
FT CHAIN 2..1110
FT /note="HCF N-terminal chain 3"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454331"
FT CHAIN 2..1081
FT /note="HCF N-terminal chain 2"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454332"
FT CHAIN 2..1019
FT /note="HCF N-terminal chain 1"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454333"
FT CHAIN 1020..2034
FT /note="HCF C-terminal chain 1"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454334"
FT CHAIN 1082..2034
FT /note="HCF C-terminal chain 2"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454335"
FT CHAIN 1111..2034
FT /note="HCF C-terminal chain 3"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454336"
FT CHAIN 1305..2034
FT /note="HCF C-terminal chain 4"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454337"
FT CHAIN 1333..2034
FT /note="HCF C-terminal chain 5"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454338"
FT CHAIN 1433..2034
FT /note="HCF C-terminal chain 6"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT /id="PRO_0000454339"
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..469
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 1156..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..1899
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1901..2017
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 1221..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2005..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1693..1723
FT /evidence="ECO:0000255"
FT COMPBIAS 414..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1241
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 2008..2034
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:0000250|UniProtKB:P51610"
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:0000250|UniProtKB:P51610"
FT MOD_RES 524
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
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 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:0000250|UniProtKB:P51610"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT MOD_RES 1849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61191"
FT MOD_RES 2016
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 1818
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
FT CROSSLNK 1819
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P51610"
SQ SEQUENCE 2034 AA; 209153 MW; 55FAB6915E666B52 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 AAAAPPSTTT 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 DRQEAAASLV TSAVGQQNGN VVRVCSNPPC
ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDARRATN
TPTVVRITVA PGALERAQGT VKPPCQTQQT NMTSTTMTVQ ATGAPCSAGP LLRPSVALET
GSHSPAFVQL ALPSVRVGLS GPSSKDVPTG RQPETYHTYT TNTPTTARSI MVAGELGTAR
VVPTSQYDCL QASSPSSTMT MTALEALLCP SATVTQVCSN PPCETHETGT TNTATTSNAG
SAQRVCSNPP CETHETGTTH TATTATSNGG AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV
SVGALIPDAT PSHGTLESGL EVVAVPTVTS QAGATLLASF STQRVCSNPP CETHETGTTH
TATTVTSNMS SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTTVSSTLP RAVTTVTQST
PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES AEVLSASQTP ELQAAVDLSS
TGDPSSVQEP TTSAVVATVV VQPPQPTQSE VDQLSLPQEL MAEAQAGTTT LMVTGLTPEE
LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA AQQAVMGTGE PMDTSEAAAA VTQAELGHLS
AEGQEGQATT IPIVLTQQEL AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE
SNCLNELASA VPSTVALLPS TATESLAPSN TFVAPQPVVV ASPAKMQAAA TLTEVANGIE
SLGVKPDLPP PPSKAPIKKE NQWFDVGVIK GTSVMVTHYF LPPDDAVQSD DDSGTVPDYN
QLKKQELQPG TAYKFRVAGI NACGRGPFSE ISAFKTCLPG FPGAPCAIKI SKSPDGAHLT
WEPPSVTSGK IIEYSVYLAI QSSQASGEPK SSTPAQLAFM RVYCGPSPSC LVQSSSLSNA
HIDYTTKPAI IFRIAARNEK GYGPATQVRW LQETSKDSSG TKPASKRPMS SPEM
