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Host cell factor 1 (HCF) (HCF-1) (C1 factor) [Cleaved into: HCF N-terminal chain 1; HCF N-terminal chain 2; HCF N-terminal chain 3; HCF N-terminal chain 4; HCF N-terminal chain 5; HCF N-terminal chain 6; HCF C-terminal chain 1; HCF C-terminal chain 2; HCF C-terminal chain 3; HCF C-terminal chain 4; HCF C-terminal chain 5; HCF C-terminal chain 6]

 HCFC1_MOUSE             Reviewed;        2045 AA.
Q61191; B1AUX1; Q684R1; Q7TSB0; Q8C2D0; Q9QWH2;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 163.
RecName: Full=Host cell factor 1;
Short=HCF;
Short=HCF-1;
AltName: Full=C1 factor;
Contains:
RecName: Full=HCF N-terminal chain 1;
Contains:
RecName: Full=HCF N-terminal chain 2;
Contains:
RecName: Full=HCF N-terminal chain 3;
Contains:
RecName: Full=HCF N-terminal chain 4;
Contains:
RecName: Full=HCF N-terminal chain 5;
Contains:
RecName: Full=HCF N-terminal chain 6;
Contains:
RecName: Full=HCF C-terminal chain 1;
Contains:
RecName: Full=HCF C-terminal chain 2;
Contains:
RecName: Full=HCF C-terminal chain 3;
Contains:
RecName: Full=HCF C-terminal chain 4;
Contains:
RecName: Full=HCF C-terminal chain 5;
Contains:
RecName: Full=HCF C-terminal chain 6;
Name=Hcfc1 {ECO:0000312|MGI:MGI:105942};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB01163.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND TISSUE
SPECIFICITY.
TISSUE=Fetal liver {ECO:0000269|PubMed:9334261};
PubMed=9334261; DOI=10.1074/jbc.272.42.26749;
Kristie T.M.;
"The mouse homologue of the human transcription factor C1 (host cell
factor). Conservation of forms and function.";
J. Biol. Chem. 272:26749-26755(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3] {ECO:0000305, ECO:0000312|EMBL:CAF25305.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305, ECO:0000312|EMBL:AAH53742.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb mesenchyme {ECO:0000269|PubMed:15489334};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-209.
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6] {ECO:0000305, ECO:0000312|EMBL:CAF25305.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 165-520.
STRAIN=NMRI; TISSUE=Embryo;
Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J.,
Pepperkok R., Wiemann S., Poustka A.;
"Towards functional annotation of all Xq28 genes: expression and
intracellular localization analyses reveal novel candidates for
disease genes.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ {ECO:0000269|PubMed:9990006};
PubMed=9990006; DOI=10.1073/pnas.96.4.1229;
Kristie T.M., Vogel J.L., Sears A.E.;
"Nuclear localization of the C1 factor (host cell factor) in sensory
neurons correlates with reactivation of herpes simplex virus from
latency.";
Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
Maltby D.A., Schoepfer R., Burlingame A.L.;
"O-linked N-acetylglucosamine proteomics of postsynaptic density
preparations using lectin weak affinity chromatography and mass
spectrometry.";
Mol. Cell. Proteomics 5:923-934(2006).
[9]
INTERACTION WITH THAP11.
PubMed=18585351; DOI=10.1016/j.cell.2008.05.047;
Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
Songyang Z., Thomson J.A., Zwaka T.P.;
"Ronin is essential for embryogenesis and the pluripotency of mouse
embryonic stem cells.";
Cell 133:1162-1174(2008).
[10]
ERRATUM.
Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
Songyang Z., Thomson J.A., Zwaka T.P.;
Cell 134:692-692(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-1516 AND
SER-1848, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-504; ARG-524 AND ARG-1216,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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.
As part of the NSL complex it may be involved in acetylation of
nucleosomal histone H4 on several lysine residues.
{ECO:0000269|PubMed:9334261, ECO:0000269|PubMed:9990006}.
-!- SUBUNIT: 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 the
MLL5-L complex, composed of at least KMT2E/MLL5, STK38, PPP1CA,
PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts directly with OGT;
the interaction, which requires the cleavage site domain,
glycosylates and promotes proteolytic processing of HCFC1 and
retains OGT in the nucleus. Interacts with TET2 and TET3.
Interacts with HCFC1R1. Component of the SET1 complex, at least
composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82,
RBBP5, ASH2L, CXXC1, HCFC1 and DPY30. Interacts (via HBM motif)
with SETD1A. Component of the NSL complex at least composed of
MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and
HCFC1 (By similarity). 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 (By similarity). Interacts with THAP11.
{ECO:0000250, ECO:0000269|PubMed:18585351,
ECO:0000269|PubMed:9334261}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9990006}.
Cytoplasm {ECO:0000269|PubMed:9990006}. Note=HCFC1R1 modulates its
subcellular localization and overexpression of HCFC1R1 leads to
accumulation of HCFC1 in the cytoplasm. Non-processed HCFC1
associates with chromatin. Colocalizes with CREB3 and CANX in the
ER (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in liver, pituitary gland, skeletal
muscle, kidney, eye and brain (at protein level). Also observed at
low level in heart, spleen and lung. {ECO:0000269|PubMed:9334261,
ECO:0000269|PubMed:9990006}.
-!- DOMAIN: The HCF repeat is a highly specific proteolytic cleavage
signal. {ECO:0000250|UniProtKB:P51610}.
-!- DOMAIN: The kelch repeats fold into a 6-bladed kelch beta-
propeller called the beta-propeller domain which mediates
interaction with HCFC1R1. {ECO:0000250}.
-!- PTM: Proteolytically cleaved at one or several PPCE--THET sites
within the HCF repeats. Cleavage is promoted by O-glycosylation
(By similarity). {ECO:0000250}.
-!- PTM: O-glycosylated. GlcNAcylation by OGT promotes proteolytic
processing (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Lys-1817 and Lys-1818 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
(By similarity). {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=CAF25305.1; Type=Frameshift; Positions=339; Evidence={ECO:0000305};
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EMBL; U53925; AAB01163.1; -; Genomic_DNA.
EMBL; U80821; AAD09225.1; -; Genomic_DNA.
EMBL; AL672002; CAM18726.1; -; Genomic_DNA.
EMBL; CH466650; EDL29851.1; -; Genomic_DNA.
EMBL; BC053742; AAH53742.1; -; mRNA.
EMBL; AK088827; BAC40597.1; -; mRNA.
EMBL; AJ627036; CAF25305.1; ALT_FRAME; mRNA.
CCDS; CCDS30218.1; -.
RefSeq; NP_032250.2; NM_008224.4.
UniGene; Mm.491126; -.
PDB; 2M26; NMR; -; A=1896-2020.
PDBsum; 2M26; -.
ProteinModelPortal; Q61191; -.
SMR; Q61191; -.
BioGrid; 200248; 10.
IntAct; Q61191; 4.
MINT; MINT-4097262; -.
STRING; 10090.ENSMUSP00000033761; -.
iPTMnet; Q61191; -.
PhosphoSitePlus; Q61191; -.
EPD; Q61191; -.
MaxQB; Q61191; -.
PaxDb; Q61191; -.
PeptideAtlas; Q61191; -.
PRIDE; Q61191; -.
Ensembl; ENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
GeneID; 15161; -.
KEGG; mmu:15161; -.
UCSC; uc009tnm.2; mouse.
CTD; 3054; -.
MGI; MGI:105942; Hcfc1.
eggNOG; ENOG410KDN3; Eukaryota.
eggNOG; ENOG410Y5WM; LUCA.
GeneTree; ENSGT00760000119086; -.
HOGENOM; HOG000293192; -.
HOVERGEN; HBG051888; -.
InParanoid; Q61191; -.
KO; K14966; -.
TreeFam; TF314757; -.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-5689603; UCH proteinases.
ChiTaRS; Hcfc1; mouse.
PRO; PR:Q61191; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031386; -.
CleanEx; MM_HCFC1; -.
ExpressionAtlas; Q61191; baseline and differential.
Genevisible; Q61191; MM.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070461; C:SAGA-type complex; IEA:Ensembl.
GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IEA:Ensembl.
GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); IEA:Ensembl.
GO; GO:0043996; F:histone acetyltransferase activity (H4-K8 specific); IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0043254; P:regulation of protein complex assembly; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0019046; P:release from viral latency; IDA:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.120.10.80; -; 2.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR006652; Kelch_1.
Pfam; PF01344; Kelch_1; 1.
SMART; SM00060; FN3; 2.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Autocatalytic cleavage; Cell cycle;
Chromatin regulator; Complete proteome; Cytoplasm; Glycoprotein;
Isopeptide bond; Kelch repeat; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P51610}.
CHAIN 2 1432 HCF N-terminal chain 6. {ECO:0000250}.
/FTId=PRO_0000016635.
CHAIN 2 1332 HCF N-terminal chain 5. {ECO:0000250}.
/FTId=PRO_0000016636.
CHAIN 2 1304 HCF N-terminal chain 4. {ECO:0000250}.
/FTId=PRO_0000016637.
CHAIN 2 1110 HCF N-terminal chain 3. {ECO:0000250}.
/FTId=PRO_0000016638.
CHAIN 2 1081 HCF N-terminal chain 2. {ECO:0000250}.
/FTId=PRO_0000016639.
CHAIN 2 1019 HCF N-terminal chain 1. {ECO:0000250}.
/FTId=PRO_0000016640.
CHAIN 1020 2045 HCF C-terminal chain 1.
{ECO:0000250|UniProtKB:P51610}.
/FTId=PRO_0000016641.
CHAIN 1082 2045 HCF C-terminal chain 2.
{ECO:0000250|UniProtKB:P51610}.
/FTId=PRO_0000016642.
CHAIN 1111 2045 HCF C-terminal chain 3.
{ECO:0000250|UniProtKB:P51610}.
/FTId=PRO_0000016643.
CHAIN 1305 2045 HCF C-terminal chain 4.
{ECO:0000250|UniProtKB:P51610}.
/FTId=PRO_0000016644.
CHAIN 1333 2045 HCF C-terminal chain 5.
{ECO:0000250|UniProtKB:P51610}.
/FTId=PRO_0000016645.
CHAIN 1433 2045 HCF C-terminal chain 6.
{ECO:0000250|UniProtKB:P51610}.
/FTId=PRO_0000016646.
REPEAT 44 89 Kelch 1. {ECO:0000255}.
REPEAT 93 140 Kelch 2. {ECO:0000255}.
REPEAT 148 194 Kelch 3. {ECO:0000255}.
REPEAT 217 265 Kelch 4. {ECO:0000255}.
REPEAT 266 313 Kelch 5. {ECO:0000255}.
DOMAIN 366 457 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REPEAT 1010 1035 HCF repeat 1. {ECO:0000255}.
REPEAT 1072 1097 HCF repeat 2. {ECO:0000255}.
REPEAT 1101 1126 HCF repeat 3. {ECO:0000255}.
REPEAT 1157 1182 HCF repeat 4; degenerate.
REPEAT 1295 1320 HCF repeat 5. {ECO:0000255}.
REPEAT 1323 1348 HCF repeat 6. {ECO:0000255}.
REPEAT 1358 1383 HCF repeat 7; degenerate.
REPEAT 1423 1448 HCF repeat 8. {ECO:0000255}.
DOMAIN 1808 1898 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1900 2016 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 500 550 Required for interaction with OGT.
{ECO:0000250}.
REGION 610 722 Interaction with SIN3A. {ECO:0000250}.
REGION 750 902 Interaction with ZBTB17. {ECO:0000250}.
REGION 813 912 Interaction with GABP2. {ECO:0000250}.
COMPBIAS 574 1500 Thr-rich. {ECO:0000255}.
COMPBIAS 1622 1674 Ala-rich. {ECO:0000255}.
COMPBIAS 1684 1720 Gln-rich. {ECO:0000255}.
SITE 1019 1020 Cleavage; by autolysis. {ECO:0000250}.
SITE 1081 1082 Cleavage; by autolysis. {ECO:0000250}.
SITE 1110 1111 Cleavage; by autolysis. {ECO:0000250}.
SITE 1304 1305 Cleavage; by autolysis. {ECO:0000250}.
SITE 1332 1333 Cleavage; by autolysis. {ECO:0000250}.
SITE 1432 1433 Cleavage; by autolysis. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 504 504 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 524 524 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 813 813 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 1204 1204 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 1216 1216 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 1500 1500 Phosphothreonine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 1506 1506 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 1516 1516 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1781 1781 Phosphoserine.
{ECO:0000250|UniProtKB:P51610}.
MOD_RES 1848 1848 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2015 2015 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 244 244 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 282 282 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 363 363 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 1817 1817 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 1818 1818 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P51610}.
CROSSLNK 2034 2034 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P51610}.
CONFLICT 483 483 V -> R (in Ref. 1; AAB01163/AAD09225).
{ECO:0000305}.
CONFLICT 520 520 P -> S (in Ref. 6; CAF25305).
{ECO:0000305}.
CONFLICT 567 568 VL -> AW (in Ref. 1; AAB01163/AAD09225).
{ECO:0000305}.
CONFLICT 711 711 Q -> H (in Ref. 1; AAD09225).
{ECO:0000305}.
CONFLICT 1104 1104 C -> S (in Ref. 1; AAB01163/AAD09225).
{ECO:0000305}.
CONFLICT 1230 1230 G -> A (in Ref. 1; AAB01163/AAD09225).
{ECO:0000305}.
STRAND 1897 1899 {ECO:0000244|PDB:2M26}.
STRAND 1905 1912 {ECO:0000244|PDB:2M26}.
STRAND 1915 1921 {ECO:0000244|PDB:2M26}.
STRAND 1924 1926 {ECO:0000244|PDB:2M26}.
STRAND 1930 1938 {ECO:0000244|PDB:2M26}.
STRAND 1965 1968 {ECO:0000244|PDB:2M26}.
HELIX 1973 1977 {ECO:0000244|PDB:2M26}.
STRAND 1984 1997 {ECO:0000244|PDB:2M26}.
STRAND 2005 2010 {ECO:0000244|PDB:2M26}.
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


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