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Coiled-coil domain-containing protein 85B (Hepatitis delta antigen-interacting protein A) (Delta-interacting protein A)

 CC85B_HUMAN             Reviewed;         202 AA.
Q15834; B2R598; Q96HA0;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
13-FEB-2019, entry version 137.
RecName: Full=Coiled-coil domain-containing protein 85B;
AltName: Full=Hepatitis delta antigen-interacting protein A;
Short=Delta-interacting protein A;
Name=CCDC85B; Synonyms=DIPA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), AND
INTERACTION WITH HEPATITIS DELTA ANTIGEN HDAG (MICROBIAL INFECTION).
TISSUE=Promyelocytic leukemia;
PubMed=8810253; DOI=10.1126/science.274.5284.90;
Brazas R., Ganem D.;
"A cellular homolog of hepatitis delta antigen: implications for viral
replication and evolution.";
Science 274:90-94(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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]
FUNCTION, INTERACTION WITH MCRS1, AND SUBCELLULAR LOCATION.
PubMed=17014843; DOI=10.1016/j.yexmp.2006.07.008;
Du X., Wang Q., Hirohashi Y., Greene M.I.;
"DIPA, which can localize to the centrosome, associates with
p78/MCRS1/MSP58 and acts as a repressor of gene transcription.";
Exp. Mol. Pathol. 81:184-190(2006).
[6]
FUNCTION, INTERACTION WITH TCF7L2, INDUCTION BY DOXORUBICIN,
MUTAGENESIS OF LEU-131, AND SUBCELLULAR LOCATION.
PubMed=17873903; DOI=10.1038/sj.onc.1210801;
Iwai A., Hijikata M., Hishiki T., Isono O., Chiba T., Shimotohno K.;
"Coiled-coil domain containing 85B suppresses the beta-catenin
activity in a p53-dependent manner.";
Oncogene 27:1520-1526(2008).
[7]
INTERACTION WITH ANKRD26.
PubMed=22666460; DOI=10.1371/journal.pone.0038130;
Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A.,
Pastan I.;
"ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA
regulate adipogenesis in 3T3-L1 cells.";
PLoS ONE 7:E38130-E38130(2012).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Functions as a transcriptional repressor
(PubMed:17014843). May inhibit the activity of CTNNB1 in a TP53-
dependent manner and thus regulate cell growth (PubMed:17873903).
May function in adipocyte differentiation, negatively regulating
mitotic clonal expansion (By similarity).
{ECO:0000250|UniProtKB:Q6PDY0, ECO:0000269|PubMed:17014843,
ECO:0000269|PubMed:17873903}.
-!- FUNCTION: (Microbial infection) Plays a role in hepatitis delta
virus (HDV) genomic replication. {ECO:0000269|PubMed:8810253}.
-!- SUBUNIT: Interacts with CEBPB (By similarity). Interacts with EURL
(By similarity). May interact with CEBPD (By similarity).
Interacts with MCRS1 (PubMed:17014843). Interacts with TCF7L2;
competes with CTNNB1 (PubMed:17873903). Interacts with ANKRD26
(PubMed:22666460). {ECO:0000250|UniProtKB:Q6PDY0,
ECO:0000269|PubMed:17014843, ECO:0000269|PubMed:17873903,
ECO:0000269|PubMed:22666460}.
-!- SUBUNIT: (Microbial infection) Interacts with the viral
phosphoprotein hepatitis delta antigen (HDAG); this interaction
affects hepatitis delta virus (HDV) genomic replication in intact
cells. {ECO:0000269|PubMed:8810253}.
-!- INTERACTION:
Q9UFG5:C19orf25; NbExp=2; IntAct=EBI-739674, EBI-741214;
Q9NX63:CHCHD3; NbExp=2; IntAct=EBI-739674, EBI-743375;
Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-739674, EBI-10247271;
Q7Z3B3:KANSL1; NbExp=2; IntAct=EBI-739674, EBI-740244;
Q04695:KRT17; NbExp=2; IntAct=EBI-739674, EBI-297873;
P02538:KRT6A; NbExp=2; IntAct=EBI-739674, EBI-702198;
Q16512:PKN1; NbExp=2; IntAct=EBI-739674, EBI-602382;
Q96NG3:TTC25; NbExp=3; IntAct=EBI-739674, EBI-1046387;
Q8TBZ8:ZNF564; NbExp=3; IntAct=EBI-739674, EBI-10273713;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17014843,
ECO:0000269|PubMed:17873903}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:17014843}.
-!- TISSUE SPECIFICITY: Widely expressed including liver.
-!- INDUCTION: Up-regulated by doxorubicin.
{ECO:0000269|PubMed:17873903}.
-!- MISCELLANEOUS: May be the cellular homolog of HDAG. Overexpression
inhibited HDV replication, whereas overexpression of HDAG reversed
the inhibition, suggesting that HDAG may assist HDV replication by
forming a complex with DIPA.
-!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
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EMBL; U63825; AAB05928.1; -; mRNA.
EMBL; AK312109; BAG35045.1; -; mRNA.
EMBL; CH471076; EAW74468.1; -; Genomic_DNA.
EMBL; BC008796; AAH08796.1; -; mRNA.
CCDS; CCDS8120.1; -.
RefSeq; NP_006839.2; NM_006848.2.
UniGene; Hs.66713; -.
ProteinModelPortal; Q15834; -.
SMR; Q15834; -.
BioGrid; 116198; 151.
CORUM; Q15834; -.
IntAct; Q15834; 140.
MINT; Q15834; -.
STRING; 9606.ENSP00000311695; -.
iPTMnet; Q15834; -.
PhosphoSitePlus; Q15834; -.
BioMuta; CCDC85B; -.
DMDM; 92090801; -.
EPD; Q15834; -.
jPOST; Q15834; -.
MaxQB; Q15834; -.
PaxDb; Q15834; -.
PeptideAtlas; Q15834; -.
PRIDE; Q15834; -.
ProteomicsDB; 60784; -.
DNASU; 11007; -.
Ensembl; ENST00000312579; ENSP00000311695; ENSG00000175602.
GeneID; 11007; -.
KEGG; hsa:11007; -.
UCSC; uc001ogf.4; human.
CTD; 11007; -.
EuPathDB; HostDB:ENSG00000175602.3; -.
GeneCards; CCDC85B; -.
HGNC; HGNC:24926; CCDC85B.
HPA; HPA054415; -.
MIM; 605360; gene.
neXtProt; NX_Q15834; -.
OpenTargets; ENSG00000175602; -.
PharmGKB; PA144596453; -.
eggNOG; KOG3819; Eukaryota.
eggNOG; ENOG410YXPD; LUCA.
GeneTree; ENSGT00940000162317; -.
HOGENOM; HOG000234335; -.
HOVERGEN; HBG107255; -.
InParanoid; Q15834; -.
KO; K16758; -.
OMA; GHHAAKV; -.
OrthoDB; 1393196at2759; -.
PhylomeDB; Q15834; -.
TreeFam; TF320243; -.
GeneWiki; CCDC85B; -.
GenomeRNAi; 11007; -.
PRO; PR:Q15834; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000175602; Expressed in 224 organ(s), highest expression level in substantia nigra.
Genevisible; Q15834; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
InterPro; IPR019359; CCDC85.
PANTHER; PTHR13546; PTHR13546; 1.
Pfam; PF10226; CCDC85; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Growth regulation; Nucleus; Reference proteome;
Repressor; Transcription; Transcription regulation.
CHAIN 1 202 Coiled-coil domain-containing protein
85B.
/FTId=PRO_0000079908.
COILED 43 90 {ECO:0000255}.
COILED 118 147 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MUTAGEN 131 131 L->A: Loss of interaction with TCF7L2 and
loss of suppression of CTNNB1 activity.
Loss of cell growth inhibition.
{ECO:0000269|PubMed:17873903}.
CONFLICT 34 34 A -> T (in Ref. 1; AAB05928).
{ECO:0000305}.
SEQUENCE 202 AA; 22091 MW; EA92D1B712A54047 CRC64;
MEAEAGGLEE LTDEEMAALG KEELVRRLRR EEAARLAALV QRGRLMQEVN RQLQGHLGEI
RELKQLNRRL QAENRELRDL CCFLDSERQR GRRAARQWQL FGTQASRAVR EDLGGCWQKL
AELEGRQEEL LRENLALKEL CLALGEEWGP RGGPSGAGGS GAGPAPELAL PPCGPRDLGD
GSSSTGSVGS PDQLPLACSP DD


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Pathways :
WP1644: DNA replication
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1689: Porphyrin and chlorophyll metabolism
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation

Related Genes :
[Or85b CG11735] Odorant receptor 85b
[HSD3B1 3BH HSDB3A] 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1) (Trophoblast antigen FDO161G)
[PIK3CD] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (PI3-kinase subunit delta) (PI3K-delta) (PI3Kdelta) (PtdIns-3-kinase subunit delta) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta) (PtdIns-3-kinase subunit p110-delta) (p110delta)
[Pik3cd] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (PI3-kinase subunit delta) (PI3K-delta) (PI3Kdelta) (PtdIns-3-kinase subunit delta) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta) (PtdIns-3-kinase subunit p110-delta) (p110delta)
[fbpB MSMEG_2078 MSMEI_2033] Diacylglycerol acyltransferase/mycolyltransferase Ag85B (DGAT) (EC 2.3.1.122) (EC 2.3.1.20) (30 kDa extracellular protein) (Acyl-CoA:diacylglycerol acyltransferase) (Antigen 85 complex B) (85B) (Ag85B) (Extracellular alpha-antigen) (Fibronectin-binding protein B) (Fbps B)
[] Capsid scaffolding protein (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease); Assembly protein (Capsid assembly protein)]
[UGT85B1 HMNGT] Cyanohydrin beta-glucosyltransferase (EC 2.4.1.85) (UDP-glucose-p-hydroxymandelonitrile glucosyltransferase)
[] Large delta antigen (L-HDAg) (p27)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[gB] Envelope glycoprotein B (gB)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[SETD2 HIF1 HYPB KIAA1732 KMT3A SET2 HSPC069] Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Hsd3b1 Hsd3b] 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Hsd3b1] 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I) (3-beta-HSD I) (3-beta-hydroxy-5-ene steroid dehydrogenase) (3-beta-hydroxy-Delta(5)-steroid dehydrogenase) (EC 1.1.1.145) (3-beta-hydroxysteroid 3-dehydrogenase) (EC 1.1.1.270) (Delta-5-3-ketosteroid isomerase) (Dihydrotestosterone oxidoreductase) (EC 1.1.1.210) (Steroid Delta-isomerase) (EC 5.3.3.1)
[HSD3B2 HSDB3B] 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II) (3-beta-HSD II) (3-beta-HSD adrenal and gonadal type) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)]
[ERG3 PSO6 SYR1 YLR056W L2150] Delta(7)-sterol 5(6)-desaturase (EC 1.14.19.20) (C-5 sterol desaturase) (Ergosterol Delta(5,6) desaturase) (Sterol-C5-desaturase)
[aroK aroB B0085_1588] Multifunctional fusion protein [Includes: Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4)]
[PRKCD] Protein kinase C delta type (EC 2.7.11.13) (Tyrosine-protein kinase PRKCD) (EC 2.7.10.2) (nPKC-delta) [Cleaved into: Protein kinase C delta type regulatory subunit; Protein kinase C delta type catalytic subunit (Sphingosine-dependent protein kinase-1) (SDK1)]
[Prkcd Pkcd] Protein kinase C delta type (EC 2.7.11.13) (Tyrosine-protein kinase PRKCD) (EC 2.7.10.2) (nPKC-delta) [Cleaved into: Protein kinase C delta type regulatory subunit; Protein kinase C delta type catalytic subunit (Sphingosine-dependent protein kinase-1) (SDK1)]
[Akap7 Akap18] A-kinase anchor protein 7 isoforms delta and gamma (AKAP-7 isoforms delta and gamma) (A-kinase anchor protein 18) (AKAP-18) (Protein kinase A-anchoring protein 7 isoforms delta and gamma) (PRKA7 isoforms delta and gamma)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)] (Fragments)

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