GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)

 HBSAG_HBVD3             Reviewed;         389 AA.
P03138;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
16-JAN-2019, entry version 99.
RecName: Full=Large envelope protein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=L glycoprotein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=L-HBsAg {ECO:0000255|HAMAP-Rule:MF_04075};
Short=LHB {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=Large S protein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=Large surface protein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=Major surface antigen {ECO:0000255|HAMAP-Rule:MF_04075};
Name=S {ECO:0000255|HAMAP-Rule:MF_04075};
Hepatitis B virus genotype D subtype ayw (isolate
France/Tiollais/1979) (HBV-D).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=490133;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=399327; DOI=10.1038/281646a0;
Galibert F., Mandart E., Fitoussi F., Tiollais P., Charnay P.;
"Nucleotide sequence of the hepatitis B virus genome (subtype ayw)
cloned in E. coli.";
Nature 281:646-650(1979).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Latvia;
PubMed=3996597; DOI=10.1016/0014-5793(85)80771-7;
Bichko V., Pushko P., Dreilina D., Pumpen P., Gren E.Y.;
"Subtype ayw variant of hepatitis B virus. DNA primary structure
analysis.";
FEBS Lett. 185:208-212(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Latvia;
PubMed=6373205;
Kozlovskaia T.M., Pumpen P.P., Borisova G.P., Dishler A.V.,
Bychko V.V.;
"Synthesis of the full amino acid sequence of the surface antigen of
the hepatitis B virus in Escherichia coli.";
Dokl. Akad. Nauk SSSR 274:1250-1253(1984).
[4]
MYRISTOYLATION AT GLY-2.
PubMed=3573147;
Persing D.H., Varmus H.E., Ganem D.;
"The preS1 protein of hepatitis B virus is acylated at its amino
terminus with myristic acid.";
J. Virol. 61:1672-1677(1987).
[5]
TRANSMEMBRANE TOPOLOGY.
PubMed=7835336;
Prange R., Streeck R.E.;
"Novel transmembrane topology of the hepatitis B virus envelope
proteins.";
EMBO J. 14:247-256(1995).
[6]
MUTAGENESIS OF GLY-2.
PubMed=7491754; DOI=10.1006/viro.1995.0002;
Gripon P., Le Seyec J., Rumin S., Guguen-Guillouzo C.;
"Myristylation of the hepatitis B virus large surface protein is
essential for viral infectivity.";
Virology 213:292-299(1995).
[7]
FUNCTION.
PubMed=9420286;
Werr M., Prange R.;
"Role for calnexin and N-linked glycosylation in the assembly and
secretion of hepatitis B virus middle envelope protein particles.";
J. Virol. 72:778-782(1998).
[8]
GLYCOSYLATION (ISOFORM M), AND ACETYLATION AT MET-1 (ISOFORM M).
STRAIN=Isolate clinical;
PubMed=10207016; DOI=10.1074/jbc.274.17.11945;
Schmitt S., Glebe D., Alving K., Tolle T.K., Linder M., Geyer H.,
Linder D., Peter-Katalinic J., Gerlich W.H., Geyer R.;
"Analysis of the pre-S2 N- and O-linked glycans of the M surface
protein from human hepatitis B virus.";
J. Biol. Chem. 274:11945-11957(1999).
[9]
GLYCOSYLATION AT THR-37 (ISOFORM M).
PubMed=15218190; DOI=10.1099/vir.0.79932-0;
Schmitt S., Glebe D., Tolle T.K., Lochnit G., Linder D., Geyer R.,
Gerlich W.H.;
"Structure of pre-S2 N- and O-linked glycans in surface proteins from
different genotypes of hepatitis B virus.";
J. Gen. Virol. 85:2045-2053(2004).
[10]
FUNCTION.
PubMed=17020942; DOI=10.1128/JVI.00621-06;
Blanchet M., Sureau C.;
"Analysis of the cytosolic domains of the hepatitis B virus envelope
proteins for their function in viral particle assembly and
infectivity.";
J. Virol. 80:11935-11945(2006).
[11]
MUTAGENESIS OF LEU-11; GLY-12 AND 13-PHE-PHE-14.
PubMed=16557545; DOI=10.1002/hep.21112;
Engelke M., Mills K., Seitz S., Simon P., Gripon P., Schnolzer M.,
Urban S.;
"Characterization of a hepatitis B and hepatitis delta virus receptor
binding site.";
Hepatology 43:750-760(2006).
[12]
MUTAGENESIS OF 11-LEU--PRO-15; 16-ASP--ASP-20; 21-PRO--ALA-25;
26-ASN--PRO-30; 31-ASP--ASN-35; 36-PRO--THR-40; 41-TRP--ASN-45;
46-LYS--GLY-50; 51-ALA--GLY-55; 56-PHE--HIS-60; 61-GLY--GLY-65;
66-TRP--ALA-70; 71-GLN--GLN-75; 76-THR--ASN-80; 81-PRO--SER-85;
86-THR--SER-90; 91-GLY--THR-95; 96-PRO--PRO-100; 101-LEU--HIS-105 AND
106-PRO--GLN-110.
PubMed=17376925; DOI=10.1128/JVI.00096-07;
Blanchet M., Sureau C.;
"Infectivity determinants of the hepatitis B virus pre-S domain are
confined to the N-terminal 75 amino acid residues.";
J. Virol. 81:5841-5849(2007).
[13]
REVIEW.
PubMed=8957666;
Bruss V., Gerhardt E., Vieluf K., Wunderlich G.;
"Functions of the large hepatitis B virus surface protein in viral
particle morphogenesis.";
Intervirology 39:23-31(1996).
[14]
REVIEW.
PubMed=9498079;
Block T.M., Lu X., Mehta A., Park J., Blumberg B.S., Dwek R.;
"Role of glycan processing in hepatitis B virus envelope protein
trafficking.";
Adv. Exp. Med. Biol. 435:207-216(1998).
[15]
REVIEW.
PubMed=15567498; DOI=10.1016/j.virusres.2004.08.016;
Bruss V.;
"Envelopment of the hepatitis B virus nucleocapsid.";
Virus Res. 106:199-209(2004).
[16]
REVIEW.
PubMed=16863502; DOI=10.1111/j.1349-7006.2006.00235.x;
Wang H.C., Huang W., Lai M.D., Su I.J.;
"Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and
hepatocarcinogenesis.";
Cancer Sci. 97:683-688(2006).
-!- FUNCTION: The large envelope protein exists in two topological
conformations, one which is termed 'external' or Le-HBsAg and the
other 'internal' or Li-HBsAg. In its external conformation the
protein attaches the virus to cell receptors and thereby
initiating infection. This interaction determines the species
specificity and liver tropism. This attachment induces virion
internalization predominantly through caveolin-mediated
endocytosis. The large envelope protein also assures fusion
between virion membrane and endosomal membrane. In its internal
conformation the protein plays a role in virion morphogenesis and
mediates the contact with the nucleocapsid like a matrix protein.
{ECO:0000255|HAMAP-Rule:MF_04075}.
-!- FUNCTION: The middle envelope protein plays an important role in
the budding of the virion. It is involved in the induction of
budding in a nucleocapsid independent way. In this process the
majority of envelope proteins bud to form subviral lipoprotein
particles of 22 nm of diameter that do not contain a nucleocapsid.
{ECO:0000255|HAMAP-Rule:MF_04075}.
-!- SUBUNIT: Li-HBsAg interacts with capsid protein and with HDV Large
delta antigen. Isoform M associates with host chaperone CANX
through its pre-S2 N glycan. This association may be essential for
M proper secretion. {ECO:0000255|HAMAP-Rule:MF_04075}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04075}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
IsoId=P03138-1; Sequence=Displayed;
Name=M; Synonyms=Middle envelope protein, MHB, M-HBsAg;
IsoId=P03138-2; Sequence=VSP_031405;
Note=Contains a N-acetylmethionine at position 1. Contains a
O-linked (GalNAc...) threonine at position 37.
{ECO:0000269|PubMed:10207016, ECO:0000269|PubMed:15218190};
Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
IsoId=P03138-3; Sequence=VSP_031404;
-!- DOMAIN: The large envelope protein is synthesized with the pre-S
region at the cytosolic side of the endoplasmic reticulum and,
hence will be within the virion after budding. Therefore the pre-S
region is not N-glycosylated. Later a post-translational
translocation of N-terminal pre-S and TM1 domains occur in about
50% of proteins at the virion surface. These molecules change
their topology by an unknown mechanism, resulting in exposure of
pre-S region at virion surface. For isoform M in contrast, the
pre-S2 region is translocated cotranslationally to the endoplasmic
reticulum lumen and is N-glycosylated. {ECO:0000255|HAMAP-
Rule:MF_04075}.
-!- PTM: Isoform M is N-terminally acetylated by host at a ratio of
90%, and N-glycosylated by host at the pre-S2 region.
{ECO:0000255|HAMAP-Rule:MF_04075, ECO:0000269|PubMed:10207016,
ECO:0000269|PubMed:15218190}.
-!- PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
-!- BIOTECHNOLOGY: Systematic vaccination of individuals at risk of
exposure to the virus has been the main method of controlling the
morbidity and mortality associated with hepatitis B. The first
hepatitis B vaccine was manufactured by the purification and
inactivation of HBsAg obtained from the plasma of chronic
hepatitis B virus carriers. The vaccine is now produced by
recombinant DNA techniques and expression of the S isoform in
yeast cells. The pre-S region do not seem to induce strong enough
antigenic response.
-!- SIMILARITY: Belongs to the orthohepadnavirus major surface antigen
family. {ECO:0000255|HAMAP-Rule:MF_04075}.
-!- SEQUENCE CAUTION:
Sequence=AAA45496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA26324.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; V01460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X02496; CAA26324.1; ALT_INIT; Genomic_DNA.
EMBL; M12393; AAA45496.1; ALT_INIT; Genomic_DNA.
PIR; A03703; SAVLAH.
SMR; P03138; -.
ELM; P03138; -.
EvolutionaryTrace; P03138; -.
Proteomes; UP000007930; Genome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
HAMAP; MF_04075; HBV_HBSAG; 1.
InterPro; IPR000349; HBV_HBSAG.
Pfam; PF00695; vMSA; 1.
1: Evidence at protein level;
Acetylation; Alternative initiation; Alternative splicing;
Caveolin-mediated endocytosis of virus by host; Complete proteome;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host-virus interaction; Lipoprotein; Membrane; Myristate;
Reference proteome; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral penetration into host cytoplasm;
Virion; Virus endocytosis by host; Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000255|HAMAP-
Rule:MF_04075}.
CHAIN 2 389 Large envelope protein.
{ECO:0000255|HAMAP-Rule:MF_04075}.
/FTId=PRO_0000038107.
TOPO_DOM 2 242 Intravirion; in internal conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 170 Virion surface; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 171 191 Helical; Name=TM1; Note=In external
conformation. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 192 242 Intravirion; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 243 263 Helical; Name=TM2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 264 337 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 338 358 Helical. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 359 364 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 365 387 Helical; Name=TM3. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 388 389 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 2 163 Pre-S. {ECO:0000255|HAMAP-Rule:MF_04075}.
REGION 2 108 Pre-S1. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 109 163 Pre-S2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
VAR_SEQ 1 163 Missing (in isoform S). {ECO:0000305}.
/FTId=VSP_031404.
VAR_SEQ 1 108 Missing (in isoform M). {ECO:0000305}.
/FTId=VSP_031405.
VARIANT 75 75 Q -> E (in strain: Latvia).
VARIANT 147 147 A -> S (in strain: Latvia).
VARIANT 150 150 L -> I (in strain: Latvia).
VARIANT 288 290 MTT -> TTP (in strain: Latvia).
MUTAGEN 2 2 G->A: Complete loss of myristoylation.
Complete loss of infectivity.
{ECO:0000269|PubMed:7491754}.
MUTAGEN 11 15 LGFFP->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 11 11 L->R: Complete loss of infectivity.
{ECO:0000269|PubMed:16557545}.
MUTAGEN 12 12 G->E: Complete loss of infectivity.
{ECO:0000269|PubMed:16557545}.
MUTAGEN 13 14 FF->SS: Complete loss of infectivity.
{ECO:0000269|PubMed:16557545}.
MUTAGEN 13 13 F->S: Complete loss of infectivity.
MUTAGEN 16 20 DHQLD->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 21 25 PAFRA->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 26 30 NTANP->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 31 35 DWDFN->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 36 40 PNKDT->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 41 45 WPDAN->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 47 50 VGAG->L: Complete loss of infectivity.
MUTAGEN 51 55 AFGLG->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 56 60 FTPPH->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 61 65 GGLLG->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 66 70 WSPQA->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 71 75 QGILQ->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 76 80 TLPAN->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 81 85 PPPAS->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 86 90 TNRQS->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 91 95 GRQPT->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 96 100 PLSPP->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 101 105 LRNTH->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 106 110 PQAMQ->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
SEQUENCE 389 AA; 42766 MW; 6DC9E682DA694F63 CRC64;
MGQNLSTSNP LGFFPDHQLD PAFRANTANP DWDFNPNKDT WPDANKVGAG AFGLGFTPPH
GGLLGWSPQA QGILQTLPAN PPPASTNRQS GRQPTPLSPP LRNTHPQAMQ WNSTTFHQTL
QDPRVRGLYF PAGGSSSGTV NPVLTTASPL SSIFSRIGDP ALNMENITSG FLGPLLVLQA
GFFLLTRILT IPQSLDSWWT SLNFLGGTTV CLGQNSQSPT SNHSPTSCPP TCPGYRWMCL
RRFIIFLFIL LLCLIFLLVL LDYQGMLPVC PLIPGSSTTS TGPCRTCMTT AQGTSMYPSC
CCTKPSDGNC TCIPIPSSWA FGKFLWEWAS ARFSWLSLLV PFVQWFVGLS PTVWLSVIWM
MWYWGPSLYS ILSPFLPLLP IFFCLWVYI


Related products :

Catalog number Product name Quantity
EIAAB11404 DAP-5,Discs large homolog 7,Disks large-associated protein 5,Disks large-associated protein DLG7,DLG7,DLGAP5,Hepatoma up-regulated protein,Homo sapiens,Human,HURP,KIAA0008
EIAAB11405 DAP-5,Discs large homolog 7,Disks large-associated protein 5,Disks large-associated protein DLG7,Dlg7,Dlgap5,Hepatoma up-regulated protein homolog,HURP,Kiaa0008,Mouse,Mus musculus
orb81766 Measles Virus Large Polymerase (58-149) protein The E.coli derived recombinant protein contains the large polymerase immunodominant regions, 58-149 amino acids. For research use only. 100
EIAAB11391 Discs large protein P-dlg,Disks large homolog 5,DLG5,Homo sapiens,Human,KIAA0583,PDLG,Placenta and prostate DLG
26-930 SFN is an adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathway. SFN binds to a large number of partners, usually by recognition of a phosp 0.05 mg
orb82659 HBV Surface Antigen adw protein HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV). The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a protein t 1 mg
orb82658 HBV Surface Antigen adr subtype protein HBsAg is the surface antigen of the Hepatitis-B-Virus (HBV). The capsid of a virus has different surface proteins from the rest of the virus. The antigen is a p 1 mg
CSB-E17341h Human Hepatitis B Virus Large Surface Protein(HBV-LP)ELISA kit, Species Human, Sample Type serum, plasma 96T
orb81768 Measles Virus Large Polymerase (2059-2183) protein The E.coli derived recombinant protein contains the large polymerase immunodominant regions, 2059-2183 amino acids. For research use only. 100
18-003-42367 Transcription elongation factor SPT5 - hSPT5; DRB sensitivity-inducing factor large subunit; DSIF large subunit; DSIF p160; Tat-cotransactivator 1 protein; Tat-CT1 protein Polyclonal 0.05 mg Aff Pur
E02H0214 Rat Hepatitis B virus Large Envelope protein ELISA , HBV-LP
E01H0214 Human Hepatitis B virus Large Envelope protein 96 Tests/kit
E02H0214 Rat Hepatitis B virus Large Envelope protein ELISA , HBV-LP 96 Tests/kit
E03H0214 Mouse Hepatitis B virus Large Envelope protein ELISA ,HBV-LP 96 Tests/kit
80-1024 Dengue large envelope protein (Subtype 2), Conjugated Proteins 1 mg
E01H0214 Human Anti-Hepatitis B virus Large Envelope protein 96 Tests/kit
E08H0214 Canine Hepatitis B virus Large Envelope protein ELISA , HBV-LP
E07H0214 Porcine Hepatitis B virus Large Envelope protein ELISA , HBV-LP
E05H0214 Guinea pig Hepatitis B virus Large Envelope protein ELISA , HBV-LP
80-1026 Dengue large envelope protein (Subtype 4), Conjugated Proteins 1 mg
E03H0214 Mouse Hepatitis B virus Large Envelope protein ELISA , HBV-LP
E14H0214 Sheep Hepatitis B virus Large Envelope protein ELISA , HBV-LP 96 Tests/kit
E11H0214 Bovine Hepatitis B virus Large Envelope protein ELISA , HBV-LP 96 Tests/kit
E01H0214 Human Hepatitis B virus Large Envelope protein ELISA , HBV-LP 96 Tests/kit
E14H0214 Sheep Hepatitis B virus Large Envelope protein ELISA , HBV-LP

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
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
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)
[S] Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)

Bibliography :
?>