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Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (PX); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Protein 3B (P3B) (VPg); 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)

 POLG_HAVHA              Reviewed;        2052 AA.
Q05794; Q67800; Q67801; Q67802; Q67803; Q67804; Q67805; Q67806;
Q67807;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
23-MAY-2018, entry version 91.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1-2A;
AltName: Full=PX;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
Contains:
RecName: Full=Protein 2BC;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3ABCD;
Short=P3;
Contains:
RecName: Full=Protein 3ABC;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B;
Short=P3B;
AltName: Full=VPg;
Contains:
RecName: Full=Protein 3CD;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28;
AltName: Full=Picornain 3C;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
Flags: Fragments;
Human hepatitis A virus genotype IA (isolate HAS-15) (HHAV) (Human
hepatitis A virus (isolate Human/Arizona/HAS-15/1979)).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Hepatovirus.
NCBI_TaxID=470424;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Sverdlov S.D., Tsarev S.A., Markova S.V., Vasilenko S.K.,
Chizhikov V.E., Petrov N.A., Kusov Y.Y., Nastashenko T.A.,
Balayan M.S.;
"Cloning and expression of hepatitis A virus genome in E. coli
cells.";
Mol. Genet. Microbiol. Virol. 6:129-133(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-906.
PubMed=3000718;
Ovchinnikov Y.A., Sverdlov E.D., Tsarev S.A., Arsenian S.G.,
Rokhlina T.O.;
"Sequence of 3372 RNA nucleotide links in the hepatitis A virus coding
for capsid VP4-VP1 and nonstructural proteins.";
Dokl. Akad. Nauk SSSR 285:1014-1018(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 758-813.
PubMed=1318940; DOI=10.1099/0022-1317-73-6-1365;
Robertson B.H., Jansen R.W., Khanna B., Totsuka A., Nainan O.V.,
Siegl G., Widell A., Margolis H.S., Isomura S., Ito K., Ishizu T.,
Moritsugu Y., Lemon S.M.;
"Genetic relatedness of hepatitis A virus strains recovered from
different geographical regions.";
J. Gen. Virol. 73:1365-1377(1992).
-!- FUNCTION: Capsid proteins VP1, VP2, and VP3 form a closed capsid
enclosing the viral positive strand RNA genome. All these proteins
contain a beta-sheet structure called beta-barrel jelly roll.
Together they form an icosahedral capsid (T=3) composed of 60
copies of each VP1, VP2, and VP3, with a diameter of approximately
300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas
VP2 and VP3 are located at the quasi-sixfold axes. The capsid
interacts with HAVCR1 to provide virion attachment to target cell
(By similarity). {ECO:0000250}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. The N-terminal domain of VP0, protein VP4, is needed
for the assembly of 12 pentamers into the icosahedral structure.
Unlike other picornaviruses, HAV VP4 does not seem to be
myristoylated and has not been detected in mature virions,
supposedly owing to its small size (By similarity). {ECO:0000250}.
-!- FUNCTION: VP1-2A precursor is a component of immature procapsids
and corresponds to an extended form of the structural protein VP1.
The C-terminal domain of VP1-2A, protein 2A, acts as an assembly
signal that allows multimerization of VP1-2A and formation of
pentamers of VP1-VP2-VP3 trimers. It is proteolytically removed
from the precursor by a host protease and does not seem to be
found in mature particles (By similarity). {ECO:0000250}.
-!- FUNCTION: Protein 2B and 2BC precursor affect membrane integrity
and cause an increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor to the 3AB and 3ABC precursors. {ECO:0000250}.
-!- FUNCTION: The 3AB precursor interacts with the 3CD precursor and
with RNA structures found at both the 5'- and 3'-termini of the
viral genome. Since the 3AB precursor contains the hydrophobic
domain 3A, it probably anchors the whole viral replicase complex
to intracellular membranes on which viral RNA synthesis occurs (By
similarity). {ECO:0000250}.
-!- FUNCTION: The 3ABC precursor is targeted to the mitochondrial
membrane where protease 3C activity cleaves and inhibits the host
antiviral protein MAVS, thereby disrupting activation of IRF3
through the IFIH1/MDA5 pathway. In vivo, the protease activity of
3ABC precursor is more efficient in cleaving the 2BC precursor
than that of protein 3C. The 3ABC precursor may therefore play a
role in the proteolytic processing of the polyprotein (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protein 3B is covalently linked to the 5'-end of both
the positive-strand and negative-strand genomic RNAs. It acts as a
genome-linked replication primer (By similarity). {ECO:0000250}.
-!- FUNCTION: Protease 3C: cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease. Also cleaves host proteins such as PCBP2 (By
similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- SUBUNIT: 3AB precursor is a homodimer. 3AB precursor interacts
with 3CD precursor. Protein 3ABC interacts with human MAVS (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1-2A: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum. May associate
with membranes through a N-terminal amphipathic helix (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3ABC: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Host mitochondrion outer membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3AB: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Interacts with membranes in a complex with viral protein 3AB.
Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum (By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages by the viral protease in vivo
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates are produced, such as P1-2A which is a
functional precursor of the structural proteins, VP0 which is a
VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a
stable and catalytically active precursor of 3A, 3B and 3C
proteins, 3AB and 3CD precursors. The assembly signal 2A is
removed from VP1-2A by a host protease. During virion maturation,
non-infectious particles are rendered infectious following
cleavage of VP0. This maturation cleavage is followed by a
conformational change of the particle (By similarity).
{ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
linked to the 5'-end of genomic RNA. This uridylylated form acts
as a nucleotide-peptide primer for the polymerase (By similarity).
{ECO:0000250}.
-!- MISCELLANEOUS: The need for an intact eIF4G factor for the
initiation of translation of HAV results in an inability to shut
off host protein synthesis by a mechanism similar to that of other
picornaviruses.
-!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
-!- CAUTION: Protein VP1 seems to have a heterogeneous C-terminus in
cell culture. It may be reduced by a few amino acids compared to
the sequence shown. {ECO:0000305}.
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EMBL; X15463; CAA33491.1; -; Genomic_RNA.
EMBL; X15464; CAA33492.1; -; Genomic_RNA.
EMBL; L07669; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; Q05794; -.
PRIDE; Q05794; -.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 2.
Gene3D; 2.60.120.20; -; 3.
InterPro; IPR024354; Hepatitis_A_VP1-2A.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF12944; HAV_VP; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 2.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
3: Inferred from homology;
ATP-binding; Capsid protein; Coiled coil;
Covalent protein-RNA linkage;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Helicase;
Host cytoplasm; Host cytoplasmic vesicle;
Host gene expression shutoff by virus; Host membrane;
Host mitochondrion; Host mitochondrion outer membrane;
Host-virus interaction; Hydrolase;
Interferon antiviral system evasion; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Transport; Viral attachment to host cell;
Viral ion channel; Viral RNA replication; Virion;
Virus entry into host cell.
CHAIN 1 2052 Genome polyprotein.
/FTId=PRO_0000311062.
CHAIN 1 245 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000311063.
CHAIN 1 23 Protein VP4. {ECO:0000255}.
/FTId=PRO_5000145525.
CHAIN 24 245 Protein VP2. {ECO:0000255}.
/FTId=PRO_5000145526.
CHAIN 246 491 Protein VP3. {ECO:0000255}.
/FTId=PRO_5000145527.
CHAIN 492 830 Protein VP1-2A. {ECO:0000255}.
/FTId=PRO_0000311064.
CHAIN 492 763 Protein VP1. {ECO:0000255}.
/FTId=PRO_5000145528.
CHAIN 764 830 Protein 2A. {ECO:0000255}.
/FTId=PRO_5000145529.
CHAIN 831 1258 Protein 2BC. {ECO:0000255}.
/FTId=PRO_0000311065.
CHAIN 831 1081 Protein 2B. {ECO:0000255}.
/FTId=PRO_5000145530.
CHAIN 1082 1258 Protein 2C. {ECO:0000255}.
/FTId=PRO_5000145531.
CHAIN 1259 2052 Protein 3ABCD. {ECO:0000255}.
/FTId=PRO_0000311066.
CHAIN 1259 1572 Protein 3ABC. {ECO:0000255}.
/FTId=PRO_0000311067.
CHAIN 1259 1353 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000311068.
CHAIN 1259 1330 Protein 3A. {ECO:0000255}.
/FTId=PRO_5000145521.
CHAIN 1331 1353 Protein 3B. {ECO:0000255}.
/FTId=PRO_5000145522.
CHAIN 1354 2052 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000311069.
CHAIN 1354 1572 Protease 3C. {ECO:0000255}.
/FTId=PRO_5000145523.
CHAIN 1573 2052 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_5000145524.
TOPO_DOM 1 1301 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1302 1316 {ECO:0000255}.
TOPO_DOM 1317 2052 Cytoplasmic. {ECO:0000255}.
DOMAIN 1354 1550 Peptidase C3.
DOMAIN 1810 1931 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
COILED 1121 1146 {ECO:0000255}.
ACT_SITE 1397 1397 For protease 3C activity. {ECO:0000250}.
ACT_SITE 1437 1437 For protease 3C activity. {ECO:0000250}.
ACT_SITE 1525 1525 For protease 3C activity. {ECO:0000250}.
SITE 23 24 Cleavage. {ECO:0000255}.
SITE 245 246 Cleavage; by protease 3C. {ECO:0000255}.
SITE 491 492 Cleavage; by protease 3C. {ECO:0000255}.
SITE 763 764 Cleavage; by host. {ECO:0000255}.
SITE 763 763 Important for VP1 folding and capsid
assembly. {ECO:0000250}.
SITE 830 831 Cleavage; by protease 3C. {ECO:0000250}.
SITE 1081 1082 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1258 1259 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1330 1331 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1353 1354 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1572 1573 Cleavage; by protease 3C. {ECO:0000250}.
MOD_RES 1333 1333 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
NON_CONS 1161 1162 {ECO:0000305}.
SEQUENCE 2052 AA; 231976 MW; 971E03905B81110A CRC64;
MNMSKQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ SSVHTAEVGS
HQIEPLKTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE VAKLDVVKLL YNEQFAVQGL
LRYHTYARFG IEIQVQINPT PFQQGGLICA MVPGDQSYGS IASLTVYPHG LLNCNINNVV
RIKVPFIYTR GAYHFKDPQY PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT
PLSTQMMRNE FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC QMFCFWRGDL
VFDFQVFPTK YHSGRLLFCF VPGNELIDVT GITLKQATTA PCAVMDITGV QSTLRFRVPW
ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY CYNRLTSPSN VASHVRVNVY LSAINLECFA
PLYHAMDVTT QVGDDSGGFS TTVSTEQNVP DPQVGIKGKA NRGKMDVSGV QAPVGAITTI
EDPVLAKKVP ETFPELKPGE SRHTSDHMSI YKFMGRSHFL CTFTFNSNNK EYTFPITLSS
TSNPPHGLPS TLRWFFNLFQ LYRGPLDLTI IITGATDVDG MAWFTPVGLA VDTPWVEKKS
ALSIDYKTAL GAVRFNTRRT GNIQIRLPWY SYLYAVSGAL DGLGDKTDST FGLVSIQIAN
YNHSDEYLSF SCYLSVTEQS EFYFPRAPLN SNAMLSTESM MSRIAAGDLE SSVDDPRSEE
DRRFESHIEC RKPYKELRLE VGKQRLKYAQ EELSNEVLPP PRKMKGLFSQ AKISLFYTEE
HEIMKFSWRG VTADTRALRR FGFSLAAGRS VWTLEMDAGV LTGRLIRLND EKWTEMKDDK
IVSLIEKFTS NKYWSKVNFP HGMLDLEEIA ANSKDFPNMS ETDLCFLLHW LNPKKINLAD
RMLGLSGVQE IKEQGVGLIA ECRTFLDSIA GTLKSMIFGF HHSVTVEIIN IVLCFIKSGI
LLYVIQQLNQ DEHSHIIGLL RVMNYADIGC SVISCGKVFS KMLETVFNWQ MDSRMMELRT
QSFSNWLRDI CSGITIFKSF KDAIYWLCTK LKDFYEVNYG KKKDVLNILK DNQQKIEKAI
EEADNFCILQ IQDVEKFDQY QTSNWSNPSP KTVYVKEAID RRLHFKVEVK PASFFKNPHN
DMLNVNLAKT NDAIKDMSCV DLIMDGHNIS LMDLLSSLVM TVEIRKQNMS EFMELWSQGI
SDDDSAVAEF FQSFPSGEPS NSKLSSFFQS VTNHKWVAVG AAVGILGLLV GGWFVYKHFS
RKEEEPIPAE GVYHGVTKPK QVIKLDADPV ESQSTLEIAG LVRKNLVQFG VGEKNGCVRW
VMNALGVKDD WLLVPSHAYK FEKDYEMMEF YFNRGGTYYS ISAGNVVIQS LDVGFQDVVL
MKVPTIPKFR DITQHFIKKG DVPRALNRLA TLVTTVNGTP MLISEGPLKM EEKATYVHKK
NDGTTVDLTV DQAWRGKGEG LPGMCGGALV SSNQSIQNAI LGIHVAGGNS ILVAKLITQE
MFQNIDKKIE SQRIMKVEFT QCSMNVVSKT LFRKSPIHHH IDKTMINFPA AMPFSKAEID
PMAMMLSKYS LPIVEEPEDY KEASVFYQNK IVGKTQLVDD FLDLDMAITG APGIDAINMD
SSPGFPYVQE KLTKRDLIWL DENGLLLGVH PRLAQRILFN TVMMENCSDL DVVFTTCPKD
ELRPLEKVLE SKTRAIDACP LDYTILCRMY WGPAISYFHL NPGFHTGVAI GIDPDRQWDE
LFKTMIRFGD VGLDLDFSAF DASLSPFMIR EAGRIMSELS GTPSHFGTAL INTIIYSKHL
LYNCCYHVCG SMPSGSPCTA LLNSIINNIN LYYVFSKIFG KSPVFFCQAL RILCYGDDVL
IVFSRDVQID NLDLIGQKIV DEFKKLGMTA TSADKNVPQL KPVSELTFLK RSFNLVEDRI
RPAISEKTIW SLIAWQRSNA EFEQNLENAQ WFAFMHGYEF YQKFYYFVQS CLEKEMIEYR
LKSYDWWRMR FY


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18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB43298 A20-binding inhibitor of NF-kappa-B activation,ABIN,Abin,Mouse,Mus musculus,mVAN,Naf1,Naf1,Nef-associated factor 1,TNFAIP3-interacting protein 1,Tnip1,VAN,Virion-associated nuclear shuttling protein
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
E1773h ELISA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA kit G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB29586 Mouse,Mus musculus,p53-induced gene 11 protein,Pig11,Tp53i11,Transformation related protein 53 inducible protein 11,Trp53i11,Tumor protein p53-inducible protein 11
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.01 mg
EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6
EIAAB43485 C20orf188,Homo sapiens,Human,Protein TAP1,Protein TRUSS,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp4-associated protein,TR
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.002 mg
EIAAB43486 Mouse,Mus musculus,Protein TAP1,Protein TRUSS,Rabex-5_Rin2-interacting protein,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator


 

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