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

Gag-Pro polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-)]

 GAG_RSVP                Reviewed;         701 AA.
P03322;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 137.
RecName: Full=Gag polyprotein;
Contains:
RecName: Full=Matrix protein p19;
Contains:
RecName: Full=p2A;
Contains:
RecName: Full=p2B;
Contains:
RecName: Full=p10;
Contains:
RecName: Full=Capsid protein p27, alternate cleaved 1;
Contains:
RecName: Full=Capsid protein p27, alternate cleaved 2;
Contains:
RecName: Full=Spacer peptide;
Short=SP;
AltName: Full=p3;
Contains:
RecName: Full=Nucleocapsid protein p12;
Contains:
RecName: Full=Protease p15;
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Name=gag;
Rous sarcoma virus (strain Prague C) (RSV-PrC).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Alpharetrovirus.
NCBI_TaxID=11888;
NCBI_TaxID=9031; Gallus gallus (Chicken).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6299578; DOI=10.1016/0092-8674(83)90071-5;
Schwartz D., Tizard R., Gilbert W.;
"Nucleotide sequence of Rous sarcoma virus.";
Cell 32:853-869(1983).
[2]
PROTEIN SEQUENCE OF 489-577.
Misono K.S., Sharief F.S., Leis J.;
"Primary structure of Rous sarcoma virus RNA-associated polypeptide.";
Fed. Proc. 39:1611-1611(1980).
[3]
PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
PubMed=8636100; DOI=10.1074/jbc.271.12.6781;
Tozser J., Bagossi P., Weber I.T., Copeland T.D., Oroszlan S.;
"Comparative studies on the substrate specificity of avian
myeloblastosis virus proteinase and lentiviral proteinases.";
J. Biol. Chem. 271:6781-6788(1996).
[4]
PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
PubMed=8627817;
Pepinsky R.B., Papayannopoulos I.A., Campbell S., Vogt V.M.;
"Analysis of Rous sarcoma virus Gag protein by mass spectrometry
indicates trimming by host exopeptidase.";
J. Virol. 70:3313-3318(1996).
[5]
RIBOSOMAL FRAMESHIFTING (GAG POLYPROTEIN).
PubMed=9813113; DOI=10.1006/jmbi.1998.2186;
Marczinke B., Fisher R., Vidakovic M., Bloys A.J., Brierley I.;
"Secondary structure and mutational analysis of the ribosomal
frameshift signal of rous sarcoma virus.";
J. Mol. Biol. 284:205-225(1998).
[6]
DOMAIN (GAG POLYPROTEIN), AND MUTAGENESIS OF PRO-172 AND
180-LEU--LEU-184.
PubMed=20392845; DOI=10.1128/JVI.00238-10;
Dilley K.A., Gregory D., Johnson M.C., Vogt V.M.;
"An LYPSL late domain in the gag protein contributes to the efficient
release and replication of Rous sarcoma virus.";
J. Virol. 84:6276-6287(2010).
[7]
SUBCELLULAR LOCATION (GAG POLYPROTEIN), DOMAIN (GAG POLYPROTEIN), AND
MUTAGENESIS OF LEU-219; 524-LYS--LYS-527 AND 549-ARG--ARG-551.
PubMed=23036987; DOI=10.1016/j.virusres.2012.09.011;
Lochmann T.L., Bann D.V., Ryan E.P., Beyer A.R., Mao A., Cochrane A.,
Parent L.J.;
"NC-mediated nucleolar localization of retroviral gag proteins.";
Virus Res. 171:304-318(2013).
[8]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 578-701, AND SUBUNIT
(PROTEASE).
PubMed=2536902; DOI=10.1038/337576a0;
Miller M., Jaskolski M., Rao J.K.M., Leis J., Wlodawer A.;
"Crystal structure of a retroviral protease proves relationship to
aspartic protease family.";
Nature 337:576-579(1989).
[9] {ECO:0000244|PDB:2RSP}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 578-701, AND SUBUNIT
(PROTEASE P15).
PubMed=2166563; DOI=10.1021/bi00477a002;
Jaskolski M., Miller M., Rao J.K., Leis J., Wlodawer A.;
"Structure of the aspartic protease from Rous sarcoma retrovirus
refined at 2-A resolution.";
Biochemistry 29:5889-5898(1990).
[10] {ECO:0000244|PDB:1BAI}
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 578-701 OF MUTANT SER-615;
ILE-619; ILE-621; MET-650; ALA-677; VAL-681; ARG-682; GLY-683; SER-684
WITH INHIBITOR.
STRAIN=S9 variant;
PubMed=9521772; DOI=10.1021/bi972183g;
Wu J., Adomat J.M., Ridky T.W., Louis J.M., Leis J., Harrison R.W.,
Weber I.T.;
"Structural basis for specificity of retroviral proteases.";
Biochemistry 37:4518-4526(1998).
[11]
STRUCTURE BY NMR OF 1-87.
PubMed=9642071; DOI=10.1006/jmbi.1998.1788;
McDonnell J.M., Fushman D., Cahill S.M., Zhou W., Wolven A.,
Wilson C.B., Nelle T.D., Resh M.D., Wills J., Cowburn D.;
"Solution structure and dynamics of the bioactive retroviral M domain
from Rous sarcoma virus.";
J. Mol. Biol. 279:921-928(1998).
[12] {ECO:0000244|PDB:1EM9, ECO:0000244|PDB:1EOQ}
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 240-393, FUNCTION (CAPSID
PROTEIN P27), AND SUBUNIT (CAPSID PROTEIN P27).
PubMed=10873863; DOI=10.1016/S0969-2126(00)00148-9;
Kingston R.L., Fitzon-Ostendorp T., Eisenmesser E.Z., Schatz G.W.,
Vogt V.M., Post C.B., Rossmann M.G.;
"Structure and self-association of the Rous sarcoma virus capsid
protein.";
Structure 8:617-628(2000).
[13] {ECO:0000244|PDB:1P7N}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 215-386, AND SUBUNIT (CAPSID
PROTEIN P27).
PubMed=14659756; DOI=10.1016/j.jmb.2003.10.034;
Nandhagopal N., Simpson A.A., Johnson M.C., Francisco A.B.,
Schatz G.W., Rossmann M.G., Vogt V.M.;
"Dimeric rous sarcoma virus capsid protein structure relevant to
immature Gag assembly.";
J. Mol. Biol. 335:275-282(2004).
[14] {ECO:0000244|PDB:3G0V, ECO:0000244|PDB:3G1G, ECO:0000244|PDB:3G1I, ECO:0000244|PDB:3G21, ECO:0000244|PDB:3G26, ECO:0000244|PDB:3G28, ECO:0000244|PDB:3G29}
X-RAY CRYSTALLOGRAPHY (0.90 ANGSTROMS) OF 389-465, SUBUNIT (CAPSID
PROTEIN P27), AND DOMAIN (CAPSID PROTEIN P27).
PubMed=19446529; DOI=10.1016/j.str.2009.03.010;
Bailey G.D., Hyun J.K., Mitra A.K., Kingston R.L.;
"Proton-linked dimerization of a retroviral capsid protein initiates
capsid assembly.";
Structure 17:737-748(2009).
[15] {ECO:0000244|PDB:2X8Q}
STRUCTURE BY ELECTRON MICROSCOPY (18.30 ANGSTROMS) OF 240-465, SUBUNIT
(CAPSID PROTEIN P27), AND DOMAIN (CAPSID PROTEIN P27).
PubMed=20228062; DOI=10.1074/JBC.M110.108209;
Hyun J.K., Radjainia M., Kingston R.L., Mitra A.K.;
"Proton-driven assembly of the Rous sarcoma virus capsid protein
results in the formation of icosahedral particles.";
J. Biol. Chem. 285:15056-15064(2010).
[16] {ECO:0000244|PDB:5A9E}
STRUCTURE BY ELECTRON MICROSCOPY (7.70 ANGSTROMS) OF 84-577, FUNCTION
(GAG POLYPROTEIN), AND SUBUNIT (GAG POLYPROTEIN).
PubMed=26223638; DOI=10.1128/JVI.01502-15;
Schur F.K., Dick R.A., Hagen W.J., Vogt V.M., Briggs J.A.;
"The structure of immature virus-like Rous sarcoma virus gag particles
reveals a structural role for the p10 domain in assembly.";
J. Virol. 89:10294-10302(2015).
[17]
FUNCTION (SPACER PEPTIDE), FUNCTION (CAPSID PROTEIN P27), AND
PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
PubMed=28588198; DOI=10.1038/s41598-017-02060-0;
Jaballah S.A., Bailey G.D., Desfosses A., Hyun J., Mitra A.K.,
Kingston R.L.;
"In vitro assembly of the Rous sarcoma virus capsid protein into
hexamer tubes at physiological temperature.";
Sci. Rep. 7:2913-2913(2017).
-!- FUNCTION: Gag polyprotein: The p10 domain folds back and interacts
with the capsid protein domain during Gag polyprotein assembly in
the immature particle (before the maturation cleavage that splits
the 2 domains). {ECO:0000269|PubMed:26223638}.
-!- FUNCTION: Capsid protein p27: Self-associates to form the
irregular polyhedron core composed of hexamers and pentamers, that
encapsulates the genomic RNA-nucleocapsid complex. Assembles as a
tube in vitro. {ECO:0000269|PubMed:10873863,
ECO:0000269|PubMed:28588198}.
-!- FUNCTION: Nucleocapsid protein p12: Binds strongly to viral
nucleic acids and promote their aggregation. Also destabilizes the
nucleic acids duplexes via highly structured zinc-binding motifs.
{ECO:0000305}.
-!- FUNCTION: Spacer peptide: Plays a role in the oligomerization of
the Gag polyprotein and in the stabilization of the immature
particle. Essential layering element during tube assembly.
{ECO:0000269|PubMed:28588198}.
-!- FUNCTION: Protease p15: Aspartyl protease that mediates
proteolytic cleavages of Gag and Gag-Pol polyproteins during or
shortly after the release of the virion from the plasma membrane.
Cleavages take place as an ordered, step-wise cascade to yield
mature proteins. This process is called maturation. Displays
maximal activity during the budding process just prior to particle
release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- SUBUNIT: Protease p15: Active as a homodimer (PubMed:2166563,
PubMed:2536902). Capsid protein p27: Homodimer (PubMed:10873863,
PubMed:14659756, PubMed:19446529, PubMed:20228062). Homomultimer
(PubMed:10873863, PubMed:14659756, PubMed:19446529,
PubMed:20228062). Gag polyprotein: Homohexamer (PubMed:26223638).
{ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:14659756,
ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062,
ECO:0000269|PubMed:2166563, ECO:0000269|PubMed:2536902,
ECO:0000269|PubMed:26223638}.
-!- SUBCELLULAR LOCATION: Matrix protein p19: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27, alternate cleaved 1:
Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27, alternate cleaved 2:
Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p12: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Gag polyprotein: Host nucleus, host
nucleolus {ECO:0000269|PubMed:23036987}. Host nucleus, host
nucleoplasm {ECO:0000269|PubMed:23036987}. Note=Shuttles between
nucleoplasm and nucleolus. {ECO:0000269|PubMed:23036987}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=Translation results in the formation of the Gag
polyprotein. Ribosomal frameshifting at the gag/pol genes
boundary produces the Gag-Pol polyprotein.
{ECO:0000269|PubMed:9813113};
Name=Gag polyprotein;
IsoId=P03322-1; Sequence=Displayed;
Note=Produced by conventional translation.
{ECO:0000269|PubMed:9813113};
Name=Gag-Pol polyprotein;
IsoId=P03354-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting.
{ECO:0000269|PubMed:9813113};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. P2B contains two L domains: a
PPXY motif which probably binds to the WW domains of HECT
(homologous to E6-AP C-terminus) E3 ubiquitin ligases and a
LYPX(n)L domain which is known to bind the Alix adaptator protein.
{ECO:0000269|PubMed:20392845}.
-!- DOMAIN: Gag polyprotein: Contains a nuclear export signal in p10
and a nucleolar localization signal in nucleocapsid protein p12.
{ECO:0000269|PubMed:23036987}.
-!- DOMAIN: Capsid protein p27: Proton-driven dimerization of the C-
terminus facilitates capsid assembly.
{ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062}.
-!- PTM: Gag polyprotein: Specific enzymatic cleavages in vivo yield
mature proteins (PubMed:8636100, PubMed:8627817). The cleavage at
the C-terminus of the Capsid protein p27 is slowly trimmed by the
viral protease, sometimes being cut internally thereby generating
the short version of the capsid protein and a capsid protein C-
terminally extended by 3 amino acids in a ratio of 2:1
(PubMed:28588198). {ECO:0000269|PubMed:28588198,
ECO:0000269|PubMed:8627817, ECO:0000269|PubMed:8636100}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J02342; AAB59932.1; -; Genomic_RNA.
EMBL; V01197; CAA24512.1; -; Genomic_DNA.
PIR; A90834; FOFV1R.
RefSeq; NP_056887.1; NC_001407.1.
PDB; 1A6S; NMR; -; A=2-87.
PDB; 1BAI; X-ray; 2.40 A; A/B=578-701.
PDB; 1EM9; X-ray; 2.05 A; A/B=240-393.
PDB; 1EOQ; NMR; -; A=394-488.
PDB; 1P7N; X-ray; 2.60 A; A=215-386.
PDB; 2IHX; NMR; -; A=503-563.
PDB; 2RSP; X-ray; 2.00 A; A/B=578-701.
PDB; 2X8Q; EM; 18.30 A; A=240-465.
PDB; 3G0V; X-ray; 2.00 A; A=389-465.
PDB; 3G1G; X-ray; 2.01 A; A/B=390-476.
PDB; 3G1I; X-ray; 2.10 A; A/B=389-465.
PDB; 3G21; X-ray; 0.90 A; A=389-465.
PDB; 3G26; X-ray; 1.55 A; A=389-465.
PDB; 3G28; X-ray; 1.64 A; A=389-465.
PDB; 3G29; X-ray; 2.50 A; A/B=389-465.
PDB; 5A9E; EM; 7.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=84-577.
PDBsum; 1A6S; -.
PDBsum; 1BAI; -.
PDBsum; 1EM9; -.
PDBsum; 1EOQ; -.
PDBsum; 1P7N; -.
PDBsum; 2IHX; -.
PDBsum; 2RSP; -.
PDBsum; 2X8Q; -.
PDBsum; 3G0V; -.
PDBsum; 3G1G; -.
PDBsum; 3G1I; -.
PDBsum; 3G21; -.
PDBsum; 3G26; -.
PDBsum; 3G28; -.
PDBsum; 3G29; -.
PDBsum; 5A9E; -.
ProteinModelPortal; P03322; -.
SMR; P03322; -.
ELM; P03322; -.
MINT; P03322; -.
MEROPS; A02.015; -.
PRIDE; P03322; -.
GeneID; 1491923; -.
KEGG; vg:1491923; -.
OrthoDB; VOG09000135; -.
BRENDA; 3.4.23.B10; 5464.
EvolutionaryTrace; P03322; -.
Proteomes; UP000007183; Genome.
GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
CDD; cd05482; HIV_retropepsin_like; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.90; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR004028; Gag_M.
InterPro; IPR000721; Gag_p24.
InterPro; IPR012344; Matrix_HIV/RSV_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR034170; Retropepsin-like_cat_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF02813; Retro_M; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00098; zf-CCHC; 1.
ProDom; PD002871; Gag_M; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Complete proteome;
Direct protein sequencing; Host nucleus; Hydrolase; Metal-binding;
Protease; Repeat; Ribosomal frameshifting; Viral capsid assembly;
Viral capsid maturation; Viral matrix protein;
Viral release from host cell; Virion; Zinc; Zinc-finger.
CHAIN 1 701 Gag polyprotein.
/FTId=PRO_0000442114.
CHAIN 1 155 Matrix protein p19.
/FTId=PRO_0000026113.
CHAIN 156 166 p2A.
/FTId=PRO_0000026114.
CHAIN 167 177 p2B.
/FTId=PRO_0000026115.
CHAIN 178 239 p10.
/FTId=PRO_0000026116.
CHAIN 240 479 Capsid protein p27, alternate cleaved 2.
/FTId=PRO_0000026117.
CHAIN 240 476 Capsid protein p27, alternate cleaved 1.
/FTId=PRO_0000442115.
PEPTIDE 477 488 Spacer peptide.
/FTId=PRO_0000026118.
CHAIN 489 577 Nucleocapsid protein p12.
/FTId=PRO_0000026119.
CHAIN 578 701 Protease p15.
/FTId=PRO_0000026120.
DOMAIN 609 690 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
ZN_FING 507 524 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 533 550 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 217 259 Involved in capsid protein dimerization.
{ECO:0000269|PubMed:14659756}.
REGION 290 298 Involved in capsid protein dimerization.
{ECO:0000269|PubMed:14659756}.
REGION 351 362 Involved in capsid protein dimerization.
{ECO:0000269|PubMed:14659756}.
MOTIF 172 175 PPXY motif.
{ECO:0000269|PubMed:20392845}.
MOTIF 180 184 LYPX(n)L motif.
{ECO:0000269|PubMed:20392845}.
MOTIF 219 229 Nuclear export signal.
{ECO:0000269|PubMed:23036987}.
MOTIF 524 527 Nuclear/nucleolar localization signal.
{ECO:0000269|PubMed:23036987}.
COMPBIAS 171 174 Poly-Pro.
ACT_SITE 614 614 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
SITE 155 156 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
SITE 166 167 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
SITE 177 178 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
SITE 239 240 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
SITE 418 418 Involved in capsid protein dimerization
upon acidification.
{ECO:0000269|PubMed:19446529}.
SITE 430 430 Involved in capsid protein dimerization
upon acidification.
{ECO:0000269|PubMed:19446529}.
SITE 476 477 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:28588198,
ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
SITE 479 480 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:28588198,
ECO:0000269|PubMed:8627817}.
SITE 488 489 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
SITE 577 578 Cleavage; by viral protease p15.
{ECO:0000269|PubMed:8627817,
ECO:0000269|PubMed:8636100}.
MUTAGEN 172 172 P->A: 75% loss of budding.
{ECO:0000269|PubMed:20392845}.
MUTAGEN 180 184 LYPSL->AAASA: 40% loss of budding.
{ECO:0000269|PubMed:20392845}.
MUTAGEN 219 219 L->A: Reduced nucleolar localization of
Gag polyprotein.
{ECO:0000269|PubMed:23036987}.
MUTAGEN 524 527 KKRK->AAAA: Complete loss of nuclear and
nucleolar localization.
{ECO:0000269|PubMed:23036987}.
MUTAGEN 549 551 RKR->AAA: Reduced localization in
nucleolus; no effect on nuclear
localization.
{ECO:0000269|PubMed:23036987}.
CONFLICT 505 505 A -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 536 536 Q -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 2 16 {ECO:0000244|PDB:1A6S}.
TURN 17 19 {ECO:0000244|PDB:1A6S}.
HELIX 25 31 {ECO:0000244|PDB:1A6S}.
HELIX 33 35 {ECO:0000244|PDB:1A6S}.
HELIX 42 46 {ECO:0000244|PDB:1A6S}.
TURN 48 51 {ECO:0000244|PDB:1A6S}.
HELIX 52 60 {ECO:0000244|PDB:1A6S}.
TURN 61 63 {ECO:0000244|PDB:1A6S}.
STRAND 67 71 {ECO:0000244|PDB:1A6S}.
HELIX 72 86 {ECO:0000244|PDB:1A6S}.
HELIX 222 230 {ECO:0000244|PDB:1P7N}.
STRAND 234 236 {ECO:0000244|PDB:1P7N}.
STRAND 241 243 {ECO:0000244|PDB:1EM9}.
STRAND 245 250 {ECO:0000244|PDB:1EM9}.
HELIX 255 268 {ECO:0000244|PDB:1EM9}.
HELIX 273 282 {ECO:0000244|PDB:1EM9}.
HELIX 289 299 {ECO:0000244|PDB:1EM9}.
HELIX 302 325 {ECO:0000244|PDB:1EM9}.
STRAND 334 337 {ECO:0000244|PDB:1P7N}.
HELIX 342 345 {ECO:0000244|PDB:1EM9}.
TURN 350 354 {ECO:0000244|PDB:1EM9}.
HELIX 356 362 {ECO:0000244|PDB:1EM9}.
HELIX 365 385 {ECO:0000244|PDB:1EM9}.
HELIX 392 394 {ECO:0000244|PDB:3G21}.
HELIX 403 415 {ECO:0000244|PDB:3G21}.
STRAND 417 419 {ECO:0000244|PDB:3G21}.
HELIX 421 423 {ECO:0000244|PDB:3G21}.
HELIX 424 435 {ECO:0000244|PDB:3G21}.
HELIX 438 444 {ECO:0000244|PDB:3G21}.
HELIX 454 462 {ECO:0000244|PDB:3G21}.
STRAND 579 581 {ECO:0000244|PDB:2RSP}.
STRAND 584 586 {ECO:0000244|PDB:2RSP}.
STRAND 589 596 {ECO:0000244|PDB:2RSP}.
STRAND 605 613 {ECO:0000244|PDB:2RSP}.
STRAND 621 623 {ECO:0000244|PDB:2RSP}.
TURN 624 626 {ECO:0000244|PDB:2RSP}.
STRAND 633 635 {ECO:0000244|PDB:2RSP}.
STRAND 650 655 {ECO:0000244|PDB:2RSP}.
STRAND 657 662 {ECO:0000244|PDB:2RSP}.
STRAND 672 674 {ECO:0000244|PDB:2RSP}.
STRAND 677 680 {ECO:0000244|PDB:2RSP}.
STRAND 682 686 {ECO:0000244|PDB:2RSP}.
HELIX 688 693 {ECO:0000244|PDB:2RSP}.
STRAND 697 699 {ECO:0000244|PDB:2RSP}.
SEQUENCE 701 AA; 74527 MW; 5FD365D9CFEF37F1 CRC64;
MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ
RAMILGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL
YPSLAGVGEQ QGQGGDTPPG AEQSRAEPGH AGQAPGPALT DWARVREELA STGPPVVAMP
VVIKTEGPAW TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLNRLKGLAD GMVGNPQGQA
ALLRPGELVA ITASALQAFR EVARLAEPAG PWADIMQGPS ESFVDFANRL IKAVEGSDLP
PSARAPVIID CFRQKSQPDI QQLIRTAPST LTTPGEIIKY VLDRQKTAPL TDQGIAAAMS
SAIQPLIMAV VNRERDGQTG SGGRARGLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCNG
MGHNAKQCRK RDGNQGQRPG KGLSSGPWPG PEPPAVSLAM TMEHKDRPLV RVILTNTGSH
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVMEAANPQ IHGIGGGIPM RKSRDMIELG
VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN L


Related products :

Catalog number Product name Quantity
20-272-190970 cleaved IKB alpha - Mouse monoclonal to cleaved IKB alpha; Major histocompatibility complex enhancer-binding protein MAD3; I-kappa-B-alpha; IkappaBalpha; IKB-alpha Monoclonal 0.05 mg
25-986 LECT1 is a glycosylated transmembrane protein that is cleaved to form a mature, secreted protein. The mature protein promotes chondrocyte growth and inhibits angiogenesis. The mature protein likely pl 0.05 mg
3741BP-50 Cathepsin L (Cleaved) Blocking Peptide target: Cathepsin L (Cleaved) 50 μg
GTX13905 Retinoblastoma_associated protein _ RB1 (cleaved) 50 µg
SCH-OBT0882 MOUSE ANTI ROTAVIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity ROTAVIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2, Applications E, WB 0.1 mg
OBT0882 MOUSE ANTI ROTAVIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity ROTAVIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2, Applications E, WB 0.1 mg
orb81775 Rubella Virus Capsid C protein The E.coli derived recombinant protein contains the Rubella Virus Capsid regions, 1-123 amino acids. For research use only. 100
NB100-56598 Retinoblastoma_associated protein _ RB1 (cleaved) 0.1 mg
20-272-190971 cleaved RB - Mouse monoclonal [ 172C1094] to cleaved RB; PP110; P105-RB; RB Monoclonal 0.05 mg
CSB-ECL013481H Human cleaved microtubule-associated protein tau (C-MAPT_C-TAU) ELISA kit 96T
CSB-ECL013481H Human cleaved microtubule-associated protein tau (C-MAPT per C-TAU) ELISA kit 96T
SCH-MCA2830 MOUSE ANTI RUBELLA VIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity RUBELLA VIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Application 0.2 mg
MCA2830 MOUSE ANTI RUBELLA VIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity RUBELLA VIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Application 0.2 mg
Q01236M Synaptosomal Protein 25kDa (SNAP-25) (a.a. 183-197) cleaved & uncleavedMouse Supernatant IgG 1mL
Q01235M Synaptosomal Protein 25kDa (SNAP-25) (a.a. 183-197) cleaved host: Mouse 1mL
MD-14-0967 Mouse Anti-Synaptosomal Protein 25kDa (SNAP-25; aa 183-197) cleaved 1 mL
GTX13905 Retinoblastoma-associated protein _ RB1 (cleaved) Mouse IgG1 antibody Ab Purified 50
orb71370 Alternate Syntide peptide This is Alternate Syntide peptide. For research use only. 1 mg
Q01236M Synaptosomal Protein 25kDa (SNAP-25) (a.a. 183-197) cleaved & uncleaved host: Mouse 1mL
MD-14-0968 Mouse Anti-Synaptosomal Protein 25kDa (SNAP-25) (aa 183-197) cleaved & uncleaved 1 mL
GWB-T00279 Anti- Synaptosomal Protein 25kDa (SNAP-25) (a.a. 183-197) cleaved Antibody - Clone B371M
GWB-T00339 Anti- Synaptosomal Protein 25kDa (SNAP-25) (a.a. 183-197) cleaved & uncleaved Antibody - Clone B372M
'GTX13905 Retinoblastoma-associated protein RB1 (cleaved) Clone '172C1094 antibody Isotype IgG1 Host Mouse 50
'GTX13905 Retinoblastoma-associated protein _ RB1 (cleaved) Clone '172C1094 antibody Isotype IgG1 Host Mouse 50
20-272-190972 cleaved PARP - Mouse monoclonal [194C1439] to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Monoclonal 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur