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HLA class I histocompatibility antigen, A-2 alpha chain (MHC class I antigen A*2)

 1A02_HUMAN              Reviewed;         365 AA.
P01892; O19619; P06338; P10313; P30444; P30445; P30446; P30514;
Q29680; Q29837; Q29899; Q95352; Q95380; Q9TPX8; Q9TPX9; Q9TPY0;
Q9TQH5; Q9TQI3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
18-JUL-2018, entry version 211.
RecName: Full=HLA class I histocompatibility antigen, A-2 alpha chain;
AltName: Full=MHC class I antigen A*2;
Flags: Precursor;
Name=HLA-A; Synonyms=HLAA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
PubMed=2982951;
Koller B.H., Orr H.T.;
"Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA-
A alleles at the nucleotide level.";
J. Immunol. 134:2727-2733(1985).
[2]
NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
PubMed=2914713; DOI=10.1007/BF00395855;
Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G.,
Giannella G., Peschle C., Boncinelli E.;
"Three new class I HLA alleles: structure of mRNAs and alternative
mechanisms of processing.";
Immunogenetics 29:80-91(1989).
[3]
NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
PubMed=2320591; DOI=10.1073/pnas.87.7.2833;
Ennis P.D., Zemmour J., Salter R.D., Parham P.;
"Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction:
frequency and nature of errors produced in amplification.";
Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 91-365.
PubMed=3863816;
Davidson W.F., Kress M., Khoury G., Jay G.;
"Comparison of HLA class I gene sequences. Derivation of locus-
specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C
genes.";
J. Biol. Chem. 260:13414-13423(1985).
[5]
NUCLEOTIDE SEQUENCE (ALLELES A*02:01; A*02:11 AND A*02:12).
PubMed=1317015; DOI=10.1038/357326a0;
Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J.,
Williams R.C., Luz R., Petzl-Erler M.L., Parham P.;
"Unusual HLA-B alleles in two tribes of Brazilian Indians.";
Nature 357:326-329(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-365 (ALLELE A*02:01).
PubMed=3874058;
Krangel M.S.;
"Unusual RNA splicing generates a secreted form of HLA-A2 in a
mutagenized B lymphoblastoid cell line.";
EMBO J. 4:1205-1210(1985).
[7]
PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01).
PubMed=92029; DOI=10.1073/pnas.76.9.4395;
Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L.,
Strominger J.L.;
"Comparison of amino acid sequences of two human histocompatibility
antigens, HLA-A2 and HLA-B7: location of putative alloantigenic
sites.";
Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979).
[8]
SEQUENCE REVISION (ALLELE A*02:01).
PubMed=6179086; DOI=10.1073/pnas.79.12.3813;
Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.;
"Structure of crossreactive human histocompatibility antigens HLA-A28
and HLA-A2: possible implications for the generation of HLA
polymorphism.";
Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
TISSUE=Blood;
PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6;
Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.;
"HLA class I allele (HLA-A2) expression defect associated with a
mutation in its enhancer B inverted CAT box in two families.";
Hum. Immunol. 41:69-73(1994).
[10]
SEQUENCE REVISION.
Balas A.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
Cox S.T.;
"Confirmation of HLA-A*0201.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELES A*02:02 AND
A*02:03).
PubMed=3497874; DOI=10.1007/BF00365911;
Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P.,
Biddison W.E.;
"DNA sequences of the genes that encode the CTL-defined HLA-A2
variants M7 and DK1.";
Immunogenetics 26:190-192(1987).
[13]
NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05).
PubMed=3496393;
Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.;
"Multiple genetic mechanisms have contributed to the generation of the
HLA-A2/A28 family of class I MHC molecules.";
J. Immunol. 139:936-941(1987).
[14]
NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05).
Domena J.D.;
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:04).
PubMed=1937577; DOI=10.1007/BF00211991;
Castano A.R., Lopez de Castro J.A.;
"Structure of the HLA-A*0204 antigen, found in South American Indians.
Spatial clustering of HLA-A2 subtype polymorphism.";
Immunogenetics 34:281-285(1991).
[16]
NUCLEOTIDE SEQUENCE OF 9-365 (ALLELE A*02:04).
PubMed=1589035; DOI=10.1038/357329a0;
Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L.,
Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H.,
Troup G.M., Hughes A.L., Letvin N.L.;
"New recombinant HLA-B alleles in a tribe of South American
Amerindians indicate rapid evolution of MHC class I loci.";
Nature 357:329-333(1992).
[17]
NUCLEOTIDE SEQUENCE (ALLELE A*02:06).
PubMed=2715640;
Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.;
"Diversity and diversification of HLA-A,B,C alleles.";
J. Immunol. 142:3937-3950(1989).
[18]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:06).
PubMed=3489037;
Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A.,
Lopez de Castro J.A.;
"Molecular analysis of an HLA-A2 functional variant CLA defined by
cytolytic T lymphocytes.";
J. Immunol. 137:1642-1649(1986).
[19]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:07).
PubMed=2448239; DOI=10.1007/BF00346586;
Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.;
"Structural analysis of HLA-A2.4 functional variant KNE. Implications
for the mapping of HLA-A2-specific T-cell epitopes.";
Immunogenetics 27:196-202(1988).
[20]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:08).
PubMed=2457548; DOI=10.1007/BF00375853;
Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.;
"Molecular analysis of HLA-A2.4 functional variant KLO: close
structural and evolutionary relatedness to the HLA-A2.2 subtype.";
Immunogenetics 28:143-152(1988).
[21]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:09).
PubMed=3258580; DOI=10.1007/BF00395130;
Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.;
"An HLA-A2 population variant with structural polymorphism in the
alpha 3 region.";
Immunogenetics 27:345-355(1988).
[22]
NUCLEOTIDE SEQUENCE (ALLELE A*02:10).
PubMed=2783680; DOI=10.1007/BF00395859;
Epstein H., Kennedy L., Holmes N.;
"An Oriental HLA-A2 subtype is closely related to a subset of
Caucasoid HLA-A2 alleles.";
Immunogenetics 29:112-116(1989).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:11).
PubMed=1559719; DOI=10.1007/BF00189898;
Castano A.R., Lopez de Castro J.A.;
"Structure of the HLA-A*0211 (A2.5) subtype: further evidence for
selection-driven diversification of HLA-A2 antigens.";
Immunogenetics 35:344-346(1992).
[24]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:13).
PubMed=8168863; DOI=10.1007/BF00189243;
Barber D.F., Fernandez J.M., Lopez de Castro J.A.;
"Primary structure of a new HLA-A2 subtype: HLA-A*0213.";
Immunogenetics 39:378-378(1994).
[25]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:16).
PubMed=7759139; DOI=10.1007/BF00164000;
Barouch D., Krausa P., Bodmer J., Browning M.J., McMichael A.J.;
"Identification of a novel HLA-A2 subtype, HLA-A*0216.";
Immunogenetics 41:388-388(1995).
[26]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:17).
TISSUE=Blood;
PubMed=7652742; DOI=10.1111/j.1399-0039.1995.tb02464.x;
Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J.,
Dupont B.;
"A novel subtype of A2 (A*0217) isolated from the South American
Indian B-cell line AMALA.";
Tissue Antigens 45:343-347(1995).
[27]
NUCLEOTIDE SEQUENCE (ALLELE A*02:18).
TISSUE=Blood;
Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M.,
Akaza T., Tadokoro K., Juji T.;
"A new A2 sequence HLA-A2K from Japanese.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[28]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:20).
TISSUE=Blood;
PubMed=9008310; DOI=10.1111/j.1399-0039.1996.tb02691.x;
Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E.,
Bordignon C.;
"HLA-A*02 subtype distribution in Caucasians from northern Italy:
identification of A*0220.";
Tissue Antigens 48:673-679(1996).
[29]
NUCLEOTIDE SEQUENCE (ALLELE A*02:21).
TISSUE=Blood;
Szmania S., Baxter-Lowe L.A.;
"Nucleotide sequence of a novel HLA-A2 gene.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[30]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*02:31).
PubMed=10689125; DOI=10.1016/S0198-8859(99)00155-X;
Ellis J.M., Henson V., Slack R., Ng J., Hartzman R.J., Hurley C.K.;
"Frequencies of HLA-A2 alleles in five U.S. population groups.
Predominance Of A*02011 and identification of HLA-A*0231.";
Hum. Immunol. 61:334-340(2000).
[31]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*02:34).
PubMed=10746792; DOI=10.1034/j.1399-0039.2000.550212.x;
Moses J.H., Greville W.D., Downes J., McClenahan W., Kennedy A.,
Dunckley H.;
"A new HLA-A*02 allele, A*0234, detected by polymerase chain reaction
using sequence-specific primers (PCR-SSP).";
Tissue Antigens 55:175-177(2000).
[32]
NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*02:35; A*02:36 AND A*02:37).
PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x;
Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R.,
Ng J., Hartzman R.J., Hurley C.K.;
"Seventeen more novel HLA-A locus alleles.";
Tissue Antigens 55:369-373(2000).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-352; SER-356
AND SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[38]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF A*02:01.
PubMed=3309677; DOI=10.1038/329506a0;
Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L.,
Wiley D.C.;
"Structure of the human class I histocompatibility antigen, HLA-A2.";
Nature 329:506-512(1987).
[39]
INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001;
Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L.,
Mulloy J.C., Jacobson S., Franchini G.;
"Free major histocompatibility complex class I heavy chain is
preferentially targeted for degradation by human T-cell
leukemia/lymphotropic virus type 1 p12(I) protein.";
J. Virol. 75:6086-6094(2001).
[40]
INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN (MICROBIAL
INFECTION), AND UBIQUITINATION.
PubMed=12006494; DOI=10.1093/emboj/21.10.2418;
Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G.,
Lehner P.J.;
"Ubiquitylation of MHC class I by the K3 viral protein signals
internalization and TSG101-dependent degradation.";
EMBO J. 21:2418-2429(2002).
[41]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-300 OF HLA-A/B2M
HETERODIMER IN COMPLEX WITH TRAC AND TRBC1, AND DISULFIDE BONDS.
PubMed=12796775; DOI=10.1038/ni942;
Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I.,
Jones E.Y.;
"A structural basis for immunodominant human T cell receptor
recognition.";
Nat. Immunol. 4:657-663(2003).
[42]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A*02:01.
PubMed=2038058; DOI=10.1016/0022-2836(91)90567-P;
Saper M.A., Bjorkman P.J., Wiley D.C.;
"Refined structure of the human histocompatibility antigen HLA-A2 at
2.6-A resolution.";
J. Mol. Biol. 219:277-319(1991).
[43]
VARIANT [LARGE SCALE ANALYSIS] GLU-176, VARIANT [LARGE SCALE ANALYSIS]
TRP-180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[44]
VARIANT [LARGE SCALE ANALYSIS] GLU-176, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[45]
VARIANT GLY-89.
PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
"Homozygous missense mutation in the LMAN2L gene segregates with
intellectual disability in a large consanguineous Pakistani family.";
J. Med. Genet. 53:138-144(2016).
-!- FUNCTION: Involved in the presentation of foreign antigens to the
immune system.
-!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2-
microglobulin). {ECO:0000269|PubMed:12796775}.
-!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 8
MIR1 protein. {ECO:0000269|PubMed:12006494}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory
protein p12I. {ECO:0000269|PubMed:11390610}.
-!- INTERACTION:
P61769:B2M; NbExp=20; IntAct=EBI-2839473, EBI-714718;
O15533:TAPBP; NbExp=10; IntAct=EBI-2839473, EBI-874801;
Q9BX59:TAPBPL; NbExp=17; IntAct=EBI-2839473, EBI-12017416;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Polyubiquitinated in a post ER compartment through
interaction with human herpesvirus 8 MIR1 protein. This targets
the protein for rapid degradation via the ubiquitin system.
{ECO:0000269|PubMed:12006494}.
-!- POLYMORPHISM: The following alleles of A-2 are known: A*02:01,
A*02:02, A*02:03, A*02:04, A*02:05, A*02:06 (A2.4A), A*02:07,
A*02:08, A*02:09, A*02:10, A*02:11 (A2.5), A*02:12, A*02:13
(A*02SLU), A*02:16, A*02:17, A*02:18 (A2K), A*02:19, A*02:20,
A*02:21, A*02:31, A*02:34 (A*AAT), A*02:35, A*02:36 and A*02:37.
The sequence shown is that of A*02:01.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA41022.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown extensively.; Evidence={ECO:0000305};
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EMBL; K02883; AAA98727.1; -; Genomic_DNA.
EMBL; M84379; AAA59606.1; -; mRNA.
EMBL; X02457; CAA26297.1; -; mRNA.
EMBL; M11887; AAA52656.1; -; mRNA.
EMBL; M19670; AAA03683.2; -; Genomic_DNA.
EMBL; AH003586; AAB02120.1; -; Genomic_DNA.
EMBL; U03863; AAA03604.1; -; mRNA.
EMBL; M86404; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X57954; CAA41022.1; ALT_SEQ; mRNA.
EMBL; U02935; AAA76608.2; -; Genomic_DNA.
EMBL; AJ555412; CAD87771.1; -; Genomic_DNA.
EMBL; U03862; AAA03603.1; -; mRNA.
EMBL; M24042; AAA59653.1; -; mRNA.
EMBL; Z23071; CAA80612.1; -; mRNA.
EMBL; M84377; AAA59603.1; -; mRNA.
EMBL; X60764; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M84378; AAA59604.1; -; mRNA.
EMBL; Z27120; CAA81644.1; -; mRNA.
EMBL; Z46633; CAA86602.1; -; mRNA.
EMBL; U18930; AAA87076.1; -; mRNA.
EMBL; D83515; BAA11935.1; -; mRNA.
EMBL; X96724; CAA65501.1; -; mRNA.
EMBL; U56825; AAB17465.1; -; mRNA.
EMBL; AH007560; AAD23437.1; -; Genomic_DNA.
EMBL; AH007704; AAD30272.1; -; Genomic_DNA.
EMBL; AH008013; AAD45690.1; -; Genomic_DNA.
EMBL; AH008012; AAD45689.1; -; Genomic_DNA.
EMBL; AH008007; AAD45324.1; -; Genomic_DNA.
PIR; B24512; HLHU10.
PIR; I37470; I37470.
PIR; I37542; I37542.
PIR; I38418; I38418.
PIR; I38442; I38442.
PIR; I38443; I38443.
PIR; I55948; HLHUA2.
PIR; I61857; I61857.
PIR; I61902; I61902.
PIR; I84448; I84448.
UniGene; Hs.181244; -.
UniGene; Hs.713441; -.
PDB; 1AKJ; X-ray; 2.65 A; A=25-300.
PDB; 1AO7; X-ray; 2.60 A; A=25-299.
PDB; 1AQD; X-ray; 2.45 A; C/F/I/L=127-141.
PDB; 1B0G; X-ray; 2.50 A; A/D=25-299.
PDB; 1B0R; X-ray; 2.90 A; A=25-299.
PDB; 1BD2; X-ray; 2.50 A; A=25-299.
PDB; 1DUY; X-ray; 2.15 A; A/D=25-299.
PDB; 1DUZ; X-ray; 1.80 A; A/D=25-299.
PDB; 1EEY; X-ray; 2.25 A; A/D=25-299.
PDB; 1EEZ; X-ray; 2.30 A; A/D=25-299.
PDB; 1HHG; X-ray; 2.60 A; A/D=25-299.
PDB; 1HHH; X-ray; 3.00 A; A=25-299.
PDB; 1HHI; X-ray; 2.50 A; A/D=25-299.
PDB; 1HHJ; X-ray; 2.50 A; A/D=25-299.
PDB; 1HHK; X-ray; 2.50 A; A/D=25-299.
PDB; 1HLA; X-ray; 3.50 A; A=25-294.
PDB; 1I1F; X-ray; 2.80 A; A/D=25-299.
PDB; 1I1Y; X-ray; 2.20 A; A/D=25-299.
PDB; 1I4F; X-ray; 1.40 A; A=25-299.
PDB; 1I7R; X-ray; 2.20 A; A/D=25-299.
PDB; 1I7T; X-ray; 2.80 A; A/D=25-299.
PDB; 1I7U; X-ray; 1.80 A; A/D=25-299.
PDB; 1IM3; X-ray; 2.20 A; A/E/I/M=25-299.
PDB; 1JF1; X-ray; 1.85 A; A=25-299.
PDB; 1JHT; X-ray; 2.15 A; A=25-299.
PDB; 1LP9; X-ray; 2.00 A; A/H=25-299.
PDB; 1OGA; X-ray; 1.40 A; A=25-300.
PDB; 1P7Q; X-ray; 3.40 A; A=25-300.
PDB; 1QEW; X-ray; 2.20 A; A=25-299.
PDB; 1QR1; X-ray; 2.40 A; A/D=25-299.
PDB; 1QRN; X-ray; 2.80 A; A=25-298.
PDB; 1QSE; X-ray; 2.80 A; A=25-298.
PDB; 1QSF; X-ray; 2.80 A; A=25-298.
PDB; 1S8D; X-ray; 2.20 A; A=25-299.
PDB; 1S9W; X-ray; 2.20 A; A=25-298.
PDB; 1S9X; X-ray; 2.50 A; A=25-298.
PDB; 1S9Y; X-ray; 2.30 A; A=25-298.
PDB; 1T1W; X-ray; 2.20 A; A=25-299.
PDB; 1T1X; X-ray; 2.20 A; A=25-299.
PDB; 1T1Y; X-ray; 2.00 A; A=25-299.
PDB; 1T1Z; X-ray; 1.90 A; A=25-299.
PDB; 1T20; X-ray; 2.20 A; A=25-299.
PDB; 1T21; X-ray; 2.19 A; A=25-299.
PDB; 1T22; X-ray; 2.20 A; A=25-299.
PDB; 1TVB; X-ray; 1.80 A; A/D=25-299.
PDB; 1TVH; X-ray; 1.80 A; A/D=25-299.
PDB; 1UR7; Model; -; A=25-299.
PDB; 2AV1; X-ray; 1.95 A; A/D=25-299.
PDB; 2AV7; X-ray; 2.05 A; A/D=25-299.
PDB; 2BNQ; X-ray; 1.70 A; A=25-300.
PDB; 2BNR; X-ray; 1.90 A; A=25-300.
PDB; 2C7U; X-ray; 2.38 A; A/D=25-300.
PDB; 2CLR; X-ray; 2.00 A; A/D=25-299.
PDB; 2F53; X-ray; 2.10 A; A=25-299.
PDB; 2F54; X-ray; 2.70 A; A/F=25-298.
PDB; 2GIT; X-ray; 1.70 A; A/D=25-299.
PDB; 2GJ6; X-ray; 2.56 A; A=25-299.
PDB; 2GT9; X-ray; 1.75 A; A/D=25-299.
PDB; 2GTW; X-ray; 1.55 A; A/D=25-299.
PDB; 2GTZ; X-ray; 1.70 A; A/D=25-299.
PDB; 2GUO; X-ray; 1.90 A; A/D=25-299.
PDB; 2J8U; X-ray; 2.88 A; A/H=25-299.
PDB; 2JCC; X-ray; 2.50 A; A/H=25-299.
PDB; 2P5E; X-ray; 1.89 A; A=25-300.
PDB; 2P5W; X-ray; 2.20 A; A=25-300.
PDB; 2PYE; X-ray; 2.30 A; A=25-300.
PDB; 2UWE; X-ray; 2.40 A; A/H=25-299.
PDB; 2V2W; X-ray; 1.60 A; A/D=25-300.
PDB; 2V2X; X-ray; 1.60 A; A/D=25-300.
PDB; 2VLJ; X-ray; 2.40 A; A=25-300.
PDB; 2VLK; X-ray; 2.50 A; A=25-300.
PDB; 2VLL; X-ray; 1.60 A; A/D=25-300.
PDB; 2VLR; X-ray; 2.30 A; A/F=25-300.
PDB; 2X4N; X-ray; 2.34 A; A/D=25-299.
PDB; 2X4O; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4P; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4Q; X-ray; 1.90 A; A/D=25-299.
PDB; 2X4R; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4S; X-ray; 2.55 A; A/D=25-299.
PDB; 2X4T; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4U; X-ray; 2.10 A; A/D=25-299.
PDB; 2X70; X-ray; 2.00 A; A/D=25-299.
PDB; 3BGM; X-ray; 1.60 A; A=25-298.
PDB; 3BH8; X-ray; 1.65 A; A=25-298.
PDB; 3BH9; X-ray; 1.70 A; A=25-299.
PDB; 3BHB; X-ray; 2.20 A; A=25-298.
PDB; 3D25; X-ray; 1.30 A; A=25-298.
PDB; 3D39; X-ray; 2.81 A; A=25-299.
PDB; 3D3V; X-ray; 2.80 A; A=25-299.
PDB; 3FQN; X-ray; 1.65 A; A=25-299.
PDB; 3FQR; X-ray; 1.70 A; A=25-299.
PDB; 3FQT; X-ray; 1.80 A; A=25-299.
PDB; 3FQU; X-ray; 1.80 A; A=25-299.
PDB; 3FQW; X-ray; 1.93 A; A=25-299.
PDB; 3FQX; X-ray; 1.70 A; A=25-299.
PDB; 3FT2; X-ray; 1.80 A; A=25-299.
PDB; 3FT3; X-ray; 1.95 A; A=25-299.
PDB; 3FT4; X-ray; 1.90 A; A=25-299.
PDB; 3GIV; X-ray; 2.00 A; A/D=25-299.
PDB; 3GJF; X-ray; 1.90 A; A/D=25-300.
PDB; 3GSN; X-ray; 2.80 A; H=25-298.
PDB; 3GSO; X-ray; 1.60 A; A=25-298.
PDB; 3GSQ; X-ray; 2.12 A; A=25-298.
PDB; 3GSR; X-ray; 1.95 A; A=25-298.
PDB; 3GSU; X-ray; 1.80 A; A=25-299.
PDB; 3GSV; X-ray; 1.90 A; A=25-299.
PDB; 3GSW; X-ray; 1.81 A; A=25-298.
PDB; 3GSX; X-ray; 2.10 A; A=25-298.
PDB; 3H7B; X-ray; 1.88 A; A/D=25-299.
PDB; 3H9H; X-ray; 2.00 A; A/D=25-299.
PDB; 3H9S; X-ray; 2.70 A; A=25-299.
PDB; 3HAE; X-ray; 2.90 A; A/D/J/P=25-300.
PDB; 3HLA; X-ray; 2.60 A; A=25-294.
PDB; 3HPJ; X-ray; 2.00 A; A/D=25-299.
PDB; 3I6G; X-ray; 2.20 A; A/D=25-299.
PDB; 3I6K; X-ray; 2.80 A; A/E=25-299.
PDB; 3IXA; X-ray; 2.10 A; A/D=25-299.
PDB; 3KLA; X-ray; 1.65 A; A/D=25-299.
PDB; 3MGO; X-ray; 2.30 A; A/D/G/J=25-299.
PDB; 3MGT; X-ray; 2.20 A; A/D/G/J=25-299.
PDB; 3MR9; X-ray; 1.93 A; A=25-300.
PDB; 3MRB; X-ray; 1.40 A; A=25-300.
PDB; 3MRC; X-ray; 1.80 A; A=25-300.
PDB; 3MRD; X-ray; 1.70 A; A=25-300.
PDB; 3MRE; X-ray; 1.10 A; A=25-300.
PDB; 3MRF; X-ray; 2.30 A; A=25-300.
PDB; 3MRG; X-ray; 1.30 A; A=25-300.
PDB; 3MRH; X-ray; 2.40 A; A=25-300.
PDB; 3MRI; X-ray; 2.10 A; A=25-300.
PDB; 3MRJ; X-ray; 1.87 A; A=25-300.
PDB; 3MRK; X-ray; 1.40 A; A=25-300.
PDB; 3MRL; X-ray; 2.41 A; A=25-300.
PDB; 3MRM; X-ray; 1.90 A; A=25-300.
PDB; 3MRN; X-ray; 2.30 A; A=25-300.
PDB; 3MRO; X-ray; 2.35 A; A=25-300.
PDB; 3MRP; X-ray; 2.10 A; A=25-300.
PDB; 3MRQ; X-ray; 2.20 A; A=25-300.
PDB; 3MRR; X-ray; 1.60 A; A=25-300.
PDB; 3MYJ; X-ray; 1.89 A; A/D=25-299.
PDB; 3O3A; X-ray; 1.80 A; A/D=25-299.
PDB; 3O3B; X-ray; 1.90 A; A/D=25-299.
PDB; 3O3D; X-ray; 1.70 A; A/D=25-299.
PDB; 3O3E; X-ray; 1.85 A; A/D=25-299.
PDB; 3O4L; X-ray; 2.54 A; A=25-300.
PDB; 3PWJ; X-ray; 1.70 A; A/D=25-299.
PDB; 3PWL; X-ray; 1.65 A; A/D=25-299.
PDB; 3PWN; X-ray; 1.60 A; A/D=25-299.
PDB; 3PWP; X-ray; 2.69 A; A=25-299.
PDB; 3QDG; X-ray; 2.69 A; A=25-299.
PDB; 3QDJ; X-ray; 2.30 A; A=25-299.
PDB; 3QDM; X-ray; 2.80 A; A=25-299.
PDB; 3QEQ; X-ray; 2.59 A; A=25-299.
PDB; 3QFD; X-ray; 1.68 A; A/D=25-299.
PDB; 3QFJ; X-ray; 2.29 A; A=25-299.
PDB; 3REW; X-ray; 1.90 A; A/D=25-299.
PDB; 3TO2; X-ray; 2.60 A; A=25-299.
PDB; 3UTQ; X-ray; 1.67 A; A=25-300.
PDB; 3UTS; X-ray; 2.71 A; A/F=25-300.
PDB; 3UTT; X-ray; 2.60 A; A/F=25-299.
PDB; 3V5D; X-ray; 2.00 A; A/D=25-299.
PDB; 3V5H; X-ray; 1.63 A; A/D=25-299.
PDB; 3V5K; X-ray; 2.31 A; A/D=25-299.
PDB; 4E5X; X-ray; 1.95 A; A/D=25-299.
PDB; 4EMZ; X-ray; 2.90 A; D/E=338-365.
PDB; 4EN2; X-ray; 2.58 A; D/E=338-365.
PDB; 4EUP; X-ray; 2.88 A; A/D=25-299.
PDB; 4FTV; X-ray; 2.74 A; A=25-299.
PDB; 4GKN; X-ray; 2.75 A; A/D=25-300.
PDB; 4GKS; X-ray; 2.35 A; A/D=25-300.
PDB; 4I4W; X-ray; 1.77 A; A=25-300.
PDB; 4JFD; X-ray; 2.46 A; A=25-300.
PDB; 4JFE; X-ray; 2.70 A; A=25-300.
PDB; 4JFF; X-ray; 2.43 A; A=25-300.
PDB; 4JFO; X-ray; 2.11 A; A/D=25-299.
PDB; 4JFP; X-ray; 1.91 A; A/D=25-300.
PDB; 4JFQ; X-ray; 1.90 A; A/D=25-300.
PDB; 4K7F; X-ray; 2.00 A; A/D=25-299.
PDB; 4L29; X-ray; 3.09 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300.
PDB; 4L3C; X-ray; 2.64 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300.
PDB; 4L3E; X-ray; 2.56 A; A=25-299.
PDB; 4MNQ; X-ray; 2.74 A; A=25-300.
PDB; 4NNX; X-ray; 2.10 A; A=25-298.
PDB; 4NNY; X-ray; 1.90 A; A=25-298.
PDB; 4NO0; X-ray; 2.70 A; A=25-300.
PDB; 4NO2; X-ray; 2.00 A; A=25-298.
PDB; 4NO3; X-ray; 1.70 A; A=25-298.
PDB; 4NO5; X-ray; 2.10 A; A=25-299.
PDB; 4OV5; X-ray; 2.20 A; C/F/I/L/O/R=128-141.
PDB; 4QOK; X-ray; 3.00 A; A=25-300.
PDB; 4U6X; X-ray; 1.68 A; A=25-300.
PDB; 4U6Y; X-ray; 1.47 A; A=25-300.
PDB; 4UQ3; X-ray; 2.10 A; A/C=25-299.
PDB; 4WJ5; X-ray; 1.65 A; A/D=25-299.
PDB; 4WUU; X-ray; 3.05 A; A=25-300.
PDB; 5C07; X-ray; 2.11 A; A/F=25-300.
PDB; 5C08; X-ray; 2.33 A; A/F=25-300.
PDB; 5C09; X-ray; 2.48 A; A/F=25-300.
PDB; 5C0A; X-ray; 2.46 A; A/F=25-300.
PDB; 5C0B; X-ray; 2.03 A; A/F=25-299.
PDB; 5C0C; X-ray; 1.97 A; A/F=25-300.
PDB; 5C0D; X-ray; 1.68 A; A=25-300.
PDB; 5C0E; X-ray; 1.49 A; A=25-300.
PDB; 5C0F; X-ray; 1.46 A; A=25-300.
PDB; 5C0G; X-ray; 1.37 A; A=25-300.
PDB; 5C0I; X-ray; 1.53 A; A=25-300.
PDB; 5C0J; X-ray; 1.64 A; A=25-300.
PDB; 5D2L; X-ray; 3.51 A; A/C/G/M=25-299.
PDB; 5D2N; X-ray; 2.10 A; A/H=25-299.
PDB; 5D9S; X-ray; 1.87 A; A=25-298.
PDB; 5DDH; X-ray; 1.50 A; A=25-298.
PDB; 5E00; X-ray; 1.70 A; A=25-299.
PDB; 5E6I; X-ray; 4.00 A; C/I/M/R=25-299.
PDB; 5E9D; X-ray; 2.51 A; A/F=25-299.
PDB; 5ENW; X-ray; 1.85 A; A=25-298.
PDB; 5EOT; X-ray; 2.10 A; A=26-298.
PDB; 5EU3; X-ray; 1.97 A; A=25-300.
PDB; 5EU4; X-ray; 2.12 A; A/D=25-300.
PDB; 5EU5; X-ray; 1.54 A; A=25-300.
PDB; 5EU6; X-ray; 2.02 A; A=25-300.
PDB; 5EUO; X-ray; 2.10 A; A/C=25-299.
PDB; 5F7D; X-ray; 2.30 A; A=26-298.
PDB; 5F9J; X-ray; 2.51 A; A=25-298.
PDB; 5FA3; X-ray; 1.86 A; A=26-298.
PDB; 5FA4; X-ray; 2.40 A; A=25-298.
PDB; 5FDW; X-ray; 2.70 A; A=25-298.
PDB; 5HHM; X-ray; 2.50 A; A/F=25-300.
PDB; 5HHN; X-ray; 2.03 A; A=25-298.
PDB; 5HHO; X-ray; 2.95 A; A=25-300.
PDB; 5HHP; X-ray; 1.90 A; A=25-298.
PDB; 5HHQ; X-ray; 2.10 A; A=25-298.
PDB; 5HYJ; X-ray; 3.06 A; A/F=25-300.
PDB; 5IRO; X-ray; 2.64 A; A/E/I/M/Q/U=25-299.
PDB; 5ISZ; X-ray; 2.06 A; A=25-299.
PDB; 5JHD; X-ray; 2.46 A; A/F=25-299.
PDB; 5JZI; X-ray; 2.50 A; A/F=25-299.
PDB; 5MEN; X-ray; 2.81 A; A=25-300.
PDB; 5MEO; X-ray; 1.77 A; A=25-300.
PDB; 5MEP; X-ray; 2.71 A; A/D=25-300.
PDB; 5MEQ; X-ray; 2.27 A; A=25-300.
PDB; 5MER; X-ray; 1.88 A; A/D=25-300.
PDB; 5N1Y; X-ray; 1.39 A; A=25-300.
PDB; 5N6B; X-ray; 1.71 A; A/D=25-300.
PDB; 5NHT; X-ray; 3.20 A; H=25-300.
PDB; 5NME; X-ray; 2.94 A; A/F=25-300.
PDB; 5NMF; X-ray; 2.89 A; A/F=25-300.
PDB; 5NMG; X-ray; 2.75 A; A/F=25-300.
PDB; 5NMH; X-ray; 1.55 A; A=25-300.
PDB; 5NMK; X-ray; 1.66 A; A=25-300.
PDB; 5NQK; X-ray; 3.25 A; H=25-300.
PDB; 5SWQ; X-ray; 2.00 A; A=25-300.
PDB; 5TEZ; X-ray; 1.70 A; A=25-299.
PDB; 5W1W; X-ray; 3.10 A; C/H/M/R=3-11.
PDB; 5WSH; X-ray; 2.00 A; A=25-299.
PDBsum; 1AKJ; -.
PDBsum; 1AO7; -.
PDBsum; 1AQD; -.
PDBsum; 1B0G; -.
PDBsum; 1B0R; -.
PDBsum; 1BD2; -.
PDBsum; 1DUY; -.
PDBsum; 1DUZ; -.
PDBsum; 1EEY; -.
PDBsum; 1EEZ; -.
PDBsum; 1HHG; -.
PDBsum; 1HHH; -.
PDBsum; 1HHI; -.
PDBsum; 1HHJ; -.
PDBsum; 1HHK; -.
PDBsum; 1HLA; -.
PDBsum; 1I1F; -.
PDBsum; 1I1Y; -.
PDBsum; 1I4F; -.
PDBsum; 1I7R; -.
PDBsum; 1I7T; -.
PDBsum; 1I7U; -.
PDBsum; 1IM3; -.
PDBsum; 1JF1; -.
PDBsum; 1JHT; -.
PDBsum; 1LP9; -.
PDBsum; 1OGA; -.
PDBsum; 1P7Q; -.
PDBsum; 1QEW; -.
PDBsum; 1QR1; -.
PDBsum; 1QRN; -.
PDBsum; 1QSE; -.
PDBsum; 1QSF; -.
PDBsum; 1S8D; -.
PDBsum; 1S9W; -.
PDBsum; 1S9X; -.
PDBsum; 1S9Y; -.
PDBsum; 1T1W; -.
PDBsum; 1T1X; -.
PDBsum; 1T1Y; -.
PDBsum; 1T1Z; -.
PDBsum; 1T20; -.
PDBsum; 1T21; -.
PDBsum; 1T22; -.
PDBsum; 1TVB; -.
PDBsum; 1TVH; -.
PDBsum; 1UR7; -.
PDBsum; 2AV1; -.
PDBsum; 2AV7; -.
PDBsum; 2BNQ; -.
PDBsum; 2BNR; -.
PDBsum; 2C7U; -.
PDBsum; 2CLR; -.
PDBsum; 2F53; -.
PDBsum; 2F54; -.
PDBsum; 2GIT; -.
PDBsum; 2GJ6; -.
PDBsum; 2GT9; -.
PDBsum; 2GTW; -.
PDBsum; 2GTZ; -.
PDBsum; 2GUO; -.
PDBsum; 2J8U; -.
PDBsum; 2JCC; -.
PDBsum; 2P5E; -.
PDBsum; 2P5W; -.
PDBsum; 2PYE; -.
PDBsum; 2UWE; -.
PDBsum; 2V2W; -.
PDBsum; 2V2X; -.
PDBsum; 2VLJ; -.
PDBsum; 2VLK; -.
PDBsum; 2VLL; -.
PDBsum; 2VLR; -.
PDBsum; 2X4N; -.
PDBsum; 2X4O; -.
PDBsum; 2X4P; -.
PDBsum; 2X4Q; -.
PDBsum; 2X4R; -.
PDBsum; 2X4S; -.
PDBsum; 2X4T; -.
PDBsum; 2X4U; -.
PDBsum; 2X70; -.
PDBsum; 3BGM; -.
PDBsum; 3BH8; -.
PDBsum; 3BH9; -.
PDBsum; 3BHB; -.
PDBsum; 3D25; -.
PDBsum; 3D39; -.
PDBsum; 3D3V; -.
PDBsum; 3FQN; -.
PDBsum; 3FQR; -.
PDBsum; 3FQT; -.
PDBsum; 3FQU; -.
PDBsum; 3FQW; -.
PDBsum; 3FQX; -.
PDBsum; 3FT2; -.
PDBsum; 3FT3; -.
PDBsum; 3FT4; -.
PDBsum; 3GIV; -.
PDBsum; 3GJF; -.
PDBsum; 3GSN; -.
PDBsum; 3GSO; -.
PDBsum; 3GSQ; -.
PDBsum; 3GSR; -.
PDBsum; 3GSU; -.
PDBsum; 3GSV; -.
PDBsum; 3GSW; -.
PDBsum; 3GSX; -.
PDBsum; 3H7B; -.
PDBsum; 3H9H; -.
PDBsum; 3H9S; -.
PDBsum; 3HAE; -.
PDBsum; 3HLA; -.
PDBsum; 3HPJ; -.
PDBsum; 3I6G; -.
PDBsum; 3I6K; -.
PDBsum; 3IXA; -.
PDBsum; 3KLA; -.
PDBsum; 3MGO; -.
PDBsum; 3MGT; -.
PDBsum; 3MR9; -.
PDBsum; 3MRB; -.
PDBsum; 3MRC; -.
PDBsum; 3MRD; -.
PDBsum; 3MRE; -.
PDBsum; 3MRF; -.
PDBsum; 3MRG; -.
PDBsum; 3MRH; -.
PDBsum; 3MRI; -.
PDBsum; 3MRJ; -.
PDBsum; 3MRK; -.
PDBsum; 3MRL; -.
PDBsum; 3MRM; -.
PDBsum; 3MRN; -.
PDBsum; 3MRO; -.
PDBsum; 3MRP; -.
PDBsum; 3MRQ; -.
PDBsum; 3MRR; -.
PDBsum; 3MYJ; -.
PDBsum; 3O3A; -.
PDBsum; 3O3B; -.
PDBsum; 3O3D; -.
PDBsum; 3O3E; -.
PDBsum; 3O4L; -.
PDBsum; 3PWJ; -.
PDBsum; 3PWL; -.
PDBsum; 3PWN; -.
PDBsum; 3PWP; -.
PDBsum; 3QDG; -.
PDBsum; 3QDJ; -.
PDBsum; 3QDM; -.
PDBsum; 3QEQ; -.
PDBsum; 3QFD; -.
PDBsum; 3QFJ; -.
PDBsum; 3REW; -.
PDBsum; 3TO2; -.
PDBsum; 3UTQ; -.
PDBsum; 3UTS; -.
PDBsum; 3UTT; -.
PDBsum; 3V5D; -.
PDBsum; 3V5H; -.
PDBsum; 3V5K; -.
PDBsum; 4E5X; -.
PDBsum; 4EMZ; -.
PDBsum; 4EN2; -.
PDBsum; 4EUP; -.
PDBsum; 4FTV; -.
PDBsum; 4GKN; -.
PDBsum; 4GKS; -.
PDBsum; 4I4W; -.
PDBsum; 4JFD; -.
PDBsum; 4JFE; -.
PDBsum; 4JFF; -.
PDBsum; 4JFO; -.
PDBsum; 4JFP; -.
PDBsum; 4JFQ; -.
PDBsum; 4K7F; -.
PDBsum; 4L29; -.
PDBsum; 4L3C; -.
PDBsum; 4L3E; -.
PDBsum; 4MNQ; -.
PDBsum; 4NNX; -.
PDBsum; 4NNY; -.
PDBsum; 4NO0; -.
PDBsum; 4NO2; -.
PDBsum; 4NO3; -.
PDBsum; 4NO5; -.
PDBsum; 4OV5; -.
PDBsum; 4QOK; -.
PDBsum; 4U6X; -.
PDBsum; 4U6Y; -.
PDBsum; 4UQ3; -.
PDBsum; 4WJ5; -.
PDBsum; 4WUU; -.
PDBsum; 5C07; -.
PDBsum; 5C08; -.
PDBsum; 5C09; -.
PDBsum; 5C0A; -.
PDBsum; 5C0B; -.
PDBsum; 5C0C; -.
PDBsum; 5C0D; -.
PDBsum; 5C0E; -.
PDBsum; 5C0F; -.
PDBsum; 5C0G; -.
PDBsum; 5C0I; -.
PDBsum; 5C0J; -.
PDBsum; 5D2L; -.
PDBsum; 5D2N; -.
PDBsum; 5D9S; -.
PDBsum; 5DDH; -.
PDBsum; 5E00; -.
PDBsum; 5E6I; -.
PDBsum; 5E9D; -.
PDBsum; 5ENW; -.
PDBsum; 5EOT; -.
PDBsum; 5EU3; -.
PDBsum; 5EU4; -.
PDBsum; 5EU5; -.
PDBsum; 5EU6; -.
PDBsum; 5EUO; -.
PDBsum; 5F7D; -.
PDBsum; 5F9J; -.
PDBsum; 5FA3; -.
PDBsum; 5FA4; -.
PDBsum; 5FDW; -.
PDBsum; 5HHM; -.
PDBsum; 5HHN; -.
PDBsum; 5HHO; -.
PDBsum; 5HHP; -.
PDBsum; 5HHQ; -.
PDBsum; 5HYJ; -.
PDBsum; 5IRO; -.
PDBsum; 5ISZ; -.
PDBsum; 5JHD; -.
PDBsum; 5JZI; -.
PDBsum; 5MEN; -.
PDBsum; 5MEO; -.
PDBsum; 5MEP; -.
PDBsum; 5MEQ; -.
PDBsum; 5MER; -.
PDBsum; 5N1Y; -.
PDBsum; 5N6B; -.
PDBsum; 5NHT; -.
PDBsum; 5NME; -.
PDBsum; 5NMF; -.
PDBsum; 5NMG; -.
PDBsum; 5NMH; -.
PDBsum; 5NMK; -.
PDBsum; 5NQK; -.
PDBsum; 5SWQ; -.
PDBsum; 5TEZ; -.
PDBsum; 5W1W; -.
PDBsum; 5WSH; -.
ProteinModelPortal; P01892; -.
SMR; P01892; -.
BioGrid; 109350; 90.
IntAct; P01892; 31.
MINT; P01892; -.
DrugBank; DB02740; 3-Indolebutyric Acid.
iPTMnet; P01892; -.
PhosphoSitePlus; P01892; -.
SwissPalm; P01892; -.
DMDM; 122138; -.
EPD; P01892; -.
PeptideAtlas; P01892; -.
PRIDE; P01892; -.
Ensembl; ENST00000457879; ENSP00000403575; ENSG00000235657.
Ensembl; ENST00000547271; ENSP00000447962; ENSG00000235657.
Ensembl; ENST00000547522; ENSP00000448077; ENSG00000227715.
DisGeNET; 3105; -.
GeneCards; HLA-A; -.
HGNC; HGNC:4931; HLA-A.
MalaCards; HLA-A; -.
MIM; 142800; gene.
neXtProt; NX_P01892; -.
HOVERGEN; HBG016709; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SIGNOR; P01892; -.
ChiTaRS; HLA-A; human.
EvolutionaryTrace; P01892; -.
Proteomes; UP000005640; Chromosome 6.
CleanEx; HS_HLA-A; -.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0042612; C:MHC class I protein complex; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0030881; F:beta-2-microglobulin binding; IDA:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0042608; F:T cell receptor binding; IDA:UniProtKB.
GO; GO:0046977; F:TAP binding; IDA:UniProtKB.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IDA:BHF-UCL.
GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; IDA:BHF-UCL.
GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:2000568; P:positive regulation of memory T cell activation; IDA:UniProtKB.
GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
InterPro; IPR010579; MHC_I_a_C.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
Pfam; PF06623; MHC_I_C; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Host-virus interaction; Immunity;
Membrane; MHC I; Phosphoprotein; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 24 {ECO:0000269|PubMed:92029}.
CHAIN 25 365 HLA class I histocompatibility antigen,
A-2 alpha chain.
/FTId=PRO_0000018814.
TOPO_DOM 25 308 Extracellular. {ECO:0000255}.
TRANSMEM 309 332 Helical. {ECO:0000255}.
TOPO_DOM 333 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 209 295 Ig-like C1-type.
REGION 25 114 Alpha-1.
REGION 115 206 Alpha-2.
REGION 207 298 Alpha-3.
REGION 299 308 Connecting peptide.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 344 344 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 125 188 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12796775}.
DISULFID 227 283 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:12796775}.
VARIANT 33 33 F -> Y (in allele A*02:05, allele
A*02:06, allele A*02:08, allele A*02:10
and allele A*02:21; dbSNP:rs2075684).
/FTId=VAR_004334.
VARIANT 54 54 D -> N (in allele A*02:21;
dbSNP:rs41549215).
/FTId=VAR_004335.
VARIANT 65 65 A -> G (in allele A*02:31;
dbSNP:rs41557613).
/FTId=VAR_016726.
VARIANT 67 67 Q -> R (in allele A*02:02, allele A*02:05
and allele A*02:08; dbSNP:rs41559117).
/FTId=VAR_004336.
VARIANT 89 89 R -> G (polymorphism; dbSNP:rs199474430).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076446.
VARIANT 90 90 K -> N (in allele A*02:08 and allele
A*02:20; dbSNP:rs199474436).
/FTId=VAR_004337.
VARIANT 94 94 H -> Q (in allele A*02:34 and allele
A*02:35; dbSNP:rs78306866).
/FTId=VAR_016727.
VARIANT 97 97 T -> I (in allele A*02:11;
dbSNP:rs199474457).
/FTId=VAR_004338.
VARIANT 98 98 H -> D (in allele A*02:11 and allele
A*02:35; dbSNP:rs1136683).
/FTId=VAR_016728.
VARIANT 119 119 V -> L (in allele A*02:02, allele
A*02:05, allele A*02:08 and allele
A*02:17; dbSNP:rs1071743).
/FTId=VAR_004339.
VARIANT 121 121 R -> M (in allele A*02:04 and allele
A*02:17; dbSNP:rs199474485).
/FTId=VAR_004340.
VARIANT 123 123 Y -> C (in allele A*02:07 and allele
A*02:18; dbSNP:rs1136697).
/FTId=VAR_004341.
VARIANT 123 123 Y -> F (in allele A*02:10 and allele
A*02:17; dbSNP:rs1136697).
/FTId=VAR_004342.
VARIANT 131 131 W -> G (in allele A*02:10;
dbSNP:rs1136702).
/FTId=VAR_004343.
VARIANT 162 162 M -> K (in allele A*02:18;
dbSNP:rs41549316).
/FTId=VAR_004344.
VARIANT 173 173 A -> T (in allele A*02:03;
dbSNP:rs1059526).
/FTId=VAR_004345.
VARIANT 176 176 V -> E (in allele A*02:03 and allele
A*02:13; dbSNP:rs9256983).
{ECO:0000244|PubMed:21269460,
ECO:0000244|PubMed:25944712}.
/FTId=VAR_004346.
VARIANT 180 180 L -> Q (in allele A*02:12, allele A*02:13
and allele A*02:37).
/FTId=VAR_004348.
VARIANT 180 180 L -> W (in allele A*02:02, allele
A*02:03, allele A*02:05 and allele
A*02:08; dbSNP:rs9260156).
{ECO:0000244|PubMed:21269460}.
/FTId=VAR_004347.
VARIANT 187 187 T -> E (in allele A*02:16; requires 2
nucleotide substitutions).
/FTId=VAR_004349.
VARIANT 190 190 E -> D (in allele A*02:36 and allele
A*02:37; dbSNP:rs879577815).
/FTId=VAR_016729.
VARIANT 191 191 W -> G (in allele A*02:36 and allele
A*02:37; dbSNP:rs3098019).
/FTId=VAR_016730.
VARIANT 260 260 A -> E (in allele A*02:09;
dbSNP:rs41540417).
/FTId=VAR_004350.
CONFLICT 115 115 G -> V (in Ref. 4; AAA52656).
{ECO:0000305}.
CONFLICT 140 140 Y -> V (in Ref. 4; AAA52656).
{ECO:0000305}.
CONFLICT 277 277 Q -> E (in Ref. 4; AAA52656).
{ECO:0000305}.
CONFLICT 318 318 F -> L (in Ref. 4; AAA52656).
{ECO:0000305}.
STRAND 27 36 {ECO:0000244|PDB:3D25}.
STRAND 41 43 {ECO:0000244|PDB:5C0G}.
STRAND 45 52 {ECO:0000244|PDB:3D25}.
STRAND 55 61 {ECO:0000244|PDB:3D25}.
STRAND 64 66 {ECO:0000244|PDB:3D25}.
STRAND 70 73 {ECO:0000244|PDB:4E5X}.
HELIX 74 78 {ECO:0000244|PDB:3D25}.
HELIX 81 108 {ECO:0000244|PDB:3D25}.
STRAND 113 115 {ECO:0000244|PDB:3D25}.
STRAND 118 127 {ECO:0000244|PDB:3D25}.
STRAND 129 131 {ECO:0000244|PDB:1B0R}.
STRAND 133 142 {ECO:0000244|PDB:3D25}.
STRAND 145 150 {ECO:0000244|PDB:3D25}.
STRAND 152 155 {ECO:0000244|PDB:5IRO}.
STRAND 157 159 {ECO:0000244|PDB:3D25}.
HELIX 162 173 {ECO:0000244|PDB:3D25}.
HELIX 176 185 {ECO:0000244|PDB:3D25}.
HELIX 187 198 {ECO:0000244|PDB:3D25}.
HELIX 200 203 {ECO:0000244|PDB:3D25}.
STRAND 210 235 {ECO:0000244|PDB:3D25}.
STRAND 238 243 {ECO:0000244|PDB:3D25}.
STRAND 246 248 {ECO:0000244|PDB:3D25}.
HELIX 249 251 {ECO:0000244|PDB:2GTW}.
STRAND 252 254 {ECO:0000244|PDB:3D25}.
STRAND 261 263 {ECO:0000244|PDB:3D25}.
STRAND 265 274 {ECO:0000244|PDB:3D25}.
STRAND 275 277 {ECO:0000244|PDB:4JFD}.
HELIX 278 280 {ECO:0000244|PDB:3D25}.
STRAND 281 286 {ECO:0000244|PDB:3D25}.
STRAND 290 292 {ECO:0000244|PDB:2V2X}.
STRAND 294 296 {ECO:0000244|PDB:3D25}.
STRAND 348 350 {ECO:0000244|PDB:4EN2}.
SEQUENCE 365 AA; 40922 MW; B54A97B24B337C08 CRC64;
MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF
DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV DLGTLRGYYN QSEAGSHTVQ
RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL
RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP
SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL
TACKV


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