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Hemoglobin subunit gamma-2 (Gamma-2-globin) (Hb F Ggamma) (Hemoglobin gamma-2 chain) (Hemoglobin gamma-G chain)

 HBG2_HUMAN              Reviewed;         147 AA.
P69892; A8MZE0; P02096; P62027; Q14491; Q68NH9; Q96FH6; Q96FH7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 140.
RecName: Full=Hemoglobin subunit gamma-2;
AltName: Full=Gamma-2-globin;
AltName: Full=Hb F Ggamma;
AltName: Full=Hemoglobin gamma-2 chain;
AltName: Full=Hemoglobin gamma-G chain;
Name=HBG2;
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].
PubMed=7438203; DOI=10.1016/0092-8674(80)90426-2;
Slightom J.L., Blechl A.E., Smithies O.;
"Human fetal G gamma- and A gamma-globin genes: complete nucleotide
sequences suggest that DNA can be exchanged between these duplicated
genes.";
Cell 21:627-638(1980).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7250702; DOI=10.1016/0378-1119(80)90103-1;
Cavallesco C., Forget B.G., Deriel J.K., Wilson L.B., Wilson J.T.,
Weissman S.M.;
"Nucleotide sequence of human G gamma globin messenger RNA.";
Gene 12:215-221(1980).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT M-CIRCLEVILLE LEU-64.
Kutlar F., Shell R.D., Elam D., Holley L., Nechtman J., Kutlar A.;
"A new G-gamma globin chain variant (His63Leu), hemoglobin M-
Circleville found in a Caucasian family.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-147.
PubMed=14087393; DOI=10.1021/bi00905a016;
Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J., Jones R.T.;
"The amino acid sequence of the gamma chain of human fetal
hemoglobin.";
Biochemistry 2:992-1008(1963).
[7]
PROTEIN SEQUENCE OF 2-60; 67-77 AND 84-147, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 122-147.
PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9;
Lang K.M., Spritz R.A.;
"Cloning specific complete polyadenylylated 3'-terminal cDNA
segments.";
Gene 33:191-196(1985).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-51; SER-53;
SER-140; SER-143 AND SER-144, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
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).
[11]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME
AND ALPHA CHAIN, AND SUBUNIT.
PubMed=881729; DOI=10.1016/S0022-2836(77)80158-7;
Frier J.A., Perutz M.F.;
"Structure of human foetal deoxyhaemoglobin.";
J. Mol. Biol. 112:97-112(1977).
[12]
ACETYLATION AT GLY-2.
PubMed=5554303;
Stegink L.D., Meyer P.D., Brummel M.C.;
"Human fetal hemoglobin F 1. Acetylation status.";
J. Biol. Chem. 246:3001-3007(1971).
[13]
VARIANT MALTA-1 ARG-118.
PubMed=5792729; DOI=10.1038/223311a0;
Cauchi M.N., Clegg J.B., Weatherall D.J.;
"Haemoglobin F(Malta): a new foetal haemoglobin variant with a high
incidence in Maltese infants.";
Nature 223:311-313(1969).
[14]
VARIANT AUCKLAND ASN-8.
PubMed=4429671;
Carrell R.W., Owen M.C., Anderson R., Berry E.;
"Haemoglobin F Auckland G gamma 7 Asp leads to Asn: further evidence
for multiple genes for the gamma chain.";
Biochim. Biophys. Acta 365:323-327(1974).
[15]
VARIANT PORT-ROYAL ALA-126.
PubMed=4846278; DOI=10.1111/j.1365-2141.1974.tb06798.x;
Brimhall B., Vedvick T.S., Jones R.T., Ahern E., Palomino E.,
Ahern V.;
"Haemoglobin F Port Royal (alpha2G gamma2 125 Glu leads to Ala).";
Br. J. Haematol. 27:313-318(1974).
[16]
VARIANT MALAYSIA CYS-2.
PubMed=4837284;
Lie-Injo L.E., Kamuzora H., Lehmann H.;
"Haemoglobin F Malaysia: alpha 2, gamma 2 1(NA1) glycine-->cysteine;
136 glycine.";
J. Med. Genet. 11:25-30(1974).
[17]
VARIANT POOLE GLY-131.
PubMed=1127124; DOI=10.1136/jcp.28.4.317;
Lee-Potter J.P., Deacon-Smith R.A., Simpkiss M.J., Kamuzora H.,
Lehmann H.;
"A new cause of haemolytic anaemia in the newborn. A description of an
unstable fetal haemoglobin: F Poole, alpha2-G-gamma2 130 tryptophan
yields glycine.";
J. Clin. Pathol. 28:317-320(1975).
[18]
VARIANTS MELBOURNE ARG-17 AND CARLTON LYS-122.
PubMed=836882; DOI=10.1016/0005-2795(77)90020-4;
Brennan S.O., Smith M.B., Carrell R.W.;
"Haemoglobin F Melbourne Ggamma 16 Gly leads to Arg and haemoglobin F
carlton Ggamma 121 Glu leads to Lys. Further evidence for varied
activity of gamma-chain genes.";
Biochim. Biophys. Acta 490:452-455(1977).
[19]
VARIANT MEINOHAMA GLY-6.
PubMed=6172403; DOI=10.3109/03630268108991687;
Ohta Y., Saito S., Fujita S., Wilson J.B., Lam H., Huisman T.H.J.;
"Hb F-Meinohama or alpha 2 gamma 2 (5 Glu replaced by Gly; 75 Ile; 136
Gly).";
Hemoglobin 5:565-570(1981).
[20]
VARIANT LODZ ARG-45.
PubMed=6814491; DOI=10.1016/0167-4838(82)90353-3;
Honig G.R., Koshy M., Schroeder W.A., Shelton J.B., Shelton J.R.;
"Hemoglobin F Lodz (G gamma I 44 Ser replaced by Arg). A newly
identified variant from an American infant of Polish descent.";
Biochim. Biophys. Acta 707:213-216(1982).
[21]
VARIANT KINGSTON ARG-56.
PubMed=6186522; DOI=10.1016/0014-5793(82)81307-0;
Serjeant G.R., Serjeant B.E., Lehmann H., Dukes M., Robb L.;
"Hb F Kingston (G gamma 55 [D6] Met leads to Arg).";
FEBS Lett. 150:77-80(1982).
[22]
VARIANT CALTECH GLN-121.
PubMed=6186635; DOI=10.3109/03630268209046451;
Shelton J.B., Shelton J.R., Espinueva Z., Huynh V., Schroeder W.A.,
Powars D.;
"Hemoglobin F-Caltech: alpha 2 G gamma 2 120Lys replaced by Gln.";
Hemoglobin 6:577-592(1982).
[23]
VARIANT COLUMBUS-GA ASN-95.
PubMed=6186636; DOI=10.3109/03630268209046452;
Nakatsuji T., Lam H., Wilson J.B., Webber B.B., Huisman T.H.J.;
"Hb F-Columbus-Ga or alpha 2 G gamma 2 94(FGl) Asp replaced by Asn.";
Hemoglobin 6:593-598(1982).
[24]
VARIANT KENNESTONE ARG-78.
PubMed=6192110; DOI=10.3109/03630268309048656;
Nakatsuji T., Lam H., Huisman T.H.J.;
"Hb F-Kennestone or alpha 2G gamma 2 (EF1)77 His leads to Arg observed
in a Caucasian baby.";
Hemoglobin 7:267-270(1983).
[25]
VARIANT LA GRANGE LYS-102.
PubMed=6206897; DOI=10.1016/0167-4838(84)90208-5;
Nakatsuji T., Shimizu K., Huisman T.H.J.;
"Hb F-La Grange or alpha 2 gamma 2 101(G3)Glu-->Lys; 75Ile; 136Gly: a
high oxygen affinity fetal hemoglobin variant observed in a Caucasian
newborn.";
Biochim. Biophys. Acta 789:224-228(1984).
[26]
VARIANT SHANGHAI ARG-67.
PubMed=2579547; DOI=10.1002/ajh.2830180303;
Zeng Y.T., Huang S.Z., Nakatsuji T., Huisman T.H.J.;
"-G gamma A gamma-thalassemia and gamma-chain variants in Chinese
newborn babies.";
Am. J. Hematol. 18:235-242(1985).
[27]
VARIANT TOKYO ILE-35.
PubMed=2581919; DOI=10.3109/03630268508996979;
Chen S.S., Wilson J.B., Webber B.B., Huisman T.H.J., Miwa S.,
Amenomori Y.;
"Hb F-Tokyo or alpha 2G gamma 2 34(B16)Val-->Ile, a silent gamma chain
variant detected by reverse phase high performance liquid
chromatography.";
Hemoglobin 9:25-32(1985).
[28]
VARIANT URUMQI GLY-23.
PubMed=2420748; DOI=10.3109/03630268609072467;
Hu H.Y., Ma M.S.;
"Hb F-Urumqi G gamma I22(B4)Asp-->Gly: a new fetal hemoglobin variant
found in a Uygur baby.";
Hemoglobin 10:15-20(1986).
[29]
VARIANTS ALBAICIN GLU-9 AND GLN-9.
PubMed=2435680;
de Pablos J.M., Wilson J.B., Kutlar A., Chen S.S., Huisman T.H.J.;
"Hb F-Albaicin or G gamma 8(A5)Lys-->Glu or Gln.";
Hemoglobin 10:655-659(1986).
[30]
VARIANTS FUCHU GLN-22 AND MINOO ARG-73.
PubMed=3120456;
Hayashi A., Wada Y., Matsuo T., Katakuse I., Matsuda H.;
"Neonatal screening and mass-spectrometric analysis of hemoglobin
variants in Japan.";
Acta Haematol. 78:114-118(1987).
[31]
VARIANT OAKLAND LYS-27.
PubMed=2442122; DOI=10.3109/03630268709005796;
Kleman K., Lubin B., Wilson J.B., Kutlar A., Webber B.B.,
Huisman T.H.J.;
"Hb F-Oakland or alpha 2G gamma I2(26)(B8)Glu-->Lys.";
Hemoglobin 11:181-183(1987).
[32]
VARIANT CLARKE ASN-66.
PubMed=2442123; DOI=10.3109/03630268709005797;
Kutlar A., Kutlar F., Wilson J.B., Webber B.B., Gonzalez Redondo J.M.,
Huisman T.H.J.;
"Hb F-Clarke or alpha 2G gamma 2(65)(E9)Lys-->Asn.";
Hemoglobin 11:185-188(1987).
[33]
VARIANT GRANADA VAL-23.
PubMed=2459082;
de Pablos J.M., Clegg J.B.;
"Hb F-Granada or alpha 2G gamma (2)22(B4)Asp-->Val: a new human fetal
hemoglobin variant.";
Hemoglobin 12:405-407(1988).
[34]
VARIANT AUSTELL LYS-41.
PubMed=2459083; DOI=10.3109/03630268808998042;
Kutlar A., Kutlar F., Wilson J.B., Webber B.B., Hu H., Huisman T.H.J.;
"Hb F-Austell or alpha 2G gamma (2)40(C6)Arg-->Lys.";
Hemoglobin 12:409-411(1988).
[35]
VARIANT TNCY TYR-64.
PubMed=2483933; DOI=10.3109/03630268908998852;
Glader B.E., Zwerdling D., Kutlar F., Kutlar A., Wilson J.B.,
Huisman T.H.J.;
"Hb F-M-Osaka or alpha 2G gamma 2(63)(E7)His-->Tyr in a Caucasian male
infant.";
Hemoglobin 13:769-773(1989).
[36]
VARIANT TNCY TYR-93.
PubMed=2470017;
Priest J.R., Watterson J., Jones R.T., Faassen A.E., Hedlund B.E.;
"Mutant fetal hemoglobin causing cyanosis in a newborn.";
Pediatrics 83:734-736(1989).
[37]
VARIANT BROOKLYN GLN-67.
PubMed=1703138; DOI=10.3109/03630269009046963;
Plaseska D., Li H.-J., Wilson J.B., Kutlar F., Kutlar A.,
Huisman T.H.J., Kulpa J.;
"Hb F-Brooklyn or alpha 2G gamma 2(66)(E10)Lys-->Gln.";
Hemoglobin 14:213-216(1990).
[38]
VARIANT ONODA TYR-147.
PubMed=1703139; DOI=10.3109/03630269009046964;
Harano T., Harano K., Doi K., Ueda S., Imai K., Ohba Y., Kutlar F.,
Huisman T.H.J.;
"Hb F-Onoda or alpha 2G gamma 2(146)(HC3)His-->Tyr, a newly discovered
fetal hemoglobin variant in a Japanese newborn.";
Hemoglobin 14:217-222(1990).
[39]
VARIANT CATALONIA ARG-16.
PubMed=1706691; DOI=10.3109/03630269009005804;
Plaseska D., Wilson J.B., Kutlar F., Font L., Baiget M.,
Huisman T.H.J.;
"Hb F-Catalonia or alpha 2G gamma(2)15(A12)Trp-->Arg.";
Hemoglobin 14:511-516(1990).
[40]
VARIANT CHARLOTTE THR-76.
PubMed=1714434; DOI=10.3109/03630269009046970;
Plaseska D., Kutlar F., Wilson J.B., Fei Y.J., Huisman T.H.J.;
"Hb F-Charlotte, an A gamma variant with a threonine residue in
position gamma 75 and a glycine residue in position gamma 136.";
Hemoglobin 14:617-625(1990).
[41]
VARIANT COSENZA GLU-26.
PubMed=1726095; DOI=10.3109/03630269109027898;
Qualtieri A., Crescibene L., Bagala A., de Marco E.V., Bria M.,
Brancati C.;
"Hb F-Cosenza or G gamma 25(B7)Gly-->Glu: a new fast-moving fetal
hemoglobin variant.";
Hemoglobin 15:509-515(1991).
[42]
VARIANT SASKATOON LYS-22.
PubMed=8144355; DOI=10.3109/03630269309043495;
Pobedimskaya D.D., Molchanova T.P., Huisman T.H.J., Harding S.R.,
Bakanec R.;
"Hb F-Saskatoon or alpha 2G gamma (2)21(B3)Glu-->Lys observed in a
North American indian newborn.";
Hemoglobin 17:547-549(1993).
[43]
VARIANT MACEDONIA-II ASN-105.
PubMed=7713741; DOI=10.3109/03630269409045769;
Plaseska D., Panovska-Popovska S., Lazarevski M., Efremov G.D.;
"Hb F-Macedonia-II [G gamma 104(G6)Lys-->Asn]: a new gamma chain
variant.";
Hemoglobin 18:373-382(1994).
[44]
VARIANT TNCY SER-42.
PubMed=7741137; DOI=10.1002/ajh.2830490108;
Kohli-Kumar M., Zwerdling T., Rucknagel D.L.;
"Hemoglobin F-Cincinnati, alpha 2G gamma 2 41(C7) Phe-->Ser in a
newborn with cyanosis.";
Am. J. Hematol. 49:43-47(1995).
[45]
VARIANTS EMIRATES GLU-60 AND SACROMONTE GLN-60.
PubMed=7558873; DOI=10.3109/03630269509036937;
Abbes S., Fitzgerald P.A., Varady E., Girot R., Pic P., Blouquit Y.,
Ducrocq R., Drupt F., Wajcman H.;
"Two fetal hemoglobin variants affecting the same residue: Hb F-
Emirates [G gamma 59(E3)Lys-->Glu] and Hb F-Sacromonte [G gamma
59(E3)Lys-->Gln].";
Hemoglobin 19:173-182(1995).
[46]
VARIANT VELETA GLY-23.
PubMed=8718700;
de Pablos Gallego J.M., Gu L.H., Leonova J.Y., Huisman T.H.J.;
"Hb F-Veleta or alpha 2 G gamma(2)40(C6)Arg-->Gly.";
Hemoglobin 19:407-411(1995).
[47]
VARIANT WAYNESBORO THR-76.
PubMed=8718701; DOI=10.3109/03630269509005834;
Gu L.H., Oner C., Huisman T.H.J.;
"The G gamma T chain (G gamma 75 Thr; 136 Gly) in Hb F-Charlotte is
the product of an A gamma gene with a limited gene conversion and that
in Hb F-Waynesboro of a mutated G gamma gene.";
Hemoglobin 19:413-418(1995).
[48]
VARIANT LESVOS THR-76.
PubMed=8566966; DOI=10.1007/BF02265278;
Papadakis M.N., Patrinos G.P., Drakoulakou O., Loutradi-Anagnostou A.;
"HbF-Lesvos: an HbF variant due to a novel G gamma mutation (G gamma
75 ATA-->ACA) detected in a Greek family.";
Hum. Genet. 97:260-262(1996).
[49]
VARIANT CALABRIA LEU-119.
PubMed=10722114; DOI=10.3109/03630260009002272;
Manca L., Cherchi L., De Rosa M.C., Giardina B., Masala B.;
"A new, electrophoretically silent, fetal hemoglobin variant: Hb F-
Calabria Ggamma118(GH1)Phe-->Leu.";
Hemoglobin 24:37-44(2000).
[50]
VARIANTS CLAMART ASN-18 AND OULED RABAH LYS-20.
PubMed=10722115; DOI=10.3109/03630260009002273;
Wajcman H., Borensztajn K., Riou J., Prome D., Hurtrel D.,
Bardakdjian J., Lena-Russo D., Amouroux I., Ducrocq R.;
"Two new Ggamma chain variants: Hb F-Clamart [gamma17(A14)Lys-->Asn]
and Hb F-Ouled Rabah [gamma19(B1)Asn-->Lys].";
Hemoglobin 24:45-52(2000).
[51]
VARIANT COIGNERES VAL-76.
PubMed=11791877; DOI=10.1081/HEM-100107881;
Wajcman H., Yapo A.P., Riou J., Prome D., Richelme-David S.,
Hurtrel D., Bardakdjian-Michau J.;
"A new Ggamma chain variant: Hb F-Coignieres
[gamma75(E19)Ile-->Val].";
Hemoglobin 25:425-428(2001).
[52]
VARIANT BONHEIDEN PRO-39.
PubMed=15645283; DOI=10.1007/s00431-004-1614-7;
Van den Driessche M., Moerman J., Moens M., Van Eldere S.,
Derclaye I., Philippe M.;
"Severe hereditary haemolytic anaemia in a Caucasian newborn: a new
fetal haemoglobin variant Hb F-Bonheiden ((G)gamma 38(C4)
Thr-->Pro).";
Eur. J. Pediatr. 164:261-262(2005).
[53]
VARIANT BRON ALA-21.
PubMed=16370494; DOI=10.1080/03630260500312725;
Lacan P., Burnichon N., Becchi M., Zanella-Cleon I., Aubry M.,
Couprie N., Francina A.;
"A new G(gamma) chain variant: Hb F-Bron [gamma20(B2)Val-->Ala].";
Hemoglobin 29:301-305(2005).
[54]
VARIANT TNCY LEU-64, AND CHARACTERIZATION OF VARIANT TNCY TYR-64.
PubMed=19065339; DOI=10.1080/03630260802507915;
Dainer E., Shell R., Miller R., Atkin J.F., Pastore M., Kutlar A.,
Zhuang L., Holley L., Davis D.H., Kutlar F.;
"Neonatal cyanosis due to a novel fetal hemoglobin: Hb F-Circleville
[Ggamma63(E7)His-->Leu, CAT>CTT].";
Hemoglobin 32:596-600(2008).
[55]
VARIANT TNCY MET-68, AND CHARACTERIZATION OF VARIANT TNCY MET-68.
PubMed=21561349; DOI=10.1056/NEJMoa1013579;
Crowley M.A., Mollan T.L., Abdulmalik O.Y., Butler A.D., Goodwin E.F.,
Sarkar A., Stolle C.A., Gow A.J., Olson J.S., Weiss M.J.;
"A hemoglobin variant associated with neonatal cyanosis and anemia.";
N. Engl. J. Med. 364:1837-1843(2011).
[56]
VARIANT TNCY HIS-106, AND CHARACTERIZATION OF VARIANT TNCY HIS-106.
PubMed=24502349; DOI=10.3109/03630269.2013.870079;
Saller E., Kohne E., Dutly F., Frischknecht H.;
"A new (G)gamma-globin variant causing low oxygen affinity: Hb F-
Brugine/Feldkirch [(G)gamma105(G7)Leu?His; HBG2: c.317T>A].";
Hemoglobin 38:84-87(2014).
-!- FUNCTION: Gamma chains make up the fetal hemoglobin F, in
combination with alpha chains.
-!- SUBUNIT: Heterotetramer of two alpha chains and two gamma chains
in fetal hemoglobin (Hb F). {ECO:0000269|PubMed:881729}.
-!- INTERACTION:
P69905:HBA2; NbExp=3; IntAct=EBI-3910089, EBI-714680;
-!- TISSUE SPECIFICITY: Red blood cells.
-!- DEVELOPMENTAL STAGE: Expressed until four or five weeks after
birth.
-!- PTM: Acetylation of Gly-2 converts Hb F to the minor Hb F1.
{ECO:0000269|PubMed:5554303}.
-!- DISEASE: Cyanosis transient neonatal (TNCY) [MIM:613977]: A
disorder characterized by cyanosis in the fetus and neonate, due
to a defect in the fetal hemoglobin chain which has reduced
affinity for oxygen. Some patients develop anemia resulting from
increased destruction of red cells containing abnormal or unstable
hemoglobin. The cyanosis resolves spontaneously by 5 to 6 months
of age or earlier, as the adult beta-globin chain is produced and
replaces the fetal gamma-globin chain.
{ECO:0000269|PubMed:19065339, ECO:0000269|PubMed:21561349,
ECO:0000269|PubMed:24502349, ECO:0000269|PubMed:2470017,
ECO:0000269|PubMed:2483933, ECO:0000269|PubMed:7741137}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-!- SEQUENCE CAUTION:
Sequence=AAB50159.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
thalassemias;
URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBG2";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M91036; AAB59428.1; -; Genomic_DNA.
EMBL; M91037; AAA58492.1; -; Genomic_DNA.
EMBL; U01317; AAA16331.1; -; Genomic_DNA.
EMBL; V00515; CAA23773.1; -; Genomic_DNA.
EMBL; M15386; AAB50159.1; ALT_INIT; mRNA.
EMBL; AY662983; AAT98611.1; -; Genomic_DNA.
EMBL; AK290492; BAF83181.1; -; mRNA.
EMBL; BC010914; AAH10914.1; -; mRNA.
EMBL; BC029387; AAH29387.1; -; mRNA.
EMBL; BC130457; AAI30458.1; -; mRNA.
EMBL; BC130459; AAI30460.1; -; mRNA.
EMBL; M11427; AAA35957.1; -; mRNA.
CCDS; CCDS7755.1; -.
PIR; A90803; HGHUA.
RefSeq; NP_000175.1; NM_000184.2.
UniGene; Hs.302145; -.
UniGene; Hs.702189; -.
PDB; 1FDH; X-ray; 2.50 A; G/H=2-147.
PDB; 4MQJ; X-ray; 1.80 A; B/D/F/H=3-147.
PDB; 4MQK; X-ray; 2.24 A; B/D/F/H=2-147.
PDBsum; 1FDH; -.
PDBsum; 4MQJ; -.
PDBsum; 4MQK; -.
ProteinModelPortal; P69892; -.
SMR; P69892; -.
BioGrid; 109298; 8.
CORUM; P69892; -.
IntAct; P69892; 9.
MINT; MINT-1200269; -.
STRING; 9606.ENSP00000338082; -.
iPTMnet; P69892; -.
PhosphoSitePlus; P69892; -.
BioMuta; HBG2; -.
DMDM; 56749861; -.
EPD; P69892; -.
MaxQB; P69892; -.
PaxDb; P69892; -.
PeptideAtlas; P69892; -.
PRIDE; P69892; -.
Ensembl; ENST00000336906; ENSP00000338082; ENSG00000196565.
Ensembl; ENST00000380259; ENSP00000369609; ENSG00000196565.
GeneID; 3048; -.
KEGG; hsa:3048; -.
UCSC; uc001maj.2; human.
CTD; 3048; -.
DisGeNET; 3048; -.
EuPathDB; HostDB:ENSG00000196565.12; -.
GeneCards; HBG2; -.
HGNC; HGNC:4832; HBG2.
HPA; CAB016143; -.
HPA; HPA043234; -.
MalaCards; HBG2; -.
MIM; 142250; gene.
MIM; 613977; phenotype.
neXtProt; NX_P69892; -.
OpenTargets; ENSG00000196565; -.
Orphanet; 280615; Hemoglobinopathy Toms River.
Orphanet; 46532; Hereditary persistence of fetal hemoglobin - beta-thalassemia.
Orphanet; 251380; Hereditary persistence of fetal hemoglobin - sickle cell disease.
PharmGKB; PA29207; -.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
GeneTree; ENSGT00760000119197; -.
HOVERGEN; HBG009709; -.
InParanoid; P69892; -.
KO; K13824; -.
PhylomeDB; P69892; -.
TreeFam; TF333268; -.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; P69892; -.
ChiTaRS; HBG2; human.
EvolutionaryTrace; P69892; -.
GeneWiki; HBG2; -.
GenomeRNAi; 3048; -.
PRO; PR:P69892; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000196565; -.
CleanEx; HS_HBG2; -.
ExpressionAtlas; P69892; baseline and differential.
Genevisible; P69892; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
CDD; cd08925; Hb-beta_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like.
InterPro; IPR002337; Haemoglobin_b.
Pfam; PF00042; Globin; 1.
PRINTS; PR00814; BETAHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disease mutation; Heme; Iron;
Metal-binding; Oxygen transport; Phosphoprotein; Polymorphism;
Reference proteome; S-nitrosylation; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:14087393,
ECO:0000269|PubMed:5554303,
ECO:0000269|Ref.7}.
CHAIN 2 147 Hemoglobin subunit gamma-2.
/FTId=PRO_0000053254.
METAL 64 64 Iron (heme distal ligand).
{ECO:0000250|UniProtKB:P80044}.
METAL 93 93 Iron (heme proximal ligand).
{ECO:0000244|PDB:1FDH,
ECO:0000244|PDB:4MQJ,
ECO:0000244|PDB:4MQK,
ECO:0000269|PubMed:881729}.
MOD_RES 2 2 N-acetylglycine; in form Hb F1.
{ECO:0000269|PubMed:5554303}.
MOD_RES 13 13 Phosphothreonine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 83 83 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 94 94 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 2 2 G -> C (in Malaysia; dbSNP:rs36006195).
{ECO:0000269|PubMed:4837284}.
/FTId=VAR_003123.
VARIANT 6 6 E -> G (in Meinohama; dbSNP:rs34263826).
{ECO:0000269|PubMed:6172403}.
/FTId=VAR_003126.
VARIANT 8 8 D -> N (in Auckland; dbSNP:rs34501593).
{ECO:0000269|PubMed:4429671}.
/FTId=VAR_003129.
VARIANT 9 9 K -> E (in Albaicin; dbSNP:rs35521813).
{ECO:0000269|PubMed:2435680}.
/FTId=VAR_020643.
VARIANT 9 9 K -> Q (in Albaicin; dbSNP:rs35521813).
{ECO:0000269|PubMed:2435680}.
/FTId=VAR_020644.
VARIANT 13 13 T -> R (in Heather; dbSNP:rs281864890).
/FTId=VAR_020645.
VARIANT 16 16 W -> R (in Catalonia; dbSNP:rs34438981).
{ECO:0000269|PubMed:1706691}.
/FTId=VAR_003131.
VARIANT 17 17 G -> R (in Melbourne; dbSNP:rs34907654).
{ECO:0000269|PubMed:836882}.
/FTId=VAR_003132.
VARIANT 18 18 K -> N (in Clamart; dbSNP:rs35621390).
{ECO:0000269|PubMed:10722115}.
/FTId=VAR_020646.
VARIANT 20 20 N -> K (in Ouled Rabah;
dbSNP:rs34018799).
{ECO:0000269|PubMed:10722115}.
/FTId=VAR_020647.
VARIANT 21 21 V -> A (in Bron; dbSNP:rs63751196).
{ECO:0000269|PubMed:16370494}.
/FTId=VAR_030496.
VARIANT 22 22 E -> K (in Saskatoon; dbSNP:rs33955330).
{ECO:0000269|PubMed:8144355}.
/FTId=VAR_003133.
VARIANT 22 22 E -> Q (in Fuchu; dbSNP:rs33955330).
{ECO:0000269|PubMed:3120456}.
/FTId=VAR_003134.
VARIANT 23 23 D -> G (in Urumqi; dbSNP:rs281864891).
{ECO:0000269|PubMed:2420748,
ECO:0000269|PubMed:8718700}.
/FTId=VAR_020648.
VARIANT 23 23 D -> V (in Granada; dbSNP:rs281864891).
{ECO:0000269|PubMed:2459082}.
/FTId=VAR_003136.
VARIANT 26 26 G -> E (in Cosenza; dbSNP:rs35687396).
{ECO:0000269|PubMed:1726095}.
/FTId=VAR_003137.
VARIANT 27 27 E -> K (in Oakland; dbSNP:rs35654328).
{ECO:0000269|PubMed:2442122}.
/FTId=VAR_003139.
VARIANT 35 35 V -> I (in Tokyo; dbSNP:rs35885783).
{ECO:0000269|PubMed:2581919}.
/FTId=VAR_003140.
VARIANT 39 39 T -> P (in Bonheiden; causes severe
hereditary hemolytic anemia;
dbSNP:rs35799058).
{ECO:0000269|PubMed:15645283}.
/FTId=VAR_030497.
VARIANT 41 41 R -> G (in Veleta; dbSNP:rs34532478).
/FTId=VAR_003144.
VARIANT 41 41 R -> K (in Austell; dbSNP:rs281864892).
{ECO:0000269|PubMed:2459083}.
/FTId=VAR_020649.
VARIANT 42 42 F -> S (in TNCY; hemoglobin Cincinnati;
dbSNP:rs34878913).
{ECO:0000269|PubMed:7741137}.
/FTId=VAR_003146.
VARIANT 45 45 S -> R (in Lodz; dbSNP:rs34017450).
{ECO:0000269|PubMed:6814491}.
/FTId=VAR_003148.
VARIANT 56 56 M -> R (in Kingston; dbSNP:rs34915311).
{ECO:0000269|PubMed:6186522}.
/FTId=VAR_003150.
VARIANT 60 60 K -> E (in Emirates; dbSNP:rs28933078).
{ECO:0000269|PubMed:7558873}.
/FTId=VAR_003151.
VARIANT 60 60 K -> Q (in Sacromonte; dbSNP:rs28933078).
{ECO:0000269|PubMed:7558873}.
/FTId=VAR_003152.
VARIANT 64 64 H -> L (in TNCY; hemoglobin M-
Circleville).
{ECO:0000269|PubMed:19065339,
ECO:0000269|Ref.3}.
/FTId=VAR_025336.
VARIANT 64 64 H -> Y (in TNCY; hemoglobin Osaka; the
presence of a tyrosine causes the
formation of a covalent link with heme
iron, so that the iron is stabilized in
the ferric form; when this occurs
methemoglobin is formed, oxygen can no
longer bind to heme and cyanosis occurs;
dbSNP:rs34474104).
{ECO:0000269|PubMed:19065339,
ECO:0000269|PubMed:2483933}.
/FTId=VAR_003154.
VARIANT 66 66 K -> N (in Clarke; dbSNP:rs34019507).
{ECO:0000269|PubMed:2442123}.
/FTId=VAR_003155.
VARIANT 67 67 K -> Q (in Brooklyn; dbSNP:rs34264694).
{ECO:0000269|PubMed:1703138}.
/FTId=VAR_003157.
VARIANT 67 67 K -> R (in Shanghai; dbSNP:rs35481866).
{ECO:0000269|PubMed:2579547}.
/FTId=VAR_003156.
VARIANT 68 68 V -> M (in TNCY; hemoglobin Toms River;
the side chain of methionine decreases
both the affinity of oxygen for binding
to the mutant hemoglobin subunit via
steric hindrance and the rate at which it
does so; the mutant methionine is
converted to aspartic acid post-
translationally; dbSNP:rs587776864).
{ECO:0000269|PubMed:21561349}.
/FTId=VAR_065950.
VARIANT 73 73 G -> R (in Minoo; dbSNP:rs281860594).
{ECO:0000269|PubMed:3120456}.
/FTId=VAR_020650.
VARIANT 76 76 I -> T (in LesVos/Waynesboro/Charlotte;
dbSNP:rs1061234).
{ECO:0000269|PubMed:1714434,
ECO:0000269|PubMed:8566966,
ECO:0000269|PubMed:8718701}.
/FTId=VAR_020651.
VARIANT 76 76 I -> V (in Coigneres; dbSNP:rs34363111).
{ECO:0000269|PubMed:11791877}.
/FTId=VAR_030498.
VARIANT 78 78 H -> R (in Kennestone; dbSNP:rs34150306).
{ECO:0000269|PubMed:6192110}.
/FTId=VAR_003162.
VARIANT 81 81 D -> N (in Marietta; dbSNP:rs63751148).
/FTId=VAR_020652.
VARIANT 93 93 H -> Y (in TNCY; hemoglobin Fort Ripley;
dbSNP:rs35103459).
{ECO:0000269|PubMed:2470017}.
/FTId=VAR_003166.
VARIANT 95 95 D -> N (in Columbus-Ga;
dbSNP:rs35812514).
{ECO:0000269|PubMed:6186636}.
/FTId=VAR_003167.
VARIANT 102 102 E -> K (in La Grange; dbSNP:rs34876238).
{ECO:0000269|PubMed:6206897}.
/FTId=VAR_003169.
VARIANT 105 105 K -> N (in Macedonia-II;
dbSNP:rs35717854).
{ECO:0000269|PubMed:7713741}.
/FTId=VAR_003170.
VARIANT 106 106 L -> H (in TNCY; hemoglobin F-Brugine/
Feldkirch; lowered affinity for oxygen).
{ECO:0000269|PubMed:24502349}.
/FTId=VAR_073159.
VARIANT 118 118 H -> R (in Malta-1; dbSNP:rs36049074).
{ECO:0000269|PubMed:5792729}.
/FTId=VAR_003171.
VARIANT 119 119 F -> L (in Calabria; dbSNP:rs35020253).
{ECO:0000269|PubMed:10722114}.
/FTId=VAR_015740.
VARIANT 121 121 K -> Q (in Caltech; dbSNP:rs34703519).
{ECO:0000269|PubMed:6186635}.
/FTId=VAR_003172.
VARIANT 122 122 E -> K (in Carlton; dbSNP:rs63750021).
{ECO:0000269|PubMed:836882}.
/FTId=VAR_020653.
VARIANT 126 126 E -> A (in Port-Royal; dbSNP:rs34997902).
{ECO:0000269|PubMed:4846278}.
/FTId=VAR_003174.
VARIANT 131 131 W -> G (in Poole; unstable;
dbSNP:rs35826780).
{ECO:0000269|PubMed:1127124}.
/FTId=VAR_003176.
VARIANT 147 147 H -> Y (in Onoda; O(2) affinity up;
dbSNP:rs34807671).
{ECO:0000269|PubMed:1703139}.
/FTId=VAR_003179.
HELIX 6 18 {ECO:0000244|PDB:4MQJ}.
HELIX 21 35 {ECO:0000244|PDB:4MQJ}.
HELIX 37 42 {ECO:0000244|PDB:4MQJ}.
HELIX 44 46 {ECO:0000244|PDB:4MQJ}.
HELIX 52 56 {ECO:0000244|PDB:4MQJ}.
HELIX 59 76 {ECO:0000244|PDB:4MQJ}.
HELIX 77 81 {ECO:0000244|PDB:4MQJ}.
HELIX 82 85 {ECO:0000244|PDB:4MQJ}.
HELIX 87 95 {ECO:0000244|PDB:4MQJ}.
HELIX 102 119 {ECO:0000244|PDB:4MQJ}.
HELIX 120 122 {ECO:0000244|PDB:4MQJ}.
HELIX 125 142 {ECO:0000244|PDB:4MQJ}.
HELIX 143 146 {ECO:0000244|PDB:4MQJ}.
SEQUENCE 147 AA; 16126 MW; 8FCDC4441B416DDE CRC64;
MGHFTEEDKA TITSLWGKVN VEDAGGETLG RLLVVYPWTQ RFFDSFGNLS SASAIMGNPK
VKAHGKKVLT SLGDAIKHLD DLKGTFAQLS ELHCDKLHVD PENFKLLGNV LVTVLAIHFG
KEFTPEVQAS WQKMVTGVAS ALSSRYH


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