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Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (IAP homolog B) (Inhibitor of apoptosis protein 2) (hIAP-2) (hIAP2) (RING finger protein 48) (RING-type E3 ubiquitin transferase BIRC2) (TNFR2-TRAF-signaling complex protein 2)

 BIRC2_HUMAN             Reviewed;         618 AA.
Q13490; B4E026; Q16516; Q4TTG0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
27-SEP-2017, entry version 185.
RecName: Full=Baculoviral IAP repeat-containing protein 2;
EC=2.3.2.27 {ECO:0000269|PubMed:18082613, ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:23453969};
AltName: Full=Cellular inhibitor of apoptosis 1;
Short=C-IAP1 {ECO:0000303|PubMed:8548810};
AltName: Full=IAP homolog B;
AltName: Full=Inhibitor of apoptosis protein 2;
Short=hIAP-2;
Short=hIAP2;
AltName: Full=RING finger protein 48;
AltName: Full=RING-type E3 ubiquitin transferase BIRC2 {ECO:0000305};
AltName: Full=TNFR2-TRAF-signaling complex protein 2;
Name=BIRC2; Synonyms=API1, MIHB, RNF48;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8548810; DOI=10.1016/0092-8674(95)90149-3;
Rothe M., Pan M.-G., Henzel W.J., Ayres T.M., Goeddel D.V.;
"The TNFR2-TRAF signaling complex contains two novel proteins related
to baculoviral inhibitor of apoptosis proteins.";
Cell 83:1243-1252(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8552191; DOI=10.1038/379349a0;
Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G.,
Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.;
"Suppression of apoptosis in mammalian cells by NAIP and a related
family of IAP genes.";
Nature 379:349-353(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=8643514; DOI=10.1073/pnas.93.10.4974;
Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.;
"Cloning and expression of apoptosis inhibitory protein homologs that
function to inhibit apoptosis and/or bind tumor necrosis factor
receptor-associated factors.";
Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-453; VAL-506 AND
SER-549.
NIEHS SNPs program;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Thymus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis, and Uterus;
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).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BIRC5/SURVIVIN.
PubMed=15665297;
Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.;
"cIAP1 Localizes to the nuclear compartment and modulates the cell
cycle.";
Cancer Res. 65:210-218(2005).
[9]
FUNCTION IN THE UBIQUITINATION OF MXD1/MAD1, AND CATALYTIC ACTIVITY.
PubMed=18082613; DOI=10.1016/j.molcel.2007.10.027;
Xu L., Zhu J., Hu X., Zhu H., Kim H.T., LaBaer J., Goldberg A.,
Yuan J.;
"c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for
Mad1.";
Mol. Cell 28:914-922(2007).
[10]
REVIEW ON FUNCTION.
PubMed=18414036; DOI=10.4161/cc.7.8.5783;
Dubrez-Daloz L., Dupoux A., Cartier J.;
"IAPs: more than just inhibitors of apoptosis proteins.";
Cell Cycle 7:1036-1046(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
REVIEW ON FUNCTION.
PubMed=20888210; DOI=10.1016/j.ceb.2010.08.025;
Lopez J., Meier P.;
"To fight or die - inhibitor of apoptosis proteins at the crossroad of
innate immunity and death.";
Curr. Opin. Cell Biol. 22:872-881(2010).
[14]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION
PATHWAY, AND CATALYTIC ACTIVITY.
PubMed=21145488; DOI=10.1016/j.molcel.2010.11.011;
Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J.,
Ditzel M., Meier P.;
"Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3
ligases.";
Mol. Cell 40:810-822(2010).
[15]
REVIEW ON FUNCTION.
PubMed=20651737; DOI=10.1038/nrc2889;
Gyrd-Hansen M., Meier P.;
"IAPs: from caspase inhibitors to modulators of NF-kappaB,
inflammation and cancer.";
Nat. Rev. Cancer 10:561-574(2010).
[16]
REVIEW ON FUNCTION.
PubMed=21447281;
Damgaard R.B., Gyrd-Hansen M.;
"Inhibitor of apoptosis (IAP) proteins in regulation of inflammation
and innate immunity.";
Discov. Med. 11:221-231(2011).
[17]
FUNCTION, INTERACTION WITH E2F1 AND TRAF2, AND SUBCELLULAR LOCATION.
PubMed=21653699; DOI=10.1074/jbc.M110.191239;
Cartier J., Berthelet J., Marivin A., Gemble S., Edmond V.,
Plenchette S., Lagrange B., Hammann A., Dupoux A., Delva L., Eymin B.,
Solary E., Dubrez L.;
"Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1
transcription factor-mediated control of cyclin transcription.";
J. Biol. Chem. 286:26406-26417(2011).
[18]
ENZYME REGULATION, AND INTERACTION WITH USP19.
PubMed=21849505; DOI=10.1074/jbc.M111.282020;
Mei Y., Hahn A.A., Hu S., Yang X.;
"The USP19 deubiquitinase regulates the stability of c-IAP1 and c-
IAP2.";
J. Biol. Chem. 286:35380-35387(2011).
[19]
FUNCTION IN THE UBIQUITINATION OF RIPK1; RIPK2; RIPK3 AND RIPK4,
INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4, AND CATALYTIC
ACTIVITY.
PubMed=21931591; DOI=10.1371/journal.pone.0022356;
Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R.,
De Medts J., Gevaert K., Declercq W., Vandenabeele P.;
"cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin
chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).";
PLoS ONE 6:E22356-E22356(2011).
[20]
REVIEW ON FUNCTION.
PubMed=22095281; DOI=10.1038/cdd.2011.163;
Darding M., Meier P.;
"IAPs: guardians of RIPK1.";
Cell Death Differ. 19:58-66(2012).
[21]
FUNCTION IN IKBKE UBIQUITINATION, AND CATALYTIC ACTIVITY.
PubMed=23453969; DOI=10.1016/j.celrep.2013.01.031;
Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.;
"IKKepsilon-mediated tumorigenesis requires K63-linked
polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase
complex.";
Cell Rep. 3:724-733(2013).
[22]
INTERACTION WITH HSP90AB1.
PubMed=25486457; DOI=10.1016/j.bbamcr.2014.11.026;
Synoradzki K., Bieganowski P.;
"Middle domain of human Hsp90 isoforms differentially binds Aha1 in
human cells and alters Hsp90 activity in yeast.";
Biochim. Biophys. Acta 1853:445-452(2015).
[23]
INTERACTION WITH UBXN1.
PubMed=25681446; DOI=10.1074/jbc.M114.631689;
Wang Y.B., Tan B., Mu R., Chang Y., Wu M., Tu H.Q., Zhang Y.C.,
Guo S.S., Qin X.H., Li T., Li W.H., Li A.L., Zhang X.M., Li H.Y.;
"Ubiquitin-associated domain-containing ubiquitin regulatory X (UBX)
protein UBXN1 is a negative regulator of nuclear factor kappaB (NF-
kappaB) signaling.";
J. Biol. Chem. 290:10395-10405(2015).
[24]
STRUCTURE BY NMR OF 266-363.
PubMed=10404221; DOI=10.1038/10701;
Hinds M.G., Norton R.S., Vaux D.L., Day C.L.;
"Solution structure of a baculoviral inhibitor of apoptosis (IAP)
repeat.";
Nat. Struct. Biol. 6:648-651(1999).
[25]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 260-352 IN COMPLEXES WITH
ZINC IONS; DIABLO AND CASP9 PEPTIDES, AND SUBUNIT.
PubMed=19153467; DOI=10.1107/S0907444908039243;
Kulathila R., Vash B., Sage D., Cornell-Kennon S., Wright K.,
Koehn J., Stams T., Clark K., Price A.;
"The structure of the BIR3 domain of cIAP1 in complex with the N-
terminal peptides of SMAC and caspase-9.";
Acta Crystallogr. D 65:58-66(2009).
[26]
STRUCTURE BY NMR OF 435-562, DOMAIN CARD, AND ENZYME REGULATION.
PubMed=21549626; DOI=10.1016/j.molcel.2011.04.008;
Lopez J., John S.W., Tenev T., Rautureau G.J., Hinds M.G.,
Francalanci F., Wilson R., Broemer M., Santoro M.M., Day C.L.,
Meier P.;
"CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses
cell proliferation and migration.";
Mol. Cell 42:569-583(2011).
-!- FUNCTION: Multi-functional protein which regulates not only
caspases and apoptosis, but also modulates inflammatory signaling
and immunity, mitogenic kinase signaling, and cell proliferation,
as well as cell invasion and metastasis. Acts as an E3 ubiquitin-
protein ligase regulating NF-kappa-B signaling and regulates both
canonical and non-canonical NF-kappa-B signaling by acting in
opposite directions: acts as a positive regulator of the canonical
pathway and suppresses constitutive activation of non-canonical
NF-kappa-B signaling. The target proteins for its E3 ubiquitin-
protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4,
CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1,
IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3
ubiquitin-protein ligase of the NEDD8 conjugation pathway,
targeting effector caspases for neddylation and inactivation. Acts
as an important regulator of innate immune signaling via
regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs)
and RIG-I like receptors (RLRs), collectively referred to as
pattern recognition receptors (PRRs). Protects cells from
spontaneous formation of the ripoptosome, a large multi-protein
complex that has the capability to kill cancer cells in a caspase-
dependent and caspase-independent manner. Suppresses ripoptosome
formation by ubiquitinating RIPK1 and CASP8. Can stimulate the
transcriptional activity of E2F1. Plays a role in the modulation
of the cell cycle. {ECO:0000269|PubMed:15665297,
ECO:0000269|PubMed:18082613, ECO:0000269|PubMed:21145488,
ECO:0000269|PubMed:21653699, ECO:0000269|PubMed:21931591,
ECO:0000269|PubMed:23453969}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:18082613,
ECO:0000269|PubMed:21145488, ECO:0000269|PubMed:21931591,
ECO:0000269|PubMed:23453969}.
-!- ENZYME REGULATION: The CARD domain inhibits the activation of E3
ubiquitin ligase activity by preventing RING domain dimerization
and E2 ubiquitin donor binding and activation. The CARD domain-
mediated autoinhibition of the E3 ubiquitin-protein ligase
activity suppresses cell proliferation and migration. USP19
regulates the stability of BIRC2/c-IAP1 by preventing its
ubiquitination. {ECO:0000269|PubMed:21549626,
ECO:0000269|PubMed:21849505}.
-!- SUBUNIT: Interacts with DIABLO/SMAC and with PRSS25; these
interactions inhibit apoptotic suppressor activity. Interacts with
CASP9. Interacts (via BIR domains) with TRAF2; the interaction is
required for IKBKE ubiquitination. Interacts with E2F1, RIPK1,
RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19. Interacts with
HSP90AB1 (PubMed:25486457). Interacts with UBXN1
(PubMed:25681446). {ECO:0000269|PubMed:15665297,
ECO:0000269|PubMed:19153467, ECO:0000269|PubMed:21653699,
ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:21931591,
ECO:0000269|PubMed:25486457, ECO:0000269|PubMed:25681446}.
-!- INTERACTION:
Q96CA5:BIRC7; NbExp=3; IntAct=EBI-514538, EBI-517623;
Q3E793:BOL1 (xeno); NbExp=3; IntAct=EBI-514538, EBI-2344281;
Q9Y3E2:BOLA1; NbExp=5; IntAct=EBI-514538, EBI-1049556;
P55210:CASP7; NbExp=2; IntAct=EBI-514538, EBI-523958;
P55211:CASP9; NbExp=9; IntAct=EBI-514538, EBI-516799;
Q9NR28:DIABLO; NbExp=6; IntAct=EBI-514538, EBI-517508;
Q96CJ1:EAF2; NbExp=3; IntAct=EBI-514538, EBI-1245604;
Q9NQT4:EXOSC5; NbExp=5; IntAct=EBI-514538, EBI-371876;
Q96CN9:GCC1; NbExp=5; IntAct=EBI-514538, EBI-746252;
P32502:GCD7 (xeno); NbExp=3; IntAct=EBI-514538, EBI-6260;
P14136:GFAP; NbExp=3; IntAct=EBI-514538, EBI-744302;
P40325:HUA1 (xeno); NbExp=3; IntAct=EBI-514538, EBI-23614;
P08949:NMB; NbExp=3; IntAct=EBI-514538, EBI-7964376;
P08949-2:NMB; NbExp=5; IntAct=EBI-514538, EBI-12302085;
Q96FW1:OTUB1; NbExp=3; IntAct=EBI-514538, EBI-1058491;
Q8N3J5:PPM1K; NbExp=5; IntAct=EBI-514538, EBI-3923368;
P63000:RAC1; NbExp=2; IntAct=EBI-514538, EBI-413628;
P38339:RGD1 (xeno); NbExp=3; IntAct=EBI-514538, EBI-15065;
Q13546:RIPK1; NbExp=3; IntAct=EBI-514538, EBI-358507;
O43353:RIPK2; NbExp=3; IntAct=EBI-514538, EBI-358522;
Q9Y572:RIPK3; NbExp=3; IntAct=EBI-514538, EBI-298250;
P57078:RIPK4; NbExp=3; IntAct=EBI-514538, EBI-4422308;
Q9NP84:TNFRSF12A; NbExp=2; IntAct=EBI-514538, EBI-2851995;
Q12933:TRAF2; NbExp=14; IntAct=EBI-514538, EBI-355744;
Q9BZW7:TSGA10; NbExp=4; IntAct=EBI-514538, EBI-744794;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-514538, EBI-741158;
Q01976:YSA1 (xeno); NbExp=3; IntAct=EBI-514538, EBI-2344265;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Agents that induce
either the extrinsic or intrinsic apoptotic pathways promote its
redistribution from the nuclear compartment to the cytoplasmic
compartment. Associated with the midbody in telophase cells, and
found diffusely in the nucleus of interphase cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13490-1; Sequence=Displayed;
Name=2;
IsoId=Q13490-2; Sequence=VSP_045314;
-!- TISSUE SPECIFICITY: Present in many fetal and adult tissues.
Mainly expressed in adult skeletal muscle, thymus, testis, ovary,
and pancreas, low or absent in brain and peripheral blood
leukocytes.
-!- DOMAIN: The BIR domains mediate nuclear localization.
{ECO:0000269|PubMed:21549626}.
-!- DOMAIN: The CARD domain is necessary to stabilize the protein and
inhibit the activation of E3 ubiquitin-protein ligase activity of
BIRC2/c-IAP1 by preventing RING domain dimerization and E2
ubiquitin donor binding and activation.
{ECO:0000269|PubMed:21549626}.
-!- PTM: Auto-ubiquitinated and degraded by the proteasome in
apoptotic cells.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/birc2/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BIRC2ID795ch11q22.html";
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EMBL; L49431; AAC41942.1; -; mRNA.
EMBL; U45879; AAC50372.1; -; mRNA.
EMBL; U37547; AAC50508.1; -; mRNA.
EMBL; AK303197; BAG64288.1; -; mRNA.
EMBL; AP000942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DQ068066; AAY46158.1; -; Genomic_DNA.
EMBL; BC016174; AAH16174.1; -; mRNA.
EMBL; BC028578; AAH28578.1; -; mRNA.
CCDS; CCDS58169.1; -. [Q13490-2]
CCDS; CCDS8316.1; -. [Q13490-1]
PIR; S68450; S68450.
RefSeq; NP_001157.1; NM_001166.4. [Q13490-1]
RefSeq; NP_001243092.1; NM_001256163.1. [Q13490-1]
RefSeq; NP_001243095.1; NM_001256166.1. [Q13490-2]
UniGene; Hs.696238; -.
UniGene; Hs.731943; -.
PDB; 1QBH; NMR; -; A=266-363.
PDB; 2L9M; NMR; -; A=435-562.
PDB; 3D9T; X-ray; 1.50 A; A/B=260-352.
PDB; 3D9U; X-ray; 2.30 A; A=260-352.
PDB; 3M1D; X-ray; 2.00 A; A/B=40-119.
PDB; 3MUP; X-ray; 2.60 A; A/B/C/D=251-363.
PDB; 3OZ1; X-ray; 3.00 A; A/B/C/D=251-363.
PDB; 3T6P; X-ray; 1.90 A; A=265-618.
PDB; 3UW4; X-ray; 1.79 A; A=266-343.
PDB; 4EB9; X-ray; 2.60 A; A/B/C/D=251-363.
PDB; 4HY4; X-ray; 1.25 A; A/B=260-352.
PDB; 4HY5; X-ray; 1.75 A; A/B=260-352.
PDB; 4KMN; X-ray; 1.52 A; A=260-357.
PDB; 4LGE; X-ray; 1.55 A; A/B=260-352.
PDB; 4LGU; X-ray; 2.00 A; A/B=260-352.
PDB; 4MTI; X-ray; 2.15 A; A/B=260-352.
PDB; 4MU7; X-ray; 1.79 A; A/B=260-352.
PDB; 5M6N; X-ray; 1.80 A; A/B=266-363.
PDBsum; 1QBH; -.
PDBsum; 2L9M; -.
PDBsum; 3D9T; -.
PDBsum; 3D9U; -.
PDBsum; 3M1D; -.
PDBsum; 3MUP; -.
PDBsum; 3OZ1; -.
PDBsum; 3T6P; -.
PDBsum; 3UW4; -.
PDBsum; 4EB9; -.
PDBsum; 4HY4; -.
PDBsum; 4HY5; -.
PDBsum; 4KMN; -.
PDBsum; 4LGE; -.
PDBsum; 4LGU; -.
PDBsum; 4MTI; -.
PDBsum; 4MU7; -.
PDBsum; 5M6N; -.
ProteinModelPortal; Q13490; -.
SMR; Q13490; -.
BioGrid; 106826; 153.
CORUM; Q13490; -.
DIP; DIP-33485N; -.
IntAct; Q13490; 79.
MINT; MINT-216174; -.
STRING; 9606.ENSP00000227758; -.
BindingDB; Q13490; -.
ChEMBL; CHEMBL5462; -.
GuidetoPHARMACOLOGY; 2791; -.
MEROPS; I32.007; -.
iPTMnet; Q13490; -.
PhosphoSitePlus; Q13490; -.
BioMuta; BIRC2; -.
DMDM; 2497238; -.
EPD; Q13490; -.
MaxQB; Q13490; -.
PaxDb; Q13490; -.
PeptideAtlas; Q13490; -.
PRIDE; Q13490; -.
DNASU; 329; -.
Ensembl; ENST00000227758; ENSP00000227758; ENSG00000110330. [Q13490-1]
Ensembl; ENST00000530675; ENSP00000431723; ENSG00000110330. [Q13490-2]
Ensembl; ENST00000613397; ENSP00000477613; ENSG00000110330. [Q13490-1]
GeneID; 329; -.
KEGG; hsa:329; -.
UCSC; uc001pgy.5; human. [Q13490-1]
CTD; 329; -.
DisGeNET; 329; -.
EuPathDB; HostDB:ENSG00000110330.8; -.
GeneCards; BIRC2; -.
HGNC; HGNC:590; BIRC2.
HPA; CAB020661; -.
HPA; HPA005513; -.
MIM; 601712; gene.
neXtProt; NX_Q13490; -.
OpenTargets; ENSG00000110330; -.
PharmGKB; PA25359; -.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
GeneTree; ENSGT00500000044782; -.
HOGENOM; HOG000232059; -.
HOVERGEN; HBG004848; -.
InParanoid; Q13490; -.
KO; K16060; -.
OMA; CSMVLAP; -.
OrthoDB; EOG091G0CXH; -.
PhylomeDB; Q13490; -.
TreeFam; TF105356; -.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
SignaLink; Q13490; -.
SIGNOR; Q13490; -.
ChiTaRS; BIRC2; human.
EvolutionaryTrace; Q13490; -.
GeneWiki; BIRC2; -.
GenomeRNAi; 329; -.
PMAP-CutDB; Q13490; -.
PRO; PR:Q13490; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110330; -.
CleanEx; HS_BIRC2; -.
ExpressionAtlas; Q13490; baseline and differential.
Genevisible; Q13490; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0001741; C:XY body; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0098770; F:FBXO family protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
GO; GO:0016740; F:transferase activity; EXP:Reactome.
GO; GO:0043130; F:ubiquitin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0060546; P:negative regulation of necroptotic process; IBA:GO_Central.
GO; GO:1902443; P:negative regulation of ripoptosome assembly involved in necroptotic process; IEA:Ensembl.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:UniProtKB.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:1902524; P:positive regulation of protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:1902527; P:positive regulation of protein monoubiquitination; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; TAS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; TAS:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
GO; GO:0060544; P:regulation of necroptotic process; IMP:UniProtKB.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0070424; P:regulation of nucleotide-binding oligomerization domain containing signaling pathway; TAS:UniProtKB.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0039535; P:regulation of RIG-I signaling pathway; TAS:UniProtKB.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; TAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
CDD; cd00022; BIR; 3.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR028795; C-IAP1.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR10044:SF150; PTHR10044:SF150; 1.
Pfam; PF00653; BIR; 3.
Pfam; PF00619; CARD; 1.
SMART; SM00238; BIR; 3.
SMART; SM00114; CARD; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS01282; BIR_REPEAT_1; 3.
PROSITE; PS50143; BIR_REPEAT_2; 3.
PROSITE; PS50209; CARD; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Metal-binding; Nucleus; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 618 Baculoviral IAP repeat-containing protein
2.
/FTId=PRO_0000122347.
REPEAT 46 113 BIR 1.
REPEAT 184 250 BIR 2.
REPEAT 269 336 BIR 3.
DOMAIN 453 543 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ZN_FING 571 606 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
METAL 306 306 Zinc.
METAL 309 309 Zinc.
METAL 326 326 Zinc.
METAL 333 333 Zinc.
VAR_SEQ 1 49 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045314.
VARIANT 453 453 M -> I (in dbSNP:rs34749508).
/FTId=VAR_049535.
VARIANT 453 453 M -> V (in dbSNP:rs370745983).
{ECO:0000269|Ref.4}.
/FTId=VAR_025016.
VARIANT 506 506 A -> V (in dbSNP:rs34510872).
{ECO:0000269|Ref.4}.
/FTId=VAR_025017.
VARIANT 549 549 P -> S (in dbSNP:rs35494784).
{ECO:0000269|Ref.4}.
/FTId=VAR_025018.
CONFLICT 157 157 S -> P (in Ref. 2; AAC50372).
{ECO:0000305}.
CONFLICT 308 308 C -> G (in Ref. 2; AAC50372).
{ECO:0000305}.
CONFLICT 414 414 Q -> L (in Ref. 2; AAC50372).
{ECO:0000305}.
CONFLICT 514 514 L -> W (in Ref. 2; AAC50372).
{ECO:0000305}.
HELIX 43 51 {ECO:0000244|PDB:3M1D}.
HELIX 52 55 {ECO:0000244|PDB:3M1D}.
HELIX 64 69 {ECO:0000244|PDB:3M1D}.
STRAND 72 74 {ECO:0000244|PDB:3M1D}.
STRAND 81 83 {ECO:0000244|PDB:3M1D}.
TURN 84 86 {ECO:0000244|PDB:3M1D}.
HELIX 99 106 {ECO:0000244|PDB:3M1D}.
HELIX 111 117 {ECO:0000244|PDB:3M1D}.
HELIX 264 266 {ECO:0000244|PDB:4HY4}.
HELIX 269 274 {ECO:0000244|PDB:4HY4}.
TURN 275 278 {ECO:0000244|PDB:4HY4}.
STRAND 279 282 {ECO:0000244|PDB:1QBH}.
STRAND 283 285 {ECO:0000244|PDB:4HY4}.
HELIX 287 292 {ECO:0000244|PDB:4HY4}.
STRAND 295 297 {ECO:0000244|PDB:4HY4}.
STRAND 304 306 {ECO:0000244|PDB:4HY4}.
TURN 307 309 {ECO:0000244|PDB:4HY4}.
STRAND 312 314 {ECO:0000244|PDB:3D9T}.
HELIX 322 329 {ECO:0000244|PDB:4HY4}.
HELIX 334 340 {ECO:0000244|PDB:4HY4}.
HELIX 342 348 {ECO:0000244|PDB:4HY4}.
HELIX 355 361 {ECO:0000244|PDB:3T6P}.
HELIX 389 391 {ECO:0000244|PDB:3T6P}.
HELIX 394 401 {ECO:0000244|PDB:3T6P}.
HELIX 406 420 {ECO:0000244|PDB:3T6P}.
HELIX 427 450 {ECO:0000244|PDB:3T6P}.
TURN 451 453 {ECO:0000244|PDB:2L9M}.
HELIX 456 463 {ECO:0000244|PDB:3T6P}.
HELIX 465 471 {ECO:0000244|PDB:3T6P}.
HELIX 476 484 {ECO:0000244|PDB:3T6P}.
STRAND 485 487 {ECO:0000244|PDB:2L9M}.
HELIX 490 497 {ECO:0000244|PDB:3T6P}.
HELIX 502 516 {ECO:0000244|PDB:3T6P}.
HELIX 518 531 {ECO:0000244|PDB:3T6P}.
HELIX 533 540 {ECO:0000244|PDB:3T6P}.
HELIX 553 555 {ECO:0000244|PDB:3T6P}.
HELIX 558 566 {ECO:0000244|PDB:3T6P}.
TURN 572 574 {ECO:0000244|PDB:3T6P}.
STRAND 575 578 {ECO:0000244|PDB:3T6P}.
STRAND 581 584 {ECO:0000244|PDB:3T6P}.
STRAND 589 591 {ECO:0000244|PDB:3T6P}.
TURN 593 595 {ECO:0000244|PDB:3T6P}.
HELIX 596 598 {ECO:0000244|PDB:3T6P}.
TURN 603 605 {ECO:0000244|PDB:3T6P}.
STRAND 611 614 {ECO:0000244|PDB:3T6P}.
SEQUENCE 618 AA; 69900 MW; C1778D328063586D CRC64;
MHKTASQRLF PGPSYQNIKS IMEDSTILSD WTNSNKQKMK YDFSCELYRM STYSTFPAGV
PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKLGDSPI QKHKQLYPSC SFIQNLVSAS
LGSTSKNTSP MRNSFAHSLS PTLEHSSLFS GSYSSLSPNP LNSRAVEDIS SSRTNPYSYA
MSTEEARFLT YHMWPLTFLS PSELARAGFY YIGPGDRVAC FACGGKLSNW EPKDDAMSEH
RRHFPNCPFL ENSLETLRFS ISNLSMQTHA ARMRTFMYWP SSVPVQPEQL ASAGFYYVGR
NDDVKCFCCD GGLRCWESGD DPWVEHAKWF PRCEFLIRMK GQEFVDEIQG RYPHLLEQLL
STSDTTGEEN ADPPIIHFGP GESSSEDAVM MNTPVVKSAL EMGFNRDLVK QTVQSKILTT
GENYKTVNDI VSALLNAEDE KREEEKEKQA EEMASDDLSL IRKNRMALFQ QLTCVLPILD
NLLKANVINK QEHDIIKQKT QIPLQARELI DTILVKGNAA ANIFKNCLKE IDSTLYKNLF
VDKNMKYIPT EDVSGLSLEE QLRRLQEERT CKVCMDKEVS VVFIPCGHLV VCQECAPSLR
KCPICRGIIK GTVRTFLS


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