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Induced myeloid leukemia cell differentiation protein Mcl-1 homolog (Bcl-2-related protein EAT/mcl1)

 MCL1_MOUSE              Reviewed;         331 AA.
P97287; D2K6L9; Q3TUS0; Q792P0; Q9CRI4;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 3.
28-FEB-2018, entry version 159.
RecName: Full=Induced myeloid leukemia cell differentiation protein Mcl-1 homolog;
AltName: Full=Bcl-2-related protein EAT/mcl1;
Name=Mcl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
TISSUE=Fetus;
PubMed=9655929; DOI=10.1016/S0167-4781(98)00059-1;
Okita H., Umezawa A., Suzuki A., Hata J.;
"Up-regulated expression of murine Mcl1/EAT, a bcl-2 related gene, in
the early stage of differentiation of murine embryonal carcinoma cells
and embryonic stem cells.";
Biochim. Biophys. Acta 1398:335-341(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR
LOCALIZATION.
STRAIN=C57BL/6J;
PubMed=19919825; DOI=10.1016/j.bbrc.2009.11.086;
Kojima S., Hyakutake A., Koshikawa N., Nakagawara A., Takenaga K.;
"MCL-1V, a novel mouse antiapoptotic MCL-1 variant, generated by RNA
splicing at a non-canonical splicing pair.";
Biochem. Biophys. Res. Commun. 391:492-497(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65, AND INDUCTION.
STRAIN=129/SvJ;
PubMed=9671497; DOI=10.1128/MCB.18.8.4883;
Chao J.-R., Wang J.-M., Lee S.-F., Peng H.-W., Lin Y.-H., Chou C.-H.,
Li J.-C., Huang H.-M., Chou C.-K., Kuo M.-L., Yen J.J.-Y.,
Yang-Yen H.-F.;
"Mcl-1 is an immediate-early gene activated by the granulocyte-
macrophage colony-stimulating factor (GM-CSF) signaling pathway and is
one component of the GM-CSF viability response.";
Mol. Cell. Biol. 18:4883-4898(1998).
[7]
FUNCTION AS INHIBITOR OF APOPTOSIS, PHOSPHORYLATION AT SER-140 BY
GSK3-ALPHA AND GSK3-BETA, AND INTERACTION WITH BCL2L11.
PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
"Glycogen synthase kinase-3 regulates mitochondrial outer membrane
permeabilization and apoptosis by destabilization of MCL-1.";
Mol. Cell 21:749-760(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH HIF3A.
PubMed=21546903; DOI=10.1038/cdd.2011.47;
Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
Fukumura H., Sogawa K.;
"Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a
negative regulator of HIF-1, through binding to pro-survival Bcl-2
family proteins.";
Cell Death Differ. 18:1711-1725(2011).
[10]
INTERACTION WITH BCL2L11.
PubMed=27013495; DOI=10.15252/embr.201541392;
Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
"The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and
enhances apoptosis.";
EMBO Rep. 17:724-738(2016).
[11]
STRUCTURE BY NMR OF 152-308, AND INTERACTION WITH BCL2L11; BMF AND
PMAIP.
PubMed=15550399; DOI=10.1074/jbc.M411434200;
Day C.L., Chen L., Richardson S.J., Harrison P.J., Huang D.C.S.,
Hinds M.G.;
"Solution structure of prosurvival Mcl-1 and characterization of its
binding by proapoptotic BH3-only ligands.";
J. Biol. Chem. 280:4738-4744(2005).
[12]
STRUCTURE BY NMR OF 148-308 IN COMPLEXES WITH WITH BBC3 AND PMAIP1.
PubMed=18589438; DOI=10.1016/j.jmb.2008.05.071;
Day C.L., Smits C., Fan F.C., Lee E.F., Fairlie W.D., Hinds M.G.;
"Structure of the BH3 domains from the p53-inducible BH3-only proteins
Noxa and Puma in complex with Mcl-1.";
J. Mol. Biol. 380:958-971(2008).
-!- FUNCTION: Involved in the regulation of apoptosis versus cell
survival, and in the maintenance of viability but not of
proliferation. Mediates its effects by interactions with a number
of other regulators of apoptosis. Isoform 2 has antiapoptotic
activity. {ECO:0000269|PubMed:16543145,
ECO:0000269|PubMed:19919825}.
-!- SUBUNIT: Interacts with HIF3A isoform 2 (via C-terminus domain)
(PubMed:21546903). Interacts with BAD, BOK, BIK, BAX, BAK1, and
TPT1. Interacts with BBC3, BMF and PMAIP1 (PubMed:15550399,
PubMed:18589438). Interacts with BOP. Interacts with BCL2L11; this
interaction may sequester BCL2L11 and prevent its pro-apoptotic
activity (PubMed:16543145, PubMed:27013495, PubMed:15550399).
{ECO:0000269|PubMed:15550399, ECO:0000269|PubMed:16543145,
ECO:0000269|PubMed:18589438, ECO:0000269|PubMed:21546903,
ECO:0000269|PubMed:27013495}.
-!- INTERACTION:
Q16611:BAK1 (xeno); NbExp=3; IntAct=EBI-707292, EBI-519866;
Q07812:BAX (xeno); NbExp=2; IntAct=EBI-707292, EBI-516580;
Q9BXH1:BBC3 (xeno); NbExp=5; IntAct=EBI-707292, EBI-519884;
O43521:BCL2L11 (xeno); NbExp=7; IntAct=EBI-707292, EBI-526406;
O54918:Bcl2l11; NbExp=4; IntAct=EBI-707292, EBI-526067;
Q9JM54:Pmaip1; NbExp=6; IntAct=EBI-707292, EBI-709183;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Mitochondrion.
Nucleus, nucleoplasm {ECO:0000250}. Note=Cytoplasmic, associated
with mitochondria.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P97287-1; Sequence=Displayed;
Name=2; Synonyms=Mck-1V;
IsoId=P97287-2; Sequence=VSP_046443;
Note=This isoform is more stable than isoform 1 in cells
undergoing apoptosis.;
-!- INDUCTION: Up-regulated by IL3 and CSF2. Up-regulated in murine
embryonal carcinoma cells in response to retinoic acid treatment.
Levels reach a maximum after 4 hours, are decreased after 8 hours
and are back to maximum after 12 hours. Levels are decreased after
24 hours and back to basal levels after 48 hours. Expression
remains constant in retinoic acid-treated embryonic stem cells.
{ECO:0000269|PubMed:9655929, ECO:0000269|PubMed:9671497}.
-!- PTM: Cleaved by CASP3 during apoptosis, yielding a pro-apoptotic
C-terminal fragment. {ECO:0000250}.
-!- PTM: Rapidly degraded in the absence of phosphorylation in the
PEST region. {ECO:0000250}.
-!- PTM: Phosphorylated on Ser-140, by GSK3, in response to
IL3/interleukin-3 withdrawal. Phosphorylation at Ser-140 induces
ubiquitination and proteasomal degradation, abrogating the anti-
apoptotic activity. Treatment with taxol or okadaic acid induces
phosphorylation on additional sites.
{ECO:0000269|PubMed:16543145}.
-!- PTM: Ubiquitinated. Ubiquitination is induced by phosphorylation
at Ser-140 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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EMBL; U35623; AAC31790.1; -; mRNA.
EMBL; GU182318; ACZ54910.1; -; mRNA.
EMBL; AK010424; BAB26927.1; -; mRNA.
EMBL; AK159504; BAE35137.1; -; mRNA.
EMBL; AK160594; BAE35901.1; -; mRNA.
EMBL; AC092479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FO082281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003839; AAH03839.1; -; mRNA.
EMBL; BC005427; AAH05427.1; -; mRNA.
EMBL; BC021638; AAH21638.1; -; mRNA.
EMBL; AF063886; AAC27929.1; -; Genomic_DNA.
CCDS; CCDS57236.1; -. [P97287-1]
RefSeq; NP_032588.1; NM_008562.3. [P97287-1]
UniGene; Mm.1639; -.
PDB; 1WSX; NMR; -; A=152-308.
PDB; 2JM6; NMR; -; B=152-308.
PDB; 2NL9; X-ray; 1.55 A; A=152-189.
PDB; 2NLA; X-ray; 2.80 A; A=152-189.
PDB; 2ROC; NMR; -; A=152-308.
PDB; 2ROD; NMR; -; A=152-308.
PDB; 3D7V; X-ray; 2.03 A; A=152-189.
PDB; 3IO9; X-ray; 2.40 A; A=152-189.
PDB; 4BPI; X-ray; 1.98 A; A=152-189.
PDB; 4BPJ; X-ray; 1.60 A; A=152-189.
PDB; 4G35; X-ray; 2.00 A; A=152-308.
PDB; 5KU9; X-ray; 2.20 A; A/B=152-308.
PDB; 5MES; X-ray; 2.24 A; A=153-221.
PDB; 5MEV; X-ray; 2.94 A; A=153-221.
PDB; 5VX2; X-ray; 1.85 A; A/C=152-221.
PDBsum; 1WSX; -.
PDBsum; 2JM6; -.
PDBsum; 2NL9; -.
PDBsum; 2NLA; -.
PDBsum; 2ROC; -.
PDBsum; 2ROD; -.
PDBsum; 3D7V; -.
PDBsum; 3IO9; -.
PDBsum; 4BPI; -.
PDBsum; 4BPJ; -.
PDBsum; 4G35; -.
PDBsum; 5KU9; -.
PDBsum; 5MES; -.
PDBsum; 5MEV; -.
PDBsum; 5VX2; -.
ProteinModelPortal; P97287; -.
SMR; P97287; -.
BioGrid; 201344; 15.
CORUM; P97287; -.
DIP; DIP-33343N; -.
ELM; P97287; -.
IntAct; P97287; 14.
MINT; P97287; -.
STRING; 10090.ENSMUSP00000044048; -.
BindingDB; P97287; -.
ChEMBL; CHEMBL5768; -.
iPTMnet; P97287; -.
PhosphoSitePlus; P97287; -.
EPD; P97287; -.
MaxQB; P97287; -.
PaxDb; P97287; -.
PeptideAtlas; P97287; -.
PRIDE; P97287; -.
Ensembl; ENSMUST00000037947; ENSMUSP00000044048; ENSMUSG00000038612. [P97287-1]
Ensembl; ENSMUST00000178686; ENSMUSP00000135915; ENSMUSG00000038612. [P97287-2]
GeneID; 17210; -.
KEGG; mmu:17210; -.
UCSC; uc029unp.1; mouse. [P97287-1]
CTD; 4170; -.
MGI; MGI:101769; Mcl1.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00510000048923; -.
HOGENOM; HOG000232116; -.
HOVERGEN; HBG003527; -.
InParanoid; P97287; -.
KO; K02539; -.
OMA; AKDTKPM; -.
OrthoDB; EOG091G0E6Q; -.
PhylomeDB; P97287; -.
TreeFam; TF315834; -.
ChiTaRS; Mcl1; mouse.
EvolutionaryTrace; P97287; -.
PRO; PR:P97287; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000038612; -.
CleanEx; MM_MCL1; -.
Genevisible; P97287; MM.
GO; GO:0097136; C:Bcl-2 family protein complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0051434; F:BH3 domain binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISO:MGI.
GO; GO:0034097; P:response to cytokine; ISO:MGI.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR013281; Apop_reg_Mc1.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF46; PTHR11256:SF46; 1.
Pfam; PF00452; Bcl-2; 1.
PRINTS; PR01866; APOPREGMCL1.
PRINTS; PR01862; BCL2FAMILY.
SUPFAM; SSF56854; SSF56854; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Cytoplasm; Developmental protein; Differentiation; Isopeptide bond;
Membrane; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 331 Induced myeloid leukemia cell
differentiation protein Mcl-1 homolog.
/FTId=PRO_0000143081.
TRANSMEM 308 330 Helical. {ECO:0000255}.
REGION 85 156 PEST-like. {ECO:0000250}.
MOTIF 190 204 BH3.
MOTIF 234 253 BH1.
MOTIF 285 300 BH2.
COMPBIAS 149 152 Poly-Glu.
SITE 108 109 Cleavage; by caspase-3. {ECO:0000250}.
SITE 138 139 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q07820}.
MOD_RES 140 140 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0000269|PubMed:16543145}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:Q07820}.
MOD_RES 144 144 Phosphothreonine; by MAPK.
{ECO:0000250|UniProtKB:Q07820}.
CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q07820}.
CROSSLNK 175 175 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q07820}.
CROSSLNK 178 178 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q07820}.
VAR_SEQ 18 63 Missing (in isoform 2).
{ECO:0000303|PubMed:19919825}.
/FTId=VSP_046443.
HELIX 154 172 {ECO:0000244|PDB:2NL9}.
STRAND 181 183 {ECO:0000244|PDB:5VX2}.
HELIX 185 202 {ECO:0000244|PDB:2NL9}.
HELIX 206 216 {ECO:0000244|PDB:2NL9}.
TURN 221 223 {ECO:0000244|PDB:1WSX}.
HELIX 227 234 {ECO:0000244|PDB:4G35}.
TURN 235 237 {ECO:0000244|PDB:4G35}.
HELIX 242 261 {ECO:0000244|PDB:4G35}.
HELIX 265 267 {ECO:0000244|PDB:4G35}.
HELIX 268 289 {ECO:0000244|PDB:4G35}.
HELIX 292 300 {ECO:0000244|PDB:4G35}.
TURN 301 303 {ECO:0000244|PDB:2ROC}.
SEQUENCE 331 AA; 35217 MW; E4FD369DB0EC6723 CRC64;
MFGLRRNAVI GLNLYCGGAS LGAGGGSPAG ARLVAEEAKA RREGGGEAAL LPGARVVARP
PPVGAEDPDV TASAERRLHK SPGLLAVPPE EMAASAAAAI VSPEEELDGC EPEAIGKRPA
VLPLLERVSE AAKSSGADGS LPSTPPPPEE EEDDLYRQSL EIISRYLREQ ATGSKDSKPL
GEAGAAGRRA LETLRRVGDG VQRNHETAFQ GMLRKLDIKN EGDVKSFSRV MVHVFKDGVT
NWGRIVTLIS FGAFVAKHLK SVNQESFIEP LAETITDVLV RTKRDWLVKQ RGWDGFVEFF
HVQDLEGGIR NVLLAFAGVA GVGAGLAYLI R


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E2097h ELISA BCL2L3,Bcl2-L-3,Bcl-2-like protein 3,Bcl-2-related protein EAT_mcl1,Homo sapiens,Human,Induced myeloid leukemia cell differentiation protein Mcl-1,MCL1,mcl1_EAT 96T
E2097h ELISA kit BCL2L3,Bcl2-L-3,Bcl-2-like protein 3,Bcl-2-related protein EAT_mcl1,Homo sapiens,Human,Induced myeloid leukemia cell differentiation protein Mcl-1,MCL1,mcl1_EAT 96T
U2097h CLIA kit BCL2L3,Bcl2-L-3,Bcl-2-like protein 3,Bcl-2-related protein EAT_mcl1,Homo sapiens,Human,Induced myeloid leukemia cell differentiation protein Mcl-1,MCL1,mcl1_EAT 96T
E1389026 Cat Induced Myeloid Leukemia Cell Differentiation Protein Mcl-1 (MCL1) ELISA Kit
CSB-EL013588RA Rat Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit 96T
CSB-EL013588DO Dog Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit 96T
CSB-EL013588CA Cat Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit 96T
CSB-EL013588DO Dog Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit SpeciesDog 96T
CSB-EL013588CA Cat Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit SpeciesCat 96T
CSB-EL013588HU Human Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit 96T
CSB-EL013588MO Mouse Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit 96T
CSB-EL013588RA Rat Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit SpeciesRat 96T
CSB-EL013588HU Human Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit SpeciesHuman 96T
CSB-EL013588MO Mouse Induced myeloid leukemia cell differentiation protein Mcl-1(MCL1) ELISA kit SpeciesMouse 96T
U2097c CLIA kit Canis familiaris,Canis lupus familiaris,Dog,Induced myeloid leukemia cell differentiation protein Mcl-1 homolog,MCL1 96T


 

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