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Induced myeloid leukemia cell differentiation protein Mcl-1 (Bcl-2-like protein 3) (Bcl2-L-3) (Bcl-2-related protein EAT/mcl1) (mcl1/EAT)

 MCL1_HUMAN              Reviewed;         350 AA.
Q07820; B2R6B2; D3DV03; D3DV04; Q9HD91; Q9NRQ3; Q9NRQ4; Q9UHR7;
Q9UHR8; Q9UHR9; Q9UNJ1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 3.
18-JUL-2018, entry version 198.
RecName: Full=Induced myeloid leukemia cell differentiation protein Mcl-1;
AltName: Full=Bcl-2-like protein 3;
Short=Bcl2-L-3;
AltName: Full=Bcl-2-related protein EAT/mcl1;
AltName: Full=mcl1/EAT;
Name=MCL1; Synonyms=BCL2L3;
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), AND VARIANT ASP-173.
TISSUE=Myeloid leukemia cell;
PubMed=7682708; DOI=10.1073/pnas.90.8.3516;
Kozopas K.M., Yang T., Buchan H.L., Zhou P., Craig R.W.;
"MCL1, a gene expressed in programmed myeloid cell differentiation,
has sequence similarity to BCL2.";
Proc. Natl. Acad. Sci. U.S.A. 90:3516-3520(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
PubMed=8790944;
Umezawa A., Maruyama T., Inazawa J., Imai S., Takano T., Hata J.;
"Induction of mcl1/EAT, Bcl-2 related gene, by retinoic acid or heat
shock in the human embryonal carcinoma cells, NCR-G3.";
Cell Struct. Funct. 21:143-150(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11130466; DOI=10.1007/PL00000728;
Akgul C., Turner P.C., White M.R.H., Edwards S.W.;
"Functional analysis of the human MCL-1 gene.";
Cell. Mol. Life Sci. 57:684-691(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANT ASP-173,
AND FUNCTION.
TISSUE=Myeloid leukemia cell, and Neuroblastoma;
PubMed=10766760; DOI=10.1074/jbc.M909572199;
Bingle C.D., Craig R.W., Swales B.M., Singleton V., Zhou P.,
Whyte M.K.B.;
"Exon skipping in Mcl-1 results in a Bcl-2 homology domain 3 only gene
product that promotes cell death.";
J. Biol. Chem. 275:22136-22146(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH BAX;
BAK1 AND BCL2L11, AND DIMERIZATION OF ISOFORMS 1 AND 2.
PubMed=10837489; DOI=10.1074/jbc.M909826199;
Bae J., Leo C.P., Hsu S.Y., Hsueh A.J.W.;
"MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member
MCL-1, encodes a proapoptotic protein possessing only the BH3
domain.";
J. Biol. Chem. 275:25255-25261(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-227.
TISSUE=Thalamus;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-227.
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary gland, 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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 182-289 (ISOFORM 1), AND VARIANT
VAL-227.
TISSUE=Ewing sarcoma;
PubMed=10634649; DOI=10.1016/S0145-2126(99)00137-X;
Okita H., Umezawa A., Fukuma M., Hata J.;
"Acute myeloid leukemia possessing jumping translocation is related to
highly elevated levels of EAT/mcl-1, a Bcl-2 related gene with anti-
apoptotic functions.";
Leuk. Res. 24:73-77(2000).
[13]
PROTEIN SEQUENCE OF N-TERMINUS OF FRAGMENTS OBTAINED BY CASPASE
CLEAVAGE, AND MUTAGENESIS OF ASP-127 AND ASP-157.
PubMed=15122313; DOI=10.1038/sj.onc.1207648;
Michels J., O'Neill J.W., Dallman C.L., Mouzakiti A., Habens F.,
Brimmell M., Zhang K.Y.J., Craig R.W., Marcusson E.G., Johnson P.W.M.,
Packham G.;
"Mcl-1 is required for Akata6 B-lymphoma cell survival and is
converted to a cell death molecule by efficient caspase-mediated
cleavage.";
Oncogene 23:4818-4827(2004).
[14]
INDUCTION.
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).
[15]
INTERACTION WITH TPT1, AND SUBCELLULAR LOCATION.
PubMed=12149273; DOI=10.1074/jbc.M207413200;
Zhang D., Li F., Weidner D., Mnjoyan Z.H., Fujise K.;
"Physical and functional interaction between myeloid cell leukemia 1
protein (MCL1) and fortilin. The potential role of MCL1 as a fortilin
chaperone.";
J. Biol. Chem. 277:37430-37438(2002).
[16]
PHOSPHORYLATION AT SER-121 AND THR-163.
PubMed=12223490; DOI=10.1074/jbc.M207951200;
Inoshita S., Takeda K., Hatai T., Terada Y., Sano M., Hata J.,
Umezawa A., Ichijo H.;
"Phosphorylation and inactivation of myeloid cell leukemia 1 by JNK in
response to oxidative stress.";
J. Biol. Chem. 277:43730-43734(2002).
[17]
INTERACTION WITH BAK1, AND SUBCELLULAR LOCATION.
PubMed=15077116; DOI=10.1038/ncb1123;
Leu J.I.-J., Dumont P., Hafey M., Murphy M.E., George D.L.;
"Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1
complex.";
Nat. Cell Biol. 6:443-450(2004).
[18]
PHOSPHORYLATION AT THR-163, AND MUTAGENESIS OF SER-162 AND THR-163.
PubMed=15241487; DOI=10.1038/sj.onc.1207692;
Domina A.M., Vrana J.A., Gregory M.A., Hann S.R., Craig R.W.;
"MCL1 is phosphorylated in the PEST region and stabilized upon ERK
activation in viable cells, and at additional sites with cytotoxic
okadaic acid or taxol.";
Oncogene 23:5301-5315(2004).
[19]
UBIQUITINATION, AND MUTAGENESIS OF LYS-5; LYS-40; LYS-136; LYS-194;
LYS-197; LYS-208 AND LYS-234.
PubMed=15989957; DOI=10.1016/j.cell.2005.06.009;
Zhong Q., Gao W., Du F., Wang X.;
"Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
polyubiquitination of Mcl-1 and regulates apoptosis.";
Cell 121:1085-1095(2005).
[20]
FUNCTION AS INHIBITOR OF APOPTOSIS, PHOSPHORYLATION AT SER-159 BY
GSK3-ALPHA AND GSK3-BETA, UBIQUITINATION, AND MUTAGENESIS OF SER-159.
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).
[21]
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).
[22]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-162 AND THR-163, AND
MUTAGENESIS OF SER-162.
PubMed=23024798; DOI=10.1371/journal.pone.0045088;
Thomas L.W., Lam C., Clark R.E., White M.R., Spiller D.G., Moots R.J.,
Edwards S.W.;
"Serine 162, an essential residue for the mitochondrial localization,
stability and anti-apoptotic function of Mcl-1.";
PLoS ONE 7:E45088-E45088(2012).
[23]
INTERACTION WITH RTL10/BOP.
PubMed=23055042; DOI=10.1007/s13238-012-2069-7;
Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q.,
Pan L., Tang H.;
"Human Bop is a novel BH3-only member of the Bcl-2 protein family.";
Protein Cell 3:790-801(2012).
[24]
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).
[25]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 151-307 IN COMPLEXES WITH
PMAIP1 AND BCL2L11.
PubMed=17389404; DOI=10.1073/pnas.0701297104;
Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J.,
Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.;
"Structural insights into the degradation of Mcl-1 induced by BH3
domains.";
Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007).
[26]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 172-327 IN COMPLEX WITH
BCL2L11.
PubMed=20562877; DOI=10.1038/nchembio.391;
Stewart M.L., Fire E., Keating A.E., Walensky L.D.;
"The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis
sensitizer.";
Nat. Chem. Biol. 6:595-601(2010).
[27]
VARIANT [LARGE SCALE ANALYSIS] LEU-231.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(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 1 inhibits apoptosis.
Isoform 2 promotes apoptosis. {ECO:0000269|PubMed:10766760,
ECO:0000269|PubMed:16543145}.
-!- SUBUNIT: Interacts with HIF3A (via C-terminus domain) (By
similarity). Interacts with BAD, BOK, BIK and BMF (By similarity).
Interacts with PMAIP1 (PubMed:17389404). Interacts with BBC3 (By
similarity). Isoform 1 interacts with BAX, BAK1 and TPT1
(PubMed:10837489, PubMed:12149273, PubMed:15077116). Heterodimer
of isoform 1 and isoform 2. Homodimers of isoform 1 or isoform 2
are not detected. Isoform 2 does not interact with pro-apoptotic
BCL2-related proteins (PubMed:10837489). Interacts with RTL10/BOP
(PubMed:23055042). Interacts with BCL2L11; may sequester BCL2L11
to prevent its pro-apoptotic activity (PubMed:10837489,
PubMed:27013495, PubMed:17389404, PubMed:20562877).
{ECO:0000250|UniProtKB:P97287, ECO:0000250|UniProtKB:Q9Z1P3,
ECO:0000269|PubMed:10837489, ECO:0000269|PubMed:12149273,
ECO:0000269|PubMed:15077116, ECO:0000269|PubMed:17389404,
ECO:0000269|PubMed:20562877, ECO:0000269|PubMed:23055042,
ECO:0000269|PubMed:27013495}.
-!- INTERACTION:
Q91AU0:- (xeno); NbExp=2; IntAct=EBI-1003422, EBI-9657017;
Q16611:BAK1; NbExp=15; IntAct=EBI-1003422, EBI-519866;
Q07812:BAX; NbExp=8; IntAct=EBI-1003422, EBI-516580;
Q9BXH1:BBC3; NbExp=3; IntAct=EBI-1003422, EBI-519884;
O43521:BCL2L11; NbExp=16; IntAct=EBI-1003422, EBI-526406;
Q14457:BECN1; NbExp=2; IntAct=EBI-1003422, EBI-949378;
P55957:BID; NbExp=2; IntAct=EBI-1003422, EBI-519672;
Q03135:CAV1; NbExp=3; IntAct=EBI-1003422, EBI-603614;
P49817:Cav1 (xeno); NbExp=3; IntAct=EBI-1003422, EBI-1161338;
Q7Z6Z7:HUWE1; NbExp=10; IntAct=EBI-1003422, EBI-625934;
Q13794:PMAIP1; NbExp=5; IntAct=EBI-1003422, EBI-707392;
Q9JM54:Pmaip1 (xeno); NbExp=2; IntAct=EBI-1003422, EBI-709183;
Q7L3V2:RTL10; NbExp=2; IntAct=EBI-1003422, EBI-10697720;
Q93008:USP9X; NbExp=10; IntAct=EBI-1003422, EBI-302524;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}. Cytoplasm. Mitochondrion. Nucleus,
nucleoplasm. Note=Cytoplasmic, associated with mitochondria.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MCL1L, MCL-1L;
IsoId=Q07820-1; Sequence=Displayed;
Name=2; Synonyms=Delta S, MCL-1S, TM;
IsoId=Q07820-2; Sequence=VSP_000532, VSP_000533;
-!- INDUCTION: Expression increases early during phorbol ester-induced
differentiation along the monocyte/macrophage pathway in myeloid
leukemia cell line ML-1. Rapidly up-regulated by CSF2 in ML-1
cells. Up-regulated by heat shock-induced differentiation.
Expression increases early during retinoic acid-induced
differentiation. {ECO:0000269|PubMed:8790944,
ECO:0000269|PubMed:9671497}.
-!- PTM: Cleaved by CASP3 during apoptosis. In intact cells cleavage
occurs preferentially after Asp-127, yielding a pro-apoptotic 28
kDa C-terminal fragment.
-!- PTM: Rapidly degraded in the absence of phosphorylation on Thr-163
in the PEST region. {ECO:0000269|PubMed:12223490,
ECO:0000269|PubMed:15241487, ECO:0000269|PubMed:23024798}.
-!- PTM: Phosphorylated on Ser-159, by GSK3, in response to
IL3/interleukin-3 withdrawal. Phosphorylation at Ser-159 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-159. {ECO:0000269|PubMed:16543145}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mcl1/";
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EMBL; L08246; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF118124; AAD13299.1; -; mRNA.
EMBL; AF147742; AAF74821.1; -; Genomic_DNA.
EMBL; AF198614; AAF64255.1; -; Genomic_DNA.
EMBL; AF198614; AAF64256.1; -; Genomic_DNA.
EMBL; AF162677; AAG00896.1; -; Genomic_DNA.
EMBL; AF162676; AAG00896.1; JOINED; Genomic_DNA.
EMBL; AF203373; AAG00904.1; -; mRNA.
EMBL; BT006640; AAP35286.1; -; mRNA.
EMBL; AK312508; BAG35409.1; -; mRNA.
EMBL; DQ088966; AAY68220.1; -; Genomic_DNA.
EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53538.1; -; Genomic_DNA.
EMBL; CH471121; EAW53539.1; -; Genomic_DNA.
EMBL; CH471121; EAW53540.1; -; Genomic_DNA.
EMBL; CH471121; EAW53541.1; -; Genomic_DNA.
EMBL; BC017197; AAH17197.1; -; mRNA.
EMBL; BC071897; AAH71897.1; -; mRNA.
EMBL; BC107735; AAI07736.1; -; mRNA.
EMBL; AF118276; AAF15309.1; -; mRNA.
EMBL; AF118277; AAF15310.1; -; mRNA.
EMBL; AF118278; AAF15311.1; -; mRNA.
CCDS; CCDS956.1; -. [Q07820-2]
CCDS; CCDS957.1; -. [Q07820-1]
PIR; A47476; A47476.
RefSeq; NP_001184249.1; NM_001197320.1.
RefSeq; NP_068779.1; NM_021960.4. [Q07820-1]
RefSeq; NP_877495.1; NM_182763.2. [Q07820-2]
UniGene; Hs.632486; -.
PDB; 2KBW; NMR; -; A=163-326.
PDB; 2MHS; NMR; -; A=171-327.
PDB; 2NL9; X-ray; 1.55 A; A=209-327.
PDB; 2NLA; X-ray; 2.80 A; A=209-327.
PDB; 2PQK; X-ray; 2.00 A; A=172-327.
PDB; 3D7V; X-ray; 2.03 A; A=209-327.
PDB; 3IO9; X-ray; 2.40 A; A=209-327.
PDB; 3KJ0; X-ray; 1.70 A; A=172-327.
PDB; 3KJ1; X-ray; 1.94 A; A=172-327.
PDB; 3KJ2; X-ray; 2.35 A; A=172-327.
PDB; 3KZ0; X-ray; 2.35 A; A/B=172-327.
PDB; 3MK8; X-ray; 2.32 A; A=172-327, B=208-228.
PDB; 3PK1; X-ray; 2.49 A; A/C=174-326.
PDB; 3TWU; X-ray; 1.80 A; B=73-88.
PDB; 3WIX; X-ray; 1.90 A; A/B/C/D=172-327.
PDB; 3WIY; X-ray; 2.15 A; A/B/C/D/E/F=172-327.
PDB; 4BPI; X-ray; 1.98 A; A=209-327.
PDB; 4BPJ; X-ray; 1.60 A; A=209-327.
PDB; 4HW2; X-ray; 2.80 A; A/B/C/D/E/F=172-323.
PDB; 4HW3; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=172-323.
PDB; 4HW4; X-ray; 1.53 A; A/B=172-327.
PDB; 4OQ5; X-ray; 2.86 A; A/B/C/D/E/F=174-326.
PDB; 4OQ6; X-ray; 1.81 A; A/B=174-326.
PDB; 4WGI; X-ray; 1.85 A; A=173-321.
PDB; 4WMR; X-ray; 1.70 A; A=173-321.
PDB; 4WMS; X-ray; 1.90 A; A=174-321.
PDB; 4WMT; X-ray; 2.35 A; A=174-321.
PDB; 4WMU; X-ray; 1.55 A; A=174-321.
PDB; 4WMV; X-ray; 2.40 A; A=174-321.
PDB; 4WMW; X-ray; 1.90 A; A=174-321.
PDB; 4WMX; X-ray; 2.00 A; A=174-321.
PDB; 4ZBF; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=172-327.
PDB; 4ZBI; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=172-327.
PDB; 5C3F; X-ray; 1.43 A; A=173-327.
PDB; 5C6H; X-ray; 2.05 A; A/C/E/G/I/K/M/O/Q/S/U/W=171-327.
PDB; 5FC4; X-ray; 1.50 A; A=172-320.
PDB; 5FDO; X-ray; 2.80 A; A/B/C/D=172-320.
PDB; 5FDR; X-ray; 2.60 A; A/B/C/D=172-327.
PDB; 5IEZ; X-ray; 2.60 A; A/B/C/D=172-327.
PDB; 5IF4; X-ray; 2.39 A; A/B=172-327.
PDB; 5JSB; X-ray; 2.74 A; A/C/E/G/I/K=172-350.
PDB; 5KU9; X-ray; 2.20 A; A/B=174-219, A/B=258-327.
PDB; 5LOF; X-ray; 2.20 A; A=173-321.
PDB; 5MES; X-ray; 2.24 A; A=241-327.
PDB; 5MEV; X-ray; 2.94 A; A=241-327.
PDB; 5UUM; X-ray; 2.35 A; A/B=172-325.
PDB; 5VKC; X-ray; 2.31 A; A/B=174-326.
PDB; 5VX2; X-ray; 1.85 A; A/C=241-327.
PDB; 5W89; X-ray; 1.42 A; A=172-321.
PDB; 5W8F; X-ray; 1.85 A; A=172-320.
PDB; 6B4L; X-ray; 2.25 A; A/B=174-326.
PDB; 6B4U; X-ray; 1.95 A; A=174-326.
PDB; 6BW2; X-ray; 2.75 A; A/B/C/D=172-327.
PDB; 6BW8; X-ray; 2.90 A; A/B/C/D=172-327.
PDBsum; 2KBW; -.
PDBsum; 2MHS; -.
PDBsum; 2NL9; -.
PDBsum; 2NLA; -.
PDBsum; 2PQK; -.
PDBsum; 3D7V; -.
PDBsum; 3IO9; -.
PDBsum; 3KJ0; -.
PDBsum; 3KJ1; -.
PDBsum; 3KJ2; -.
PDBsum; 3KZ0; -.
PDBsum; 3MK8; -.
PDBsum; 3PK1; -.
PDBsum; 3TWU; -.
PDBsum; 3WIX; -.
PDBsum; 3WIY; -.
PDBsum; 4BPI; -.
PDBsum; 4BPJ; -.
PDBsum; 4HW2; -.
PDBsum; 4HW3; -.
PDBsum; 4HW4; -.
PDBsum; 4OQ5; -.
PDBsum; 4OQ6; -.
PDBsum; 4WGI; -.
PDBsum; 4WMR; -.
PDBsum; 4WMS; -.
PDBsum; 4WMT; -.
PDBsum; 4WMU; -.
PDBsum; 4WMV; -.
PDBsum; 4WMW; -.
PDBsum; 4WMX; -.
PDBsum; 4ZBF; -.
PDBsum; 4ZBI; -.
PDBsum; 5C3F; -.
PDBsum; 5C6H; -.
PDBsum; 5FC4; -.
PDBsum; 5FDO; -.
PDBsum; 5FDR; -.
PDBsum; 5IEZ; -.
PDBsum; 5IF4; -.
PDBsum; 5JSB; -.
PDBsum; 5KU9; -.
PDBsum; 5LOF; -.
PDBsum; 5MES; -.
PDBsum; 5MEV; -.
PDBsum; 5UUM; -.
PDBsum; 5VKC; -.
PDBsum; 5VX2; -.
PDBsum; 5W89; -.
PDBsum; 5W8F; -.
PDBsum; 6B4L; -.
PDBsum; 6B4U; -.
PDBsum; 6BW2; -.
PDBsum; 6BW8; -.
ProteinModelPortal; Q07820; -.
SMR; Q07820; -.
BioGrid; 110338; 72.
ComplexPortal; CPX-304; MCL1:PMAIP1 complex.
ComplexPortal; CPX-481; MCL-1-BIM complex. [Q07820-1]
CORUM; Q07820; -.
DIP; DIP-231N; -.
ELM; Q07820; -.
IntAct; Q07820; 35.
MINT; Q07820; -.
STRING; 9606.ENSP00000358022; -.
BindingDB; Q07820; -.
ChEMBL; CHEMBL4361; -.
GuidetoPHARMACOLOGY; 2847; -.
iPTMnet; Q07820; -.
PhosphoSitePlus; Q07820; -.
BioMuta; MCL1; -.
DMDM; 83304396; -.
EPD; Q07820; -.
MaxQB; Q07820; -.
PaxDb; Q07820; -.
PeptideAtlas; Q07820; -.
PRIDE; Q07820; -.
ProteomicsDB; 58540; -.
ProteomicsDB; 58541; -. [Q07820-2]
DNASU; 4170; -.
Ensembl; ENST00000307940; ENSP00000309973; ENSG00000143384. [Q07820-2]
Ensembl; ENST00000369026; ENSP00000358022; ENSG00000143384. [Q07820-1]
GeneID; 4170; -.
KEGG; hsa:4170; -.
UCSC; uc001euz.4; human. [Q07820-1]
CTD; 4170; -.
DisGeNET; 4170; -.
EuPathDB; HostDB:ENSG00000143384.12; -.
GeneCards; MCL1; -.
HGNC; HGNC:6943; MCL1.
HPA; CAB002781; -.
HPA; CAB068195; -.
HPA; HPA008455; -.
HPA; HPA031125; -.
MIM; 159552; gene.
neXtProt; NX_Q07820; -.
OpenTargets; ENSG00000143384; -.
PharmGKB; PA30688; -.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00510000048923; -.
HOVERGEN; HBG003527; -.
InParanoid; Q07820; -.
KO; K02539; -.
OMA; AKDTKPM; -.
OrthoDB; EOG091G0E6Q; -.
PhylomeDB; Q07820; -.
TreeFam; TF315834; -.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; Q07820; -.
ChiTaRS; MCL1; human.
EvolutionaryTrace; Q07820; -.
GeneWiki; MCL1; -.
GenomeRNAi; 4170; -.
PMAP-CutDB; Q07820; -.
PRO; PR:Q07820; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143384; -.
CleanEx; HS_MCL1; -.
ExpressionAtlas; Q07820; baseline and differential.
Genevisible; Q07820; HS.
GO; GO:0097136; C:Bcl-2 family protein complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0051434; F:BH3 domain binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0008320; F:protein transmembrane transporter activity; TAS:UniProtKB.
GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
GO; GO:0019725; P:cellular homeostasis; NAS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
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; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:BHF-UCL.
GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
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; IGI:ParkinsonsUK-UCL.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:MGI.
GO; GO:0034097; P:response to cytokine; IDA: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;
Direct protein sequencing; Isopeptide bond; Membrane; Mitochondrion;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 350 Induced myeloid leukemia cell
differentiation protein Mcl-1.
/FTId=PRO_0000143080.
TRANSMEM 328 348 Helical. {ECO:0000255}.
REGION 104 175 PEST-like.
MOTIF 209 223 BH3.
MOTIF 252 272 BH1.
MOTIF 304 319 BH2.
SITE 127 128 Cleavage; by caspase-3.
SITE 157 158 Cleavage; by caspase-3.
MOD_RES 121 121 Phosphoserine.
{ECO:0000269|PubMed:12223490}.
MOD_RES 159 159 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0000269|PubMed:16543145}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000269|PubMed:23024798}.
MOD_RES 163 163 Phosphothreonine; by MAPK.
{ECO:0000269|PubMed:12223490,
ECO:0000269|PubMed:15241487,
ECO:0000269|PubMed:23024798}.
CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 40 40 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 194 194 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 231 271 MLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFG
-> WVCGVLPCRGPRRWHQECAAGFCRCCWSRSWFGISNKI
ALL (in isoform 2).
{ECO:0000303|PubMed:10837489}.
/FTId=VSP_000532.
VAR_SEQ 272 350 Missing (in isoform 2).
{ECO:0000303|PubMed:10837489}.
/FTId=VSP_000533.
VARIANT 173 173 E -> D (in dbSNP:rs2737820).
{ECO:0000269|PubMed:10766760,
ECO:0000269|PubMed:7682708}.
/FTId=VAR_024021.
VARIANT 227 227 A -> V (in dbSNP:rs11580946).
{ECO:0000269|PubMed:10634649,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.8}.
/FTId=VAR_024022.
VARIANT 231 231 M -> L (in dbSNP:rs140449444).
{ECO:0000269|PubMed:18987736}.
/FTId=VAR_054157.
MUTAGEN 5 5 K->R: Reduced ubiquitination.
{ECO:0000269|PubMed:15989957}.
MUTAGEN 40 40 K->R: Reduced ubiquitination.
{ECO:0000269|PubMed:15989957}.
MUTAGEN 127 127 D->A: Abolishes formation of 28 and 17
kDa cleavage products by CASP3. Abolishes
cleavage by caspase-3; when associated
with A-157.
{ECO:0000269|PubMed:15122313}.
MUTAGEN 136 136 K->R: Reduced ubiquitination.
{ECO:0000269|PubMed:15989957}.
MUTAGEN 157 157 D->A: Abolishes formation of 23 and 21
kDa cleavage products by CASP3. Abolishes
cleavage by caspase-3; when associated
with A-127.
{ECO:0000269|PubMed:15122313}.
MUTAGEN 159 159 S->A: Loss of phosphorylation by GSK3 and
loss of ubiquitination increasing protein
stability. {ECO:0000269|PubMed:16543145}.
MUTAGEN 162 162 S->A: Abolishes mitochondrial
localization and decreases stability.
{ECO:0000269|PubMed:15241487,
ECO:0000269|PubMed:23024798}.
MUTAGEN 162 162 S->A: No effect.
{ECO:0000269|PubMed:15241487,
ECO:0000269|PubMed:23024798}.
MUTAGEN 163 163 T->A,E: No effect on mitochondrial
localization.
{ECO:0000269|PubMed:15241487}.
MUTAGEN 163 163 T->A: Abolishes phosphorylation by MAPK.
No effect on phosphorylation induced by
okadaic acid or taxol.
{ECO:0000269|PubMed:15241487}.
MUTAGEN 194 194 K->R: Reduced ubiquitination.
{ECO:0000269|PubMed:15989957}.
MUTAGEN 197 197 K->R: Reduced ubiquitination.
{ECO:0000269|PubMed:15989957}.
MUTAGEN 208 208 K->R: No effect on ubiquitination.
{ECO:0000269|PubMed:15989957}.
MUTAGEN 234 234 K->R: No effect on ubiquitination.
{ECO:0000269|PubMed:15989957}.
HELIX 173 187 {ECO:0000244|PDB:5W89}.
TURN 189 191 {ECO:0000244|PDB:3MK8}.
STRAND 200 202 {ECO:0000244|PDB:3KJ1}.
HELIX 204 223 {ECO:0000244|PDB:5W89}.
HELIX 225 235 {ECO:0000244|PDB:5W89}.
HELIX 240 255 {ECO:0000244|PDB:5W89}.
HELIX 261 280 {ECO:0000244|PDB:5W89}.
HELIX 284 286 {ECO:0000244|PDB:5W89}.
HELIX 287 308 {ECO:0000244|PDB:5W89}.
HELIX 311 318 {ECO:0000244|PDB:5W89}.
SEQUENCE 350 AA; 37337 MW; D85821AC59275F1F CRC64;
MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS
AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM
SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE
IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE
DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR
TKRDWLVKQR GWDGFVEFFH VEDLEGGIRN VLLAFAGVAG VGAGLAYLIR


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