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UniProtKB/Swiss-Prot entry Q07820


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MCL1_HUMAN
Primary accession number Q07820
Secondary accession numbers B2R6B2 Q9HD91 Q9NRQ3 Q9NRQ4 Q9UHR7 Q9UHR8 Q9UHR9 Q9UNJ1
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on December 6, 2005 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 97)
Name and origin of the protein
Protein name Induced myeloid leukemia cell differentiation protein Mcl-1
Synonyms Bcl-2-related protein EAT/mcl1
mcl1/EAT
Bcl-2-like protein 3
Bcl2-L-3
Gene name
Name: MCL1
Synonyms: BCL2L3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-173.
TISSUE=Myeloid leukemia cell;
DOI=10.1073/pnas.90.8.3516; PubMed=7682708 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1007/PL00000728; PubMed=11130466 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1074/jbc.M909572199; PubMed=10766760 [NCBI, ExPASy, EBI, Israel, Japan]
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), AND INTERACTION WITH BAX; BAK1; BCL2L11 AND BETWEEN ISOFORMS 1 AND 2.
DOI=10.1074/jbc.M909826199; PubMed=10837489 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA] (ISOFORM 1).
TISSUE=Mammary gland, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 182-289 (ISOFORM 1), AND VARIANT VAL-227.
TISSUE=Ewing sarcoma;
DOI=10.1016/S0145-2126(99)00137-X; PubMed=10634649 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
PROTEIN SEQUENCE OF N-TERMINUS OF FRAGMENTS OBTAINED BY CASPASE CLEAVAGE, AND MUTAGENESIS OF ASP-127 AND ASP-157.
DOI=10.1038/sj.onc.1207648; PubMed=15122313 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
INDUCTION.
PubMed=9671497 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
INTERACTION WITH TPT1, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M207413200; PubMed=12149273 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
PHOSPHORYLATION AT SER-121 AND THR-163.
DOI=10.1074/jbc.M207951200; PubMed=12223490 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
INTERACTION WITH BAK, AND SUBCELLULAR LOCATION.
DOI=10.1038/ncb1123; PubMed=15077116 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
PHOSPHORYLATION AT THR-163, AND MUTAGENESIS OF SER-162 AND THR-163.
DOI=10.1038/sj.onc.1207692; PubMed=15241487 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
UBIQUITINATION, AND MUTAGENESIS OF LYS-5; LYS-40; LYS-136; LYS-194; LYS-197; LYS-208 AND LYS-234.
DOI=10.1016/j.cell.2005.06.009; PubMed=15989957 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-163, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 151-307 IN COMPLEXES WITH PMAIP1 AND BCL2L11.
DOI=10.1073/pnas.0701297104; PubMed=17389404 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 172-327 IN COMPLEX WITH BCL2L11.
Bare E., Grant R.A., Keating A.E.;
"X-ray crystal structure of human MCL-1 in complex with BIM BH3.";
Submitted (JUN-2007) to the PDB data bank.
[22]
VARIANT [LARGE SCALE ANALYSIS] LEU-231.
DOI=10.1038/nature07485; PubMed=18987736 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L08246; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AF118124; AAD13299.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF147742; AAF74821.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF198614; AAF64255.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF198614; AAF64256.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162677; AAG00896.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF162676; AAG00896.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF203373; AAG00904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006640; AAP35286.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312508; BAG35409.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ088966; AAY68220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356356; CAI15503.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356356; CAI15504.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017197; AAH17197.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071897; AAH71897.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107735; AAI07736.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF118276; AAF15309.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF118277; AAF15310.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF118278; AAF15311.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00030356; -.
IPI00221306; -.
PIR A47476; A47476.
RefSeq NP_068779.1; -.
NP_877495.1; -.
UniGene Hs.713518
3D structure databases
PDB
2NL9; X-ray; 1.55 A; A=209-327.[ExPASy / RCSB / EBI]
2NLA; X-ray; 2.80 A; A=209-327.[ExPASy / RCSB / EBI]
2PQK; X-ray; 2.00 A; A=172-327.[ExPASy / RCSB / EBI]
3D7V; X-ray; 2.03 A; A=171-327.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2NL9; -.
2NLA; -.
2PQK; -.
3D7V; -.
ModBase Q07820.
Protein-protein interaction databases
DIP DIP:231N; -.
IntAct Q07820; 9.
PTM databases
PhosphoSite Q07820; -.
Enzyme and pathway databases
Pathway_Interaction_DB hif1_tfpathway; HIF-1-alpha transcription factor network.
il6_7pathway; IL6-mediated signaling events.
Organism-specific databases
GeneCards GC01M148813; -.
H-InvDB HIX0001031; -.
HGNC HGNC:6943; MCL1.
GenAtlas MCL1.
HPA CAB002781; -.
HPA008455; -.
MIM 159552; gene. [NCBI / EBI]
PharmGKB PA30688; -.
Gene expression databases
ArrayExpress Q07820; -.
Bgee Q07820; -.
CleanEx HS_MCL1; -.
GermOnline ENSG00000143384; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741; Cellular component: mitochondrial outer membrane (traceable author statement from UniProtKB).
GO:0005654; Cellular component: nucleoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0015266; Molecular function: protein channel activity (traceable author statement from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0006915; Biological process: apoptosis (inferred from direct assay from UniProtKB).
GO:0001709; Biological process: cell fate determination (non-traceable author statement from UniProtKB).
GO:0019725; Biological process: cellular homeostasis (non-traceable author statement from UniProtKB).
GO:0007275; Biological process: multicellular organismal development (inferred from electronic annotation from UniProtKB-KW).
GO:0034097; Biological process: response to cytokine stimulus (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR013281; Apop_reg_Mc1.
IPR002475; BCL2_apoptsis.
IPR000712; Bcl2_BH.
Graphical view of domain structure.
Pfam PF00452; Bcl-2; 1.
Pfam graphical view of domain structure.
PRINTS PR01866; APOPREGMCL1.
PR01862; BCL2FAMILY.
SMART SM00337; BCL; 1.
SMART graphical view of domain structure.
PROSITE PS50062; BCL2_FAMILY; 1.
PS01080; BH1; 1.
PS01258; BH2; 1.
PS01259; BH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q07820; -.
Genome annotation databases
Ensembl ENSG00000143384; Homo sapiens. [Contig view]
GeneID 4170; -.
KEGG hsa:4170; -.
Phylogenomic databases
HOVERGEN Q07820; -.
OMA Q07820; GYEPEPL.
Other
NextBio 16422; -.
PMAP-CutDB Q07820; -.
SOURCE MCL1; Homo sapiens.
ProtoNet Q07820.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Isopeptide bond; Membrane; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Transmembrane; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   350  350     Induced myeloid leukemia cell differentiation protein Mcl-1. PRO_0000143080
TRANSMEM   328   348  21     Potential. 
REGION   104   175  72     PEST-like. 
MOTIF   209   223  15     BH3. 
MOTIF   252   272  21     BH1. 
MOTIF   304   319  16     BH2. 
SITE   127   128  2     Cleavage; by caspase-3. 
SITE   157   158  2     Cleavage; by caspase-3. 
MOD_RES   121   121        Phosphoserine. 
MOD_RES   163   163        Phosphothreonine; by MAPK. 
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        MLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVT LISFG -> WVCGVLPCRGPRRWHQECAAGFCRCCWSRSWFGISN KIALL (in isoform 2). VSP_000532
VAR_SEQ   272   350        Missing (in isoform 2). VSP_000533
VARIANT   173   173  1     E -> D (in dbSNP:rs2737820 [NCBI]). VAR_024021 [3D]
VARIANT   227   227  1     A -> V (in dbSNP:rs11580946 [NCBI]). VAR_024022 [3D]
VARIANT   231   231  1     M -> L. VAR_054157 [3D]
MUTAGEN   5     5        K->R: Reduced ubiquitination. 
MUTAGEN   40    40        K->R: Reduced ubiquitination. 
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. 
MUTAGEN   136   136        K->R: Reduced ubiquitination. 
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. 
MUTAGEN   162   162        S->A: No effect. 
MUTAGEN   163   163        T->A: Abolishes phosphorylation by MAPK. No effect on phosphorylation induced by okadaic acid or taxol. 
MUTAGEN   194   194        K->R: Reduced ubiquitination. 
MUTAGEN   197   197        K->R: Reduced ubiquitination. 
MUTAGEN   208   208        K->R: No effect on ubiquitination. 
MUTAGEN   234   234        K->R: No effect on ubiquitination. 
HELIX   173   191  19      
HELIX   204   221  18      
HELIX   225   235  11      
HELIX   244   253  10      
HELIX   254   256  3      
HELIX   261   281  21      
HELIX   288   301  14      
HELIX   303   308  6      
TURN   309   311  3      
HELIX   312   318  7      
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 37337 Da [This is the MW of the unprocessed precursor] CRC64: D85821AC59275F1F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS 

        70         80         90        100        110        120 
AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM 

       130        140        150        160        170        180 
SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE 

       190        200        210        220        230        240 
IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE 

       250        260        270        280        290        300 
DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR 

       310        320        330        340        350 
TKRDWLVKQR GWDGFVEFFH VEDLEGGIRN VLLAFAGVAG VGAGLAYLIR 

Q07820 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
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