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Protein

Induced myeloid leukemia cell differentiation protein Mcl-1

Gene

MCL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • BH3 domain binding Source: BHF-UCL
  • protein channel activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: GO_Central

GO - Biological processi

  • apoptotic mitochondrial changes Source: Ensembl
  • cell fate determination Source: UniProtKB
  • cellular homeostasis Source: UniProtKB
  • extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: GO_Central
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of anoikis Source: UniProtKB
  • negative regulation of apoptotic process Source: BHF-UCL
  • negative regulation of autophagy Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB
  • negative regulation of intrinsic apoptotic signaling pathway Source: GO_Central
  • positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • regulation of response to DNA damage stimulus Source: MGI
  • response to cytokine Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143384-MONOMER.
SIGNORiQ07820.

Names & Taxonomyi

Protein namesi
Recommended name:
Induced myeloid leukemia cell differentiation protein Mcl-1
Alternative name(s):
Bcl-2-like protein 3
Short name:
Bcl2-L-3
Bcl-2-related protein EAT/mcl1
mcl1/EAT
Gene namesi
Name:MCL1
Synonyms:BCL2L3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6943. MCL1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei328 – 348HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • Bcl-2 family protein complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • mitochondrial matrix Source: Ensembl
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: MGI
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5K → R: Reduced ubiquitination. 1 Publication1
Mutagenesisi40K → R: Reduced ubiquitination. 1 Publication1
Mutagenesisi127D → A: Abolishes formation of 28 and 17 kDa cleavage products by CASP3. Abolishes cleavage by caspase-3; when associated with A-157. 1 Publication1
Mutagenesisi136K → R: Reduced ubiquitination. 1 Publication1
Mutagenesisi157D → A: Abolishes formation of 23 and 21 kDa cleavage products by CASP3. Abolishes cleavage by caspase-3; when associated with A-127. 1 Publication1
Mutagenesisi159S → A: Loss of phosphorylation by GSK3 and loss of ubiquitination increasing protein stability. 1 Publication1
Mutagenesisi162S → A: Abolishes mitochondrial localization and decreases stability. 2 Publications1
Mutagenesisi162S → A: No effect. 2 Publications1
Mutagenesisi163T → A or E: No effect on mitochondrial localization. 1 Publication1
Mutagenesisi163T → A: Abolishes phosphorylation by MAPK. No effect on phosphorylation induced by okadaic acid or taxol. 1 Publication1
Mutagenesisi194K → R: Reduced ubiquitination. 1 Publication1
Mutagenesisi197K → R: Reduced ubiquitination. 1 Publication1
Mutagenesisi208K → R: No effect on ubiquitination. 1 Publication1
Mutagenesisi234K → R: No effect on ubiquitination. 1 Publication1

Organism-specific databases

DisGeNETi4170.
OpenTargetsiENSG00000143384.
PharmGKBiPA30688.

Chemistry databases

ChEMBLiCHEMBL4361.
GuidetoPHARMACOLOGYi2847.

Polymorphism and mutation databases

BioMutaiMCL1.
DMDMi83304396.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001430801 – 350Induced myeloid leukemia cell differentiation protein Mcl-1Add BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei121Phosphoserine1 Publication1
Cross-linki136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei159Phosphoserine; by GSK3-alpha and GSK3-beta1 Publication1
Modified residuei162Phosphoserine1 Publication1
Modified residuei163Phosphothreonine; by MAPK3 Publications1
Cross-linki194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modificationi

Cleaved by CASP3 during apoptosis. In intact cells cleavage occurs preferentially after Asp-127, yielding a pro-apoptotic 28 kDa C-terminal fragment.
Rapidly degraded in the absence of phosphorylation on Thr-163 in the PEST region.3 Publications
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.1 Publication
Ubiquitinated. Ubiquitination is induced by phosphorylation at Ser-159.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei127 – 128Cleavage; by caspase-32
Sitei157 – 158Cleavage; by caspase-32

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ07820.
MaxQBiQ07820.
PaxDbiQ07820.
PeptideAtlasiQ07820.
PRIDEiQ07820.

PTM databases

iPTMnetiQ07820.
PhosphoSitePlusiQ07820.

Miscellaneous databases

PMAP-CutDBQ07820.

Expressioni

Inductioni

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.2 Publications

Gene expression databases

BgeeiENSG00000143384.
CleanExiHS_MCL1.
ExpressionAtlasiQ07820. baseline and differential.
GenevisibleiQ07820. HS.

Organism-specific databases

HPAiCAB002781.
CAB068195.
HPA008455.
HPA031125.

Interactioni

Subunit structurei

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 BOP (PubMed:23055042). Interacts with BCL2L11; may sequester BCL2L11 to prevent its pro-apoptotic activity (PubMed:10837489, PubMed:27013495, PubMed:17389404, PubMed:20562877).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q91AU02EBI-1003422,EBI-9657017From a different organism.
BAK1Q1661112EBI-1003422,EBI-519866
BAXQ078126EBI-1003422,EBI-516580
BBC3Q9BXH13EBI-1003422,EBI-519884
BCL2L11O4352115EBI-1003422,EBI-526406
BECN1Q144572EBI-1003422,EBI-949378
BOPQ7L3V22EBI-1003422,EBI-10697720
CAV1Q031353EBI-1003422,EBI-603614
Cav1P498173EBI-1003422,EBI-1161338From a different organism.
PMAIP1Q137945EBI-1003422,EBI-707392
Pmaip1Q9JM542EBI-1003422,EBI-709183From a different organism.

GO - Molecular functioni

  • BH3 domain binding Source: BHF-UCL
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: GO_Central

Protein-protein interaction databases

BioGridi110338. 63 interactors.
DIPiDIP-231N.
IntActiQ07820. 28 interactors.
MINTiMINT-89669.
STRINGi9606.ENSP00000358022.

Chemistry databases

BindingDBiQ07820.

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi173 – 191Combined sources19
Beta strandi200 – 202Combined sources3
Helixi203 – 223Combined sources21
Helixi225 – 235Combined sources11
Helixi240 – 243Combined sources4
Helixi244 – 253Combined sources10
Helixi254 – 256Combined sources3
Helixi261 – 280Combined sources20
Helixi284 – 286Combined sources3
Helixi287 – 308Combined sources22
Helixi311 – 319Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KBWNMR-A163-326[»]
2MHSNMR-A171-327[»]
2NL9X-ray1.55A209-327[»]
2NLAX-ray2.80A209-327[»]
2PQKX-ray2.00A172-327[»]
3D7VX-ray2.03A209-327[»]
3IO9X-ray2.40A209-327[»]
3KJ0X-ray1.70A172-327[»]
3KJ1X-ray1.94A172-327[»]
3KJ2X-ray2.35A172-327[»]
3KZ0X-ray2.35A/B172-327[»]
3MK8X-ray2.32A172-327[»]
B208-228[»]
3PK1X-ray2.49A/C174-326[»]
3TWUX-ray1.80B73-88[»]
3WIXX-ray1.90A/B/C/D172-327[»]
3WIYX-ray2.15A/B/C/D/E/F172-327[»]
4BPIX-ray1.98A209-327[»]
4BPJX-ray1.60A209-327[»]
4HW2X-ray2.80A/B/C/D/E/F172-323[»]
4HW3X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L172-323[»]
4HW4X-ray1.53A/B172-327[»]
4OQ5X-ray2.86A/B/C/D/E/F174-326[»]
4OQ6X-ray1.81A/B174-326[»]
4WGIX-ray1.85A173-321[»]
4WMRX-ray1.70A173-321[»]
4WMSX-ray1.90A174-321[»]
4WMTX-ray2.35A174-321[»]
4WMUX-ray1.55A174-321[»]
4WMVX-ray2.40A174-321[»]
4WMWX-ray1.90A174-321[»]
4WMXX-ray2.00A174-321[»]
4ZBFX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L172-327[»]
4ZBIX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L172-327[»]
5C3FX-ray1.43A173-327[»]
5C6HX-ray2.05A/C/E/G/I/K/M/O/Q/S/U/W171-327[»]
5FC4X-ray1.50A172-320[»]
5FDOX-ray2.80A/B/C/D172-320[»]
5FDRX-ray2.60A/B/C/D172-327[»]
ProteinModelPortaliQ07820.
SMRiQ07820.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07820.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni104 – 175PEST-likeAdd BLAST72

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi209 – 223BH3Add BLAST15
Motifi252 – 272BH1Add BLAST21
Motifi304 – 319BH2Add BLAST16

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00510000048923.
HOVERGENiHBG003527.
InParanoidiQ07820.
KOiK02539.
OMAiAKDTKPM.
OrthoDBiEOG091G0E6Q.
PhylomeDBiQ07820.
TreeFamiTF315834.

Family and domain databases

InterProiIPR013281. Apop_reg_Mc1.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
[Graphical view]
PRINTSiPR01866. APOPREGMCL1.
PR01862. BCL2FAMILY.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q07820-1) [UniParc]FASTAAdd to basket
Also known as: MCL1L, MCL-1L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG
60 70 80 90 100
GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA
110 120 130 140 150
PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES
160 170 180 190 200
GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG
210 220 230 240 250
RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM
260 270 280 290 300
IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR
310 320 330 340 350
TKRDWLVKQR GWDGFVEFFH VEDLEGGIRN VLLAFAGVAG VGAGLAYLIR
Length:350
Mass (Da):37,337
Last modified:December 6, 2005 - v3
Checksum:iD85821AC59275F1F
GO
Isoform 2 (identifier: Q07820-2) [UniParc]FASTAAdd to basket
Also known as: Delta S, MCL-1S, TM

The sequence of this isoform differs from the canonical sequence as follows:
     231-271: MLRKLDIKNE...GRIVTLISFG → WVCGVLPCRG...FGISNKIALL
     272-350: Missing.

Show »
Length:271
Mass (Da):28,662
Checksum:iFAE0BF9E126523EF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024021173E → D.2 PublicationsCorresponds to variant rs2737820dbSNPEnsembl.1
Natural variantiVAR_024022227A → V.3 PublicationsCorresponds to variant rs11580946dbSNPEnsembl.1
Natural variantiVAR_054157231M → L.1 PublicationCorresponds to variant rs140449444dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000532231 – 271MLRKL…LISFG → WVCGVLPCRGPRRWHQECAA GFCRCCWSRSWFGISNKIAL L in isoform 2. 1 PublicationAdd BLAST41
Alternative sequenceiVSP_000533272 – 350Missing in isoform 2. 1 PublicationAdd BLAST79

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08246 mRNA. No translation available.
AF118124 mRNA. Translation: AAD13299.1.
AF147742 Genomic DNA. Translation: AAF74821.1.
AF198614 Genomic DNA. Translation: AAF64255.1.
AF198614 Genomic DNA. Translation: AAF64256.1.
AF162677, AF162676 Genomic DNA. Translation: AAG00896.1.
AF203373 mRNA. Translation: AAG00904.1.
BT006640 mRNA. Translation: AAP35286.1.
AK312508 mRNA. Translation: BAG35409.1.
DQ088966 Genomic DNA. Translation: AAY68220.1.
AL356356 Genomic DNA. Translation: CAI15503.1.
AL356356 Genomic DNA. Translation: CAI15504.1.
CH471121 Genomic DNA. Translation: EAW53538.1.
CH471121 Genomic DNA. Translation: EAW53539.1.
CH471121 Genomic DNA. Translation: EAW53540.1.
CH471121 Genomic DNA. Translation: EAW53541.1.
BC017197 mRNA. Translation: AAH17197.1.
BC071897 mRNA. Translation: AAH71897.1.
BC107735 mRNA. Translation: AAI07736.1.
AF118276 mRNA. Translation: AAF15309.1.
AF118277 mRNA. Translation: AAF15310.1.
AF118278 mRNA. Translation: AAF15311.1.
CCDSiCCDS956.1. [Q07820-2]
CCDS957.1. [Q07820-1]
PIRiA47476.
RefSeqiNP_001184249.1. NM_001197320.1.
NP_068779.1. NM_021960.4. [Q07820-1]
NP_877495.1. NM_182763.2. [Q07820-2]
UniGeneiHs.632486.

Genome annotation databases

EnsembliENST00000307940; ENSP00000309973; ENSG00000143384. [Q07820-2]
ENST00000369026; ENSP00000358022; ENSG00000143384. [Q07820-1]
GeneIDi4170.
KEGGihsa:4170.
UCSCiuc001euz.4. human. [Q07820-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08246 mRNA. No translation available.
AF118124 mRNA. Translation: AAD13299.1.
AF147742 Genomic DNA. Translation: AAF74821.1.
AF198614 Genomic DNA. Translation: AAF64255.1.
AF198614 Genomic DNA. Translation: AAF64256.1.
AF162677, AF162676 Genomic DNA. Translation: AAG00896.1.
AF203373 mRNA. Translation: AAG00904.1.
BT006640 mRNA. Translation: AAP35286.1.
AK312508 mRNA. Translation: BAG35409.1.
DQ088966 Genomic DNA. Translation: AAY68220.1.
AL356356 Genomic DNA. Translation: CAI15503.1.
AL356356 Genomic DNA. Translation: CAI15504.1.
CH471121 Genomic DNA. Translation: EAW53538.1.
CH471121 Genomic DNA. Translation: EAW53539.1.
CH471121 Genomic DNA. Translation: EAW53540.1.
CH471121 Genomic DNA. Translation: EAW53541.1.
BC017197 mRNA. Translation: AAH17197.1.
BC071897 mRNA. Translation: AAH71897.1.
BC107735 mRNA. Translation: AAI07736.1.
AF118276 mRNA. Translation: AAF15309.1.
AF118277 mRNA. Translation: AAF15310.1.
AF118278 mRNA. Translation: AAF15311.1.
CCDSiCCDS956.1. [Q07820-2]
CCDS957.1. [Q07820-1]
PIRiA47476.
RefSeqiNP_001184249.1. NM_001197320.1.
NP_068779.1. NM_021960.4. [Q07820-1]
NP_877495.1. NM_182763.2. [Q07820-2]
UniGeneiHs.632486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KBWNMR-A163-326[»]
2MHSNMR-A171-327[»]
2NL9X-ray1.55A209-327[»]
2NLAX-ray2.80A209-327[»]
2PQKX-ray2.00A172-327[»]
3D7VX-ray2.03A209-327[»]
3IO9X-ray2.40A209-327[»]
3KJ0X-ray1.70A172-327[»]
3KJ1X-ray1.94A172-327[»]
3KJ2X-ray2.35A172-327[»]
3KZ0X-ray2.35A/B172-327[»]
3MK8X-ray2.32A172-327[»]
B208-228[»]
3PK1X-ray2.49A/C174-326[»]
3TWUX-ray1.80B73-88[»]
3WIXX-ray1.90A/B/C/D172-327[»]
3WIYX-ray2.15A/B/C/D/E/F172-327[»]
4BPIX-ray1.98A209-327[»]
4BPJX-ray1.60A209-327[»]
4HW2X-ray2.80A/B/C/D/E/F172-323[»]
4HW3X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L172-323[»]
4HW4X-ray1.53A/B172-327[»]
4OQ5X-ray2.86A/B/C/D/E/F174-326[»]
4OQ6X-ray1.81A/B174-326[»]
4WGIX-ray1.85A173-321[»]
4WMRX-ray1.70A173-321[»]
4WMSX-ray1.90A174-321[»]
4WMTX-ray2.35A174-321[»]
4WMUX-ray1.55A174-321[»]
4WMVX-ray2.40A174-321[»]
4WMWX-ray1.90A174-321[»]
4WMXX-ray2.00A174-321[»]
4ZBFX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L172-327[»]
4ZBIX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L172-327[»]
5C3FX-ray1.43A173-327[»]
5C6HX-ray2.05A/C/E/G/I/K/M/O/Q/S/U/W171-327[»]
5FC4X-ray1.50A172-320[»]
5FDOX-ray2.80A/B/C/D172-320[»]
5FDRX-ray2.60A/B/C/D172-327[»]
ProteinModelPortaliQ07820.
SMRiQ07820.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110338. 63 interactors.
DIPiDIP-231N.
IntActiQ07820. 28 interactors.
MINTiMINT-89669.
STRINGi9606.ENSP00000358022.

Chemistry databases

BindingDBiQ07820.
ChEMBLiCHEMBL4361.
GuidetoPHARMACOLOGYi2847.

PTM databases

iPTMnetiQ07820.
PhosphoSitePlusiQ07820.

Polymorphism and mutation databases

BioMutaiMCL1.
DMDMi83304396.

Proteomic databases

EPDiQ07820.
MaxQBiQ07820.
PaxDbiQ07820.
PeptideAtlasiQ07820.
PRIDEiQ07820.

Protocols and materials databases

DNASUi4170.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307940; ENSP00000309973; ENSG00000143384. [Q07820-2]
ENST00000369026; ENSP00000358022; ENSG00000143384. [Q07820-1]
GeneIDi4170.
KEGGihsa:4170.
UCSCiuc001euz.4. human. [Q07820-1]

Organism-specific databases

CTDi4170.
DisGeNETi4170.
GeneCardsiMCL1.
HGNCiHGNC:6943. MCL1.
HPAiCAB002781.
CAB068195.
HPA008455.
HPA031125.
MIMi159552. gene.
neXtProtiNX_Q07820.
OpenTargetsiENSG00000143384.
PharmGKBiPA30688.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4728. Eukaryota.
ENOG41123S0. LUCA.
GeneTreeiENSGT00510000048923.
HOVERGENiHBG003527.
InParanoidiQ07820.
KOiK02539.
OMAiAKDTKPM.
OrthoDBiEOG091G0E6Q.
PhylomeDBiQ07820.
TreeFamiTF315834.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143384-MONOMER.
SIGNORiQ07820.

Miscellaneous databases

ChiTaRSiMCL1. human.
EvolutionaryTraceiQ07820.
GeneWikiiMCL1.
GenomeRNAii4170.
PMAP-CutDBQ07820.
PROiQ07820.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143384.
CleanExiHS_MCL1.
ExpressionAtlasiQ07820. baseline and differential.
GenevisibleiQ07820. HS.

Family and domain databases

InterProiIPR013281. Apop_reg_Mc1.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
[Graphical view]
PRINTSiPR01866. APOPREGMCL1.
PR01862. BCL2FAMILY.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCL1_HUMAN
AccessioniPrimary (citable) accession number: Q07820
Secondary accession number(s): B2R6B2
, D3DV03, D3DV04, Q9HD91, Q9NRQ3, Q9NRQ4, Q9UHR7, Q9UHR8, Q9UHR9, Q9UNJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 6, 2005
Last modified: November 30, 2016
This is version 180 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.