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Protein

Modulator of apoptosis 1

Gene

MOAP1

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

Functioni

Required for death receptor-dependent apoptosis. When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation.1 Publication

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • apoptotic signaling pathway Source: BHF-UCL
  • extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
  • extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  • protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165943-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Modulator of apoptosis 1
Short name:
MAP-1
Short name:
MAP1
Alternative name(s):
Paraneoplastic antigen Ma4
Gene namesi
Name:MOAP1
Synonyms:PNMA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:16658. MOAP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: LIFEdb
  • cytosol Source: BHF-UCL
  • mitochondrial outer membrane Source: BHF-UCL
  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi120 – 127Missing : Abrogates interaction with BAX, resulting in a nonapoptotic protein. 1 Publication8
Mutagenesisi120L → E: Weakened interaction with BAX, resulting in a nonapoptotic protein. 1 Publication1
Mutagenesisi125 – 127GHE → VLA: Abrogates interaction with BAX, resulting in a nonapoptotic protein. 1 Publication3
Mutagenesisi161 – 166KYKKLR → AYAALA: No effect on RASSF1-binding. 1 Publication6
Mutagenesisi178 – 180EEE → AAA: No effect on RASSF1-binding; interacts with BAX in the absence of RASSF1. 3
Mutagenesisi202 – 205KRRR → AAAA: Loss of RASSF1-binding; interacts with BAX in the absence of RASSF1. 1 Publication4

Organism-specific databases

DisGeNETi64112.
OpenTargetsiENSG00000165943.
ENSG00000278268.
PharmGKBiPA134908381.

Polymorphism and mutation databases

BioMutaiMOAP1.
DMDMi37999755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001552051 – 351Modulator of apoptosis 1Add BLAST351

Post-translational modificationi

Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this modification is inhibited by TRIM39.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ96BY2.
PaxDbiQ96BY2.
PeptideAtlasiQ96BY2.
PRIDEiQ96BY2.

PTM databases

iPTMnetiQ96BY2.
PhosphoSitePlusiQ96BY2.

Expressioni

Tissue specificityi

Widely expressed, with high levels in heart and brain.1 Publication

Gene expression databases

BgeeiENSG00000165943.
CleanExiHS_MOAP1.
GenevisibleiQ96BY2. HS.

Organism-specific databases

HPAiHPA000939.

Interactioni

Subunit structurei

Homodimer. Under normal circumstances, held in an inactive conformation by an intramolecular interaction. Binding to RASSF1 isoform A (RASSF1A) relieves this inhibitory interaction and allows further binding to BAX. Binds also to BCL2 and BCLX. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their respective cognate ligand, after internalization. Interacts with TRIM39. Interacts with RASSF6 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CAMK2DQ135573EBI-739825,EBI-351018
LATS1Q6PJG33EBI-739825,EBI-10253976
MBIPQ9NS73-53EBI-739825,EBI-10182361
PNMA5Q96PV43EBI-739825,EBI-10171633
THOC1Q96FV95EBI-739825,EBI-1765605

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi122069. 24 interactors.
DIPiDIP-49959N.
IntActiQ96BY2. 16 interactors.
MINTiMINT-1438458.
STRINGi9606.ENSP00000298894.

Structurei

3D structure databases

ProteinModelPortaliQ96BY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni120 – 127BH3-like8
Regioni202 – 205RASSF1-binding4

Domaini

The BH3-like domain is required for association with BAX and for mediating apoptosis. The three BH domains (BH1, BH2, and BH3) of BAX are all required for mediating protein-protein interaction.

Sequence similaritiesi

Belongs to the PNMA family.Curated

Phylogenomic databases

eggNOGiENOG410IIH9. Eukaryota.
ENOG410YK5I. LUCA.
GeneTreeiENSGT00530000062986.
HOGENOMiHOG000013079.
HOVERGENiHBG052488.
InParanoidiQ96BY2.
OMAiIPEMWAP.
OrthoDBiEOG091G0BG9.
PhylomeDBiQ96BY2.
TreeFamiTF335054.

Family and domain databases

InterProiIPR026523. PNMA.
[Graphical view]
PANTHERiPTHR23095. PTHR23095. 1 hit.
PfamiPF14893. PNMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96BY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLRLLEDWC RGMDMNPRKA LLIAGISQSC SVAEIEEALQ AGLAPLGEYR
60 70 80 90 100
LLGRMFRRDE NRKVALVGLT AETSHALVPK EIPGKGGIWR VIFKPPDPDN
110 120 130 140 150
TFLSRLNEFL AGEGMTVGEL SRALGHENGS LDPEQGMIPE MWAPMLAQAL
160 170 180 190 200
EALQPALQCL KYKKLRVFSG RESPEPGEEE FGRWMFHTTQ MIKAWQVPDV
210 220 230 240 250
EKRRRLLESL RGPALDVIRV LKINNPLITV DECLQALEEV FGVTDNPREL
260 270 280 290 300
QVKYLTTYQK DEEKLSAYVL RLEPLLQKLV QRGAIERDAV NQARLDQVIA
310 320 330 340 350
GAVHKTIRRE LNLPEDGPAP GFLQLLVLIK DYEAAEEEEA LLQAILEGNF

T
Length:351
Mass (Da):39,513
Last modified:December 1, 2001 - v1
Checksum:i5310142AC02B563C
GO

Sequence cautioni

The sequence BAB14788 differs from that shown. Reason: Frameshift at position 102.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti244T → A in BAB14788 (PubMed:14702039).Curated1
Sequence conflicti258Y → H in BAB14788 (PubMed:14702039).Curated1
Sequence conflicti259Q → H in AAG31786 (PubMed:11060313).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305550 mRNA. Translation: AAG31786.1.
AK024029 mRNA. Translation: BAB14788.1. Sequence problems.
AK315522 mRNA. Translation: BAG37903.1.
CH471061 Genomic DNA. Translation: EAW81516.1.
BC015044 mRNA. Translation: AAH15044.1.
CCDSiCCDS9908.1.
RefSeqiNP_071434.2. NM_022151.4.
UniGeneiHs.24719.

Genome annotation databases

EnsembliENST00000298894; ENSP00000298894; ENSG00000165943.
ENST00000556883; ENSP00000451594; ENSG00000165943.
ENST00000616515; ENSP00000482284; ENSG00000278268.
ENST00000627896; ENSP00000486260; ENSG00000278268.
GeneIDi64112.
KEGGihsa:64112.
UCSCiuc001ybj.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305550 mRNA. Translation: AAG31786.1.
AK024029 mRNA. Translation: BAB14788.1. Sequence problems.
AK315522 mRNA. Translation: BAG37903.1.
CH471061 Genomic DNA. Translation: EAW81516.1.
BC015044 mRNA. Translation: AAH15044.1.
CCDSiCCDS9908.1.
RefSeqiNP_071434.2. NM_022151.4.
UniGeneiHs.24719.

3D structure databases

ProteinModelPortaliQ96BY2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122069. 24 interactors.
DIPiDIP-49959N.
IntActiQ96BY2. 16 interactors.
MINTiMINT-1438458.
STRINGi9606.ENSP00000298894.

PTM databases

iPTMnetiQ96BY2.
PhosphoSitePlusiQ96BY2.

Polymorphism and mutation databases

BioMutaiMOAP1.
DMDMi37999755.

Proteomic databases

MaxQBiQ96BY2.
PaxDbiQ96BY2.
PeptideAtlasiQ96BY2.
PRIDEiQ96BY2.

Protocols and materials databases

DNASUi64112.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298894; ENSP00000298894; ENSG00000165943.
ENST00000556883; ENSP00000451594; ENSG00000165943.
ENST00000616515; ENSP00000482284; ENSG00000278268.
ENST00000627896; ENSP00000486260; ENSG00000278268.
GeneIDi64112.
KEGGihsa:64112.
UCSCiuc001ybj.4. human.

Organism-specific databases

CTDi64112.
DisGeNETi64112.
GeneCardsiMOAP1.
HGNCiHGNC:16658. MOAP1.
HPAiHPA000939.
MIMi609485. gene.
neXtProtiNX_Q96BY2.
OpenTargetsiENSG00000165943.
ENSG00000278268.
PharmGKBiPA134908381.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIH9. Eukaryota.
ENOG410YK5I. LUCA.
GeneTreeiENSGT00530000062986.
HOGENOMiHOG000013079.
HOVERGENiHBG052488.
InParanoidiQ96BY2.
OMAiIPEMWAP.
OrthoDBiEOG091G0BG9.
PhylomeDBiQ96BY2.
TreeFamiTF335054.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165943-MONOMER.

Miscellaneous databases

ChiTaRSiMOAP1. human.
GeneWikiiMOAP1.
GenomeRNAii64112.
PROiQ96BY2.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165943.
CleanExiHS_MOAP1.
GenevisibleiQ96BY2. HS.

Family and domain databases

InterProiIPR026523. PNMA.
[Graphical view]
PANTHERiPTHR23095. PTHR23095. 1 hit.
PfamiPF14893. PNMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMOAP1_HUMAN
AccessioniPrimary (citable) accession number: Q96BY2
Secondary accession number(s): B2RDF6, Q9H833, Q9HAS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 114 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.