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Q96BY2

- MOAP1_HUMAN

UniProt

Q96BY2 - MOAP1_HUMAN

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Protein
Modulator of apoptosis 1
Gene
MOAP1, PNMA4
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. protein binding Source: HGNC
  2. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

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

Keywords - Biological processi

Apoptosis

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:16658. MOAP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: BHF-UCL
  3. mitochondrial outer membrane Source: BHF-UCL
  4. mitochondrion Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1278Missing: Abrogates interaction with BAX, resulting in a nonapoptotic protein. 1 Publication
Mutagenesisi120 – 1201L → E: Weakened interaction with BAX, resulting in a nonapoptotic protein. 1 Publication
Mutagenesisi125 – 1273GHE → VLA: Abrogates interaction with BAX, resulting in a nonapoptotic protein. 1 Publication
Mutagenesisi161 – 1666KYKKLR → AYAALA: No effect on RASSF1-binding.
Mutagenesisi178 – 1803EEE → AAA: No effect on RASSF1-binding; interacts with BAX in the absence of RASSF1.
Mutagenesisi202 – 2054KRRR → AAAA: Loss of RASSF1-binding; interacts with BAX in the absence of RASSF1. 1 Publication

Organism-specific databases

PharmGKBiPA134908381.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Modulator of apoptosis 1
PRO_0000155205Add
BLAST

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

PaxDbiQ96BY2.
PRIDEiQ96BY2.

PTM databases

PhosphoSiteiQ96BY2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ96BY2.
CleanExiHS_MOAP1.
GenevestigatoriQ96BY2.

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.2 Publications

Protein-protein interaction databases

BioGridi122069. 13 interactions.
IntActiQ96BY2. 9 interactions.
MINTiMINT-1438458.

Structurei

3D structure databases

ProteinModelPortaliQ96BY2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1278BH3-like
Regioni202 – 2054RASSF1-binding

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.

Phylogenomic databases

eggNOGiNOG145999.
HOGENOMiHOG000013079.
HOVERGENiHBG052488.
InParanoidiQ96BY2.
OMAiIPEMWAP.
OrthoDBiEOG708VZW.
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

MTLRLLEDWC RGMDMNPRKA LLIAGISQSC SVAEIEEALQ AGLAPLGEYR    50
LLGRMFRRDE NRKVALVGLT AETSHALVPK EIPGKGGIWR VIFKPPDPDN 100
TFLSRLNEFL AGEGMTVGEL SRALGHENGS LDPEQGMIPE MWAPMLAQAL 150
EALQPALQCL KYKKLRVFSG RESPEPGEEE FGRWMFHTTQ MIKAWQVPDV 200
EKRRRLLESL RGPALDVIRV LKINNPLITV DECLQALEEV FGVTDNPREL 250
QVKYLTTYQK DEEKLSAYVL RLEPLLQKLV QRGAIERDAV NQARLDQVIA 300
GAVHKTIRRE LNLPEDGPAP GFLQLLVLIK DYEAAEEEEA LLQAILEGNF 350
T 351
Length:351
Mass (Da):39,513
Last modified:December 1, 2001 - v1
Checksum:i5310142AC02B563C
GO

Sequence cautioni

The sequence BAB14788.1 differs from that shown. Reason: Frameshift at position 102.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441T → A in BAB14788. 1 Publication
Sequence conflicti258 – 2581Y → H in BAB14788. 1 Publication
Sequence conflicti259 – 2591Q → H in AAG31786. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi64112.
KEGGihsa:64112.
UCSCiuc001ybj.3. human.

Polymorphism databases

DMDMi37999755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9908.1.
RefSeqi NP_071434.2. NM_022151.4.
UniGenei Hs.24719.

3D structure databases

ProteinModelPortali Q96BY2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122069. 13 interactions.
IntActi Q96BY2. 9 interactions.
MINTi MINT-1438458.

PTM databases

PhosphoSitei Q96BY2.

Polymorphism databases

DMDMi 37999755.

Proteomic databases

PaxDbi Q96BY2.
PRIDEi Q96BY2.

Protocols and materials databases

DNASUi 64112.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298894 ; ENSP00000298894 ; ENSG00000165943 .
ENST00000556883 ; ENSP00000451594 ; ENSG00000165943 .
GeneIDi 64112.
KEGGi hsa:64112.
UCSCi uc001ybj.3. human.

Organism-specific databases

CTDi 64112.
GeneCardsi GC14M093648.
HGNCi HGNC:16658. MOAP1.
HPAi HPA000939.
MIMi 609485. gene.
neXtProti NX_Q96BY2.
PharmGKBi PA134908381.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145999.
HOGENOMi HOG000013079.
HOVERGENi HBG052488.
InParanoidi Q96BY2.
OMAi IPEMWAP.
OrthoDBi EOG708VZW.
PhylomeDBi Q96BY2.
TreeFami TF335054.

Miscellaneous databases

ChiTaRSi MOAP1. human.
GeneWikii MOAP1.
GenomeRNAii 64112.
NextBioi 65976.
PROi Q96BY2.
SOURCEi Search...

Gene expression databases

Bgeei Q96BY2.
CleanExi HS_MOAP1.
Genevestigatori Q96BY2.

Family and domain databases

InterProi IPR026523. PNMA.
[Graphical view ]
PANTHERi PTHR23095. PTHR23095. 1 hit.
Pfami PF14893. PNMA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains."
    Tan K.O., Tan K.M.L., Chan S.-L., Yee K.S.Y., Bevort M., Ang K.C., Yu V.C.
    J. Biol. Chem. 276:2802-2807(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MUTAGENESIS OF LEU-120; 120-LEU--ARG-127 AND 125-GLY--GLU-127.
    Tissue: Cerebellum.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retinoblastoma and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  5. "The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death."
    Baksh S., Tommasi S., Fenton S., Yu V.C., Martins L.M., Pfeifer G.P., Latif F., Downward J., Neel B.G.
    Mol. Cell 18:637-650(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASSF1, INTRAMOLECULAR INTERACTION, MUTAGENESIS OF 161-LYS--ARG-166; 178-GLU--ALA-181 AND 202-LYS--ARG-205, FUNCTION.
  6. "Paraneoplastic antigen-like 5 gene (PNMA5) is preferentially expressed in the association areas in a primate specific manner."
    Takaji M., Komatsu Y., Watakabe A., Hashikawa T., Yamamori T.
    Cereb. Cortex 19:2865-2879(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process."
    Lee S.S., Fu N.Y., Sukumaran S.K., Wan K.F., Wan Q., Yu V.C.
    Exp. Cell Res. 315:1313-1325(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM39.
  8. "The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1."
    Huang N.J., Zhang L., Tang W., Chen C., Yang C.S., Kornbluth S.
    J. Cell Biol. 197:361-367(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY APC/C-CDH1.

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: July 9, 2014
This is version 94 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

External Data

Dasty 3

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