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Q96BY2

- MOAP1_HUMAN

UniProt

Q96BY2 - MOAP1_HUMAN

Protein

Modulator of apoptosis 1

Gene

MOAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1278Missing: Abrogates interaction with BAX, resulting in a nonapoptotic protein. 2 Publications
    Mutagenesisi120 – 1201L → E: Weakened interaction with BAX, resulting in a nonapoptotic protein. 2 Publications
    Mutagenesisi125 – 1273GHE → VLA: Abrogates interaction with BAX, resulting in a nonapoptotic protein. 1 Publication
    Mutagenesisi161 – 1666KYKKLR → AYAALA: No effect on RASSF1-binding. 1 Publication
    Mutagenesisi178 – 1803EEE → AAA: No effect on RASSF1-binding; interacts with BAX in the absence of RASSF1. 1 Publication
    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 1PRO_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.By similarity

    Protein-protein interaction databases

    BioGridi122069. 13 interactions.
    DIPiDIP-49959N.
    IntActiQ96BY2. 9 interactions.
    MINTiMINT-1438458.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96BY2.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti244 – 2441T → A in BAB14788. (PubMed:14702039)Curated
    Sequence conflicti258 – 2581Y → H in BAB14788. (PubMed:14702039)Curated
    Sequence conflicti259 – 2591Q → H in AAG31786. (PubMed:11060313)Curated

    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.
    DIPi DIP-49959N.
    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

    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: October 1, 2014
    This is version 95 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