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Q9ERH6

- MOAP1_MOUSE

UniProt

Q9ERH6 - MOAP1_MOUSE

Protein

Modulator of apoptosis 1

Gene

Moap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Mar 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 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    2. apoptotic nuclear changes Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modulator of apoptosis 1
    Short name:
    MAP-1
    Gene namesi
    Name:Moap1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1915555. Moap1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Modulator of apoptosis 1PRO_0000155207Add
    BLAST

    Post-translational modificationi

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

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9ERH6.
    PRIDEiQ9ERH6.

    PTM databases

    PhosphoSiteiQ9ERH6.

    Expressioni

    Tissue specificityi

    Widely expressed, including in the brain. High expression levels in testis.1 Publication

    Gene expression databases

    BgeeiQ9ERH6.
    CleanExiMM_MOAP1.
    GenevestigatoriQ9ERH6.

    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 By similarity. Interacts with TRIM39 By similarity. Interacts with RASSF6.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000043336.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni120 – 1278BH3-like
    Regioni204 – 2074RASSF1-bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi335 – 3406Poly-Glu

    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 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the PNMA family.Curated

    Phylogenomic databases

    eggNOGiNOG145999.
    GeneTreeiENSGT00530000062986.
    HOGENOMiHOG000013079.
    HOVERGENiHBG052488.
    InParanoidiQ9ERH6.
    OMAiIPEMWAP.
    OrthoDBiEOG708VZW.
    PhylomeDBiQ9ERH6.
    TreeFamiTF335054.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q9ERH6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLRLLEDWC RGMDMNPRKA LLVAGIPPTC GVADIEEALQ AGLAPLGEHR    50
    LLGRMFRRDE NKNVALIGLT VETGSALVPK EIPAKGGVWR VIFKPPDTDS 100
    DFLCRLNEFL KGEGMTMGEL TRVLGNRNDP LGLDPGIMIP EIRAPMLAQA 150
    LNEALKPTLQ YLRYKKLSVF SGRDPPGPGE EEFESWMFHT SQVMKTWQVS 200
    DVEKRRRLIE SLRGPAFEII RVLKINNPFI TVAECLKTLE TIFGIIDNPR 250
    ALQVKYLTTY QKTDEKLSAY VLRLEPLLQK LVQKGAIEKE VVNQARLDQV 300
    IAGAVHKSVR RELGLPEGSP APGLLQLLTL IKDKEAEEEE VLLQAELEGY 350
    CT 352
    Length:352
    Mass (Da):39,404
    Last modified:March 1, 2001 - v1
    Checksum:i8F4630D080495D98
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571R → K in AAH55374. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305551 mRNA. Translation: AAG31787.1.
    AK019599 mRNA. Translation: BAB31810.1.
    BC014715 mRNA. Translation: AAH14715.1.
    BC055374 mRNA. Translation: AAH55374.1.
    CCDSiCCDS26122.1.
    RefSeqiNP_001136409.1. NM_001142937.2.
    NP_071718.1. NM_022323.7.
    UniGeneiMm.291222.
    Mm.489678.

    Genome annotation databases

    EnsembliENSMUST00000173760; ENSMUSP00000133459; ENSMUSG00000096458.
    ENSMUST00000178384; ENSMUSP00000137010; ENSMUSG00000096458.
    GeneIDi64113.
    KEGGimmu:64113.
    UCSCiuc011yqo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305551 mRNA. Translation: AAG31787.1 .
    AK019599 mRNA. Translation: BAB31810.1 .
    BC014715 mRNA. Translation: AAH14715.1 .
    BC055374 mRNA. Translation: AAH55374.1 .
    CCDSi CCDS26122.1.
    RefSeqi NP_001136409.1. NM_001142937.2.
    NP_071718.1. NM_022323.7.
    UniGenei Mm.291222.
    Mm.489678.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000043336.

    PTM databases

    PhosphoSitei Q9ERH6.

    Proteomic databases

    PaxDbi Q9ERH6.
    PRIDEi Q9ERH6.

    Protocols and materials databases

    DNASUi 64113.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000173760 ; ENSMUSP00000133459 ; ENSMUSG00000096458 .
    ENSMUST00000178384 ; ENSMUSP00000137010 ; ENSMUSG00000096458 .
    GeneIDi 64113.
    KEGGi mmu:64113.
    UCSCi uc011yqo.2. mouse.

    Organism-specific databases

    CTDi 64112.
    MGIi MGI:1915555. Moap1.

    Phylogenomic databases

    eggNOGi NOG145999.
    GeneTreei ENSGT00530000062986.
    HOGENOMi HOG000013079.
    HOVERGENi HBG052488.
    InParanoidi Q9ERH6.
    OMAi IPEMWAP.
    OrthoDBi EOG708VZW.
    PhylomeDBi Q9ERH6.
    TreeFami TF335054.

    Miscellaneous databases

    NextBioi 319919.
    PROi Q9ERH6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ERH6.
    CleanExi MM_MOAP1.
    Genevestigatori Q9ERH6.

    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].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    3. "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].
      Strain: C57BL/6NCr.
      Tissue: Hematopoietic and Kidney.
    4. "RASSF6 is a novel member of the RASSF family of tumor suppressors."
      Allen N.P., Donninger H., Vos M.D., Eckfeld K., Hesson L., Gordon L., Birrer M.J., Latif F., Clark G.J.
      Oncogene 26:6203-6211(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASSF6.
    5. "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.

    Entry informationi

    Entry nameiMOAP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9ERH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 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

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3