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Q9Z1B5

- MD2L1_MOUSE

UniProt

Q9Z1B5 - MD2L1_MOUSE

Protein

Mitotic spindle assembly checkpoint protein MAD2A

Gene

Mad2l1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. mitotic sister chromatid segregation Source: MGI
    2. mitotic spindle assembly checkpoint Source: MGI
    3. negative regulation of apoptotic process Source: UniProtKB
    4. negative regulation of mitotic anaphase-promoting complex activity Source: Ensembl
    5. negative regulation of mitotic metaphase/anaphase transition Source: MGI
    6. negative regulation of protein catabolic process Source: UniProtKB
    7. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitotic spindle assembly checkpoint protein MAD2A
    Alternative name(s):
    Mitotic arrest deficient 2-like protein 1
    Short name:
    MAD2-like protein 1
    Gene namesi
    Name:Mad2l1
    Synonyms:Mad2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1860374. Mad2l1.

    Subcellular locationi

    Nucleus By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonspindle pole By similarity
    Note: Recruited by MAD1L1 to unattached kinetochores By similarity. Recruited to the nuclear pore complex by TPR during interphase By similarity. Recruited to kinetochores in late prometaphase after BUB1, CENPF, BUB1B and CENPE. Kinetochore association requires the presence of NEK2 By similarity.By similarity

    GO - Cellular componenti

    1. chromosome, centromeric region Source: MGI
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. kinetochore Source: MGI
    5. mitotic spindle Source: UniProtKB
    6. nuclear pore Source: Ensembl
    7. nucleus Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. spindle pole Source: MGI

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 205204Mitotic spindle assembly checkpoint protein MAD2APRO_0000126118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei170 – 1701PhosphoserineBy similarity
    Modified residuei195 – 1951PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on multiple serine residues. The level of phosphorylation varies during the cell cycle and is highest during mitosis. Phosphorylation abolishes interaction with MAD1L1 and reduces interaction with CDC20. Phosphorylated by NEK2 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z1B5.
    PaxDbiQ9Z1B5.
    PRIDEiQ9Z1B5.

    PTM databases

    PhosphoSiteiQ9Z1B5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z1B5.
    BgeeiQ9Z1B5.
    GenevestigatoriQ9Z1B5.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Heterotetramer with MAD1L1. Formation of a heterotetrameric core complex containing two molecules each of MAD1L1 and of MAD2L1 promotes binding of another molecule of MAD2L1 to each MAD2L1, resulting in a heterohexamer. Interacts with CDC20, MAD2L1BP and with ADAM17/TACE. Dimeric MAD2L1 in the closed conformation interacts with CDC20. Monomeric MAD2L1 in the open conformation does not interact with CDC20. CDC20 competes with MAD1L1 for MAD2L1 binding. Interacts with TPR. Binds to UBD during mitosis. Kinetochore association is repressed by UBD By similarity. Interacts with NEK2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sgol2Q7TSY83EBI-2552918,EBI-2552468

    Protein-protein interaction databases

    BioGridi207818. 31 interactions.
    IntActiQ9Z1B5. 30 interactions.
    MINTiMINT-123716.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z1B5.
    SMRiQ9Z1B5. Positions 11-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 197184HORMAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni195 – 20511Required for assuming the closed conformation and for interaction with CDC20By similarityAdd
    BLAST

    Domaini

    The protein has two highly different native conformations, an inactive open conformation that cannot bind CDC20 and that predominates in cytosolic monomers, and an active closed conformation. The protein in the closed conformation preferentially dimerizes with another molecule in the open conformation, but can also form a dimer with a molecule in the closed conformation. Formation of a heterotetrameric core complex containing two molecules of MAD1L1 and of MAD2L1 in the closed conformation promotes binding of another molecule of MAD2L1 in the open conformation and the conversion of the open to the closed form, and thereby promotes interaction with CDC20 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the MAD2 family.Curated
    Contains 1 HORMA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG263853.
    GeneTreeiENSGT00390000007908.
    HOGENOMiHOG000199586.
    HOVERGENiHBG105691.
    InParanoidiQ9Z1B5.
    KOiK02537.
    OMAiPREKSIK.
    OrthoDBiEOG7288SG.
    PhylomeDBiQ9Z1B5.
    TreeFamiTF101084.

    Family and domain databases

    Gene3Di3.30.900.10. 1 hit.
    InterProiIPR003511. HORMA_DNA-bd.
    IPR027097. Mad2.
    [Graphical view]
    PANTHERiPTHR11842:SF11. PTHR11842:SF11. 1 hit.
    PfamiPF02301. HORMA. 1 hit.
    [Graphical view]
    SUPFAMiSSF56019. SSF56019. 1 hit.
    PROSITEiPS50815. HORMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Z1B5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQQLAREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG    50
    LTLLTTTDPE LIKYLNNVVE QLKEWLYKCS VQKLVVVISN IESGEVLERW 100
    QFDIECDKTA KEEGVRREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS 150
    FDLLIYTDKD LVVPEKWEES GPQFITNCEE VRLRSFTTTI HKVNSMVAYK 200
    TPVND 205
    Length:205
    Mass (Da):23,598
    Last modified:January 11, 2001 - v2
    Checksum:iA9F3F28BC4C9738E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571T → A in AAD09238. 1 PublicationCurated
    Sequence conflicti178 – 1781C → S in AAD09238. 1 PublicationCurated
    Sequence conflicti201 – 2011T → I in AAD09238. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83902 mRNA. Translation: AAD09238.1.
    AF261919 Genomic DNA. Translation: AAF69525.1.
    AK082934 mRNA. Translation: BAC38700.1.
    CCDSiCCDS20210.1.
    RefSeqiNP_062372.2. NM_019499.4.
    XP_006506469.1. XM_006506406.1.
    UniGeneiMm.489653.

    Genome annotation databases

    EnsembliENSMUST00000101343; ENSMUSP00000098897; ENSMUSG00000029910.
    ENSMUST00000116605; ENSMUSP00000112304; ENSMUSG00000029910.
    GeneIDi56150.
    KEGGimmu:56150.
    UCSCiuc009cen.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U83902 mRNA. Translation: AAD09238.1 .
    AF261919 Genomic DNA. Translation: AAF69525.1 .
    AK082934 mRNA. Translation: BAC38700.1 .
    CCDSi CCDS20210.1.
    RefSeqi NP_062372.2. NM_019499.4.
    XP_006506469.1. XM_006506406.1.
    UniGenei Mm.489653.

    3D structure databases

    ProteinModelPortali Q9Z1B5.
    SMRi Q9Z1B5. Positions 11-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207818. 31 interactions.
    IntActi Q9Z1B5. 30 interactions.
    MINTi MINT-123716.

    PTM databases

    PhosphoSitei Q9Z1B5.

    Proteomic databases

    MaxQBi Q9Z1B5.
    PaxDbi Q9Z1B5.
    PRIDEi Q9Z1B5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000101343 ; ENSMUSP00000098897 ; ENSMUSG00000029910 .
    ENSMUST00000116605 ; ENSMUSP00000112304 ; ENSMUSG00000029910 .
    GeneIDi 56150.
    KEGGi mmu:56150.
    UCSCi uc009cen.1. mouse.

    Organism-specific databases

    CTDi 4085.
    MGIi MGI:1860374. Mad2l1.

    Phylogenomic databases

    eggNOGi NOG263853.
    GeneTreei ENSGT00390000007908.
    HOGENOMi HOG000199586.
    HOVERGENi HBG105691.
    InParanoidi Q9Z1B5.
    KOi K02537.
    OMAi PREKSIK.
    OrthoDBi EOG7288SG.
    PhylomeDBi Q9Z1B5.
    TreeFami TF101084.

    Enzyme and pathway databases

    Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.

    Miscellaneous databases

    NextBioi 311932.
    PROi Q9Z1B5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z1B5.
    Bgeei Q9Z1B5.
    Genevestigatori Q9Z1B5.

    Family and domain databases

    Gene3Di 3.30.900.10. 1 hit.
    InterProi IPR003511. HORMA_DNA-bd.
    IPR027097. Mad2.
    [Graphical view ]
    PANTHERi PTHR11842:SF11. PTHR11842:SF11. 1 hit.
    Pfami PF02301. HORMA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56019. SSF56019. 1 hit.
    PROSITEi PS50815. HORMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel component of the spindle assembly checkpoint in mammalian cells."
      Jin D.-Y., Jeang K.-T.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    2. "Chromosome missegregation and apoptosis in mice lacking the mitotic checkpoint protein Mad2."
      Dobles M., Liberal V., Scott M.L., Benezra R., Sorger P.K.
      Cell 101:635-645(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129.
    3. "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.

    Entry informationi

    Entry nameiMD2L1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z1B5
    Secondary accession number(s): Q9JI53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 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