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Q13257

- MD2L1_HUMAN

UniProt

Q13257 - MD2L1_HUMAN

Protein

Mitotic spindle assembly checkpoint protein MAD2A

Gene

MAD2L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.3 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. mitotic cell cycle Source: Reactome
    3. mitotic cell cycle checkpoint Source: UniProtKB
    4. mitotic sister chromatid segregation Source: Ensembl
    5. mitotic spindle assembly checkpoint Source: Reactome
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of mitotic anaphase-promoting complex activity Source: UniProtKB
    8. negative regulation of mitotic cell cycle Source: MGI
    9. negative regulation of protein catabolic process Source: UniProtKB
    10. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    11. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
    12. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_1041. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
    REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_491. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitotic spindle assembly checkpoint protein MAD2A
    Short name:
    HsMAD2
    Alternative name(s):
    Mitotic arrest deficient 2-like protein 1
    Short name:
    MAD2-like protein 1
    Gene namesi
    Name:MAD2L1
    Synonyms:MAD2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6763. MAD2L1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytosol Source: UniProtKB
    3. kinetochore Source: UniProtKB
    4. mitotic spindle Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB
    7. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131L → A: Leads to formation the closed conformation and homodimerization. 1 Publication
    Mutagenesisi75 – 751W → A: Prevents interaction with CDC20 and leads to formation of the closed conformation; when associated with A-133. 1 Publication
    Mutagenesisi133 – 1331R → A: Prevents aggregation and promotes formation of monomeric protein that slowly interconverts between the open and closed conformation. 1 Publication
    Mutagenesisi153 – 1531L → A: Leads to formation of the closed conformation; when associated with A-133. 1 Publication
    Mutagenesisi156 – 1561Y → A: Leads to formation of the closed conformation; when associated with A-133. 1 Publication
    Mutagenesisi170 – 1701S → A: Reduces phosphorylation on serine residues; when associated with A-178. Abolishes phosphorylation on serine residues; when associated with A-178 and A-195. 1 Publication
    Mutagenesisi170 – 1701S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-178 and D-195. 1 Publication
    Mutagenesisi178 – 1781S → A: Reduces phosphorylation on serine residues; when associated with A-170. Abolishes phosphorylation on serine residues; when associated with A-170 and A-195. 1 Publication
    Mutagenesisi178 – 1781S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-195. 1 Publication
    Mutagenesisi186 – 1861F → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. 1 Publication
    Mutagenesisi188 – 1881T → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. 1 Publication
    Mutagenesisi191 – 1911H → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. 1 Publication
    Mutagenesisi195 – 1951S → A: Abolishes phosphorylation on serine residues; when associated with A-170 and A-178. 1 Publication
    Mutagenesisi195 – 1951S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-178. 1 Publication
    Mutagenesisi197 – 1971V → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. 1 Publication
    Mutagenesisi199 – 1991Y → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. 1 Publication

    Organism-specific databases

    PharmGKBiPA30521.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 205204Mitotic spindle assembly checkpoint protein MAD2APRO_0000126117Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei170 – 1701Phosphoserine2 Publications
    Modified residuei178 – 1781Phosphoserine2 Publications
    Modified residuei195 – 1951Phosphoserine2 Publications

    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 NEK2.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13257.
    PaxDbiQ13257.
    PeptideAtlasiQ13257.
    PRIDEiQ13257.

    PTM databases

    PhosphoSiteiQ13257.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13257.
    BgeeiQ13257.
    CleanExiHS_MAD2L1.
    GenevestigatoriQ13257.

    Organism-specific databases

    HPAiHPA003348.

    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. Interacts with isoform 1 and isoform 2 of NEK2.14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-78203,EBI-78203
    ADAM17P785363EBI-78203,EBI-78188
    CDC20Q1283416EBI-78203,EBI-367462
    MAD1L1Q9Y6D911EBI-78203,EBI-742610
    MAD2L1BPQ150137EBI-78203,EBI-712181
    SGOL2Q562F610EBI-78203,EBI-989213

    Protein-protein interaction databases

    BioGridi110260. 47 interactions.
    DIPiDIP-29653N.
    IntActiQ13257. 29 interactions.
    MINTiMINT-108270.
    STRINGi9606.ENSP00000296509.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Beta strandi7 – 93
    Helixi13 – 3422
    Helixi40 – 423
    Beta strandi43 – 486
    Beta strandi51 – 566
    Helixi59 – 7719
    Beta strandi78 – 803
    Beta strandi81 – 9010
    Turni91 – 933
    Beta strandi96 – 10611
    Helixi108 – 1114
    Beta strandi116 – 1183
    Helixi121 – 13919
    Beta strandi149 – 1579
    Helixi160 – 1623
    Beta strandi167 – 1693
    Beta strandi173 – 1753
    Beta strandi177 – 1826
    Beta strandi189 – 20012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DUJNMR-A11-195[»]
    1GO4X-ray2.05A/B/C/D1-205[»]
    1KLQNMR-A11-205[»]
    1S2HNMR-A1-205[»]
    2QYFX-ray2.30A/C1-205[»]
    2V64X-ray2.90A/C/F2-205[»]
    D/E/H118-205[»]
    2VFXX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L1-205[»]
    3GMHX-ray3.95A/B/C/D/E/F/G/H/I/J/K/L11-205[»]
    ProteinModelPortaliQ13257.
    SMRiQ13257. Positions 2-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13257.

    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 CDC20Add
    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 CDC20.5 Publications

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG263853.
    HOGENOMiHOG000199586.
    HOVERGENiHBG105691.
    InParanoidiQ13257.
    KOiK02537.
    OMAiPREKSIK.
    OrthoDBiEOG7288SG.
    PhylomeDBiQ13257.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13257-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG    50
    LTLLVTTDLE LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW 100
    QFDIECDKTA KDDSAPREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS 150
    FDLLIYTDKD LVVPEKWEES GPQFITNSEE VRLRSFTTTI HKVNSMVAYK 200
    IPVND 205
    Length:205
    Mass (Da):23,510
    Last modified:November 1, 1996 - v1
    Checksum:iB8DCBF0043836764
    GO
    Isoform 2 (identifier: Q13257-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-90: DWLYKCSVQKLVVVISN → VHPEKSLRKLSRMKSVQ
         91-205: Missing.

    Show »
    Length:90
    Mass (Da):10,335
    Checksum:i8209F5A7A7D8D09B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161S → C in BAD97153. 1 PublicationCurated
    Sequence conflicti190 – 1901I → V in AAH70283. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei74 – 9017DWLYK…VVISN → VHPEKSLRKLSRMKSVQ in isoform 2. 2 PublicationsVSP_047644Add
    BLAST
    Alternative sequencei91 – 205115Missing in isoform 2. 2 PublicationsVSP_047645Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65410 mRNA. Translation: AAC50781.1.
    AF202273
    , AF202269, AF202270, AF202271, AF202272 Genomic DNA. Translation: AAK38174.1.
    U31278 mRNA. Translation: AAC52060.1.
    AJ000186 mRNA. Translation: CAA03943.1.
    AB056160 Genomic DNA. Translation: BAB63410.1.
    AF394735 mRNA. Translation: AAN74648.1.
    AK298228 mRNA. Translation: BAG60497.1.
    AK313827 mRNA. Translation: BAG36562.1.
    AK223433 mRNA. Translation: BAD97153.1.
    AC097173 Genomic DNA. Translation: AAY40945.1.
    CH471056 Genomic DNA. Translation: EAX05271.1.
    CH471056 Genomic DNA. Translation: EAX05273.1.
    BC000356 mRNA. Translation: AAH00356.1.
    BC005945 mRNA. Translation: AAH05945.1.
    BC070283 mRNA. Translation: AAH70283.1.
    CCDSiCCDS3715.1. [Q13257-1]
    PIRiG01942.
    RefSeqiNP_002349.1. NM_002358.3. [Q13257-1]
    UniGeneiHs.591697.

    Genome annotation databases

    EnsembliENST00000296509; ENSP00000296509; ENSG00000164109. [Q13257-1]
    ENST00000333047; ENSP00000332295; ENSG00000164109. [Q13257-2]
    GeneIDi4085.
    KEGGihsa:4085.
    UCSCiuc003idl.2. human. [Q13257-1]
    uc003idm.2. human.

    Polymorphism databases

    DMDMi12230256.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65410 mRNA. Translation: AAC50781.1 .
    AF202273
    , AF202269 , AF202270 , AF202271 , AF202272 Genomic DNA. Translation: AAK38174.1 .
    U31278 mRNA. Translation: AAC52060.1 .
    AJ000186 mRNA. Translation: CAA03943.1 .
    AB056160 Genomic DNA. Translation: BAB63410.1 .
    AF394735 mRNA. Translation: AAN74648.1 .
    AK298228 mRNA. Translation: BAG60497.1 .
    AK313827 mRNA. Translation: BAG36562.1 .
    AK223433 mRNA. Translation: BAD97153.1 .
    AC097173 Genomic DNA. Translation: AAY40945.1 .
    CH471056 Genomic DNA. Translation: EAX05271.1 .
    CH471056 Genomic DNA. Translation: EAX05273.1 .
    BC000356 mRNA. Translation: AAH00356.1 .
    BC005945 mRNA. Translation: AAH05945.1 .
    BC070283 mRNA. Translation: AAH70283.1 .
    CCDSi CCDS3715.1. [Q13257-1 ]
    PIRi G01942.
    RefSeqi NP_002349.1. NM_002358.3. [Q13257-1 ]
    UniGenei Hs.591697.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DUJ NMR - A 11-195 [» ]
    1GO4 X-ray 2.05 A/B/C/D 1-205 [» ]
    1KLQ NMR - A 11-205 [» ]
    1S2H NMR - A 1-205 [» ]
    2QYF X-ray 2.30 A/C 1-205 [» ]
    2V64 X-ray 2.90 A/C/F 2-205 [» ]
    D/E/H 118-205 [» ]
    2VFX X-ray 1.95 A/B/C/D/E/F/G/H/I/J/K/L 1-205 [» ]
    3GMH X-ray 3.95 A/B/C/D/E/F/G/H/I/J/K/L 11-205 [» ]
    ProteinModelPortali Q13257.
    SMRi Q13257. Positions 2-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110260. 47 interactions.
    DIPi DIP-29653N.
    IntActi Q13257. 29 interactions.
    MINTi MINT-108270.
    STRINGi 9606.ENSP00000296509.

    PTM databases

    PhosphoSitei Q13257.

    Polymorphism databases

    DMDMi 12230256.

    Proteomic databases

    MaxQBi Q13257.
    PaxDbi Q13257.
    PeptideAtlasi Q13257.
    PRIDEi Q13257.

    Protocols and materials databases

    DNASUi 4085.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296509 ; ENSP00000296509 ; ENSG00000164109 . [Q13257-1 ]
    ENST00000333047 ; ENSP00000332295 ; ENSG00000164109 . [Q13257-2 ]
    GeneIDi 4085.
    KEGGi hsa:4085.
    UCSCi uc003idl.2. human. [Q13257-1 ]
    uc003idm.2. human.

    Organism-specific databases

    CTDi 4085.
    GeneCardsi GC04M120980.
    HGNCi HGNC:6763. MAD2L1.
    HPAi HPA003348.
    MIMi 601467. gene.
    neXtProti NX_Q13257.
    PharmGKBi PA30521.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263853.
    HOGENOMi HOG000199586.
    HOVERGENi HBG105691.
    InParanoidi Q13257.
    KOi K02537.
    OMAi PREKSIK.
    OrthoDBi EOG7288SG.
    PhylomeDBi Q13257.
    TreeFami TF101084.

    Enzyme and pathway databases

    Reactomei REACT_1041. Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
    REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_491. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi MAD2L1. human.
    EvolutionaryTracei Q13257.
    GeneWikii MAD2L1.
    GenomeRNAii 4085.
    NextBioi 16010.
    PROi Q13257.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13257.
    Bgeei Q13257.
    CleanExi HS_MAD2L1.
    Genevestigatori Q13257.

    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 human mitotic checkpoint gene: hsMAD2."
      Li Y., Benezra R.
      Science 274:246-248(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic structure of the human MAD2 gene and mutation analysis in human lung and breast cancers."
      Gemma A., Hosoya Y., Seike M., Uematsu K., Kurimoto F., Hibino S., Yoshimura A., Shibuya M., Kudoh S., Emi M.
      Lung Cancer 32:289-295(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Jin D.-Y., Jeang K.-T.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Klebert S., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Complete human MAD2 gene."
      Nobori T.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Identifying a new variant of MAD2L1."
      Yin F., Fan D.M.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    7. "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] (ISOFORMS 1 AND 2).
      Tissue: Lung.
    8. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    9. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM 1).
      Tissue: Bone marrow and Muscle.
    12. Bienvenut W.V., Dhillon A.S., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-7; 36-45; 123-129 AND 193-205, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    13. "The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation."
      Fang G., Yu H., Kirschner M.W.
      Genes Dev. 12:1871-1883(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC20.
    14. "Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2-beta."
      Nelson K.K., Schlondorff J., Blobel C.P.
      Biochem. J. 343:673-680(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADAM17.
    15. "Identification of a MAD2-binding protein, CMT2, and its role in mitosis."
      Habu T., Kim S.H., Weinstein J., Matsumoto T.
      EMBO J. 21:6419-6428(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAD2L1BP.
    16. "Mad2 phosphorylation regulates its association with Mad1 and the APC/C."
      Wassmann K., Liberal V., Benezra R.
      EMBO J. 22:797-806(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-170; SER-178 AND SER-195, INTERACTION WITH MAD1L1 AND CDC20, MUTAGENESIS OF SER-170; SER-178 AND SER-195.
    17. "NEK2A interacts with MAD1 and possibly functions as a novel integrator of the spindle checkpoint signaling."
      Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J., Wang Y., Yao X.
      J. Biol. Chem. 279:20049-20057(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression."
      Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.
      J. Cell Sci. 117:1577-1589(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH UBD.
    20. "Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint."
      Lee S.H., Sterling H., Burlingame A., McCormick F.
      Genes Dev. 22:2926-2931(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TPR; MAD1L1 AND CDC20, SUBCELLULAR LOCATION.
    21. "Perturbation of the chromosomal binding of RCC1, Mad2 and survivin causes spindle assembly defects and mitotic catastrophe."
      Ho C.-Y., Wong C.-H., Li H.-Y.
      J. Cell. Biochem. 105:835-846(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. "The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational switching."
      Skinner J.J., Wood S., Shorter J., Englander S.W., Black B.E.
      J. Cell Biol. 183:761-768(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    23. "Nek2 targets the mitotic checkpoint proteins Mad2 and Cdc20: a mechanism for aneuploidy in cancer."
      Liu Q., Hirohashi Y., Du X., Greene M.I., Wang Q.
      Exp. Mol. Pathol. 88:225-233(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20."
      Luo X., Fang G., Coldiron M., Lin Y., Yu H., Kirschner M.W., Wagner G.
      Nat. Struct. Biol. 7:224-229(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 11-195, FUNCTION, DOMAIN, INTERACTION WITH CDC20.
    26. "Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint."
      Sironi L., Mapelli M., Knapp S., De Antoni A., Jeang K.-T., Musacchio A.
      EMBO J. 21:2496-2506(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT ALA-133 IN COMPLEX WITH MAD1L1, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-133, INTERACTION WITH MAD1L1.
    27. "The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20."
      Luo X., Tang Z., Rizo J., Yu H.
      Mol. Cell 9:59-71(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 11-205 IN COMPLEX WITH PEPTIDE LIGAND, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH CDC20 AND MAD1L1.
    28. "The Mad2 spindle checkpoint protein has two distinct natively folded states."
      Luo X., Tang Z., Xia G., Wassmann K., Matsumoto T., Rizo J., Yu H.
      Nat. Struct. Mol. Biol. 11:338-345(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, DOMAIN, SUBUNIT, FUNCTION, INTERACTION WITH MAD1L1, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint."
      Mapelli M., Massimiliano L., Santaguida S., Musacchio A.
      Cell 131:730-743(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF DIMER CONTAINING BOTH CONFORMERS, INTERACTION OF THE TWO MAD2L1 CONFORMERS.
    30. "p31comet blocks Mad2 activation through structural mimicry."
      Yang M., Li B., Tomchick D.R., Machius M., Rizo J., Yu H., Luo X.
      Cell 131:744-755(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEXES WITH MAD2L1BP, INTERACTION WITH MAD2L1BP.
    31. "Insights into Mad2 regulation in the spindle checkpoint revealed by the crystal structure of the symmetric Mad2 dimer."
      Yang M., Li B., Liu C.-J., Tomchick D.R., Machius M., Rizo J., Yu H., Luo X.
      PLoS Biol. 6:E50-E50(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF HOMODIMER OF MUTANT ALA-13 IN THE CLOSED CONFORMATION, DOMAIN, SUBUNIT, MUTAGENESIS OF LEU-13; TRP-75; LEU-153; TYR-156; PHE-186; THR-188; HIS-191; VAL-197 AND TYR-199.

    Entry informationi

    Entry nameiMD2L1_HUMAN
    AccessioniPrimary (citable) accession number: Q13257
    Secondary accession number(s): Q53F56
    , Q548X9, Q6IRW7, Q8IZX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 146 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3