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Q9UI95

- MD2L2_HUMAN

UniProt

Q9UI95 - MD2L2_HUMAN

Protein

Mitotic spindle assembly checkpoint protein MAD2B

Gene

MAD2L2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.5 Publications

    GO - Molecular functioni

    1. JUN kinase binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA polymerase II activating transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. actin filament organization Source: BHF-UCL
    2. DNA damage response, signal transduction resulting in transcription Source: UniProtKB
    3. DNA repair Source: Reactome
    4. double-strand break repair Source: UniProtKB
    5. mitotic nuclear division Source: UniProtKB-KW
    6. mitotic spindle assembly checkpoint Source: ProtInc
    7. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
    8. negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
    9. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
    10. negative regulation of mitotic anaphase-promoting complex activity Source: UniProtKB
    11. negative regulation of protein catabolic process Source: UniProtKB
    12. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    13. negative regulation of transcription by competitive promoter binding Source: BHF-UCL
    14. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    15. negative regulation of transcription regulatory region DNA binding Source: BHF-UCL
    16. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
    17. positive regulation of transcription, DNA-templated Source: UniProtKB
    18. regulation of cell growth Source: UniProtKB
    19. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, Mitosis, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_822. Translesion synthesis by Pol zeta.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitotic spindle assembly checkpoint protein MAD2B
    Alternative name(s):
    Mitotic arrest deficient 2-like protein 2
    Short name:
    MAD2-like protein 2
    REV7 homolog
    Short name:
    hREV7
    Gene namesi
    Name:MAD2L2
    Synonyms:MAD2B, REV7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6764. MAD2L2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. spindle Source: UniProtKB
    5. zeta DNA polymerase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631Y → A: Alters interaction with REV3L. Loss of interaction with REV3L; when associated with A-171. 1 Publication
    Mutagenesisi124 – 1241R → A: Induces structural changes that increase affinity for REV3L and REV1. No effect on interaction with REV1; when associated with A-171. 1 Publication
    Mutagenesisi171 – 1711W → A: Alters interaction with REV3L and REV1. Loss of interaction with REV3L; when associated with A-63. No effect on interaction with REV1; when associated with A-124. 1 Publication
    Mutagenesisi186 – 1861L → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication
    Mutagenesisi200 – 2001Q → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication
    Mutagenesisi202 – 2021Y → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication

    Organism-specific databases

    PharmGKBiPA398.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Mitotic spindle assembly checkpoint protein MAD2BPRO_0000126119Add
    BLAST

    Proteomic databases

    MaxQBiQ9UI95.
    PaxDbiQ9UI95.
    PRIDEiQ9UI95.

    PTM databases

    PhosphoSiteiQ9UI95.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9UI95.
    BgeeiQ9UI95.
    CleanExiHS_MAD2L2.
    GenevestigatoriQ9UI95.

    Organism-specific databases

    HPAiCAB008110.

    Interactioni

    Subunit structurei

    Homooligomer Probable. Interacts with REV1. Interacts with ADAM9. Interacts with CHAMP1. Interacts with REV3L. Interacts with FZR1 (in complex with the anaphase promoting complex APC). Interacts with CDC20; PubMed:11459825 could not detect the interaction. Interacts with RAN. Interacts with ELK1; the interaction is direct and recruits MAD2L2 to ELK1-specific promoters. May interact with the JNK kinases MAPK8 and/or MAPK9 to stimulate ELK1 phosphorylation and transcriptional activity upon DNA damage. Interacts with TCF7L2; prevents its binding to promoters and negatively modulates its transcriptional activity. Interacts with YY1AP1. Interacts with S.flexneri protein ipaB; prevents the interaction of MAD2L2 with FZR1 and CDC20 resulting in an activation of the anaphase-promoting complex APC and a cell cycle arrest. Interacts with PRCC; the interaction is direct. Interacts with POGZ.14 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAM9Q134433EBI-77889,EBI-77903
    CDC20Q128342EBI-77889,EBI-367462
    CDC27P302602EBI-77889,EBI-994813
    CHAMP1Q96JM33EBI-77889,EBI-2560420
    FZR1Q9UM112EBI-77889,EBI-724997
    ipaBP180117EBI-77889,EBI-490239From a different organism.
    REV3LO606735EBI-77889,EBI-2871302

    Protein-protein interaction databases

    BioGridi115722. 22 interactions.
    IntActiQ9UI95. 13 interactions.
    MINTiMINT-108350.
    STRINGi9606.ENSP00000235310.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 3321
    Helixi39 – 413
    Beta strandi42 – 476
    Beta strandi50 – 556
    Helixi58 – 7619
    Beta strandi80 – 889
    Beta strandi90 – 923
    Beta strandi94 – 10310
    Helixi115 – 13117
    Helixi133 – 1353
    Beta strandi145 – 1528
    Helixi157 – 1637
    Beta strandi171 – 1733
    Helixi176 – 1794
    Beta strandi182 – 19312
    Beta strandi198 – 20710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ABDX-ray1.90A/B1-211[»]
    3ABEX-ray2.60C1-211[»]
    3VU7X-ray2.80C1-211[»]
    4EXTX-ray1.90C7-209[»]
    4GK0X-ray2.70A/B1-211[»]
    4GK5X-ray3.21A/B1-211[»]
    ProteinModelPortaliQ9UI95.
    SMRiQ9UI95. Positions 1-209.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UI95.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 203191HORMAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni21 – 155135Mediates interaction with REV1 and REV3L and homodimerizationAdd
    BLAST
    Regioni150 – 21162Mediates interaction with ipaBAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HORMA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG292947.
    HOGENOMiHOG000231083.
    HOVERGENiHBG052443.
    KOiK13728.
    OrthoDBiEOG7SN8FC.
    PhylomeDBiQ9UI95.
    TreeFamiTF101085.

    Family and domain databases

    Gene3Di3.30.900.10. 1 hit.
    InterProiIPR003511. HORMA_DNA-bd.
    [Graphical view]
    PfamiPF02301. HORMA. 1 hit.
    [Graphical view]
    SUPFAMiSSF56019. SSF56019. 1 hit.
    PROSITEiPS50815. HORMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UI95-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTLTRQDLN FGQVVADVLC EFLEVAVHLI LYVREVYPVG IFQKRKKYNV    50
    PVQMSCHPEL NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF 100
    EITQPPLLSI SSDSLLSHVE QLLRAFILKI SVCDAVLDHN PPGCTFTVLV 150
    HTREAATRNM EKIQVIKDFP WILADEQDVH MHDPRLIPLK TMTSDILKMQ 200
    LYVEERAHKG S 211
    Length:211
    Mass (Da):24,334
    Last modified:January 11, 2001 - v2
    Checksum:i1DE6353EF7D650B9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171D → A in AAD30290. (PubMed:10366450)Curated
    Sequence conflicti96 – 961E → D in AAF20267. 1 PublicationCurated
    Sequence conflicti199 – 1991M → V in AAF20267. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072933 mRNA. Translation: AAD41647.1.
    AF080398 mRNA. Translation: AAF20267.1.
    AF139365 mRNA. Translation: AAD30290.1.
    AF157482 mRNA. Translation: AAF34357.1.
    AK027327 mRNA. Translation: BAG51305.1.
    AK094316 mRNA. Translation: BAG52858.1.
    DQ017900 Genomic DNA. Translation: AAY26393.1.
    AL031731 Genomic DNA. Translation: CAI20218.1.
    CH471130 Genomic DNA. Translation: EAW71697.1.
    BC015244 mRNA. Translation: AAH15244.1.
    CCDSiCCDS134.1.
    RefSeqiNP_001120797.1. NM_001127325.1.
    NP_006332.3. NM_006341.3.
    UniGeneiHs.19400.

    Genome annotation databases

    EnsembliENST00000235310; ENSP00000235310; ENSG00000116670.
    ENST00000376667; ENSP00000365855; ENSG00000116670.
    ENST00000376692; ENSP00000365882; ENSG00000116670.
    GeneIDi10459.
    KEGGihsa:10459.
    UCSCiuc001asp.3. human.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072933 mRNA. Translation: AAD41647.1 .
    AF080398 mRNA. Translation: AAF20267.1 .
    AF139365 mRNA. Translation: AAD30290.1 .
    AF157482 mRNA. Translation: AAF34357.1 .
    AK027327 mRNA. Translation: BAG51305.1 .
    AK094316 mRNA. Translation: BAG52858.1 .
    DQ017900 Genomic DNA. Translation: AAY26393.1 .
    AL031731 Genomic DNA. Translation: CAI20218.1 .
    CH471130 Genomic DNA. Translation: EAW71697.1 .
    BC015244 mRNA. Translation: AAH15244.1 .
    CCDSi CCDS134.1.
    RefSeqi NP_001120797.1. NM_001127325.1.
    NP_006332.3. NM_006341.3.
    UniGenei Hs.19400.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ABD X-ray 1.90 A/B 1-211 [» ]
    3ABE X-ray 2.60 C 1-211 [» ]
    3VU7 X-ray 2.80 C 1-211 [» ]
    4EXT X-ray 1.90 C 7-209 [» ]
    4GK0 X-ray 2.70 A/B 1-211 [» ]
    4GK5 X-ray 3.21 A/B 1-211 [» ]
    ProteinModelPortali Q9UI95.
    SMRi Q9UI95. Positions 1-209.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115722. 22 interactions.
    IntActi Q9UI95. 13 interactions.
    MINTi MINT-108350.
    STRINGi 9606.ENSP00000235310.

    PTM databases

    PhosphoSitei Q9UI95.

    Proteomic databases

    MaxQBi Q9UI95.
    PaxDbi Q9UI95.
    PRIDEi Q9UI95.

    Protocols and materials databases

    DNASUi 10459.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000235310 ; ENSP00000235310 ; ENSG00000116670 .
    ENST00000376667 ; ENSP00000365855 ; ENSG00000116670 .
    ENST00000376692 ; ENSP00000365882 ; ENSG00000116670 .
    GeneIDi 10459.
    KEGGi hsa:10459.
    UCSCi uc001asp.3. human.

    Organism-specific databases

    CTDi 10459.
    GeneCardsi GC01M011734.
    HGNCi HGNC:6764. MAD2L2.
    HPAi CAB008110.
    MIMi 604094. gene.
    neXtProti NX_Q9UI95.
    PharmGKBi PA398.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292947.
    HOGENOMi HOG000231083.
    HOVERGENi HBG052443.
    KOi K13728.
    OrthoDBi EOG7SN8FC.
    PhylomeDBi Q9UI95.
    TreeFami TF101085.

    Enzyme and pathway databases

    Reactomei REACT_822. Translesion synthesis by Pol zeta.

    Miscellaneous databases

    ChiTaRSi MAD2L2. human.
    EvolutionaryTracei Q9UI95.
    GeneWikii MAD2L2.
    GenomeRNAii 10459.
    NextBioi 39659.
    PROi Q9UI95.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UI95.
    Bgeei Q9UI95.
    CleanExi HS_MAD2L2.
    Genevestigatori Q9UI95.

    Family and domain databases

    Gene3Di 3.30.900.10. 1 hit.
    InterProi IPR003511. HORMA_DNA-bd.
    [Graphical view ]
    Pfami PF02301. HORMA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56019. SSF56019. 1 hit.
    PROSITEi PS50815. HORMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM9.
    2. "Identification of a novel human homolog of the MAD2 protein that interacts with the h-warts protein."
      Hirota T., Nakamura H., Tada K., Marumoto T., Saya H.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Characterization of MAD2B and other mitotic spindle checkpoint genes."
      Cahill D.P., da Costa L.T., Carson-Walter E.B., Kinzler K.W., Vogelstein B., Lengauer C.
      Genomics 58:181-187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2."
      Murakumo Y., Roth T., Ishii H., Rasio D., Numata S., Croce C.M., Fishel R.
      J. Biol. Chem. 275:4391-4397(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH REV3L.
    5. "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: Cerebellum and Embryo.
    6. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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.
    10. "Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1."
      Pfleger C.M., Salic A., Lee E., Kirschner M.W.
      Genes Dev. 15:1759-1764(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FZR1.
    11. "MAD2B is an inhibitor of the anaphase-promoting complex."
      Chen J., Fang G.
      Genes Dev. 15:1765-1770(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FZR1 AND CDC20.
    12. "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7."
      Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M., Fishel R., Takahashi M.
      J. Biol. Chem. 276:35644-35651(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH REV1 AND REV3L, HOMOOLIGOMERIZATION.
    13. "Impairment of MAD2B-PRCC interaction in mitotic checkpoint defective t(X;1)-positive renal cell carcinomas."
      Weterman M.A., van Groningen J.J., Tertoolen L., van Kessel A.G.
      Proc. Natl. Acad. Sci. U.S.A. 98:13808-13813(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRCC, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    14. "A bacterial effector targets Mad2L2, an APC inhibitor, to modulate host cell cycling."
      Iwai H., Kim M., Yoshikawa Y., Ashida H., Ogawa M., Fujita Y., Muller D., Kirikae T., Jackson P.K., Kotani S., Sasakawa C.
      Cell 130:611-623(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APC REGULATION, INTERACTION WITH SHIGELLA FLEXNERI IPAB; FZR1 AND CDC20, SUBCELLULAR LOCATION.
    15. "Hepatocellular carcinoma-associated gene 2 interacts with MAD2L2."
      Li L., Shi Y., Wu H., Wan B., Li P., Zhou L., Shi H., Huo K.
      Mol. Cell. Biochem. 304:297-304(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YY1AP1, SUBCELLULAR LOCATION.
    16. "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1."
      Zhang L., Yang S.H., Sharrocks A.D.
      Mol. Cell. Biol. 27:2861-2869(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ELK1 AND JNK KINASES.
    17. "MAD2B, a novel TCF4-binding protein, modulates TCF4-mediated epithelial-mesenchymal transdifferentiation."
      Hong C.F., Chou Y.T., Lin Y.S., Wu C.W.
      J. Biol. Chem. 284:19613-19622(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TCF7L2.
    18. "The mitotic arrest deficient protein MAD2B interacts with the small GTPase RAN throughout the cell cycle."
      Medendorp K., van Groningen J.J., Vreede L., Hetterschijt L., van den Hurk W.H., de Bruijn D.R., Brugmans L., van Kessel A.G.
      PLoS ONE 4:E7020-E7020(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAN, SUBCELLULAR LOCATION.
    19. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
      Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
      Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POGZ.
    20. "CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
      Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
      EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHAMP1, SUBCELLULAR LOCATION.
    21. "Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1."
      Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S., Akashi S., Takeda S., Shimizu T., Sato M.
      J. Biol. Chem. 285:12299-12307(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH REV3L, MUTAGENESIS OF TYR-63; ARG-124; TRP-171; LEU-186; GLN-200 AND TYR-202, INTERACTION WITH REV1.

    Entry informationi

    Entry nameiMD2L2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UI95
    Secondary accession number(s): B3KNE3
    , Q5TGW7, Q9UNA7, Q9Y6I6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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