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Q9Y6D9

- MD1L1_HUMAN

UniProt

Q9Y6D9 - MD1L1_HUMAN

Protein

Mitotic spindle assembly checkpoint protein MAD1

Gene

MAD1L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (27 Sep 2004)
      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. May recruit MAD2L1 to unattached kinetochores. Has a role in the correct positioning of the septum. Required for anchoring MAD2L1 to the nuclear periphery. Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. mitotic anaphase Source: UniProtKB
    2. mitotic cell cycle Source: Reactome
    3. mitotic cell cycle checkpoint Source: UniProtKB
    4. mitotic metaphase Source: UniProtKB
    5. mitotic nuclear division Source: UniProtKB-KW
    6. mitotic spindle assembly checkpoint Source: Reactome
    7. mitotic telophase Source: UniProtKB
    8. regulation of metaphase plate congression Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_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_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitotic spindle assembly checkpoint protein MAD1
    Alternative name(s):
    Mitotic arrest deficient 1-like protein 1
    Short name:
    MAD1-like protein 1
    Mitotic checkpoint MAD1 protein homolog
    Short name:
    HsMAD1
    Short name:
    hMAD1
    Tax-binding protein 181
    Gene namesi
    Name:MAD1L1
    Synonyms:MAD1, TXBP181
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6762. MAD1L1.

    Subcellular locationi

    Nucleus. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle
    Note: From the beginning to the end of mitosis, it is seen to move from a diffusely nuclear distribution to the centrosome, to the spindle midzone and finally to the midbody. Colocalizes with NEK2 at the kinetochore.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. centrosome Source: UniProtKB
    3. condensed chromosome kinetochore Source: UniProtKB-SubCell
    4. cytoplasm Source: HPA
    5. cytosol Source: Reactome
    6. kinetochore Source: UniProtKB
    7. mitotic spindle Source: UniProtKB
    8. nucleus Source: HPA
    9. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in MAD1L1 are involved in the development and/or progression of various types of cancer.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    PharmGKBiPA372.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 718718Mitotic spindle assembly checkpoint protein MAD1PRO_0000213800Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei61 – 611N6-acetyllysine1 Publication
    Modified residuei214 – 2141Phosphoserine1 Publication
    Modified residuei428 – 4281Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated; by BUB1. Become hyperphosphorylated in late S through M phases or after mitotic spindle damage.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6D9.
    PaxDbiQ9Y6D9.
    PeptideAtlasiQ9Y6D9.
    PRIDEiQ9Y6D9.

    PTM databases

    PhosphoSiteiQ9Y6D9.

    Expressioni

    Tissue specificityi

    Expressed weakly at G0/G1 and highly at late S and G2/M phase.

    Inductioni

    Increased by p53/TP53.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y6D9.
    BgeeiQ9Y6D9.
    CleanExiHS_MAD1L1.
    GenevestigatoriQ9Y6D9.

    Organism-specific databases

    HPAiCAB015338.
    HPA003635.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimerizes with MAD2L1 in order to form a tetrameric MAD1L1-MAD2L1 core complex. Perturbation of the original MAD1L1-MAD2L1 structure by the spindle checkpoint may decrease MAD2L1 affinity for MAD1L1. CDC20 can compete with MAD1L1 for MAD2L1 binding, until the attachment and/or tension dampen the checkpoint signal, preventing further release of MAD2L1 on to CDC20. Also able to interact with the BUB1/BUB3 complex and the viral Tax protein. Interacts with NEK2. Interacts with TPR; the interactions occurs in a microtubule-independent manner.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAD2L1Q1325711EBI-742610,EBI-78203
    MAXP612442EBI-742610,EBI-751711
    TPRP122702EBI-742610,EBI-1048528

    Protein-protein interaction databases

    BioGridi113971. 30 interactions.
    DIPiDIP-29654N.
    IntActiQ9Y6D9. 23 interactions.
    MINTiMINT-1435591.
    STRINGi9606.ENSP00000382562.

    Structurei

    Secondary structure

    1
    718
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi494 – 52835
    Turni537 – 5393
    Beta strandi540 – 5478
    Helixi549 – 57527
    Helixi599 – 63739
    Beta strandi638 – 6447
    Turni645 – 6473
    Beta strandi648 – 6536
    Beta strandi663 – 6675
    Beta strandi675 – 6784
    Helixi683 – 6853
    Helixi687 – 6937
    Helixi700 – 71516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GO4X-ray2.05E/F/G/H485-584[»]
    4DZOX-ray1.76A/B597-718[»]
    ProteinModelPortaliQ9Y6D9.
    SMRiQ9Y6D9. Positions 485-584, 598-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6D9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni380 – 532153Necessary for interaction with NEK2Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili46 – 632587Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MAD1 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG275166.
    HOGENOMiHOG000004808.
    HOVERGENiHBG052441.
    KOiK06638.
    OMAiGAEEKMQ.
    PhylomeDBiQ9Y6D9.
    TreeFamiTF101083.

    Family and domain databases

    InterProiIPR008672. Mad1.
    [Graphical view]
    PANTHERiPTHR23168. PTHR23168. 1 hit.
    PfamiPF05557. MAD. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6D9-1) [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

    MEDLGENTMV LSTLRSLNNF ISQRVEGGSG LDISTSAPGS LQMQYQQSMQ    50
    LEERAEQIRS KSHLIQVERE KMQMELSHKR ARVELERAAS TSARNYEREV 100
    DRNQELLTRI RQLQEREAGA EEKMQEQLER NRQCQQNLDA ASKRLREKED 150
    SLAQAGETIN ALKGRISELQ WSVMDQEMRV KRLESEKQEL QEQLDLQHKK 200
    CQEANQKIQE LQASQEARAD HEQQIKDLEQ KLSLQEQDAA IVKNMKSELV 250
    RLPRLERELK QLREESAHLR EMRETNGLLQ EELEGLQRKL GRQEKMQETL 300
    VGLELENERL LAKLQSWERL DQTMGLSIRT PEDLSRFVVE LQQRELALKD 350
    KNSAVTSSAR GLEKARQQLQ EELRQVSGQL LEERKKRETH EALARRLQKR 400
    VLLLTKERDG MRAILGSYDS ELTPAEYSPQ LTRRMREAED MVQKVHSHSA 450
    EMEAQLSQAL EELGGQKQRA DMLEMELKML KSQSSSAEQS FLFSREEADT 500
    LRLKVEELEG ERSRLEEEKR MLEAQLERRA LQGDYDQSRT KVLHMSLNPT 550
    SVARQRLRED HSQLQAECER LRGLLRAMER GGTVPADLEA AAASLPSSKE 600
    VAELKKQVES AELKNQRLKE VFQTKIQEFR KACYTLTGYQ IDITTENQYR 650
    LTSLYAEHPG DCLIFKATSP SGSKMQLLET EFSHTVGELI EVHLRRQDSI 700
    PAFLSSLTLE LFSRQTVA 718
    Length:718
    Mass (Da):83,067
    Last modified:September 27, 2004 - v2
    Checksum:iDA65529856A37EE3
    GO
    Isoform 2 (identifier: Q9Y6D9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-65: MEDLGENTMV...EQIRSKSHLI → MLPARGCVRK...PCIWPCPWHT
         66-157: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:626
    Mass (Da):72,286
    Checksum:iC0506A8710806387
    GO

    Sequence cautioni

    The sequence AAC52059.1 differs from that shown. Reason: Frameshift at position 663.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1902EL → DV in AAC52059. (PubMed:9546394)Curated
    Sequence conflicti189 – 1902EL → DV in AAD24498. (PubMed:10049595)Curated
    Sequence conflicti260 – 2601K → E in AAC52059. (PubMed:9546394)Curated
    Sequence conflicti260 – 2601K → E in AAD24498. (PubMed:10049595)Curated
    Sequence conflicti268 – 2681Missing in AAC52059. (PubMed:9546394)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291S → L in a lymphoid cancer cell line; somatic mutation. 1 Publication
    VAR_019707
    Natural varianti59 – 591R → C in a prostate cancer cell line; somatic mutation. 1 Publication
    Corresponds to variant rs28939694 [ dbSNP | Ensembl ].
    VAR_019708
    Natural varianti160 – 1601N → S.1 Publication
    VAR_019709
    Natural varianti299 – 2991T → A in lung cancer cell line; somatic mutation. 1 Publication
    VAR_019710
    Natural varianti360 – 3601R → Q in a prostate cancer cell line; somatic mutation. 1 Publication
    VAR_019711
    Natural varianti500 – 5001T → M.2 Publications
    Corresponds to variant rs193231481 [ dbSNP | Ensembl ].
    VAR_019712
    Natural varianti511 – 5111E → K.1 Publication
    VAR_019713
    Natural varianti516 – 5161E → K in a breast cancer cell line; somatic mutation. 1 Publication
    VAR_019714
    Natural varianti556 – 5561R → C in a prostate cancer cell line; somatic mutation. 1 Publication
    VAR_019715
    Natural varianti556 – 5561R → H in one individual with lung cancer. 1 Publication
    VAR_019716
    Natural varianti558 – 5581R → H in a cancer cell line. 3 Publications
    Corresponds to variant rs1801368 [ dbSNP | Ensembl ].
    VAR_019717
    Natural varianti569 – 5691E → K in a breast cancer cell line; somatic mutation. 1 Publication
    VAR_019718
    Natural varianti572 – 5721R → H in a cancer cell line. 1 Publication
    Corresponds to variant rs1801500 [ dbSNP | Ensembl ].
    VAR_019719

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6565MEDLG…KSHLI → MLPARGCVRKRTVWPRLARV LIVTLLTLELSYAPLPCQLS GVPYNTGDPVGRWARPCIWP CPWHT in isoform 2. 1 PublicationVSP_056160Add
    BLAST
    Alternative sequencei66 – 15792Missing in isoform 2. 1 PublicationVSP_056161Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33822 mRNA. Translation: AAC52059.1. Frameshift.
    AF123318 mRNA. Translation: AAD20359.1.
    AF083811 mRNA. Translation: AAD24498.1.
    AK090959 mRNA. Translation: BAG52253.1.
    AC005282 Genomic DNA. No translation available.
    AC006433 Genomic DNA. No translation available.
    AC069288 Genomic DNA. Translation: AAS07503.1.
    AC104129 Genomic DNA. Translation: AAP21876.1.
    AC110781 Genomic DNA. No translation available.
    BC009964 mRNA. Translation: AAH09964.1.
    CCDSiCCDS43539.1.
    RefSeqiNP_001013858.1. NM_001013836.1.
    NP_001013859.1. NM_001013837.1.
    NP_003541.2. NM_003550.2.
    XP_005249933.1. XM_005249876.1.
    XP_006715851.1. XM_006715788.1.
    UniGeneiHs.654838.

    Genome annotation databases

    EnsembliENST00000265854; ENSP00000265854; ENSG00000002822.
    ENST00000399654; ENSP00000382562; ENSG00000002822.
    ENST00000402746; ENSP00000384155; ENSG00000002822.
    ENST00000406869; ENSP00000385334; ENSG00000002822.
    GeneIDi8379.
    KEGGihsa:8379.
    UCSCiuc003sle.1. human.

    Polymorphism databases

    DMDMi52783153.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33822 mRNA. Translation: AAC52059.1 . Frameshift.
    AF123318 mRNA. Translation: AAD20359.1 .
    AF083811 mRNA. Translation: AAD24498.1 .
    AK090959 mRNA. Translation: BAG52253.1 .
    AC005282 Genomic DNA. No translation available.
    AC006433 Genomic DNA. No translation available.
    AC069288 Genomic DNA. Translation: AAS07503.1 .
    AC104129 Genomic DNA. Translation: AAP21876.1 .
    AC110781 Genomic DNA. No translation available.
    BC009964 mRNA. Translation: AAH09964.1 .
    CCDSi CCDS43539.1.
    RefSeqi NP_001013858.1. NM_001013836.1.
    NP_001013859.1. NM_001013837.1.
    NP_003541.2. NM_003550.2.
    XP_005249933.1. XM_005249876.1.
    XP_006715851.1. XM_006715788.1.
    UniGenei Hs.654838.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GO4 X-ray 2.05 E/F/G/H 485-584 [» ]
    4DZO X-ray 1.76 A/B 597-718 [» ]
    ProteinModelPortali Q9Y6D9.
    SMRi Q9Y6D9. Positions 485-584, 598-716.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113971. 30 interactions.
    DIPi DIP-29654N.
    IntActi Q9Y6D9. 23 interactions.
    MINTi MINT-1435591.
    STRINGi 9606.ENSP00000382562.

    PTM databases

    PhosphoSitei Q9Y6D9.

    Polymorphism databases

    DMDMi 52783153.

    Proteomic databases

    MaxQBi Q9Y6D9.
    PaxDbi Q9Y6D9.
    PeptideAtlasi Q9Y6D9.
    PRIDEi Q9Y6D9.

    Protocols and materials databases

    DNASUi 8379.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265854 ; ENSP00000265854 ; ENSG00000002822 .
    ENST00000399654 ; ENSP00000382562 ; ENSG00000002822 .
    ENST00000402746 ; ENSP00000384155 ; ENSG00000002822 .
    ENST00000406869 ; ENSP00000385334 ; ENSG00000002822 .
    GeneIDi 8379.
    KEGGi hsa:8379.
    UCSCi uc003sle.1. human.

    Organism-specific databases

    CTDi 8379.
    GeneCardsi GC07M001855.
    HGNCi HGNC:6762. MAD1L1.
    HPAi CAB015338.
    HPA003635.
    MIMi 602686. gene.
    neXtProti NX_Q9Y6D9.
    PharmGKBi PA372.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG275166.
    HOGENOMi HOG000004808.
    HOVERGENi HBG052441.
    KOi K06638.
    OMAi GAEEKMQ.
    PhylomeDBi Q9Y6D9.
    TreeFami TF101083.

    Enzyme and pathway databases

    Reactomei 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_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi MAD1L1. human.
    EvolutionaryTracei Q9Y6D9.
    GeneWikii Mad1.
    GenomeRNAii 8379.
    NextBioi 31368.
    PROi Q9Y6D9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6D9.
    Bgeei Q9Y6D9.
    CleanExi HS_MAD1L1.
    Genevestigatori Q9Y6D9.

    Family and domain databases

    InterProi IPR008672. Mad1.
    [Graphical view ]
    PANTHERi PTHR23168. PTHR23168. 1 hit.
    Pfami PF05557. MAD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1."
      Jin D.-Y., Spencer F., Jeang K.-T.
      Cell 93:81-91(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), HOMODIMERIZATION, HETEROTETRAMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH MAD2L1 AND VIRAL TAX.
    2. "Phosphorylation of human MAD1 by the BUB1 kinase in vitro."
      Seeley T.W., Wang L., Zhen J.Y.
      Biochem. Biophys. Res. Commun. 257:589-595(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY BUB1, INTERACTION WITH BUB1/BUB3 COMPLEX.
      Tissue: Testis.
    3. "Mitotic checkpoint locus MAD1L1 maps to human chromosome 7p22 and mouse chromosome 5."
      Jin D.-Y., Kozak C.A., Pangilinan F., Spencer F., Green E.D., Jeang K.-T.
      Genomics 55:363-364(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, FUNCTION.
    4. "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] (ISOFORM 2).
      Tissue: Amygdala.
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Pancreas.
    7. "Multiple tumor suppressor pathways negatively regulate telomerase."
      Lin S.Y., Elledge S.J.
      Cell 113:881-889(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "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, INTERACTION WITH NEK2.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "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 AND MAD2L1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator."
      Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E., Tavares A., Johansen J., Johansen K.M., Maiato H.
      J. Cell Biol. 184:647-657(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TPR.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis."
      Nakano H., Funasaka T., Hashizume C., Wong R.W.
      J. Biol. Chem. 285:10841-10849(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TPR, SUBCELLULAR LOCATION.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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 493-579 IN COMPLEX WITH MAD2L1, COMPETITIVE INHIBITOR OF MAD2L1-CDC20 INTERACTION.
    23. "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: VARIANTS HIS-558 AND HIS-572.
    24. "Search for in vivo somatic mutations in the mitotic checkpoint gene, hMAD1, in human lung cancers."
      Nomoto S., Haruki N., Takahashi T., Masuda A., Koshikawa T., Takahashi T., Fujii Y., Osada H., Takahashi T.
      Oncogene 18:7180-7183(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LUNG CANCER ALA-299, VARIANTS SER-160; MET-500; LYS-511; HIS-556 AND HIS-558.
    25. Cited for: VARIANTS CANCER LEU-29; CYS-59; GLN-360; LYS-516; CYS-556 AND LYS-569, VARIANTS MET-500 AND HIS-558.

    Entry informationi

    Entry nameiMD1L1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6D9
    Secondary accession number(s): B3KR41
    , Q13312, Q75MI0, Q86UM4, Q9UNH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 125 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3