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Q13257 (MD2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MAD2L1
Synonyms:MAD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.25 Ref.27 Ref.28

Subunit structure

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. Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Subcellular location

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. Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.27

Domain

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. Ref.25 Ref.26 Ref.27 Ref.28 Ref.31

Post-translational modification

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. Ref.16 Ref.23

Sequence similarities

Belongs to the MAD2 family.

Contains 1 HORMA domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle checkpoint

Inferred from direct assay Ref.1. Source: UniProtKB

mitotic sister chromatid segregation

Inferred from electronic annotation. Source: Ensembl

mitotic spindle assembly checkpoint

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 20870947. Source: UniProtKB

negative regulation of mitotic anaphase-promoting complex activity

Inferred from direct assay PubMed 11459825. Source: UniProtKB

negative regulation of protein catabolic process

Inferred from direct assay PubMed 11459825. Source: UniProtKB

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from mutant phenotype PubMed 20870947. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.20. Source: UniProtKB

kinetochore

Inferred from direct assay PubMed 19229290PubMed 20133940. Source: UniProtKB

mitotic spindle

Inferred from direct assay PubMed 20133940. Source: UniProtKB

nucleus

Inferred from direct assay Ref.20PubMed 20870947. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20870947Ref.1. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 16525508Ref.29PubMed 21772247. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10200259Ref.25Ref.26PubMed 15525512Ref.30Ref.20PubMed 19273613PubMed 20133940. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.29. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13257-1)

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.
Isoform 2 (identifier: Q13257-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 205204Mitotic spindle assembly checkpoint protein MAD2A
PRO_0000126117

Regions

Domain14 – 197184HORMA
Region195 – 20511Required for assuming the closed conformation and for interaction with CDC20

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue1701Phosphoserine Ref.16
Modified residue1781Phosphoserine Ref.16
Modified residue1951Phosphoserine Ref.16

Natural variations

Alternative sequence74 – 9017DWLYK…VVISN → VHPEKSLRKLSRMKSVQ in isoform 2.
VSP_047644
Alternative sequence91 – 205115Missing in isoform 2.
VSP_047645

Experimental info

Mutagenesis131L → A: Leads to formation the closed conformation and homodimerization. Ref.31
Mutagenesis751W → A: Prevents interaction with CDC20 and leads to formation of the closed conformation; when associated with A-133. Ref.31
Mutagenesis1331R → A: Prevents aggregation and promotes formation of monomeric protein that slowly interconverts between the open and closed conformation. Ref.26
Mutagenesis1531L → A: Leads to formation of the closed conformation; when associated with A-133. Ref.31
Mutagenesis1561Y → A: Leads to formation of the closed conformation; when associated with A-133. Ref.31
Mutagenesis1701S → A: Reduces phosphorylation on serine residues; when associated with A-178. Abolishes phosphorylation on serine residues; when associated with A-178 and A-195. Ref.16
Mutagenesis1701S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-178 and D-195. Ref.16
Mutagenesis1781S → A: Reduces phosphorylation on serine residues; when associated with A-170. Abolishes phosphorylation on serine residues; when associated with A-170 and A-195. Ref.16
Mutagenesis1781S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-195. Ref.16
Mutagenesis1861F → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.31
Mutagenesis1881T → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.31
Mutagenesis1911H → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.31
Mutagenesis1951S → A: Abolishes phosphorylation on serine residues; when associated with A-170 and A-178. Ref.16
Mutagenesis1951S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-178. Ref.16
Mutagenesis1971V → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.31
Mutagenesis1991Y → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.31
Sequence conflict161S → C in BAD97153. Ref.8
Sequence conflict1901I → V in AAH70283. Ref.11

Secondary structure

..................................... 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B8DCBF0043836764

FASTA20523,510
        10         20         30         40         50         60 
MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE 

        70         80         90        100        110        120 
LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW QFDIECDKTA KDDSAPREKS 

       130        140        150        160        170        180 
QKAIQDEIRS VIRQITATVT FLPLLEVSCS FDLLIYTDKD LVVPEKWEES GPQFITNSEE 

       190        200 
VRLRSFTTTI HKVNSMVAYK IPVND 

« Hide

Isoform 2 [UniParc].

Checksum: 8209F5A7A7D8D09B
Show »

FASTA9010,335

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"FAT10 plays a role in the regulation of chromosomal stability."
Ren J., Kan A., Leong S.H., Ooi L.L.P.J., Jeang K.-T., Chong S.S., Kon O.L., Lee C.G.L.
J. Biol. Chem. 281:11413-11421(2006) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U65410 mRNA. Translation: AAC50781.1.
AF202273 expand/collapse EMBL AC list , 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.
CCDSCCDS3715.1. [Q13257-1]
PIRG01942.
RefSeqNP_002349.1. NM_002358.3. [Q13257-1]
UniGeneHs.591697.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ13257.
SMRQ13257. Positions 2-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110260. 47 interactions.
DIPDIP-29653N.
IntActQ13257. 28 interactions.
MINTMINT-108270.
STRING9606.ENSP00000296509.

PTM databases

PhosphoSiteQ13257.

Polymorphism databases

DMDM12230256.

Proteomic databases

MaxQBQ13257.
PaxDbQ13257.
PeptideAtlasQ13257.
PRIDEQ13257.

Protocols and materials databases

DNASU4085.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296509; ENSP00000296509; ENSG00000164109. [Q13257-1]
ENST00000333047; ENSP00000332295; ENSG00000164109. [Q13257-2]
GeneID4085.
KEGGhsa:4085.
UCSCuc003idl.2. human. [Q13257-1]

Organism-specific databases

CTD4085.
GeneCardsGC04M120980.
HGNCHGNC:6763. MAD2L1.
HPAHPA003348.
MIM601467. gene.
neXtProtNX_Q13257.
PharmGKBPA30521.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263853.
HOGENOMHOG000199586.
HOVERGENHBG105691.
InParanoidQ13257.
KOK02537.
OMAPREKSIK.
OrthoDBEOG7288SG.
PhylomeDBQ13257.
TreeFamTF101084.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpressQ13257.
BgeeQ13257.
CleanExHS_MAD2L1.
GenevestigatorQ13257.

Family and domain databases

Gene3D3.30.900.10. 1 hit.
InterProIPR003511. HORMA_DNA-bd.
IPR027097. Mad2.
[Graphical view]
PANTHERPTHR11842:SF11. PTHR11842:SF11. 1 hit.
PfamPF02301. HORMA. 1 hit.
[Graphical view]
SUPFAMSSF56019. SSF56019. 1 hit.
PROSITEPS50815. HORMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAD2L1. human.
EvolutionaryTraceQ13257.
GeneWikiMAD2L1.
GenomeRNAi4085.
NextBio16010.
PROQ13257.
SOURCESearch...

Entry information

Entry nameMD2L1_HUMAN
AccessionPrimary (citable) accession number: Q13257
Secondary accession number(s): Q53F56 expand/collapse secondary AC list , Q548X9, Q6IRW7, Q8IZX3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM