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Q13257

- MD2L1_HUMAN

UniProt

Q13257 - MD2L1_HUMAN

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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

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 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
Complete GO annotation...

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. cytosol Source: UniProtKB
  2. kinetochore Source: UniProtKB
  3. mitotic spindle Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. perinuclear region of cytoplasm Source: UniProtKB
  6. spindle pole Source: Ensembl
Complete GO annotation...

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 – 1701Phosphoserine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication

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

BgeeiQ13257.
CleanExiHS_MAD2L1.
ExpressionAtlasiQ13257. baseline and differential.
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. 49 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 – 54Combined sources
Beta strandi7 – 93Combined sources
Helixi13 – 3422Combined sources
Helixi40 – 423Combined sources
Beta strandi43 – 486Combined sources
Beta strandi51 – 566Combined sources
Helixi59 – 7719Combined sources
Beta strandi78 – 803Combined sources
Beta strandi81 – 9010Combined sources
Turni91 – 933Combined sources
Beta strandi96 – 10611Combined sources
Helixi108 – 1114Combined sources
Beta strandi116 – 1183Combined sources
Helixi121 – 13919Combined sources
Beta strandi149 – 1579Combined sources
Helixi160 – 1623Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi189 – 20012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000007908.
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

        10         20         30         40         50
MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG
60 70 80 90 100
LTLLVTTDLE LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW
110 120 130 140 150
QFDIECDKTA KDDSAPREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS
160 170 180 190 200
FDLLIYTDKD LVVPEKWEES GPQFITNSEE VRLRSFTTTI HKVNSMVAYK

IPVND
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 49 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.
GeneTreei ENSGT00390000007908.
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

Bgeei Q13257.
CleanExi HS_MAD2L1.
ExpressionAtlasi Q13257. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 148 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