[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1126/science.274.5285.246; PubMed=8824189 [NCBI, ExPASy, EBI, Israel, Japan] Li Y., Benezra R.; "Identification of a human mitotic checkpoint gene: hsMAD2."; Science 274:246-248(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Jin D.-Y., Jeang K.-T.; Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA]. Klebert S., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.; Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Nobori T.; "Complete human MAD2 gene."; Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Bone marrow, and Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	PROTEIN SEQUENCE OF 2-7; 36-45; 123-129 AND 193-205, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. TISSUE=Hepatoma; Bienvenut W.V., Dhillon A.S., Kolch W.; Submitted (FEB-2008) to UniProtKB.
[7]	INTERACTION WITH CDC20. PubMed=9637688 [NCBI, ExPASy, EBI, Israel, Japan] Fang G., Yu H., Kirschner M.W.; "The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation."; Genes Dev. 12:1871-1883(1998).
[8]	INTERACTION WITH ADAM17. DOI=10.1042/0264-6021:3430673; PubMed=10527948 [NCBI, ExPASy, EBI, Israel, Japan] Nelson K.K., Schlondorff J., Blobel C.P.; "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."; Biochem. J. 343:673-680(1999).
[9]	INTERACTION WITH MAD2L1BP. DOI=10.1093/emboj/cdf659; PubMed=12456649 [NCBI, ExPASy, EBI, Israel, Japan] Habu T., Kim S.H., Weinstein J., Matsumoto T.; "Identification of a MAD2-binding protein, CMT2, and its role in mitosis."; EMBO J. 21:6419-6428(2002).
[10]	STRUCTURE BY NMR OF 11-195. DOI=10.1038/73338; PubMed=10700282 [NCBI, ExPASy, EBI, Israel, Japan] Luo X., Fang G., Coldiron M., Lin Y., Yu H., Kirschner M.W., Wagner G.; "Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20."; Nat. Struct. Biol. 7:224-229(2000).

Comments

FUNCTION: Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and delays the onset of anaphase when this process is not complete. It inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate.
SUBUNIT: Interacts with CDC20, MAD2L1BP and with ADAM17/TACE.
INTERACTION:
P78536:ADAM17; NbExp=2; IntAct=EBI-78203, EBI-78188;
Q12834:CDC20; NbExp=1; IntAct=EBI-78203, EBI-367462;
Q15013:MAD2L1BP; NbExp=2; IntAct=EBI-78203, EBI-712181;
Q6XUX3:RIPK5; NbExp=1; IntAct=EBI-78203, EBI-1049520;
SUBCELLULAR LOCATION: Nucleus.
SIMILARITY: Belongs to the MAD2 family.
SIMILARITY: Contains 1 HORMA domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MAD2L1ID304.html";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U65410; AAC50781.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U31278; AAC52060.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ000186; CAA03943.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB056160; BAB63410.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000356; AAH00356.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005945; AAH05945.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

G01942; G01942.

NP_002349.1; -.

3D structure databases

PDB

1DUJ; NMR; -; A=11-195.	[ExPASy / RCSB / EBI]
1GO4; X-ray; 2.05 A; A/B/C/D=1-205.	[ExPASy / RCSB / EBI]
1KLQ; NMR; -; A=11-205.	[ExPASy / RCSB / EBI]
1S2H; NMR; -; A=1-205.	[ExPASy / RCSB / EBI]
2QYF; X-ray; 2.30 A; A/C=1-205.	[ExPASy / RCSB / EBI]
2V64; X-ray; 2.90 A; A/C/D/E/F/H=2-205.	[ExPASy / RCSB / EBI]
2VFX; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-205.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DUJ; -.
1GO4; -.
1KLQ; -.
1S2H; -.
2QYF; -.
2V64; -.
2VFX; -.

ModBase

Q13257.

Protein-protein interaction databases

IntAct

Q13257; -.

PTM databases

PhosphoSite

Q13257; -.

Enzyme and pathway databases

Reactome

REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017; APC-Cdc20 mediated degradation of Nek2A.

Organism-specific databases

H-InvDB

HIX0004473; -.
HIX0038013; -.

HGNC:6763; MAD2L1.

601467; gene. [NCBI / EBI]

PharmGKB

PA30521; -.

GeneCards

Q13257.

Gene expression databases

ArrayExpress

Q13257; -.

CleanEx

HS_MAD2L1; -.

GermOnline

ENSG00000164109; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0000776;	Cellular component: kinetochore (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031145;	Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0007067;	Biological process: mitosis (traceable author statement from ProtInc).
GO:0007093;	Biological process: mitotic cell cycle checkpoint (traceable author statement from ProtInc).
GO:0051436;	Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.

Family and domain databases

InterPro

IPR003511; HORMA_DNA_bd.
Graphical view of domain structure.

Pfam

PF02301; HORMA; 1.
Pfam graphical view of domain structure.

PROSITE

PS50815; HORMA; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q13257.

Proteomic databases

PeptideAtlas

Q13257; -.

Genome annotation databases

Ensembl

ENSG00000164109; Homo sapiens. [Contig view]

GeneID

4085; -.

KEGG

hsa:4085; -.

Phylogenomic databases

HOGENOM

Q13257; -.

HOVERGEN

Q13257; -.

Other

LinkHub

Q13257; -.

SOURCE

MAD2L1; Homo sapiens.

ProtoNet

Q13257.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Cell cycle; Cell division; Direct protein sequencing; Mitosis; Nucleus.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 205`	`204`	`Mitotic spindle assembly checkpoint protein MAD2A.`	`PRO_0000126117`
`DOMAIN`	`14 197`	`184`	`HORMA.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`HELIX`	`13 34`	`22`
`HELIX`	`40 42`	`3`
`STRAND`	`43 48`	`6`
`STRAND`	`51 56`	`6`
`HELIX`	`59 77`	`19`
`STRAND`	`81 90`	`10`
`TURN`	`91 93`	`3`
`STRAND`	`96 106`	`11`
`HELIX`	`108 111`	`4`
`HELIX`	`121 137`	`17`
`HELIX`	`138 140`	`3`
`STRAND`	`149 160`	`12`
`STRAND`	`167 169`	`3`
`STRAND`	`179 182`	`4`
`STRAND`	`189 199`	`11`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 23510 Da [This is the MW of the unprocessed precursor]

CRC64: B8DCBF0043836764 [This is a checksum on the sequence]

        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

Q13257 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools