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Q9Z1B5 (MD2L1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitotic spindle assembly checkpoint protein MAD2A
Alternative name(s):
Mitotic arrest deficient 2-like protein 1
Short name=MAD2-like protein 1
Gene names
Name:Mad2l1
Synonyms:Mad2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

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. Kinetochore association is repressed by UBD By similarity. Interacts with NEK2 By similarity.

Subcellular location

Nucleus By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Note: Recruited by MAD1L1 to unattached kinetochores By similarity. Recruited to the nuclear pore complex by TPR during interphase By similarity. Recruited to kinetochores in late prometaphase after BUB1, CENPF, BUB1B and CENPE. Kinetochore association requires the presence of NEK2 By similarity.

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 By similarity.

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 By similarity.

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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitotic sister chromatid segregation

Inferred from mutant phenotype Ref.2. Source: MGI

mitotic spindle assembly checkpoint

Inferred from mutant phenotype PubMed 11201745. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 20870947. Source: UniProtKB

negative regulation of mitotic anaphase-promoting complex activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitotic metaphase/anaphase transition

Traceable author statement PubMed 12147697. Source: MGI

negative regulation of protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from mutant phenotype PubMed 20870947. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from direct assay PubMed 12355205. Source: MGI

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

kinetochore

Inferred from direct assay PubMed 10964468PubMed 19075002PubMed 19376971. Source: MGI

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear pore

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

spindle pole

Inferred from direct assay PubMed 10964468. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 21666598. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sgol2Q7TSY83EBI-2552918,EBI-2552468

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 205204Mitotic spindle assembly checkpoint protein MAD2A
PRO_0000126118

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1701Phosphoserine By similarity
Modified residue1951Phosphoserine By similarity

Experimental info

Sequence conflict1571T → A in AAD09238. Ref.1
Sequence conflict1781C → S in AAD09238. Ref.1
Sequence conflict2011T → I in AAD09238. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z1B5 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: A9F3F28BC4C9738E

FASTA20523,598
        10         20         30         40         50         60 
MAQQLAREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLTTTDPE 

        70         80         90        100        110        120 
LIKYLNNVVE QLKEWLYKCS VQKLVVVISN IESGEVLERW QFDIECDKTA KEEGVRREKS 

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

       190        200 
VRLRSFTTTI HKVNSMVAYK TPVND 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel component of the spindle assembly checkpoint in mammalian cells."
Jin D.-Y., Jeang K.-T.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[2]"Chromosome missegregation and apoptosis in mice lacking the mitotic checkpoint protein Mad2."
Dobles M., Liberal V., Scott M.L., Benezra R., Sorger P.K.
Cell 101:635-645(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U83902 mRNA. Translation: AAD09238.1.
AF261919 Genomic DNA. Translation: AAF69525.1.
AK082934 mRNA. Translation: BAC38700.1.
CCDSCCDS20210.1.
RefSeqNP_062372.2. NM_019499.4.
XP_006506469.1. XM_006506406.1.
UniGeneMm.489653.

3D structure databases

ProteinModelPortalQ9Z1B5.
SMRQ9Z1B5. Positions 11-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207818. 31 interactions.
IntActQ9Z1B5. 30 interactions.
MINTMINT-123716.

PTM databases

PhosphoSiteQ9Z1B5.

Proteomic databases

MaxQBQ9Z1B5.
PaxDbQ9Z1B5.
PRIDEQ9Z1B5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000101343; ENSMUSP00000098897; ENSMUSG00000029910.
ENSMUST00000116605; ENSMUSP00000112304; ENSMUSG00000029910.
GeneID56150.
KEGGmmu:56150.
UCSCuc009cen.1. mouse.

Organism-specific databases

CTD4085.
MGIMGI:1860374. Mad2l1.

Phylogenomic databases

eggNOGNOG263853.
GeneTreeENSGT00390000007908.
HOGENOMHOG000199586.
HOVERGENHBG105691.
InParanoidQ9Z1B5.
KOK02537.
OMAPREKSIK.
OrthoDBEOG7288SG.
PhylomeDBQ9Z1B5.
TreeFamTF101084.

Gene expression databases

ArrayExpressQ9Z1B5.
BgeeQ9Z1B5.
GenevestigatorQ9Z1B5.

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

NextBio311932.
PROQ9Z1B5.
SOURCESearch...

Entry information

Entry nameMD2L1_MOUSE
AccessionPrimary (citable) accession number: Q9Z1B5
Secondary accession number(s): Q9JI53
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot