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Q9Z1B5

- MD2L1_MOUSE

UniProt

Q9Z1B5 - MD2L1_MOUSE

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Protein

Mitotic spindle assembly checkpoint protein MAD2A

Gene
Mad2l1, Mad2a
Organism
Mus musculus (Mouse)
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 By similarity.

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. mitotic sister chromatid segregation Source: MGI
  2. mitotic spindle assembly checkpoint Source: MGI
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of mitotic anaphase-promoting complex activity Source: Ensembl
  5. negative regulation of mitotic metaphase/anaphase transition Source: MGI
  6. negative regulation of protein catabolic process Source: UniProtKB
  7. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitotic spindle assembly checkpoint protein MAD2A
Alternative name(s):
Mitotic arrest deficient 2-like protein 1
Short name:
MAD2-like protein 1
Gene namesi
Name:Mad2l1
Synonyms:Mad2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1860374. Mad2l1.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromosome, centromeric region Source: MGI
  2. condensed chromosome kinetochore Source: UniProtKB-SubCell
  3. cytosol Source: UniProtKB
  4. kinetochore Source: MGI
  5. mitotic spindle Source: UniProtKB
  6. nuclear pore Source: Ensembl
  7. nucleus Source: UniProtKB
  8. perinuclear region of cytoplasm Source: UniProtKB
  9. spindle pole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 205204Mitotic spindle assembly checkpoint protein MAD2APRO_0000126118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei170 – 1701Phosphoserine By similarity
Modified residuei195 – 1951Phosphoserine By similarity

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 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Z1B5.
PaxDbiQ9Z1B5.
PRIDEiQ9Z1B5.

PTM databases

PhosphoSiteiQ9Z1B5.

Expressioni

Gene expression databases

ArrayExpressiQ9Z1B5.
BgeeiQ9Z1B5.
GenevestigatoriQ9Z1B5.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Sgol2Q7TSY83EBI-2552918,EBI-2552468

Protein-protein interaction databases

BioGridi207818. 31 interactions.
IntActiQ9Z1B5. 30 interactions.
MINTiMINT-123716.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1B5.
SMRiQ9Z1B5. Positions 11-205.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 197184HORMAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni195 – 20511Required for assuming the closed conformation and for interaction with CDC20 By similarityAdd
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 By similarity.

Sequence similaritiesi

Belongs to the MAD2 family.
Contains 1 HORMA domain.

Phylogenomic databases

eggNOGiNOG263853.
GeneTreeiENSGT00390000007908.
HOGENOMiHOG000199586.
HOVERGENiHBG105691.
InParanoidiQ9Z1B5.
KOiK02537.
OMAiPREKSIK.
OrthoDBiEOG7288SG.
PhylomeDBiQ9Z1B5.
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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z1B5-1 [UniParc]FASTAAdd to Basket

« Hide

MAQQLAREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG    50
LTLLTTTDPE LIKYLNNVVE QLKEWLYKCS VQKLVVVISN IESGEVLERW 100
QFDIECDKTA KEEGVRREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS 150
FDLLIYTDKD LVVPEKWEES GPQFITNCEE VRLRSFTTTI HKVNSMVAYK 200
TPVND 205
Length:205
Mass (Da):23,598
Last modified:January 11, 2001 - v2
Checksum:iA9F3F28BC4C9738E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571T → A in AAD09238. 1 Publication
Sequence conflicti178 – 1781C → S in AAD09238. 1 Publication
Sequence conflicti201 – 2011T → I in AAD09238. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83902 mRNA. Translation: AAD09238.1.
AF261919 Genomic DNA. Translation: AAF69525.1.
AK082934 mRNA. Translation: BAC38700.1.
CCDSiCCDS20210.1.
RefSeqiNP_062372.2. NM_019499.4.
XP_006506469.1. XM_006506406.1.
UniGeneiMm.489653.

Genome annotation databases

EnsembliENSMUST00000101343; ENSMUSP00000098897; ENSMUSG00000029910.
ENSMUST00000116605; ENSMUSP00000112304; ENSMUSG00000029910.
GeneIDi56150.
KEGGimmu:56150.
UCSCiuc009cen.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U83902 mRNA. Translation: AAD09238.1 .
AF261919 Genomic DNA. Translation: AAF69525.1 .
AK082934 mRNA. Translation: BAC38700.1 .
CCDSi CCDS20210.1.
RefSeqi NP_062372.2. NM_019499.4.
XP_006506469.1. XM_006506406.1.
UniGenei Mm.489653.

3D structure databases

ProteinModelPortali Q9Z1B5.
SMRi Q9Z1B5. Positions 11-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207818. 31 interactions.
IntActi Q9Z1B5. 30 interactions.
MINTi MINT-123716.

PTM databases

PhosphoSitei Q9Z1B5.

Proteomic databases

MaxQBi Q9Z1B5.
PaxDbi Q9Z1B5.
PRIDEi Q9Z1B5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000101343 ; ENSMUSP00000098897 ; ENSMUSG00000029910 .
ENSMUST00000116605 ; ENSMUSP00000112304 ; ENSMUSG00000029910 .
GeneIDi 56150.
KEGGi mmu:56150.
UCSCi uc009cen.1. mouse.

Organism-specific databases

CTDi 4085.
MGIi MGI:1860374. Mad2l1.

Phylogenomic databases

eggNOGi NOG263853.
GeneTreei ENSGT00390000007908.
HOGENOMi HOG000199586.
HOVERGENi HBG105691.
InParanoidi Q9Z1B5.
KOi K02537.
OMAi PREKSIK.
OrthoDBi EOG7288SG.
PhylomeDBi Q9Z1B5.
TreeFami TF101084.

Enzyme and pathway databases

Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_207679. Separation of Sister Chromatids.
REACT_222875. APC/C:Cdc20 mediated degradation of mitotic proteins.

Miscellaneous databases

NextBioi 311932.
PROi Q9Z1B5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z1B5.
Bgeei Q9Z1B5.
Genevestigatori Q9Z1B5.

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 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.
    , 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.

Entry informationi

Entry nameiMD2L1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1B5
Secondary accession number(s): Q9JI53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: September 3, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi