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Entry version 152 (13 Feb 2019)
Sequence version 2 (11 Jan 2001)
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Protein

Mitotic spindle assembly checkpoint protein MAD2A

Gene

Mad2l1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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).By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-141405 Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components
R-MMU-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Mad2l1
Synonyms:Mad2a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1860374 Mad2l1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001261182 – 205Mitotic spindle assembly checkpoint protein MAD2AAdd BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei130PhosphoserineBy similarity1
Modified residuei170PhosphoserineBy similarity1
Modified residuei185PhosphoserineBy similarity1
Modified residuei195PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9Z1B5

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9Z1B5

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9Z1B5

PRoteomics IDEntifications database

More...
PRIDEi
Q9Z1B5

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q9Z1B5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Z1B5

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9Z1B5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000029910 Expressed in 294 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9Z1B5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9Z1B5 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (via ubiquitin-like 1 domain) during mitosis. Kinetochore association is repressed by UBD (By similarity). Interacts with NEK2 (By similarity). Interacts with HSF1; this interaction occurs in mitosis (By similarity).By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Sgo2Q7TSY83EBI-2552918,EBI-2552468

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
207818, 106 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3968 Mitotic Checkpoint Complex
CPX-87 Mitotic spindle assembly checkpoint Mad1-Mad2 complex
CPX-90 Mitotic spindle assembly checkpoint complex MAD2

Protein interaction database and analysis system

More...
IntActi
Q9Z1B5, 108 interactors

Molecular INTeraction database

More...
MINTi
Q9Z1B5

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000098897

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9Z1B5

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9Z1B5

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini14 – 197HORMAPROSITE-ProRule annotationAdd BLAST184

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni195 – 205Required for assuming the closed conformation and for interaction with CDC20By similarityAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MAD2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3285 Eukaryota
ENOG410XSD7 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153395

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000199586

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG105691

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z1B5

KEGG Orthology (KO)

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KOi
K02537

Identification of Orthologs from Complete Genome Data

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OMAi
VHRIEAM

Database of Orthologous Groups

More...
OrthoDBi
1197019at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Z1B5

TreeFam database of animal gene trees

More...
TreeFami
TF101084

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.900.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003511 HORMA_dom
IPR036570 HORMA_dom_sf
IPR027097 Mad2

The PANTHER Classification System

More...
PANTHERi
PTHR11842:SF11 PTHR11842:SF11, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02301 HORMA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56019 SSF56019, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50815 HORMA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z1B5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQQLAREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG
60 70 80 90 100
LTLLTTTDPE LIKYLNNVVE QLKEWLYKCS VQKLVVVISN IESGEVLERW
110 120 130 140 150
QFDIECDKTA KEEGVRREKS QKAIQDEIRS VIRQITATVT FLPLLEVSCS
160 170 180 190 200
FDLLIYTDKD LVVPEKWEES GPQFITNCEE VRLRSFTTTI HKVNSMVAYK

TPVND
Length:205
Mass (Da):23,598
Last modified:January 11, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA9F3F28BC4C9738E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti157T → A in AAD09238 (Ref. 1) Curated1
Sequence conflicti178C → S in AAD09238 (Ref. 1) Curated1
Sequence conflicti201T → I in AAD09238 (Ref. 1) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U83902 mRNA Translation: AAD09238.1
AF261919 Genomic DNA Translation: AAF69525.1
AK082934 mRNA Translation: BAC38700.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20210.1

NCBI Reference Sequences

More...
RefSeqi
NP_062372.2, NM_019499.4
XP_006506469.1, XM_006506406.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.489653

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000101343; ENSMUSP00000098897; ENSMUSG00000029910
ENSMUST00000116605; ENSMUSP00000112304; ENSMUSG00000029910

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
56150

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:56150

UCSC genome browser

More...
UCSCi
uc009cen.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006506406.3
UniGeneiMm.489653

3D structure databases

ProteinModelPortaliQ9Z1B5
SMRiQ9Z1B5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207818, 106 interactors
ComplexPortaliCPX-3968 Mitotic Checkpoint Complex
CPX-87 Mitotic spindle assembly checkpoint Mad1-Mad2 complex
CPX-90 Mitotic spindle assembly checkpoint complex MAD2
IntActiQ9Z1B5, 108 interactors
MINTiQ9Z1B5
STRINGi10090.ENSMUSP00000098897

PTM databases

iPTMnetiQ9Z1B5
PhosphoSitePlusiQ9Z1B5

Proteomic databases

EPDiQ9Z1B5
MaxQBiQ9Z1B5
PaxDbiQ9Z1B5
PRIDEiQ9Z1B5
TopDownProteomicsiQ9Z1B5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4085
MGIiMGI:1860374 Mad2l1

Phylogenomic databases

eggNOGiKOG3285 Eukaryota
ENOG410XSD7 LUCA
GeneTreeiENSGT00940000153395
HOGENOMiHOG000199586
HOVERGENiHBG105691
InParanoidiQ9Z1B5
KOiK02537
OMAiVHRIEAM
OrthoDBi1197019at2759
PhylomeDBiQ9Z1B5
TreeFamiTF101084

Enzyme and pathway databases

ReactomeiR-MMU-141405 Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components
R-MMU-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9Z1B5

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000029910 Expressed in 294 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ9Z1B5 baseline and differential
GenevisibleiQ9Z1B5 MM

Family and domain databases

Gene3Di3.30.900.10, 1 hit
InterProiView protein in InterPro
IPR003511 HORMA_dom
IPR036570 HORMA_dom_sf
IPR027097 Mad2
PANTHERiPTHR11842:SF11 PTHR11842:SF11, 1 hit
PfamiView protein in Pfam
PF02301 HORMA, 1 hit
SUPFAMiSSF56019 SSF56019, 1 hit
PROSITEiView protein in PROSITE
PS50815 HORMA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMD2L1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Z1B5
Secondary accession number(s): Q9JI53
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: February 13, 2019
This is version 152 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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