Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mitotic spindle assembly checkpoint protein MAD2B

Gene

MAD2L2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.5 Publications

GO - Molecular functioni

  • JUN kinase binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL

GO - Biological processi

  • actin filament organization Source: BHF-UCL
  • cell division Source: UniProtKB-KW
  • DNA damage response, signal transduction resulting in transcription Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • error-prone translesion synthesis Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • mitotic spindle assembly checkpoint Source: ProtInc
  • negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  • negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • negative regulation of protein catabolic process Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • negative regulation of transcription by competitive promoter binding Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of transcription regulatory region DNA binding Source: BHF-UCL
  • negative regulation of ubiquitin protein ligase activity Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of cell growth Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Mitosis, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000116670-MONOMER.
ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
SIGNORiQ9UI95.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitotic spindle assembly checkpoint protein MAD2B
Alternative name(s):
Mitotic arrest deficient 2-like protein 2
Short name:
MAD2-like protein 2
REV7 homolog
Short name:
hREV7
Gene namesi
Name:MAD2L2
Synonyms:MAD2B, REV7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6764. MAD2L2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB
  • zeta DNA polymerase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63Y → A: Alters interaction with REV3L. Loss of interaction with REV3L; when associated with A-171. 1 Publication1
Mutagenesisi124R → A: Induces structural changes that increase affinity for REV3L and REV1. No effect on interaction with REV1; when associated with A-171. 1 Publication1
Mutagenesisi171W → A: Alters interaction with REV3L and REV1. Loss of interaction with REV3L; when associated with A-63. No effect on interaction with REV1; when associated with A-124. 1 Publication1
Mutagenesisi186L → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication1
Mutagenesisi200Q → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication1
Mutagenesisi202Y → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication1

Organism-specific databases

DisGeNETi10459.
OpenTargetsiENSG00000116670.
PharmGKBiPA398.

Polymorphism and mutation databases

BioMutaiMAD2L2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001261191 – 211Mitotic spindle assembly checkpoint protein MAD2BAdd BLAST211

Proteomic databases

EPDiQ9UI95.
MaxQBiQ9UI95.
PaxDbiQ9UI95.
PeptideAtlasiQ9UI95.
PRIDEiQ9UI95.
TopDownProteomicsiQ9UI95.

PTM databases

iPTMnetiQ9UI95.
PhosphoSitePlusiQ9UI95.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000116670.
CleanExiHS_MAD2L2.
ExpressionAtlasiQ9UI95. baseline and differential.
GenevisibleiQ9UI95. HS.

Organism-specific databases

HPAiCAB008110.
HPA024176.

Interactioni

Subunit structurei

Homooligomer (Probable). Interacts with REV1. Interacts with ADAM9. Interacts with CHAMP1. Interacts with FZR1 (in complex with the anaphase promoting complex APC). Interacts with CDC20; PubMed:11459825 could not detect the interaction. Interacts with RAN. Interacts with ELK1; the interaction is direct and recruits MAD2L2 to ELK1-specific promoters. May interact with the JNK kinases MAPK8 and/or MAPK9 to stimulate ELK1 phosphorylation and transcriptional activity upon DNA damage. Interacts with TCF7L2; prevents its binding to promoters and negatively modulates its transcriptional activity. Interacts with YY1AP1. Interacts with S.flexneri protein ipaB; prevents the interaction of MAD2L2 with FZR1 and CDC20 resulting in an activation of the anaphase-promoting complex APC and a cell cycle arrest. Interacts with PRCC; the interaction is direct. Interacts with POGZ. Heterodimer with REV3L. This dimer forms the minimal DNA polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase catalytic activity, although its activity is very low in this context. Component of the tetrameric Pol-zeta complex (Pol-zeta4), which consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully active form of DNA polymerase zeta (PubMed:24449906).Curated15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM9Q134433EBI-77889,EBI-77903
CAMK2BQ135543EBI-77889,EBI-1058722
CDC20Q128342EBI-77889,EBI-367462
CDC27P302602EBI-77889,EBI-994813
CHAMP1Q96JM34EBI-77889,EBI-2560420
FZR1Q9UM112EBI-77889,EBI-724997
IKZF1Q134223EBI-77889,EBI-745305
ipaBP180117EBI-77889,EBI-490239From a different organism.
KCTD9Q7L2733EBI-77889,EBI-4397613
RELQ048643EBI-77889,EBI-307352
REV3LO606735EBI-77889,EBI-2871302
SFI1A8K8P3-43EBI-77889,EBI-10321817
TCF4P158843EBI-77889,EBI-533224
TRIM27P143733EBI-77889,EBI-719493

GO - Molecular functioni

  • JUN kinase binding Source: UniProtKB
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi115722. 57 interactors.
IntActiQ9UI95. 38 interactors.
MINTiMINT-108350.
STRINGi9606.ENSP00000235310.

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 33Combined sources21
Helixi39 – 41Combined sources3
Beta strandi42 – 47Combined sources6
Beta strandi50 – 55Combined sources6
Helixi58 – 76Combined sources19
Beta strandi80 – 88Combined sources9
Beta strandi90 – 92Combined sources3
Beta strandi94 – 103Combined sources10
Helixi115 – 131Combined sources17
Helixi133 – 135Combined sources3
Beta strandi145 – 152Combined sources8
Helixi157 – 163Combined sources7
Beta strandi171 – 173Combined sources3
Helixi176 – 179Combined sources4
Beta strandi182 – 193Combined sources12
Beta strandi198 – 207Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ABDX-ray1.90A/B1-211[»]
3ABEX-ray2.60C1-211[»]
3VU7X-ray2.80C1-211[»]
4EXTX-ray1.90C7-209[»]
4GK0X-ray2.70A/B1-211[»]
4GK5X-ray3.21A/B1-211[»]
ProteinModelPortaliQ9UI95.
SMRiQ9UI95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UI95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 203HORMAPROSITE-ProRule annotationAdd BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 155Mediates interaction with REV1 and REV3L and homodimerizationAdd BLAST135
Regioni150 – 211Mediates interaction with ipaBAdd BLAST62

Sequence similaritiesi

Contains 1 HORMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3186. Eukaryota.
ENOG4111I7Q. LUCA.
GeneTreeiENSGT00500000044946.
HOGENOMiHOG000231083.
HOVERGENiHBG052443.
InParanoidiQ9UI95.
KOiK13728.
PhylomeDBiQ9UI95.
TreeFamiTF101085.

Family and domain databases

Gene3Di3.30.900.10. 1 hit.
InterProiIPR003511. HORMA_dom.
[Graphical view]
PfamiPF02301. HORMA. 1 hit.
[Graphical view]
SUPFAMiSSF56019. SSF56019. 1 hit.
PROSITEiPS50815. HORMA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UI95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLTRQDLN FGQVVADVLC EFLEVAVHLI LYVREVYPVG IFQKRKKYNV
60 70 80 90 100
PVQMSCHPEL NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF
110 120 130 140 150
EITQPPLLSI SSDSLLSHVE QLLRAFILKI SVCDAVLDHN PPGCTFTVLV
160 170 180 190 200
HTREAATRNM EKIQVIKDFP WILADEQDVH MHDPRLIPLK TMTSDILKMQ
210
LYVEERAHKG S
Length:211
Mass (Da):24,334
Last modified:January 11, 2001 - v2
Checksum:i1DE6353EF7D650B9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17D → A in AAD30290 (PubMed:10366450).Curated1
Sequence conflicti96E → D in AAF20267 (Ref. 2) Curated1
Sequence conflicti199M → V in AAF20267 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072933 mRNA. Translation: AAD41647.1.
AF080398 mRNA. Translation: AAF20267.1.
AF139365 mRNA. Translation: AAD30290.1.
AF157482 mRNA. Translation: AAF34357.1.
AK027327 mRNA. Translation: BAG51305.1.
AK094316 mRNA. Translation: BAG52858.1.
DQ017900 Genomic DNA. Translation: AAY26393.1.
AL031731 Genomic DNA. Translation: CAI20218.1.
CH471130 Genomic DNA. Translation: EAW71697.1.
BC015244 mRNA. Translation: AAH15244.1.
CCDSiCCDS134.1.
RefSeqiNP_001120797.1. NM_001127325.1.
NP_006332.3. NM_006341.3.
XP_011538809.1. XM_011540507.1.
UniGeneiHs.19400.

Genome annotation databases

EnsembliENST00000235310; ENSP00000235310; ENSG00000116670.
ENST00000376667; ENSP00000365855; ENSG00000116670.
ENST00000376692; ENSP00000365882; ENSG00000116670.
GeneIDi10459.
KEGGihsa:10459.
UCSCiuc001asp.4. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072933 mRNA. Translation: AAD41647.1.
AF080398 mRNA. Translation: AAF20267.1.
AF139365 mRNA. Translation: AAD30290.1.
AF157482 mRNA. Translation: AAF34357.1.
AK027327 mRNA. Translation: BAG51305.1.
AK094316 mRNA. Translation: BAG52858.1.
DQ017900 Genomic DNA. Translation: AAY26393.1.
AL031731 Genomic DNA. Translation: CAI20218.1.
CH471130 Genomic DNA. Translation: EAW71697.1.
BC015244 mRNA. Translation: AAH15244.1.
CCDSiCCDS134.1.
RefSeqiNP_001120797.1. NM_001127325.1.
NP_006332.3. NM_006341.3.
XP_011538809.1. XM_011540507.1.
UniGeneiHs.19400.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ABDX-ray1.90A/B1-211[»]
3ABEX-ray2.60C1-211[»]
3VU7X-ray2.80C1-211[»]
4EXTX-ray1.90C7-209[»]
4GK0X-ray2.70A/B1-211[»]
4GK5X-ray3.21A/B1-211[»]
ProteinModelPortaliQ9UI95.
SMRiQ9UI95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115722. 57 interactors.
IntActiQ9UI95. 38 interactors.
MINTiMINT-108350.
STRINGi9606.ENSP00000235310.

PTM databases

iPTMnetiQ9UI95.
PhosphoSitePlusiQ9UI95.

Polymorphism and mutation databases

BioMutaiMAD2L2.

Proteomic databases

EPDiQ9UI95.
MaxQBiQ9UI95.
PaxDbiQ9UI95.
PeptideAtlasiQ9UI95.
PRIDEiQ9UI95.
TopDownProteomicsiQ9UI95.

Protocols and materials databases

DNASUi10459.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000235310; ENSP00000235310; ENSG00000116670.
ENST00000376667; ENSP00000365855; ENSG00000116670.
ENST00000376692; ENSP00000365882; ENSG00000116670.
GeneIDi10459.
KEGGihsa:10459.
UCSCiuc001asp.4. human.

Organism-specific databases

CTDi10459.
DisGeNETi10459.
GeneCardsiMAD2L2.
HGNCiHGNC:6764. MAD2L2.
HPAiCAB008110.
HPA024176.
MIMi604094. gene.
neXtProtiNX_Q9UI95.
OpenTargetsiENSG00000116670.
PharmGKBiPA398.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3186. Eukaryota.
ENOG4111I7Q. LUCA.
GeneTreeiENSGT00500000044946.
HOGENOMiHOG000231083.
HOVERGENiHBG052443.
InParanoidiQ9UI95.
KOiK13728.
PhylomeDBiQ9UI95.
TreeFamiTF101085.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000116670-MONOMER.
ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
SIGNORiQ9UI95.

Miscellaneous databases

ChiTaRSiMAD2L2. human.
EvolutionaryTraceiQ9UI95.
GeneWikiiMAD2L2.
GenomeRNAii10459.
PROiQ9UI95.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116670.
CleanExiHS_MAD2L2.
ExpressionAtlasiQ9UI95. baseline and differential.
GenevisibleiQ9UI95. HS.

Family and domain databases

Gene3Di3.30.900.10. 1 hit.
InterProiIPR003511. HORMA_dom.
[Graphical view]
PfamiPF02301. HORMA. 1 hit.
[Graphical view]
SUPFAMiSSF56019. SSF56019. 1 hit.
PROSITEiPS50815. HORMA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMD2L2_HUMAN
AccessioniPrimary (citable) accession number: Q9UI95
Secondary accession number(s): B3KNE3
, Q5TGW7, Q9UNA7, Q9Y6I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 141 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.