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Protein

Mitotic spindle assembly checkpoint protein MAD2B

Gene

Mad2l2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.

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
Gene namesi
Name:Mad2l2
Synonyms:Mad2b, Rev7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1919140. Mad2l2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Mitotic spindle assembly checkpoint protein MAD2BPRO_0000126120Add
BLAST

Proteomic databases

MaxQBiQ9D752.
PaxDbiQ9D752.
PRIDEiQ9D752.

PTM databases

PhosphoSiteiQ9D752.

Expressioni

Gene expression databases

BgeeiQ9D752.
CleanExiMM_MAD2L2.
ExpressionAtlasiQ9D752. baseline and differential.
GenevisibleiQ9D752. MM.

Interactioni

Subunit structurei

Homooligomer. Interacts with ADAM9. Interacts with CHAMP1. Interacts with REV3L. Interacts with FZR1 (in complex with the anaphase promoting complex APC). May interact with CDC20. 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 PRCC; the interaction is direct. Interacts with POGZ (By similarity). Interacts with REV1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi215010. 30 interactions.
IntActiQ9D752. 28 interactions.
STRINGi10090.ENSMUSP00000030860.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Turni6 – 83Combined sources
Helixi11 – 3323Combined sources
Helixi39 – 413Combined sources
Beta strandi42 – 476Combined sources
Beta strandi50 – 556Combined sources
Helixi58 – 7619Combined sources
Beta strandi80 – 889Combined sources
Beta strandi94 – 10310Combined sources
Beta strandi109 – 1113Combined sources
Turni112 – 1165Combined sources
Helixi117 – 13115Combined sources
Helixi133 – 1364Combined sources
Beta strandi145 – 15410Combined sources
Helixi157 – 1626Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 1794Combined sources
Beta strandi182 – 19211Combined sources
Beta strandi198 – 20811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FJOX-ray2.72C1-210[»]
ProteinModelPortaliQ9D752.
SMRiQ9D752. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 203191HORMAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 155135Mediates interaction with REV1 and REV3L and homodimerizationBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 HORMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3186. Eukaryota.
ENOG4111I7Q. LUCA.
GeneTreeiENSGT00500000044946.
HOGENOMiHOG000231083.
HOVERGENiHBG052443.
InParanoidiQ9D752.
KOiK13728.
OMAiNNNPPGC.
OrthoDBiEOG7SN8FC.
PhylomeDBiQ9D752.
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.

Q9D752-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLTRQDLN FGQVVADVLS EFLEVAVHLI LYVREVYPVG IFQKRKKYNV
60 70 80 90 100
PVQMSCHPEL NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF
110 120 130 140 150
EITQPPLLSI NSDSLLSHVE QLLRAFILKI SVCDAVLDHN PPGCTFTVLV
160 170 180 190 200
HTREAATRNM EKIQVIKDFP WILADEQDVH MHDPRLIPLK TMTSDILKMQ
210
LYVEERAHKN S
Length:211
Mass (Da):24,402
Last modified:April 26, 2004 - v2
Checksum:i0E47D0D8AC28AB5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931T → M in BAB26376 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009587 mRNA. Translation: BAB26376.1.
AK150216 mRNA. Translation: BAE29386.1.
AK165627 mRNA. Translation: BAE38303.1.
BC011282 mRNA. Translation: AAH11282.1.
BC071264 mRNA. Translation: AAH71264.1.
CCDSiCCDS18932.1.
RefSeqiNP_001292349.1. NM_001305420.1.
NP_082261.2. NM_027985.3.
XP_006536038.1. XM_006535975.2.
XP_006536039.1. XM_006535976.1.
XP_006539246.1. XM_006539183.1.
XP_006539249.1. XM_006539186.1.
XP_006539250.1. XM_006539187.2.
UniGeneiMm.9648.

Genome annotation databases

EnsembliENSMUST00000030860; ENSMUSP00000030860; ENSMUSG00000029003.
ENSMUST00000084129; ENSMUSP00000081146; ENSMUSG00000029003.
GeneIDi71890.
KEGGimmu:71890.
UCSCiuc008vub.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009587 mRNA. Translation: BAB26376.1.
AK150216 mRNA. Translation: BAE29386.1.
AK165627 mRNA. Translation: BAE38303.1.
BC011282 mRNA. Translation: AAH11282.1.
BC071264 mRNA. Translation: AAH71264.1.
CCDSiCCDS18932.1.
RefSeqiNP_001292349.1. NM_001305420.1.
NP_082261.2. NM_027985.3.
XP_006536038.1. XM_006535975.2.
XP_006536039.1. XM_006535976.1.
XP_006539246.1. XM_006539183.1.
XP_006539249.1. XM_006539186.1.
XP_006539250.1. XM_006539187.2.
UniGeneiMm.9648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FJOX-ray2.72C1-210[»]
ProteinModelPortaliQ9D752.
SMRiQ9D752. Positions 1-210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215010. 30 interactions.
IntActiQ9D752. 28 interactions.
STRINGi10090.ENSMUSP00000030860.

PTM databases

PhosphoSiteiQ9D752.

Proteomic databases

MaxQBiQ9D752.
PaxDbiQ9D752.
PRIDEiQ9D752.

Protocols and materials databases

DNASUi71890.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030860; ENSMUSP00000030860; ENSMUSG00000029003.
ENSMUST00000084129; ENSMUSP00000081146; ENSMUSG00000029003.
GeneIDi71890.
KEGGimmu:71890.
UCSCiuc008vub.2. mouse.

Organism-specific databases

CTDi10459.
MGIiMGI:1919140. Mad2l2.

Phylogenomic databases

eggNOGiKOG3186. Eukaryota.
ENOG4111I7Q. LUCA.
GeneTreeiENSGT00500000044946.
HOGENOMiHOG000231083.
HOVERGENiHBG052443.
InParanoidiQ9D752.
KOiK13728.
OMAiNNNPPGC.
OrthoDBiEOG7SN8FC.
PhylomeDBiQ9D752.
TreeFamiTF101085.

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.

Miscellaneous databases

PROiQ9D752.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D752.
CleanExiMM_MAD2L2.
ExpressionAtlasiQ9D752. baseline and differential.
GenevisibleiQ9D752. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    Tissue: Bone marrow and Tongue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Limb and Mammary tumor.
  3. "Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis."
    Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K., Kisker C., Friedberg E.C.
    EMBO J. 22:6621-6630(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REV1.

Entry informationi

Entry nameiMD2L2_MOUSE
AccessioniPrimary (citable) accession number: Q9D752
Secondary accession number(s): Q3TMY6, Q91VP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: June 8, 2016
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.