MD2L2_MOUSE
ID MD2L2_MOUSE Reviewed; 211 AA.
AC Q9D752; Q3TMY6; Q91VP1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mitotic spindle assembly checkpoint protein MAD2B;
DE AltName: Full=Mitotic arrest deficient 2-like protein 2;
DE Short=MAD2-like protein 2;
GN Name=Mad2l2; Synonyms=Mad2b, Rev7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH REV1.
RX PubMed=14657033; DOI=10.1093/emboj/cdg626;
RA Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K.,
RA Kisker C., Friedberg E.C.;
RT "Mouse Rev1 protein interacts with multiple DNA polymerases involved in
RT translesion DNA synthesis.";
RL EMBO J. 22:6621-6630(2003).
CC -!- FUNCTION: Adapter protein able to interact with different proteins and
CC involved in different biological processes. Mediates the interaction
CC between the error-prone DNA polymerase zeta catalytic subunit REV3L and
CC the inserter polymerase REV1, thereby mediating the second polymerase
CC switching in translesion DNA synthesis. Translesion DNA synthesis
CC releases the replication blockade of replicative polymerases, stalled
CC in presence of DNA lesions. Component of the shieldin complex, which
CC plays an important role in repair of DNA double-stranded breaks (DSBs).
CC During G1 and S phase of the cell cycle, the complex functions
CC downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and
CC suppress DNA end resection. Mediates various NHEJ-dependent processes
CC including immunoglobulin class-switch recombination, and fusion of
CC unprotected telomeres. May also regulate another aspect of cellular
CC response to DNA damage through regulation of the JNK-mediated
CC phosphorylation and activation of the transcriptional activator ELK1.
CC Inhibits the FZR1- and probably CDC20-mediated activation of the
CC anaphase promoting complex APC thereby regulating progression through
CC the cell cycle. Regulates TCF7L2-mediated gene transcription and may
CC play a role in epithelial-mesenchymal transdifferentiation.
CC {ECO:0000250|UniProtKB:Q9UI95}.
CC -!- SUBUNIT: Homooligomer (By similarity). Heterodimer with REV3L (By
CC similarity). This dimer forms the minimal DNA polymerase zeta complex
CC (Pol-zeta2), with REV3L bearing DNA polymerase catalytic activity,
CC although its activity is very low in this context (By similarity).
CC Component of the tetrameric Pol-zeta complex (Pol-zeta4), which
CC consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully
CC active form of DNA polymerase zeta (By similarity). Component of the
CC shieldin complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7.
CC Within the complex, SHLD2 forms a scaffold which interacts with a
CC SHLD3-MAD2L2 subcomplex via its N-terminus, and with SHLD1 via its C-
CC terminus (By similarity). Interacts with REV1 (PubMed:14657033).
CC Interacts with ADAM9 (By similarity). Interacts with CHAMP1 (By
CC similarity). Interacts with FZR1 (in complex with the anaphase
CC promoting complex APC) (By similarity). May interact with CDC20 (By
CC similarity). Interacts with RAN (By similarity). Interacts with ELK1;
CC the interaction is direct and recruits MAD2L2 to ELK1-specific
CC promoters (By similarity). May interact with the JNK kinases MAPK8
CC and/or MAPK9 to stimulate ELK1 phosphorylation and transcriptional
CC activity upon DNA damage (By similarity). Interacts with TCF7L2;
CC prevents its binding to promoters and negatively modulates its
CC transcriptional activity (By similarity). Interacts with YY1AP1 (By
CC similarity). Interacts with PRCC; the interaction is direct (By
CC similarity). Interacts with POGZ (By similarity).
CC {ECO:0000250|UniProtKB:Q9UI95, ECO:0000269|PubMed:14657033}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UI95}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UI95}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9UI95}. Chromosome
CC {ECO:0000250|UniProtKB:Q9UI95}. Note=Recruited to sites of chromosomal
CC double-stranded breaks during G1 and S phase of the cell cycle.
CC {ECO:0000250|UniProtKB:Q9UI95}.
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DR EMBL; AK009587; BAB26376.1; -; mRNA.
DR EMBL; AK150216; BAE29386.1; -; mRNA.
DR EMBL; AK165627; BAE38303.1; -; mRNA.
DR EMBL; BC011282; AAH11282.1; -; mRNA.
DR EMBL; BC071264; AAH71264.1; -; mRNA.
DR CCDS; CCDS18932.1; -.
DR RefSeq; NP_001292349.1; NM_001305420.1.
DR RefSeq; NP_082261.2; NM_027985.3.
DR RefSeq; XP_006539246.1; XM_006539183.2.
DR RefSeq; XP_006539249.1; XM_006539186.1.
DR RefSeq; XP_006539250.1; XM_006539187.2.
DR PDB; 4FJO; X-ray; 2.72 A; C=1-210.
DR PDB; 5O8K; X-ray; 1.80 A; A=1-211.
DR PDB; 6EKJ; X-ray; 1.60 A; A=1-211.
DR PDB; 6EKL; X-ray; 1.60 A; A=1-211.
DR PDB; 6EKM; X-ray; 2.76 A; A=1-211.
DR PDBsum; 4FJO; -.
DR PDBsum; 5O8K; -.
DR PDBsum; 6EKJ; -.
DR PDBsum; 6EKL; -.
DR PDBsum; 6EKM; -.
DR AlphaFoldDB; Q9D752; -.
DR SMR; Q9D752; -.
DR BioGRID; 215010; 31.
DR ComplexPortal; CPX-3483; Shieldin complex.
DR IntAct; Q9D752; 27.
DR STRING; 10090.ENSMUSP00000030860; -.
DR PhosphoSitePlus; Q9D752; -.
DR EPD; Q9D752; -.
DR MaxQB; Q9D752; -.
DR PaxDb; Q9D752; -.
DR PRIDE; Q9D752; -.
DR ProteomicsDB; 295983; -.
DR Antibodypedia; 3766; 203 antibodies from 30 providers.
DR DNASU; 71890; -.
DR Ensembl; ENSMUST00000030860; ENSMUSP00000030860; ENSMUSG00000029003.
DR Ensembl; ENSMUST00000084129; ENSMUSP00000081146; ENSMUSG00000029003.
DR GeneID; 71890; -.
DR KEGG; mmu:71890; -.
DR UCSC; uc008vub.2; mouse.
DR CTD; 10459; -.
DR MGI; MGI:1919140; Mad2l2.
DR VEuPathDB; HostDB:ENSMUSG00000029003; -.
DR eggNOG; KOG3186; Eukaryota.
DR GeneTree; ENSGT00940000153395; -.
DR InParanoid; Q9D752; -.
DR OMA; CEDFPWI; -.
DR OrthoDB; 1630737at2759; -.
DR PhylomeDB; Q9D752; -.
DR TreeFam; TF101085; -.
DR Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR BioGRID-ORCS; 71890; 34 hits in 98 CRISPR screens.
DR ChiTaRS; Mad2l2; mouse.
DR PRO; PR:Q9D752; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D752; protein.
DR Bgee; ENSMUSG00000029003; Expressed in undifferentiated genital tubercle and 230 other tissues.
DR ExpressionAtlas; Q9D752; baseline and differential.
DR Genevisible; Q9D752; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; IC:ComplexPortal.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISS:UniProtKB.
DR GO; GO:0008432; F:JUN kinase binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042772; P:DNA damage response, signal transduction resulting in transcription; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:0002208; P:somatic diversification of immunoglobulins involved in immune response; IC:ComplexPortal.
DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; IC:ComplexPortal.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR045091; Mad2-like.
DR PANTHER; PTHR11842; PTHR11842; 1.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
DR PROSITE; PS50815; HORMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Cytoskeleton; DNA damage; DNA repair; Mitosis; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..211
FT /note="Mitotic spindle assembly checkpoint protein MAD2B"
FT /id="PRO_0000126120"
FT DOMAIN 13..203
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT REGION 21..155
FT /note="Mediates interaction with REV1 and REV3L and
FT homodimerization"
FT /evidence="ECO:0000250"
FT CONFLICT 193
FT /note="T -> M (in Ref. 1; BAB26376)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4FJO"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 10..33
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4FJO"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6EKJ"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5O8K"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6EKJ"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:6EKJ"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:6EKJ"
SQ SEQUENCE 211 AA; 24402 MW; 0E47D0D8AC28AB5C CRC64;
MTTLTRQDLN FGQVVADVLS EFLEVAVHLI LYVREVYPVG IFQKRKKYNV PVQMSCHPEL
NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF EITQPPLLSI NSDSLLSHVE
QLLRAFILKI SVCDAVLDHN PPGCTFTVLV HTREAATRNM EKIQVIKDFP WILADEQDVH
MHDPRLIPLK TMTSDILKMQ LYVEERAHKN S
