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Q9UI95

- MD2L2_HUMAN

UniProt

Q9UI95 - MD2L2_HUMAN

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Protein

Mitotic spindle assembly checkpoint protein MAD2B

Gene
MAD2L2, MAD2B, REV7
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. JUN kinase binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. RNA polymerase II activating transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. actin filament organization Source: BHF-UCL
  2. DNA damage response, signal transduction resulting in transcription Source: UniProtKB
  3. DNA repair Source: Reactome
  4. double-strand break repair Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB-KW
  6. mitotic spindle assembly checkpoint Source: ProtInc
  7. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  8. negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  9. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  10. negative regulation of mitotic anaphase-promoting complex activity Source: UniProtKB
  11. negative regulation of protein catabolic process Source: UniProtKB
  12. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  13. negative regulation of transcription by competitive promoter binding Source: BHF-UCL
  14. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  15. negative regulation of transcription regulatory region DNA binding Source: BHF-UCL
  16. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  17. positive regulation of transcription, DNA-templated Source: UniProtKB
  18. regulation of cell growth Source: UniProtKB
  19. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_822. Translesion synthesis by Pol zeta.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6764. MAD2L2.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonspindle. Cytoplasm 5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. spindle Source: UniProtKB
  5. zeta DNA polymerase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631Y → A: Alters interaction with REV3L. Loss of interaction with REV3L; when associated with A-171. 1 Publication
Mutagenesisi124 – 1241R → A: Induces structural changes that increase affinity for REV3L and REV1. No effect on interaction with REV1; when associated with A-171. 1 Publication
Mutagenesisi171 – 1711W → 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 Publication
Mutagenesisi186 – 1861L → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication
Mutagenesisi200 – 2001Q → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication
Mutagenesisi202 – 2021Y → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. 1 Publication

Organism-specific databases

PharmGKBiPA398.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Mitotic spindle assembly checkpoint protein MAD2BPRO_0000126119Add
BLAST

Proteomic databases

MaxQBiQ9UI95.
PaxDbiQ9UI95.
PRIDEiQ9UI95.

PTM databases

PhosphoSiteiQ9UI95.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

ArrayExpressiQ9UI95.
BgeeiQ9UI95.
CleanExiHS_MAD2L2.
GenevestigatoriQ9UI95.

Organism-specific databases

HPAiCAB008110.

Interactioni

Subunit structurei

Homooligomer Inferred. Interacts with REV1. Interacts with ADAM9. Interacts with CHAMP1. Interacts with REV3L. Interacts with FZR1 (in complex with the anaphase promoting complex APC). Interacts with CDC20; 1 Publication 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.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM9Q134433EBI-77889,EBI-77903
CDC20Q128342EBI-77889,EBI-367462
CDC27P302602EBI-77889,EBI-994813
CHAMP1Q96JM33EBI-77889,EBI-2560420
FZR1Q9UM112EBI-77889,EBI-724997
ipaBP180117EBI-77889,EBI-490239From a different organism.
REV3LO606735EBI-77889,EBI-2871302

Protein-protein interaction databases

BioGridi115722. 22 interactions.
IntActiQ9UI95. 13 interactions.
MINTiMINT-108350.
STRINGi9606.ENSP00000235310.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 3321
Helixi39 – 413
Beta strandi42 – 476
Beta strandi50 – 556
Helixi58 – 7619
Beta strandi80 – 889
Beta strandi90 – 923
Beta strandi94 – 10310
Helixi115 – 13117
Helixi133 – 1353
Beta strandi145 – 1528
Helixi157 – 1637
Beta strandi171 – 1733
Helixi176 – 1794
Beta strandi182 – 19312
Beta strandi198 – 20710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-209.

Miscellaneous databases

EvolutionaryTraceiQ9UI95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 203191HORMAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 155135Mediates interaction with REV1 and REV3L and homodimerizationAdd
BLAST
Regioni150 – 21162Mediates interaction with ipaBAdd
BLAST

Sequence similaritiesi

Contains 1 HORMA domain.

Phylogenomic databases

eggNOGiNOG292947.
HOGENOMiHOG000231083.
HOVERGENiHBG052443.
KOiK13728.
OrthoDBiEOG7SN8FC.
PhylomeDBiQ9UI95.
TreeFamiTF101085.

Family and domain databases

Gene3Di3.30.900.10. 1 hit.
InterProiIPR003511. HORMA_DNA-bd.
[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

MTTLTRQDLN FGQVVADVLC EFLEVAVHLI LYVREVYPVG IFQKRKKYNV    50
PVQMSCHPEL NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF 100
EITQPPLLSI SSDSLLSHVE QLLRAFILKI SVCDAVLDHN PPGCTFTVLV 150
HTREAATRNM EKIQVIKDFP WILADEQDVH MHDPRLIPLK TMTSDILKMQ 200
LYVEERAHKG S 211
Length:211
Mass (Da):24,334
Last modified:January 11, 2001 - v2
Checksum:i1DE6353EF7D650B9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171D → A in AAD30290. 1 Publication
Sequence conflicti96 – 961E → D in AAF20267. 1 Publication
Sequence conflicti199 – 1991M → V in AAF20267. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UniGeneiHs.19400.

Genome annotation databases

EnsembliENST00000235310; ENSP00000235310; ENSG00000116670.
ENST00000376667; ENSP00000365855; ENSG00000116670.
ENST00000376692; ENSP00000365882; ENSG00000116670.
GeneIDi10459.
KEGGihsa:10459.
UCSCiuc001asp.3. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS134.1.
RefSeqi NP_001120797.1. NM_001127325.1.
NP_006332.3. NM_006341.3.
UniGenei Hs.19400.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ABD X-ray 1.90 A/B 1-211 [» ]
3ABE X-ray 2.60 C 1-211 [» ]
3VU7 X-ray 2.80 C 1-211 [» ]
4EXT X-ray 1.90 C 7-209 [» ]
4GK0 X-ray 2.70 A/B 1-211 [» ]
4GK5 X-ray 3.21 A/B 1-211 [» ]
ProteinModelPortali Q9UI95.
SMRi Q9UI95. Positions 1-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115722. 22 interactions.
IntActi Q9UI95. 13 interactions.
MINTi MINT-108350.
STRINGi 9606.ENSP00000235310.

PTM databases

PhosphoSitei Q9UI95.

Proteomic databases

MaxQBi Q9UI95.
PaxDbi Q9UI95.
PRIDEi Q9UI95.

Protocols and materials databases

DNASUi 10459.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000235310 ; ENSP00000235310 ; ENSG00000116670 .
ENST00000376667 ; ENSP00000365855 ; ENSG00000116670 .
ENST00000376692 ; ENSP00000365882 ; ENSG00000116670 .
GeneIDi 10459.
KEGGi hsa:10459.
UCSCi uc001asp.3. human.

Organism-specific databases

CTDi 10459.
GeneCardsi GC01M011734.
HGNCi HGNC:6764. MAD2L2.
HPAi CAB008110.
MIMi 604094. gene.
neXtProti NX_Q9UI95.
PharmGKBi PA398.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292947.
HOGENOMi HOG000231083.
HOVERGENi HBG052443.
KOi K13728.
OrthoDBi EOG7SN8FC.
PhylomeDBi Q9UI95.
TreeFami TF101085.

Enzyme and pathway databases

Reactomei REACT_822. Translesion synthesis by Pol zeta.

Miscellaneous databases

ChiTaRSi MAD2L2. human.
EvolutionaryTracei Q9UI95.
GeneWikii MAD2L2.
GenomeRNAii 10459.
NextBioi 39659.
PROi Q9UI95.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UI95.
Bgeei Q9UI95.
CleanExi HS_MAD2L2.
Genevestigatori Q9UI95.

Family and domain databases

Gene3Di 3.30.900.10. 1 hit.
InterProi IPR003511. HORMA_DNA-bd.
[Graphical view ]
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. "Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2-beta."
    Nelson K.K., Schlondorff J., Blobel C.P.
    Biochem. J. 343:673-680(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ADAM9.
  2. "Identification of a novel human homolog of the MAD2 protein that interacts with the h-warts protein."
    Hirota T., Nakamura H., Tada K., Marumoto T., Saya H.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Characterization of MAD2B and other mitotic spindle checkpoint genes."
    Cahill D.P., da Costa L.T., Carson-Walter E.B., Kinzler K.W., Vogelstein B., Lengauer C.
    Genomics 58:181-187(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2."
    Murakumo Y., Roth T., Ishii H., Rasio D., Numata S., Croce C.M., Fishel R.
    J. Biol. Chem. 275:4391-4397(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH REV3L.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum and Embryo.
  6. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Skin.
  10. "Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1."
    Pfleger C.M., Salic A., Lee E., Kirschner M.W.
    Genes Dev. 15:1759-1764(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FZR1.
  11. "MAD2B is an inhibitor of the anaphase-promoting complex."
    Chen J., Fang G.
    Genes Dev. 15:1765-1770(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FZR1 AND CDC20.
  12. "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7."
    Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M., Fishel R., Takahashi M.
    J. Biol. Chem. 276:35644-35651(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REV1 AND REV3L, HOMOOLIGOMERIZATION.
  13. "Impairment of MAD2B-PRCC interaction in mitotic checkpoint defective t(X;1)-positive renal cell carcinomas."
    Weterman M.A., van Groningen J.J., Tertoolen L., van Kessel A.G.
    Proc. Natl. Acad. Sci. U.S.A. 98:13808-13813(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRCC, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  14. "A bacterial effector targets Mad2L2, an APC inhibitor, to modulate host cell cycling."
    Iwai H., Kim M., Yoshikawa Y., Ashida H., Ogawa M., Fujita Y., Muller D., Kirikae T., Jackson P.K., Kotani S., Sasakawa C.
    Cell 130:611-623(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APC REGULATION, INTERACTION WITH SHIGELLA FLEXNERI IPAB; FZR1 AND CDC20, SUBCELLULAR LOCATION.
  15. "Hepatocellular carcinoma-associated gene 2 interacts with MAD2L2."
    Li L., Shi Y., Wu H., Wan B., Li P., Zhou L., Shi H., Huo K.
    Mol. Cell. Biochem. 304:297-304(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YY1AP1, SUBCELLULAR LOCATION.
  16. "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1."
    Zhang L., Yang S.H., Sharrocks A.D.
    Mol. Cell. Biol. 27:2861-2869(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ELK1 AND JNK KINASES.
  17. "MAD2B, a novel TCF4-binding protein, modulates TCF4-mediated epithelial-mesenchymal transdifferentiation."
    Hong C.F., Chou Y.T., Lin Y.S., Wu C.W.
    J. Biol. Chem. 284:19613-19622(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TCF7L2.
  18. "The mitotic arrest deficient protein MAD2B interacts with the small GTPase RAN throughout the cell cycle."
    Medendorp K., van Groningen J.J., Vreede L., Hetterschijt L., van den Hurk W.H., de Bruijn D.R., Brugmans L., van Kessel A.G.
    PLoS ONE 4:E7020-E7020(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAN, SUBCELLULAR LOCATION.
  19. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
    Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
    Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POGZ.
  20. "CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule attachment."
    Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K., Mizuno K., Yasui A., Hirota T., Tanaka K.
    EMBO J. 30:130-144(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHAMP1, SUBCELLULAR LOCATION.
  21. "Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1."
    Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S., Akashi S., Takeda S., Shimizu T., Sato M.
    J. Biol. Chem. 285:12299-12307(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH REV3L, MUTAGENESIS OF TYR-63; ARG-124; TRP-171; LEU-186; GLN-200 AND TYR-202, INTERACTION WITH REV1.

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: September 3, 2014
This is version 118 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

External Data

Dasty 3

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