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Q9UI95 (MD2L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MAD2L2
Synonyms:MAD2B, REV7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.14 Ref.16 Ref.17

Subunit structure

Homooligomer Probable. 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; Ref.10 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. Ref.1 Ref.4 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle. Cytoplasm Ref.13 Ref.14 Ref.15 Ref.18 Ref.20.

Tissue specificity

Ubiquitously expressed. Ref.13

Sequence similarities

Contains 1 HORMA domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
Mitosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction resulting in transcription

Inferred from direct assay Ref.16. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

actin filament organization

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

double-strand break repair

Inferred from genetic interaction PubMed 15988022. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle assembly checkpoint

Traceable author statement Ref.3. Source: ProtInc

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

negative regulation of cell-cell adhesion mediated by cadherin

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

negative regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

negative regulation of mitotic anaphase-promoting complex activity

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of protein catabolic process

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.17. Source: BHF-UCL

negative regulation of transcription by competitive promoter binding

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.17. Source: BHF-UCL

negative regulation of transcription regulatory region DNA binding

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.16. Source: UniProtKB

regulation of cell growth

Inferred from genetic interaction PubMed 15988022. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

spindle

Inferred from direct assay Ref.20. Source: UniProtKB

zeta DNA polymerase complex

Inferred from direct assay Ref.21. Source: UniProtKB

   Molecular_functionJUN kinase binding

Inferred from direct assay Ref.16. Source: UniProtKB

RNA polymerase II activating transcription factor binding

Inferred from physical interaction Ref.17. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.11Ref.12Ref.13Ref.16Ref.15Ref.19Ref.20. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Mitotic spindle assembly checkpoint protein MAD2B
PRO_0000126119

Regions

Domain13 – 203191HORMA
Region21 – 155135Mediates interaction with REV1 and REV3L and homodimerization
Region150 – 21162Mediates interaction with ipaB

Experimental info

Mutagenesis631Y → A: Alters interaction with REV3L. Loss of interaction with REV3L; when associated with A-171. Ref.21
Mutagenesis1241R → A: Induces structural changes that increase affinity for REV3L and REV1. No effect on interaction with REV1; when associated with A-171. Ref.21
Mutagenesis1711W → 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. Ref.21
Mutagenesis1861L → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. Ref.21
Mutagenesis2001Q → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. Ref.21
Mutagenesis2021Y → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. Ref.21
Sequence conflict171D → A in AAD30290. Ref.3
Sequence conflict961E → D in AAF20267. Ref.2
Sequence conflict1991M → V in AAF20267. Ref.2

Secondary structure

................................ 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UI95 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 1DE6353EF7D650B9

FASTA21124,334
        10         20         30         40         50         60 
MTTLTRQDLN FGQVVADVLC EFLEVAVHLI LYVREVYPVG IFQKRKKYNV PVQMSCHPEL 

        70         80         90        100        110        120 
NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF EITQPPLLSI SSDSLLSHVE 

       130        140        150        160        170        180 
QLLRAFILKI SVCDAVLDHN PPGCTFTVLV HTREAATRNM EKIQVIKDFP WILADEQDVH 

       190        200        210 
MHDPRLIPLK TMTSDILKMQ LYVEERAHKG S 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS134.1.
RefSeqNP_001120797.1. NM_001127325.1.
NP_006332.3. NM_006341.3.
UniGeneHs.19400.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9UI95.
SMRQ9UI95. Positions 1-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115722. 22 interactions.
IntActQ9UI95. 13 interactions.
MINTMINT-108350.
STRING9606.ENSP00000235310.

PTM databases

PhosphoSiteQ9UI95.

Proteomic databases

MaxQBQ9UI95.
PaxDbQ9UI95.
PRIDEQ9UI95.

Protocols and materials databases

DNASU10459.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000235310; ENSP00000235310; ENSG00000116670.
ENST00000376667; ENSP00000365855; ENSG00000116670.
ENST00000376692; ENSP00000365882; ENSG00000116670.
GeneID10459.
KEGGhsa:10459.
UCSCuc001asp.3. human.

Organism-specific databases

CTD10459.
GeneCardsGC01M011734.
HGNCHGNC:6764. MAD2L2.
HPACAB008110.
MIM604094. gene.
neXtProtNX_Q9UI95.
PharmGKBPA398.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292947.
HOGENOMHOG000231083.
HOVERGENHBG052443.
KOK13728.
OrthoDBEOG7SN8FC.
PhylomeDBQ9UI95.
TreeFamTF101085.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ9UI95.
BgeeQ9UI95.
CleanExHS_MAD2L2.
GenevestigatorQ9UI95.

Family and domain databases

Gene3D3.30.900.10. 1 hit.
InterProIPR003511. HORMA_DNA-bd.
[Graphical view]
PfamPF02301. HORMA. 1 hit.
[Graphical view]
SUPFAMSSF56019. SSF56019. 1 hit.
PROSITEPS50815. HORMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAD2L2. human.
EvolutionaryTraceQ9UI95.
GeneWikiMAD2L2.
GenomeRNAi10459.
NextBio39659.
PROQ9UI95.
SOURCESearch...

Entry information

Entry nameMD2L2_HUMAN
AccessionPrimary (citable) accession number: Q9UI95
Secondary accession number(s): B3KNE3 expand/collapse secondary AC list , Q5TGW7, Q9UNA7, Q9Y6I6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM