Q9UI95 (MD2L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MAD2L2
Synonyms:	MAD2B, REV7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle. 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 process	Cell cycle Cell division DNA damage Mitosis Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction resulting in transcription Inferred from direct assay Ref.16. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW double-strand break repair Inferred from genetic interaction. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle spindle assembly checkpoint Traceable author statement. Source: ProtInc negative regulation of mitotic anaphase-promoting complex activity Inferred from direct assay Ref.11. Source: UniProtKB positive regulation of peptidyl-serine phosphorylation Inferred from direct assay Ref.16. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.16. Source: UniProtKB regulation of cell growth Inferred from genetic interaction. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome spindle Inferred from direct assay Ref.20. Source: UniProtKB zeta DNA polymerase complex Inferred from direct assay Ref.21. Source: UniProtKB
Molecular function	JUN kinase binding Inferred from direct assay Ref.16. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAM9	Q13443	3	EBI-77889,EBI-77903
CDC20	Q12834	2	EBI-77889,EBI-367462
CDC27	P30260	2	EBI-77889,EBI-994813
FZR1	Q9UM11	2	EBI-77889,EBI-724997
ipaB	P18011	7	EBI-77889,EBI-490239	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Mitotic spindle assembly checkpoint protein MAD2B

PRO_0000126119

Regions

Domain

13 – 203

191

HORMA

Region

21 – 155

135

Mediates interaction with REV1 and REV3L and homodimerization

Region

150 – 211

62

Mediates interaction with ipaB

Experimental info

Mutagenesis

63

1

Y → A: Alters interaction with REV3L. Loss of interaction with REV3L; when associated with A-171. Ref.21

Mutagenesis

124

1

R → A: Induces structural changes that increase affinity for REV3L and REV1. No effect on interaction with REV1; when associated with A-171. Ref.21

Mutagenesis

171

1

W → 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

Mutagenesis

186

1

L → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. Ref.21

Mutagenesis

200

1

Q → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. Ref.21

Mutagenesis

202

1

Y → A: Significantly prevents interaction with REV1; no effect on interaction with REV3L. Ref.21

Sequence conflict

17

1

D → A in AAD30290. Ref.3

Sequence conflict

96

1

E → D in AAF20267. Ref.2

Sequence conflict

199

1

M → V in AAF20267. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

211

Helix Strand Turn

Details...

Helix

14 – 33

20

Beta strand

42 – 47

6

Beta strand

50 – 55

6

Helix

58 – 76

19

Beta strand

80 – 88

9

Beta strand

94 – 103

10

Helix

115 – 131

17

Helix

133 – 135

3

Beta strand

145 – 152

8

Beta strand

171 – 173

3

Helix

176 – 179

4

Beta strand

182 – 193

12

Beta strand

198 – 207

10

Sequences

	Sequence		Length	Mass (Da)
	Q9UI95 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 1DE6353EF7D650B9	FASTA	211	24,334
	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

References

	« Hide 'large scale' referencesShow '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: 10527948] [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: 10366450] [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: 10660610] [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: 14702039] [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: 16710414] [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. , 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: 15489334] [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: 11459825] [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: 11459826] [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: 11485998] [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: 11717438] [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: 17719540] [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: 17541814] [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: 17296730] [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: 19443654] [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: 19753112] [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: 20850016] [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: 21063390] [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: 20164194] [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

NIEHS-SNPs

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.

IPI

IPI00006109.

RefSeq

NP_001120797.1. NM_001127325.1.
NP_006332.3. NM_006341.3.

UniGene

Hs.19400.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ABD	X-ray	1.90	A/B	1-211	[»]
3ABE	X-ray	2.60	C	1-211	[»]

ProteinModelPortal

Q9UI95.

SMR

Q9UI95. Positions 11-210.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UI95. 10 interactions.

MINT

MINT-108350.

STRING

Q9UI95.

Polymorphism databases

DMDM

12643889.

Proteomic databases

PRIDE

Q9UI95.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000235310; ENSP00000235310; ENSG00000116670.
ENST00000376667; ENSP00000365855; ENSG00000116670.
ENST00000376692; ENSP00000365882; ENSG00000116670.

GeneID

10459.

KEGG

hsa:10459.

UCSC

uc001asp.1. human.

Organism-specific databases

CTD

10459.

GeneCards

GC01M011668.

H-InvDB

HIX0000127.

HGNC

HGNC:6764. MAD2L2.

HPA

CAB008110.

MIM

604094. gene.

neXtProt

NX_Q9UI95.

PharmGKB

PA398.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18060.

GeneTree

ENSGT00500000044946.

HOVERGEN

HBG052443.

OrthoDB

EOG4NVZMB.

PhylomeDB

Q9UI95.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q9UI95.

Bgee

Q9UI95.

CleanEx

HS_MAD2L2.

Genevestigator

Q9UI95.

GermOnline

ENSG00000116670. Homo sapiens.

Family and domain databases

InterPro

IPR003511. HORMA_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.900.10. G3DSA:3.30.900.10. 1 hit.

KO

K13728.

Pfam

PF02301. HORMA. 1 hit.
[Graphical view]

SUPFAM

SSF56019. HORMA_DNA_bd. 1 hit.

PROSITE

PS50815. HORMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

39659.

SOURCE

Search...

Entry information

Entry name

MD2L2_HUMAN

Accession

Primary (citable) accession number: Q9UI95
Secondary accession number(s): B3KNE3 , Q5TGW7, Q9UNA7, Q9Y6I6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.