Reviewed, UniProtKB/Swiss-Prot Q13257 (MD2L1_HUMAN)

Names and origin

Protein names

Recommended name:
    Mitotic spindle assembly checkpoint protein MAD2A
      Short name=HsMAD2
Alternative name(s):
    Mitotic arrest deficient 2-like protein 1
      Short name=MAD2-like protein 1

Gene names

Name:	MAD2L1
Synonyms:	MAD2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate. Ref.23 Ref.25 Ref.26
Subunit structure	Monomer and homodimer. Heterotetramer with MAD1L1. Formation of a heterotetrameric core complex containing two molecules each of MAD1L1 and of MAD2L1 promotes binding of another molecule of MAD2L1 to each MAD2L1, resulting in a heterohexamer. Interacts with CDC20, MAD2L1BP and with ADAM17/TACE. Dimeric MAD2L1 in the closed conformation interacts with CDC20. Monomeric MAD2L1 in the open conformation does not interact with CDC20. CDC20 competes with MAD1L1 for MAD2L1 binding. Interacts with TPR. Ref.23 Ref.25 Ref.26 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.24 Ref.27 Ref.28 Ref.29
Subcellular location	Nucleus. Kinetochore. Cytoplasm. Note: Recruited by MAD1L1 to unattached kinetochores Probable. Recruited to the nuclear pore complex by TPR during interphase. Recruited to kinetochores in late prometaphase after BUB1, CENPF, BUB1B and CENPE. Kinetochore association requires the presence of NEK2. Ref.25 Ref.18 Ref.19
Domain	The protein has two highly different native conformations, an inactive open conformation that cannot bind CDC20 and that predominates in cytosolic monomers, and an active closed conformation. The protein in the closed conformation preferentially dimerizes with another molecule in the open conformation, but can also form a dimer with a molecule in the closed conformation. Formation of a heterotetrameric core complex containing two molecules of MAD1L1 and of MAD2L1 in the closed conformation promotes binding of another molecule of MAD2L1 in the open conformation and the conversion of the open to the closed form, and thereby promotes interaction with CDC20. Ref.23 Ref.25 Ref.26 Ref.24 Ref.29
Post-translational modification	Phosphorylated on multiple serine residues. The level of phosphorylation varies during the cell cycle and is highest during mitosis. Phosphorylation abolishes interaction with MAD1L1 and reduces interaction with CDC20. Ref.15 Ref.22
Sequence similarities	Belongs to the MAD2 family. Contains 1 HORMA domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Kinetochore Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Ref.18 Ref.24 Ref.25 Inferred from direct assay. Source: UniProtKB nucleus Ref.18 Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	protein homodimerization activity Ref.27 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAM17	P78536	2	EBI-78203,EBI-78188
CDC20	Q12834	1	EBI-78203,EBI-367462
DSTYK	Q6XUX3	1	EBI-78203,EBI-1049520
MAD1L1	Q9Y6D9	2	EBI-78203,EBI-742610
MAD2L1BP	Q15013	2	EBI-78203,EBI-712181

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11

Chain

2 – 205

204

Mitotic spindle assembly checkpoint protein MAD2A

PRO_0000126117

Regions

Domain

14 – 197

184

HORMA

Region

195 – 205

11

Required for assuming the closed conformation and for interaction with CDC20

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

170

1

Phosphoserine Probable

Modified residue

178

1

Phosphoserine Probable

Modified residue

195

1

Phosphoserine Ref.15 Ref.22

Experimental info

Mutagenesis

13

1

L → A: Leads to formation the closed conformation and homodimerization. Ref.29

Mutagenesis

75

1

W → A: Prevents interaction with CDC20 and leads to formation of the closed conformation; when associated with A-133. Ref.29

Mutagenesis

133

1

R → A: Prevents aggregation and promotes formation of monomeric protein that slowly interconverts between the open and closed conformation. Ref.24

Mutagenesis

153

1

L → A: Leads to formation of the closed conformation; when associated with A-133. Ref.29

Mutagenesis

156

1

Y → A: Leads to formation of the closed conformation; when associated with A-133. Ref.29

Mutagenesis

170

1

S → A: Reduces phosphorylation on serine residues; when associated with A-178. Abolishes phosphorylation on serine residues; when associated with A-178 and A-195. Ref.15

Mutagenesis

170

1

S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-178 and D-195. Ref.15

Mutagenesis

178

1

S → A: Reduces phosphorylation on serine residues; when associated with A-170. Abolishes phosphorylation on serine residues; when associated with A-170 and A-195. Ref.15

Mutagenesis

178

1

S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-195. Ref.15

Mutagenesis

186

1

F → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.29

Mutagenesis

188

1

T → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.29

Mutagenesis

191

1

H → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.29

Mutagenesis

195

1

S → A: Abolishes phosphorylation on serine residues; when associated with A-170 and A-178. Ref.15

Mutagenesis

195

1

S → D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-178. Ref.15

Mutagenesis

197

1

V → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.29

Mutagenesis

199

1

Y → A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133. Ref.29

Sequence conflict

16

1

S → C in BAD97153. Ref.7

Sequence conflict

190

1

I → V in AAH70283. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

205

Helix Strand Turn

Details...

Helix

13 – 34

22

Helix

40 – 42

3

Beta strand

43 – 48

6

Beta strand

51 – 56

6

Helix

59 – 77

19

Beta strand

81 – 90

10

Turn

91 – 93

3

Beta strand

96 – 106

11

Helix

108 – 111

4

Helix

121 – 137

17

Helix

138 – 140

3

Beta strand

149 – 160

12

Beta strand

167 – 169

3

Beta strand

179 – 182

4

Beta strand

189 – 199

11

Sequences

	Sequence		Length	Mass (Da)
	Q13257-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B8DCBF0043836764	FASTA	205	23,510
	10 20 30 40 50 60 MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE 70 80 90 100 110 120 LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW QFDIECDKTA KDDSAPREKS 130 140 150 160 170 180 QKAIQDEIRS VIRQITATVT FLPLLEVSCS FDLLIYTDKD LVVPEKWEES GPQFITNSEE 190 200 VRLRSFTTTI HKVNSMVAYK IPVND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human mitotic checkpoint gene: hsMAD2." Li Y., Benezra R. Science 274:246-248(1996) [PubMed: 8824189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure of the human MAD2 gene and mutation analysis in human lung and breast cancers." Gemma A., Hosoya Y., Seike M., Uematsu K., Kurimoto F., Hibino S., Yoshimura A., Shibuya M., Kudoh S., Emi M. Lung Cancer 32:289-295(2001) [PubMed: 11390010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Jin D.-Y., Jeang K.-T. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Klebert S., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[5]	"Complete human MAD2 gene." Nobori T. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"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: Lung.
[7]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[8]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: Bone marrow and Muscle.
[11]	Bienvenut W.V., Dhillon A.S., Kolch W. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-7; 36-45; 123-129 AND 193-205, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Hepatoma.
[12]	"The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation." Fang G., Yu H., Kirschner M.W. Genes Dev. 12:1871-1883(1998) [PubMed: 9637688] [Abstract] Cited for: INTERACTION WITH CDC20.
[13]	"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: INTERACTION WITH ADAM17.
[14]	"Identification of a MAD2-binding protein, CMT2, and its role in mitosis." Habu T., Kim S.H., Weinstein J., Matsumoto T. EMBO J. 21:6419-6428(2002) [PubMed: 12456649] [Abstract] Cited for: INTERACTION WITH MAD2L1BP.
[15]	"Mad2 phosphorylation regulates its association with Mad1 and the APC/C." Wassmann K., Liberal V., Benezra R. EMBO J. 22:797-806(2003) [PubMed: 12574116] [Abstract] Cited for: PHOSPHORYLATION AT SER-170; SER-178 AND SER-195, INTERACTION WITH MAD1L1 AND CDC20, MUTAGENESIS OF SER-170; SER-178 AND SER-195.
[16]	"NEK2A interacts with MAD1 and possibly functions as a novel integrator of the spindle checkpoint signaling." Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J., Wang Y., Yao X. J. Biol. Chem. 279:20049-20057(2004) [PubMed: 14978040] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression." Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S. J. Cell Sci. 117:1577-1589(2004) [PubMed: 15020684] [Abstract] Cited for: SUBCELLULAR LOCATION.
[18]	"Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint." Lee S.H., Sterling H., Burlingame A., McCormick F. Genes Dev. 22:2926-2931(2008) [PubMed: 18981471] [Abstract] Cited for: INTERACTION WITH TPR; MAD1L1 AND CDC20, SUBCELLULAR LOCATION.
[19]	"Perturbation of the chromosomal binding of RCC1, Mad2 and survivin causes spindle assembly defects and mitotic catastrophe." Ho C.-Y., Wong C.-H., Li H.-Y. J. Cell. Biochem. 105:835-846(2008) [PubMed: 18712773] [Abstract] Cited for: SUBCELLULAR LOCATION.
[20]	"The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational switching." Skinner J.J., Wood S., Shorter J., Englander S.W., Black B.E. J. Cell Biol. 183:761-768(2008) [PubMed: 19029339] [Abstract] Cited for: REVIEW.
[21]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, MASS SPECTROMETRY. Tissue: T-cell.
[23]	"Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20." Luo X., Fang G., Coldiron M., Lin Y., Yu H., Kirschner M.W., Wagner G. Nat. Struct. Biol. 7:224-229(2000) [PubMed: 10700282] [Abstract] Cited for: STRUCTURE BY NMR OF 11-195, FUNCTION, DOMAIN, INTERACTION WITH CDC20.
[24]	"Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint." Sironi L., Mapelli M., Knapp S., De Antoni A., Jeang K.-T., Musacchio A. EMBO J. 21:2496-2506(2002) [PubMed: 12006501] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT ALA-133 IN COMPLEX WITH MAD1L1, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-133, INTERACTION WITH MAD1L1.
[25]	"The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20." Luo X., Tang Z., Rizo J., Yu H. Mol. Cell 9:59-71(2002) [PubMed: 11804586] [Abstract] Cited for: STRUCTURE BY NMR OF 11-205 IN COMPLEX WITH PEPTIDE LIGAND, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH CDC20 AND MAD1L1.
[26]	"The Mad2 spindle checkpoint protein has two distinct natively folded states." Luo X., Tang Z., Xia G., Wassmann K., Matsumoto T., Rizo J., Yu H. Nat. Struct. Mol. Biol. 11:338-345(2004) [PubMed: 15024386] [Abstract] Cited for: STRUCTURE BY NMR, DOMAIN, SUBUNIT, FUNCTION, INTERACTION WITH MAD1L1, MASS SPECTROMETRY.
[27]	"The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint." Mapelli M., Massimiliano L., Santaguida S., Musacchio A. Cell 131:730-743(2007) [PubMed: 18022367] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF DIMER CONTAINING BOTH CONFORMERS, INTERACTION OF THE TWO MAD2L1 CONFORMERS.
[28]	"p31comet blocks Mad2 activation through structural mimicry." Yang M., Li B., Tomchick D.R., Machius M., Rizo J., Yu H., Luo X. Cell 131:744-755(2007) [PubMed: 18022368] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEXES WITH MAD2L1BP, INTERACTION WITH MAD2L1BP.
[29]	"Insights into Mad2 regulation in the spindle checkpoint revealed by the crystal structure of the symmetric Mad2 dimer." Yang M., Li B., Liu C.-J., Tomchick D.R., Machius M., Rizo J., Yu H., Luo X. PLoS Biol. 6:E50-E50(2008) [PubMed: 18318601] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF HOMODIMER OF MUTANT ALA-13 IN THE CLOSED CONFORMATION, DOMAIN, SUBUNIT, MUTAGENESIS OF LEU-13; TRP-75; LEU-153; TYR-156; PHE-186; THR-188; HIS-191; VAL-197 AND TYR-199.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U65410 mRNA. Translation: AAC50781.1.
AF202273 , AF202269, AF202270, AF202271, AF202272 Genomic DNA. Translation: AAK38174.1.
U31278 mRNA. Translation: AAC52060.1.
AJ000186 mRNA. Translation: CAA03943.1.
AB056160 Genomic DNA. Translation: BAB63410.1.
AK313827 mRNA. Translation: BAG36562.1.
AK223433 mRNA. Translation: BAD97153.1.
AC097173 Genomic DNA. Translation: AAY40945.1.
CH471056 Genomic DNA. Translation: EAX05273.1.
BC000356 mRNA. Translation: AAH00356.1.
BC005945 mRNA. Translation: AAH05945.1.
BC070283 mRNA. Translation: AAH70283.1.

IPI

IPI00012369.

PIR

G01942.

RefSeq

NP_002349.1.

UniGene

Hs.591697

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DUJ	NMR	-	A	11-195	[»]
1GO4	X-ray	2.05	A/B/C/D	1-205	[»]
1KLQ	NMR	-	A	11-205	[»]
1S2H	NMR	-	A	1-205	[»]
2QYF	X-ray	2.30	A/C	1-205	[»]
2V64	X-ray	2.90	A/C/D/E/F/H	2-205	[»]
2VFX	X-ray	1.95	A/B/C/D/E/F/G/H/I/J/K/L	1-205	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29653N.

IntAct

Q13257. 14 interactions.

STRING

Q13257.

PTM databases

PhosphoSite

Q13257.

Proteomic databases

PeptideAtlas

Q13257.

PRIDE

Q13257.

Genome annotation databases

Ensembl

ENST00000296509; ENSP00000296509; ENSG00000164109; Homo sapiens. [Genome view]

GeneID

4085.

KEGG

hsa:4085.

UCSC

uc003idl.1. human.

Organism-specific databases

CTD

4085.

GeneCards

GC04M121260.

H-InvDB

HIX0004473.
HIX0038013.

HGNC

HGNC:6763. MAD2L1.

MIM

601467. gene.

PharmGKB

PA30521.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19758.

HOGENOM

HBG314247.

HOVERGEN

Q13257.

InParanoid

Q13257.

OMA

VERWQFD.

OrthoDB

EOG9ZGRZM.

PhylomeDB

Q13257.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpress

Q13257.

Bgee

Q13257.

CleanEx

HS_MAD2L1.

Genevestigator

Q13257.

GermOnline

ENSG00000164109. Homo sapiens.

Family and domain databases

InterPro

IPR003511. HORMA_DNA_bd.
[Graphical view]

Pfam

PF02301. HORMA. 1 hit.
[Graphical view]

PROSITE

PS50815. HORMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16010.

SOURCE

Search...

Entry information

Entry name

MD2L1_HUMAN

Accession

Primary (citable) accession number: Q13257
Secondary accession number(s): Q53F56, Q548X9, Q6IRW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.