Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q15013 (MD2BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAD2L1-binding protein
Alternative name(s):
Caught by MAD2 protein
Gene names
Name:MAD2L1BP
Synonyms:CMT2, KIAA0110
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function to silence the spindle checkpoint and allow mitosis to proceed through anaphase by binding MAD2L1 after it has become dissociated from the MAD2L1-CDC20 complex. Ref.6 Ref.8

Subunit structure

Interacts with MAD2L1. Ref.6 Ref.8

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle. Note: During early mitosis, unevenly distributed throughout the nucleoplasm. From metaphase to anaphase, concentrated on the spindle. Ref.6 Ref.8

Developmental stage

During the cell cycle, levels increase and then remain constant until late mitosis after which they drop. Ref.6

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7

Sequence similarities

Belongs to the MAD2L1BP family.

Sequence caution

The sequence BAG59665.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmitotic cell cycle checkpoint

Inferred from mutant phenotype Ref.8. Source: UniProtKB

regulation of exit from mitosis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from direct assay. Source: UniProtKB

nucleus

Inferred from direct assay. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAD2L1Q132574EBI-712181,EBI-78203
TRIP13Q156455EBI-712181,EBI-358993

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274MAD2L1-binding protein
PRO_0000096310

Regions

Region45 – 7834Interaction with MAD2L1

Amino acid modifications

Modified residue291Phosphoserine Ref.7
Modified residue391Phosphothreonine Ref.7

Experimental info

Mutagenesis831Q → A: Loss of interaction with MAD2L1 and disruption of ability to overcome spindle checkpoint-dependent mitotic arrest; when associated with A-191. Ref.8
Mutagenesis1911F → A: Loss of interaction with MAD2L1 and disruption of ability to overcome spindle checkpoint-dependent mitotic arrest; when associated with A-83. Ref.8
Sequence conflict1331S → G in BAG59665. Ref.2
Sequence conflict2741E → D in CAG33174. Ref.3

Secondary structure

............................. 274
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15013 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5C49FBE1F456105C

FASTA27431,052
        10         20         30         40         50         60 
MAAPEAEVLS SAAVPDLEWY EKSEETHASQ IELLETSSTQ EPLNASEAFC PRDCMVPVVF 

        70         80         90        100        110        120 
PGPVSQEGCC QFTCELLKHI MYQRQQLPLP YEQLKHFYRK PSPQAEEMLK KKPRATTEVS 

       130        140        150        160        170        180 
SRKCQQALAE LESVLSHLED FFARTLVPRV LILLGGNALS PKEFYELDLS LLAPYSVDQS 

       190        200        210        220        230        240 
LSTAACLRRL FRAIFMADAF SELQAPPLMG TVVMAQGHRN CGEDWFRPKL NYRVPSRGHK 

       250        260        270 
LTVTLSCGRP SIRTTAWEDY IWFQAPVTFK GFRE 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed: 7788527] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[2]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Lung.
[6]"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: POSSIBLE FUNCTION, INTERACTION WITH MAD2L1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND THR-39, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"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 36-274 IN COMPLEX WITH MAD2L1, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAD2L1, MUTAGENESIS OF GLN-83 AND PHE-191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14811 mRNA. Translation: BAA03552.1.
AK297172 mRNA. Translation: BAG59665.1. Different initiation.
CR456893 mRNA. Translation: CAG33174.1.
AL136131 Genomic DNA. Translation: CAC19507.1.
BC002904 mRNA. Translation: AAH02904.1.
IPIIPI00014173.
RefSeqNP_001003690.1. NM_001003690.1.
NP_055443.1. NM_014628.2.
UniGeneHs.122346.
Hs.715485.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QYFX-ray2.30B/D36-274[»]
ProteinModelPortalQ15013.
SMRQ15013. Positions 54-273.
ModBaseSearch...

Protein-protein interaction databases

IntActQ15013. 11 interactions.
MINTMINT-1368732.
STRINGQ15013.

PTM databases

PhosphoSiteQ15013.

Polymorphism databases

DMDM3123048.

Proteomic databases

PRIDEQ15013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372171; ENSP00000361244; ENSG00000124688.
ENST00000426254; ENSP00000409010; ENSG00000124688.
GeneID9587.
KEGGhsa:9587.
UCSCuc003ovv.1. human.

Organism-specific databases

CTD9587.
GeneCardsGC06P043597.
HGNCHGNC:21059. MAD2L1BP.
neXtProtNX_Q15013.
PharmGKBPA134911020.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08208.
GeneTreeENSGT00390000003812.
HOVERGENHBG052442.
PhylomeDBQ15013.

Gene expression databases

ArrayExpressQ15013.
BgeeQ15013.
CleanExHS_MAD2L1BP.
GenevestigatorQ15013.
GermOnlineENSG00000124688. Homo sapiens.

Family and domain databases

InterProIPR009511. MAD1/Cdc20-bound-Mad2-bd.
[Graphical view]
PfamPF06581. p31comet. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio35973.

Entry information

Entry nameMD2BP_HUMAN
AccessionPrimary (citable) accession number: Q15013
Secondary accession number(s): B4DLV3, Q6IBB1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 83 of the entry and version 1 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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families