Q15013 (MD2BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: MAD2L1-binding protein Alternative name(s): Caught by MAD2 protein | ||||
| Gene names |
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| 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 | 274 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| Subcellular location | Nucleus. Cytoplasm › cytoskeleton › spindle. 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 component | Cytoplasm Cytoskeleton Nucleus |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | mitotic cell cycle checkpoint Inferred from mutant phenotype Ref.8. Source: UniProtKB regulation of exit from mitosisInferred from mutant phenotype Ref.6. Source: UniProtKB |
| Cellular component | cytoplasm Inferred from direct assay. Source: UniProtKB nucleusInferred from direct assay. Source: UniProtKB spindleInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein binding Inferred from physical interaction Ref.8. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| MAD2L1 | Q13257 | 4 | EBI-712181,EBI-78203 | |
| TRIP13 | Q15645 | 5 | EBI-712181,EBI-358993 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 274 | 274 | MAD2L1-binding protein | PRO_0000096310 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Region | 45 – 78 | 34 | Interaction with MAD2L1 | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 29 | 1 | Phosphoserine Ref.7 | ||||||||||||||||||||||||||||||||||
| Modified residue | 39 | 1 | Phosphothreonine Ref.7 | ||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||
| Mutagenesis | 83 | 1 | Q → A: Loss of interaction with MAD2L1 and disruption of ability to overcome spindle checkpoint-dependent mitotic arrest; when associated with A-191. Ref.8 | ||||||||||||||||||||||||||||||||||
| Mutagenesis | 191 | 1 | F → 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 conflict | 133 | 1 | S → G in BAG59665. Ref.2 | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 274 | 1 | E → D in CAG33174. Ref.3 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 59 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 67 – 83 | 17 | |||||||||||||||||||||||||||||||||||
| Beta strand | 86 – 89 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 91 – 94 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 126 – 144 | 19 | |||||||||||||||||||||||||||||||||||
| Beta strand | 149 – 156 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 158 – 160 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 162 – 168 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 183 – 196 | 14 | |||||||||||||||||||||||||||||||||||
| Turn | 197 – 200 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 210 – 218 | 9 | |||||||||||||||||||||||||||||||||||
| Beta strand | 224 – 229 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 239 – 246 | 8 | |||||||||||||||||||||||||||||||||||
| Turn | 254 – 259 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 260 – 264 | 5 | |||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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. | ||||||||||||
| IPI | IPI00014173. | ||||||||||||
| RefSeq | NP_001003690.1. NM_001003690.1. NP_055443.1. NM_014628.2. | ||||||||||||
| UniGene | Hs.122346. Hs.715485. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q15013. | ||||||||||||
| SMR | Q15013. Positions 54-273. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q15013. 11 interactions. | ||||||||||||
| MINT | MINT-1368732. | ||||||||||||
| STRING | Q15013. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q15013. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 3123048. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q15013. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000372171; ENSP00000361244; ENSG00000124688. ENST00000426254; ENSP00000409010; ENSG00000124688. | ||||||||||||
| GeneID | 9587. | ||||||||||||
| KEGG | hsa:9587. | ||||||||||||
| UCSC | uc003ovv.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 9587. | ||||||||||||
| GeneCards | GC06P043597. | ||||||||||||
| HGNC | HGNC:21059. MAD2L1BP. | ||||||||||||
| neXtProt | NX_Q15013. | ||||||||||||
| PharmGKB | PA134911020. | ||||||||||||
| HUGE | Search... | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG08208. | ||||||||||||
| GeneTree | ENSGT00390000003812. | ||||||||||||
| HOVERGEN | HBG052442. | ||||||||||||
| PhylomeDB | Q15013. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q15013. | ||||||||||||
| Bgee | Q15013. | ||||||||||||
| CleanEx | HS_MAD2L1BP. | ||||||||||||
| Genevestigator | Q15013. | ||||||||||||
| GermOnline | ENSG00000124688. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR009511. MAD1/Cdc20-bound-Mad2-bd. [Graphical view] | ||||||||||||
| Pfam | PF06581. p31comet. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 35973. | ||||||||||||
Entry information
| Entry name | MD2BP_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q15013 Secondary accession number(s): B4DLV3, Q6IBB1 | ||||||||
| Entry history |
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| 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. | ||||||||
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 |

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