MD2BP_HUMAN
ID MD2BP_HUMAN Reviewed; 274 AA.
AC Q15013; B4DLV3; E9PAT7; Q6IBB1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=MAD2L1-binding protein;
DE AltName: Full=Caught by MAD2 protein;
DE AltName: Full=p31(comet) {ECO:0000303|PubMed:18022368};
GN Name=MAD2L1BP; Synonyms=CMT2, KIAA0110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-224 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP POSSIBLE FUNCTION, INTERACTION WITH MAD2L1, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12456649; DOI=10.1093/emboj/cdf659;
RA Habu T., Kim S.H., Weinstein J., Matsumoto T.;
RT "Identification of a MAD2-binding protein, CMT2, and its role in mitosis.";
RL EMBO J. 21:6419-6428(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 36-274 IN COMPLEX WITH MAD2L1,
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAD2L1, AND MUTAGENESIS OF
RP GLN-83 AND PHE-191.
RX PubMed=18022368; DOI=10.1016/j.cell.2007.08.048;
RA Yang M., Li B., Tomchick D.R., Machius M., Rizo J., Yu H., Luo X.;
RT "p31comet blocks Mad2 activation through structural mimicry.";
RL Cell 131:744-755(2007).
CC -!- FUNCTION: May function to silence the spindle checkpoint and allow
CC mitosis to proceed through anaphase by binding MAD2L1 after it has
CC become dissociated from the MAD2L1-CDC20 complex.
CC {ECO:0000269|PubMed:18022368}.
CC -!- SUBUNIT: Interacts with MAD2L1. {ECO:0000269|PubMed:12456649,
CC ECO:0000269|PubMed:18022368}.
CC -!- INTERACTION:
CC Q15013; Q8TC99: FNDC8; NbExp=3; IntAct=EBI-712181, EBI-12903902;
CC Q15013; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-712181, EBI-10172004;
CC Q15013; Q9BT40: INPP5K; NbExp=11; IntAct=EBI-712181, EBI-749162;
CC Q15013; Q13257: MAD2L1; NbExp=18; IntAct=EBI-712181, EBI-78203;
CC Q15013; Q13287: NMI; NbExp=3; IntAct=EBI-712181, EBI-372942;
CC Q15013; Q562F6: SGO2; NbExp=2; IntAct=EBI-712181, EBI-989213;
CC Q15013; Q15645: TRIP13; NbExp=9; IntAct=EBI-712181, EBI-358993;
CC Q15013; O43829: ZBTB14; NbExp=6; IntAct=EBI-712181, EBI-10176632;
CC Q15013; O95125: ZNF202; NbExp=3; IntAct=EBI-712181, EBI-751960;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Note=During early mitosis, unevenly distributed throughout the
CC nucleoplasm. From metaphase to anaphase, concentrated on the spindle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15013-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15013-3; Sequence=VSP_046268;
CC -!- DEVELOPMENTAL STAGE: During the cell cycle, levels increase and then
CC remain constant until late mitosis after which they drop.
CC {ECO:0000269|PubMed:12456649}.
CC -!- SIMILARITY: Belongs to the MAD2L1BP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG59665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D14811; BAA03552.1; -; mRNA.
DR EMBL; AK297172; BAG59665.1; ALT_INIT; mRNA.
DR EMBL; CR456893; CAG33174.1; -; mRNA.
DR EMBL; AL136131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002904; AAH02904.1; -; mRNA.
DR EMBL; AL537692; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47431.1; -. [Q15013-3]
DR CCDS; CCDS4904.1; -. [Q15013-1]
DR RefSeq; NP_001003690.1; NM_001003690.1. [Q15013-3]
DR RefSeq; NP_055443.1; NM_014628.2. [Q15013-1]
DR PDB; 2QYF; X-ray; 2.30 A; B/D=36-274.
DR PDB; 6F0X; EM; 4.60 A; P=1-274.
DR PDBsum; 2QYF; -.
DR PDBsum; 6F0X; -.
DR AlphaFoldDB; Q15013; -.
DR SMR; Q15013; -.
DR BioGRID; 114955; 64.
DR DIP; DIP-34492N; -.
DR IntAct; Q15013; 30.
DR MINT; Q15013; -.
DR STRING; 9606.ENSP00000410818; -.
DR iPTMnet; Q15013; -.
DR PhosphoSitePlus; Q15013; -.
DR BioMuta; MAD2L1BP; -.
DR EPD; Q15013; -.
DR jPOST; Q15013; -.
DR MassIVE; Q15013; -.
DR MaxQB; Q15013; -.
DR PaxDb; Q15013; -.
DR PeptideAtlas; Q15013; -.
DR PRIDE; Q15013; -.
DR ProteomicsDB; 19077; -.
DR ProteomicsDB; 60365; -. [Q15013-1]
DR Antibodypedia; 30554; 311 antibodies from 31 providers.
DR DNASU; 9587; -.
DR Ensembl; ENST00000372171.5; ENSP00000361244.4; ENSG00000124688.14. [Q15013-1]
DR Ensembl; ENST00000451025.6; ENSP00000410818.2; ENSG00000124688.14. [Q15013-3]
DR GeneID; 9587; -.
DR KEGG; hsa:9587; -.
DR MANE-Select; ENST00000372171.5; ENSP00000361244.4; NM_014628.3; NP_055443.1.
DR UCSC; uc003ovu.4; human. [Q15013-1]
DR CTD; 9587; -.
DR DisGeNET; 9587; -.
DR GeneCards; MAD2L1BP; -.
DR HGNC; HGNC:21059; MAD2L1BP.
DR HPA; ENSG00000124688; Low tissue specificity.
DR MIM; 618136; gene.
DR neXtProt; NX_Q15013; -.
DR OpenTargets; ENSG00000124688; -.
DR PharmGKB; PA134911020; -.
DR VEuPathDB; HostDB:ENSG00000124688; -.
DR eggNOG; ENOG502QTUF; Eukaryota.
DR GeneTree; ENSGT00390000003812; -.
DR HOGENOM; CLU_079654_0_0_1; -.
DR InParanoid; Q15013; -.
DR OMA; ATAWEDY; -.
DR OrthoDB; 1492026at2759; -.
DR PhylomeDB; Q15013; -.
DR TreeFam; TF331730; -.
DR PathwayCommons; Q15013; -.
DR SignaLink; Q15013; -.
DR SIGNOR; Q15013; -.
DR BioGRID-ORCS; 9587; 235 hits in 1092 CRISPR screens.
DR ChiTaRS; MAD2L1BP; human.
DR EvolutionaryTrace; Q15013; -.
DR GeneWiki; MAD2L1BP; -.
DR GenomeRNAi; 9587; -.
DR Pharos; Q15013; Tbio.
DR PRO; PR:Q15013; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15013; protein.
DR Bgee; ENSG00000124688; Expressed in mucosa of transverse colon and 185 other tissues.
DR Genevisible; Q15013; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; IMP:UniProtKB.
DR InterPro; IPR009511; MAD1/Cdc20-bound-Mad2-bd.
DR PANTHER; PTHR15681; PTHR15681; 1.
DR Pfam; PF06581; p31comet; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..274
FT /note="MAD2L1-binding protein"
FT /id="PRO_0000096310"
FT REGION 45..78
FT /note="Interaction with MAD2L1"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..15
FT /note="MAAPEAEVLSSAAVP -> MARVPLGRSLTLSPRLEHNGMTSAHHNFRLPGS
FT RDSPASASQVAEII (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_046268"
FT MUTAGEN 83
FT /note="Q->A: Loss of interaction with MAD2L1 and disruption
FT of ability to overcome spindle checkpoint-dependent mitotic
FT arrest; when associated with A-191."
FT /evidence="ECO:0000269|PubMed:18022368"
FT MUTAGEN 191
FT /note="F->A: Loss of interaction with MAD2L1 and disruption
FT of ability to overcome spindle checkpoint-dependent mitotic
FT arrest; when associated with A-83."
FT /evidence="ECO:0000269|PubMed:18022368"
FT CONFLICT 133
FT /note="S -> G (in Ref. 2; BAG59665)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="E -> D (in Ref. 3; CAG33174)"
FT /evidence="ECO:0000305"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2QYF"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2QYF"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2QYF"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2QYF"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2QYF"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:2QYF"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:2QYF"
FT TURN 254..259
FT /evidence="ECO:0007829|PDB:2QYF"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2QYF"
SQ SEQUENCE 274 AA; 31052 MW; 5C49FBE1F456105C CRC64;
MAAPEAEVLS SAAVPDLEWY EKSEETHASQ IELLETSSTQ EPLNASEAFC PRDCMVPVVF
PGPVSQEGCC QFTCELLKHI MYQRQQLPLP YEQLKHFYRK PSPQAEEMLK KKPRATTEVS
SRKCQQALAE LESVLSHLED FFARTLVPRV LILLGGNALS PKEFYELDLS LLAPYSVDQS
LSTAACLRRL FRAIFMADAF SELQAPPLMG TVVMAQGHRN CGEDWFRPKL NYRVPSRGHK
LTVTLSCGRP SIRTTAWEDY IWFQAPVTFK GFRE
