MDM1_MOUSE
ID MDM1_MOUSE Reviewed; 708 AA.
AC Q9D067; Q61841; Q61842; Q9DBR6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nuclear protein MDM1;
DE AltName: Full=Mdm4 transformed 3T3 cell double minute 1 protein;
DE AltName: Full=Mouse double minute 1;
GN Name=Mdm1; Synonyms=Mdm-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=3182840; DOI=10.1016/s0021-9258(18)37511-2;
RA Snyder L.C., Trusko S.P., Freeman N., Eshleman J.R., Fakharzadeh S.S.,
RA George D.L.;
RT "A gene amplified in a transformed mouse cell line undergoes complex
RT transcriptional processing and encodes a nuclear protein.";
RL J. Biol. Chem. 263:17150-17158(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-315;
RP SER-418; SER-555 AND SER-556, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT duplication.";
RL Mol. Biol. Cell 26:3788-3802(2015).
CC -!- FUNCTION: Microtubule-binding protein that negatively regulates
CC centriole duplication. Binds to and stabilizes microtubules.
CC {ECO:0000250|UniProtKB:Q8TC05}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3182840}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8TC05}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392}.
CC Note=Localizes to the centriole lumen. {ECO:0000269|PubMed:26337392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms may exist.;
CC Name=1;
CC IsoId=Q9D067-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D067-2; Sequence=VSP_027551, VSP_027552;
CC Name=3; Synonyms=Mdm1a;
CC IsoId=Q9D067-3; Sequence=VSP_027549, VSP_027550;
CC Name=4;
CC IsoId=Q9D067-4; Sequence=VSP_027548;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC testis. {ECO:0000269|PubMed:3182840}.
CC -!- SIMILARITY: Belongs to the MDM1 family. {ECO:0000305}.
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DR EMBL; M20823; AAA39511.1; -; mRNA.
DR EMBL; M20824; AAA39512.1; -; mRNA.
DR EMBL; AK004789; BAB23566.1; -; mRNA.
DR EMBL; AK011769; BAB27830.1; -; mRNA.
DR CCDS; CCDS36069.1; -. [Q9D067-1]
DR PIR; A31794; A31794.
DR PIR; B31794; B31794.
DR RefSeq; NP_001156376.1; NM_001162904.1.
DR RefSeq; NP_001156377.1; NM_001162905.1.
DR RefSeq; NP_034915.2; NM_010785.2.
DR RefSeq; NP_683724.2; NM_148922.3. [Q9D067-1]
DR AlphaFoldDB; Q9D067; -.
DR SMR; Q9D067; -.
DR STRING; 10090.ENSMUSP00000127919; -.
DR iPTMnet; Q9D067; -.
DR PhosphoSitePlus; Q9D067; -.
DR jPOST; Q9D067; -.
DR MaxQB; Q9D067; -.
DR PaxDb; Q9D067; -.
DR PeptideAtlas; Q9D067; -.
DR PRIDE; Q9D067; -.
DR ProteomicsDB; 292204; -. [Q9D067-1]
DR ProteomicsDB; 292205; -. [Q9D067-2]
DR ProteomicsDB; 292206; -. [Q9D067-3]
DR ProteomicsDB; 292207; -. [Q9D067-4]
DR Antibodypedia; 29303; 135 antibodies from 24 providers.
DR DNASU; 17245; -.
DR Ensembl; ENSMUST00000020437; ENSMUSP00000020437; ENSMUSG00000020212. [Q9D067-1]
DR GeneID; 17245; -.
DR KEGG; mmu:17245; -.
DR UCSC; uc007hds.2; mouse. [Q9D067-3]
DR UCSC; uc007hdt.2; mouse. [Q9D067-1]
DR CTD; 56890; -.
DR MGI; MGI:96951; Mdm1.
DR VEuPathDB; HostDB:ENSMUSG00000020212; -.
DR eggNOG; ENOG502QVRV; Eukaryota.
DR GeneTree; ENSGT00390000004106; -.
DR InParanoid; Q9D067; -.
DR OrthoDB; 350018at2759; -.
DR PhylomeDB; Q9D067; -.
DR BioGRID-ORCS; 17245; 5 hits in 73 CRISPR screens.
DR PRO; PR:Q9D067; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D067; protein.
DR Bgee; ENSMUSG00000020212; Expressed in spermatid and 163 other tissues.
DR ExpressionAtlas; Q9D067; baseline and differential.
DR Genevisible; Q9D067; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR InterPro; IPR029136; MDM1.
DR PANTHER; PTHR32078; PTHR32078; 1.
DR Pfam; PF15501; MDM1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..708
FT /note="Nuclear protein MDM1"
FT /id="PRO_0000299060"
FT REGION 79..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..355
FT /evidence="ECO:0000255"
FT MOTIF 9..15
FT /note="ST]-E-Y-X(3)-F motif 1; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 193..199
FT /note="ST]-E-Y-X(3)-F motif 2; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 236..242
FT /note="ST]-E-Y-X(3)-F motif 3; required for efficient
FT microtubule binding"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 307..313
FT /note="ST]-E-Y-X(3)-F motif 4; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT COMPBIAS 116..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQN4"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQN4"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT VAR_SEQ 171..215
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:3182840"
FT /id="VSP_027548"
FT VAR_SEQ 217..222
FT /note="FRNKSQ -> AQEMRF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:3182840"
FT /id="VSP_027549"
FT VAR_SEQ 223..708
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:3182840"
FT /id="VSP_027550"
FT VAR_SEQ 607
FT /note="D -> EG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3182840"
FT /id="VSP_027551"
FT VAR_SEQ 652..672
FT /note="MGKPRTNNLQLHPHDAFNDED -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3182840"
FT /id="VSP_027552"
FT CONFLICT 40
FT /note="R -> K (in Ref. 2; BAB27830)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="S -> L (in Ref. 1; AAA39511)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="K -> E (in Ref. 2; BAB23566)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="Q -> P (in Ref. 2; BAB23566)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="D -> G (in Ref. 1; AAA39511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 79689 MW; FF3BE0BA5167FB28 CRC64;
MPVRFKGLSE YQRNFLWKKS YLSESYNPSV GQKYSWAGLR SDQLGITKEP GFISKRRVPY
HDPQISKYLE WNGTVRKKDT LVPPEPQAFG TPKPQEAEQG EDANQEAVLS LEASRVPKRT
RSHSADSRAE GVSDTVEKHQ GVTRSHAPVS ADVELRPSSK QPLSQSIDPR LDRHLRKKAG
LAVVPTNNAL RNSEYQRQFV WKTSKESAPV FASNQVFRNK SQIIPQFQGN TFTHETEYKR
NFKGLTPVKE PKSREYLKGN SSLEMLTPVK KADEPLDLEV DMASEDSDQS VKKPASWRHQ
RLGKVNSEYR AKFLSPAQYF YKAGAWTRVK ENLSNQVKEL REKAESYRKR VQGTHFSRDH
LNQIMSDSNC CWDVSSVTSS EGTVSSNIRA LDLAGDLTNH RTPQKHPPTK LEERKVASGE
QPLKNSTRRL EMPEPAASVR RKLAWDAEES TKEDTQEEPR AEEDGREERG QDKQTCAVEL
EKPDTQTPKA DRLTEGSETS SVSSGKGGRL PTPRLRELGI QRTHHDLTTP AVGGAVLVSP
SKVKPPGLEQ RRRASSQDGL ETLKKDITKK GKPRPMSLLT SPAAGMKTVD PLPLREDCEA
NVLRFADTLP VSKILDRQPS TPGQLPPCAP PYCHPSSRIQ GRLRDPEFQH NMGKPRTNNL
QLHPHDAFND EDADRLSEIS ARSAVSSLRA FQTLARAQKR KENFWGKP
