Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Nuclear protein MDM1 (Mdm4 transformed 3T3 cell double minute 1 protein) (Mouse double minute 1)

 MDM1_MOUSE              Reviewed;         708 AA.
Q9D067; Q61841; Q61842; Q9DBR6;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 2.
25-OCT-2017, entry version 93.
RecName: Full=Nuclear protein MDM1;
AltName: Full=Mdm4 transformed 3T3 cell double minute 1 protein;
AltName: Full=Mouse double minute 1;
Name=Mdm1; Synonyms=Mdm-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=3182840;
Snyder L.C., Trusko S.P., Freeman N., Eshleman J.R., Fakharzadeh S.S.,
George D.L.;
"A gene amplified in a transformed mouse cell line undergoes complex
transcriptional processing and encodes a nuclear protein.";
J. Biol. Chem. 263:17150-17158(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-315;
SER-418; SER-555 AND SER-556, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
SUBCELLULAR LOCATION.
PubMed=26337392; DOI=10.1091/mbc.E15-04-0235;
Van de Mark D., Kong D., Loncarek J., Stearns T.;
"MDM1 is a microtubule-binding protein that negatively regulates
centriole duplication.";
Mol. Biol. Cell 26:3788-3802(2015).
-!- FUNCTION: Microtubule-binding protein that negatively regulates
centriole duplication. Binds to and stabilizes microtubules.
{ECO:0000250|UniProtKB:Q8TC05}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3182840}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q8TC05}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000269|PubMed:26337392}. Note=Localizes to the centriole
lumen. {ECO:0000269|PubMed:26337392}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms may exist.;
Name=1;
IsoId=Q9D067-1; Sequence=Displayed;
Name=2;
IsoId=Q9D067-2; Sequence=VSP_027551, VSP_027552;
Name=3; Synonyms=Mdm1a;
IsoId=Q9D067-3; Sequence=VSP_027549, VSP_027550;
Name=4;
IsoId=Q9D067-4; Sequence=VSP_027548;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
the testis. {ECO:0000269|PubMed:3182840}.
-!- SIMILARITY: Belongs to the MDM1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M20823; AAA39511.1; -; mRNA.
EMBL; M20824; AAA39512.1; -; mRNA.
EMBL; AK004789; BAB23566.1; -; mRNA.
EMBL; AK011769; BAB27830.1; -; mRNA.
CCDS; CCDS36069.1; -. [Q9D067-1]
PIR; A31794; A31794.
PIR; B31794; B31794.
RefSeq; NP_001156376.1; NM_001162904.1.
RefSeq; NP_001156377.1; NM_001162905.1.
RefSeq; NP_034915.2; NM_010785.2.
RefSeq; NP_683724.2; NM_148922.3. [Q9D067-1]
UniGene; Mm.101191; -.
UniGene; Mm.442618; -.
ProteinModelPortal; Q9D067; -.
STRING; 10090.ENSMUSP00000127919; -.
iPTMnet; Q9D067; -.
PhosphoSitePlus; Q9D067; -.
PaxDb; Q9D067; -.
PeptideAtlas; Q9D067; -.
PRIDE; Q9D067; -.
Ensembl; ENSMUST00000020437; ENSMUSP00000020437; ENSMUSG00000020212. [Q9D067-1]
GeneID; 17245; -.
KEGG; mmu:17245; -.
UCSC; uc007hds.2; mouse. [Q9D067-3]
UCSC; uc007hdt.2; mouse. [Q9D067-1]
CTD; 56890; -.
MGI; MGI:96951; Mdm1.
eggNOG; ENOG410II1Y; Eukaryota.
eggNOG; ENOG410Y0E2; LUCA.
GeneTree; ENSGT00390000004106; -.
HOVERGEN; HBG108124; -.
InParanoid; Q9D067; -.
KO; K17886; -.
PhylomeDB; Q9D067; -.
PRO; PR:Q9D067; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020212; -.
CleanEx; MM_MDM1; -.
ExpressionAtlas; Q9D067; baseline and differential.
Genevisible; Q9D067; MM.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0097730; C:non-motile cilium; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
InterPro; IPR029136; MDM1.
PANTHER; PTHR32078; PTHR32078; 1.
Pfam; PF15501; MDM1; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 708 Nuclear protein MDM1.
/FTId=PRO_0000299060.
COILED 322 355 {ECO:0000255}.
MOTIF 9 15 ST]-E-Y-X(3)-F motif 1; required for
efficient microtubule binding and
stabilization.
{ECO:0000250|UniProtKB:Q8TC05}.
MOTIF 193 199 ST]-E-Y-X(3)-F motif 2; required for
efficient microtubule binding and
stabilization.
{ECO:0000250|UniProtKB:Q8TC05}.
MOTIF 236 242 ST]-E-Y-X(3)-F motif 3; required for
efficient microtubule binding.
{ECO:0000250|UniProtKB:Q8TC05}.
MOTIF 307 313 ST]-E-Y-X(3)-F motif 4; required for
efficient microtubule binding and
stabilization.
{ECO:0000250|UniProtKB:Q8TC05}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PQN4}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PQN4}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 555 555 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000250|UniProtKB:Q8TC05}.
VAR_SEQ 171 215 Missing (in isoform 4).
{ECO:0000303|PubMed:3182840}.
/FTId=VSP_027548.
VAR_SEQ 217 222 FRNKSQ -> AQEMRF (in isoform 3).
{ECO:0000303|PubMed:3182840}.
/FTId=VSP_027549.
VAR_SEQ 223 708 Missing (in isoform 3).
{ECO:0000303|PubMed:3182840}.
/FTId=VSP_027550.
VAR_SEQ 607 607 D -> EG (in isoform 2).
{ECO:0000303|PubMed:3182840}.
/FTId=VSP_027551.
VAR_SEQ 652 672 MGKPRTNNLQLHPHDAFNDED -> N (in isoform
2). {ECO:0000303|PubMed:3182840}.
/FTId=VSP_027552.
CONFLICT 40 40 R -> K (in Ref. 2; BAB27830).
{ECO:0000305}.
CONFLICT 438 438 S -> L (in Ref. 1; AAA39511).
{ECO:0000305}.
CONFLICT 442 442 K -> E (in Ref. 2; BAB23566).
{ECO:0000305}.
CONFLICT 456 456 Q -> P (in Ref. 2; BAB23566).
{ECO:0000305}.
CONFLICT 472 472 D -> G (in Ref. 1; AAA39511).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
26-405 MDM1 is a nuclear protein similar to the mouse double minute 1 protein. The mouse gene is located in double minute (DM) chromatin particles and is amplified in the mouse transformed 3T3 cell line, and 0.05 mg
GWB-92CA28 MDM4 (Mdm4. transformed 3T3 cell double minute 4. p53 binding protein (mouse))
GWB-A3FB35 MDM4 (Mdm4. transformed 3T3 cell double minute 4. p53 binding protein (mouse))
MTBS1 MTBP Gene Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) binding protein, 104kDa
ABP-PAB-10353 Transformed mouse 3T3 cell double minute 2, N_terminus (MDM2) polyclonal antibody 100 ug
ABP-PAB-10356 Transformed mouse 3T3 cell double minute 2, C_terminus (MDM2) polyclonal antibody 100 ug
CSB-EL015131MO Mouse Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) binding protein, 104kDa (MTBP) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL015131HU Human Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) binding protein, 104kDa (MTBP) ELISA kit, Species Human, Sample Type serum, plasma 96T
GWB-BF9EAB Mdm2 Transformed 3T3 Cell Double Minute 2 (MDM2_MTBP) Rabbit anti-Human Polyclonal (aa122-139) Antibody
18-003-42909 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Polyclonal 0.1 mg Protein A
20-003-40022 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Monoclonal 0.1 mg Protein A
18-003-42909 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Polyclonal 0.05 mg Aff Pur
20-003-40022 Mdm4 protein - p53-binding protein Mdm4; Mdm2-like p53-binding protein; Mdmx protein; Double minute 4 protein Monoclonal 0.05 mg Aff Pur
GWB-BF9EAB Mdm2 Transformed 3T3 Cell Double Minute 2 (MDM2 MTBP) Rabbit anti-Human Polyclonal (aa122-139) Antibody
BMDV10088 MDM 2 Protein (Murine Double Minute 2), 90_95kD, Clone SMP14, Mab anti_Human, Mouse, Rat; paraffin, IH 0.5 ml.
AXL7269M MDM 2 Protein (Murine Double Minute 2), native & denatured, Clone SMP14, Mab anti_Human, Mouse 1 ml.
MEDCLA115/2 MDM 2 Protein (Murine Double Minute 2), Rabbit anti_; paraffin 0.2 ml.
MEDCLA116-1 MDM 2 Protein (Murine Double Minute 2), Clone 1B10, Mab anti_; frozen_paraffin, IH 1 ml.
MEDCLA116-01 MDM 2 Protein (Murine Double Minute 2), Clone 1B10, Mab anti_; frozen_paraffin, IH 0.1 ml.
bs-1043P Peptides: MDM2 (urine double minute 2) Protein Length:12-25 amino acids. 200ug lyophilized
GWB-C49A21 Mouse Double Minute 2, Homolog Of; P53-binding Protein (MDM2) Rabbit anti-Mouse Polyclonal (aa177-195) Antibody
GWB-21CB31 Mouse Double Minute 2 Homolog Of; P53-binding Protein (MDM2) Mouse anti-Human Monoclonal (aa154-167) (SMP14) Antibody
18-783-75624 RABBIT ANTI MOUSE MDM2 (pSer185) - EC 6.3.2.-; p53-binding protein Mdm2; Oncoprotein Mdm2; Double minute 2 protein Polyclonal 0.05 mg
PR-843 MDM2 Mouse Double Minute 2human oncoprotein, recombinant, E. coli 10
PR-843 MDM2His Mouse Double Minute 2 human oncoprotein, recombinant, E. coli 10


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur