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Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein)

 MISP_HUMAN              Reviewed;         679 AA.
Q8IVT2;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 118.
RecName: Full=Mitotic interactor and substrate of PLK1 {ECO:0000303|PubMed:23574715};
AltName: Full=Mitotic spindle positioning protein {ECO:0000312|HGNC:HGNC:27000};
Name=MISP {ECO:0000312|HGNC:HGNC:27000};
Synonyms=C19orf21 {ECO:0000312|HGNC:HGNC:27000};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; THR-287 AND
SER-400, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164; THR-172; THR-219;
THR-224; SER-284; THR-287; SER-394; SER-395; SER-397; SER-400;
SER-430; SER-541; SER-543; SER-575; THR-577; SER-582 AND SER-675, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; THR-164; SER-214;
THR-219; THR-287; THR-377; SER-394; SER-395; SER-400; SER-471;
SER-541; SER-575; THR-577 AND SER-582, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
FUNCTION, INTERACTION WITH DCTN1; MAPRE1 AND PTK2, SUBCELLULAR
LOCATION, AND PHOSPHORYLATION BY CDK1.
PubMed=23574715; DOI=10.4161/cc.24602;
Maier B., Kirsch M., Anderhub S., Zentgraf H., Kraemer A.;
"The novel actin/focal adhesion-associated protein MISP is involved in
mitotic spindle positioning in human cells.";
Cell Cycle 12:1457-1471(2013).
[8]
FUNCTION, INTERACTION WITH ACTIN AND DCTN1, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-78; THR-164; THR-172;
SER-214; THR-224; SER-284; THR-287; THR-377; SER-382; SER-394;
SER-395; SER-397; SER-575; SER-582 AND SER-586, AND MUTAGENESIS OF
SER-78; THR-164; THR-172; SER-214; THR-224; SER-284; THR-287; THR-377;
SER-382; SER-394; SER-395; SER-397; SER-471; SER-575; SER-582 AND
SER-586.
PubMed=23509069; DOI=10.1083/jcb.201207050;
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L.,
Ponting C.P., Goenczy P., Hoffmann I.;
"MISP is a novel Plk1 substrate required for proper spindle
orientation and mitotic progression.";
J. Cell Biol. 200:773-787(2013).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-156; THR-164;
THR-179; THR-224; SER-348; SER-394; SER-395; SER-397; SER-400;
SER-471; SER-541; SER-543 AND SER-575, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Plays a role in mitotic spindle orientation and mitotic
progression. Regulates the distribution of dynactin at the cell
cortex in a PLK1-dependent manner, thus stabilizing cortical and
astral microtubule attachments required for proper mitotic spindle
positioning. May link microtubules to the actin cytospkeleton and
focal adhesions. May be required for directed cell migration and
centrosome orientation. May also be necessary for proper stacking
of the Golgi apparatus. {ECO:0000269|PubMed:23509069,
ECO:0000269|PubMed:23574715}.
-!- SUBUNIT: Associates with F-actin. Interacts with DCTN1; this
interaction regulates DCTN1 distribution at the cell cortex.
Interacts with PTK2/FAK and MAPRE1. {ECO:0000269|PubMed:23509069,
ECO:0000269|PubMed:23574715}.
-!- INTERACTION:
Q8TAP6:CEP76; NbExp=4; IntAct=EBI-2555085, EBI-742887;
Q9H0I2:ENKD1; NbExp=4; IntAct=EBI-2555085, EBI-744099;
Q9UKT9:IKZF3; NbExp=4; IntAct=EBI-2555085, EBI-747204;
P25800:LMO1; NbExp=4; IntAct=EBI-2555085, EBI-8639312;
Q6NUQ1:RINT1; NbExp=4; IntAct=EBI-2555085, EBI-726876;
Q12933:TRAF2; NbExp=4; IntAct=EBI-2555085, EBI-355744;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasm,
cytoskeleton. Cytoplasm, cell cortex. Note=Predominantly localizes
to cortical actin structures during interphase and mitosis.
Present in retraction fibers, which are formed at former adhesion
sites during mitosis, and at spicular membrane protrusions in re-
attaching cytokinetic cells. Partially colocalizes with
cytoplasmic F-actin. Not detected at microtubules at interphase,
nor at spindle during mitosis.
-!- DEVELOPMENTAL STAGE: Regulated in a cell-cycle dependent manner.
Weakly expressed in G1 and S phases. Expression increases in G2/M
phases and persisting until the end of mitosis (at protein level).
{ECO:0000269|PubMed:23509069}.
-!- PTM: Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase
for PLK1 phosphorylation. Phosphorylation by PLK1 is required for
proper spindle orientation at metaphase.
{ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:23574715}.
-!- SIMILARITY: Belongs to the MISP family. {ECO:0000305}.
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EMBL; BC042125; AAH42125.1; -; mRNA.
EMBL; BC052236; AAH52236.1; -; mRNA.
CCDS; CCDS12042.1; -.
PIR; T00636; T00636.
RefSeq; NP_775752.1; NM_173481.3.
RefSeq; XP_011525987.1; XM_011527685.2.
RefSeq; XP_011525988.1; XM_011527686.2.
UniGene; Hs.439180; -.
ProteinModelPortal; Q8IVT2; -.
BioGrid; 125982; 58.
IntAct; Q8IVT2; 77.
MINT; MINT-4992628; -.
STRING; 9606.ENSP00000215582; -.
iPTMnet; Q8IVT2; -.
PhosphoSitePlus; Q8IVT2; -.
BioMuta; MISP; -.
DMDM; 73620663; -.
EPD; Q8IVT2; -.
MaxQB; Q8IVT2; -.
PaxDb; Q8IVT2; -.
PeptideAtlas; Q8IVT2; -.
PRIDE; Q8IVT2; -.
Ensembl; ENST00000215582; ENSP00000215582; ENSG00000099812.
GeneID; 126353; -.
KEGG; hsa:126353; -.
UCSC; uc002lpo.4; human.
CTD; 126353; -.
EuPathDB; HostDB:ENSG00000099812.8; -.
GeneCards; MISP; -.
H-InvDB; HIX0027524; -.
HGNC; HGNC:27000; MISP.
HPA; HPA049511; -.
HPA; HPA062232; -.
MIM; 615289; gene.
neXtProt; NX_Q8IVT2; -.
OpenTargets; ENSG00000099812; -.
PharmGKB; PA134861073; -.
eggNOG; ENOG410IP6Q; Eukaryota.
eggNOG; ENOG41127B9; LUCA.
GeneTree; ENSGT00510000049581; -.
HOGENOM; HOG000111983; -.
HOVERGEN; HBG081352; -.
InParanoid; Q8IVT2; -.
OMA; DHRREGL; -.
OrthoDB; EOG091G012B; -.
PhylomeDB; Q8IVT2; -.
TreeFam; TF334067; -.
ChiTaRS; MISP; human.
GenomeRNAi; 126353; -.
PRO; PR:Q8IVT2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000099812; -.
CleanEx; HS_C19orf21; -.
Genevisible; Q8IVT2; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
InterPro; IPR029304; AKAP2_C.
Pfam; PF15304; AKAP2_C; 1.
1: Evidence at protein level;
Actin-binding; Cell cycle; Cell division; Cell junction; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 679 Mitotic interactor and substrate of PLK1.
/FTId=PRO_0000079381.
COILED 545 569 {ECO:0000255}.
MOD_RES 78 78 Phosphoserine; by CDK1; in vitro.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 164 164 Phosphothreonine; by CDK1; in vitro.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 172 172 Phosphothreonine; by CDK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:23509069}.
MOD_RES 179 179 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 214 214 Phosphoserine; by CDK1; in vitro.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:23509069}.
MOD_RES 219 219 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 224 224 Phosphothreonine; by CDK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 284 284 Phosphoserine; by CDK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:23509069}.
MOD_RES 287 287 Phosphothreonine; by CDK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:23509069}.
MOD_RES 348 348 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 377 377 Phosphothreonine; by CDK1; in vitro.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:23509069}.
MOD_RES 382 382 Phosphoserine; by CDK1; in vitro.
{ECO:0000269|PubMed:23509069}.
MOD_RES 394 394 Phosphoserine; by PLK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 395 395 Phosphoserine; by PLK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 397 397 Phosphoserine; by PLK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 471 471 Phosphoserine; by PLK1; in vitro.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 575 575 Phosphoserine; by CDK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23509069}.
MOD_RES 577 577 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 582 582 Phosphoserine; by PLK1; in vitro.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:23509069}.
MOD_RES 586 586 Phosphoserine; by PLK1; in vitro.
{ECO:0000269|PubMed:23509069}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 99 99 A -> T (in dbSNP:rs45477999).
/FTId=VAR_061629.
VARIANT 156 156 S -> G (in dbSNP:rs3746173).
/FTId=VAR_033754.
VARIANT 232 232 K -> R (in dbSNP:rs3746175).
/FTId=VAR_033755.
VARIANT 269 269 S -> N (in dbSNP:rs35384259).
/FTId=VAR_050910.
VARIANT 653 653 E -> G (in dbSNP:rs8107847).
/FTId=VAR_033756.
MUTAGEN 78 78 S->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-164;
A-172; A-214; A-224; A-284; A-287; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 164 164 T->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-172; A-214; A-224; A-284; A-287; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 172 172 T->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-214; A-224; A-284; A-287; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 214 214 S->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-172; A-224; A-284; A-287; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 224 224 T->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-172; A-214; A-284; A-287; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 284 284 S->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-172; A-214; A-224; A-287; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 287 287 T->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-172; A-214; A-224; A-284; A-377
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 377 377 T->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-172; A-214; A-224; A-284; A-287
and A-575. {ECO:0000269|PubMed:23509069}.
MUTAGEN 382 382 S->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-394;
A-395; A-397; A-471; A-582 and A-586.
{ECO:0000269|PubMed:23509069}.
MUTAGEN 394 394 S->A: Drastic reduction in PLK1
phosphorylation in vitro, no effect on
cortical localization; when associated
with A-382; A-395; A-397; A-471; A-582
and A-586. {ECO:0000269|PubMed:23509069}.
MUTAGEN 394 394 S->D: No effect on cortical localization;
when associated with D-395; D-397; D-471;
D-582 and D-586.
{ECO:0000269|PubMed:23509069}.
MUTAGEN 395 395 S->A: Drastic reduction in PLK1
phosphorylation in vitro, no effect on
cortical localization; when associated
with A-382; A-394; A-397; A-471; A-582
and A-586. {ECO:0000269|PubMed:23509069}.
MUTAGEN 395 395 S->D: No effect on cortical localization;
when associated with D-394; D-397; D-471;
D-582 and D-586.
{ECO:0000269|PubMed:23509069}.
MUTAGEN 397 397 S->A: Drastic reduction in PLK1
phosphorylation in vitro, no effect on
cortical localization; when associated
with A-382; A-394; A-395; A-471; A-582
and A-586. {ECO:0000269|PubMed:23509069}.
MUTAGEN 397 397 S->D: No effect on cortical localization;
when associated with D-394; D-395; D-471;
D-582 and D-586.
{ECO:0000269|PubMed:23509069}.
MUTAGEN 471 471 S->A: Drastic reduction in PLK1
phosphorylation in vitro, no effect on
cortical localization; when associated
with A-382; A-394; A-395; A-397; A-582
and A-586. {ECO:0000269|PubMed:23509069}.
MUTAGEN 471 471 S->D: No effect on cortical localization;
when associated with D-394; D-395; D-397;
D-582 and D-586.
{ECO:0000269|PubMed:23509069}.
MUTAGEN 575 575 S->A: Almost complete loss of CDK1
phosphorylation in vitro, loss of PLK1-
binding, no effect on cortical
localization; when associated with A-78;
A-164; A-172; A-214; A-224; A-284; A-287
and A-377. {ECO:0000269|PubMed:23509069}.
MUTAGEN 582 582 S->A: Drastic reduction in PLK1
phosphorylation in vitro, no effect on
cortical localization; when associated
with A-382; A-394; A-395; A-397; A-471
and A-586. {ECO:0000269|PubMed:23509069}.
MUTAGEN 582 582 S->D: No effect on cortical localization;
when associated with D-394; D-395; D-397;
D-471 and D-586.
{ECO:0000269|PubMed:23509069}.
MUTAGEN 586 586 S->A: Drastic reduction in PLK1
phosphorylation in vitro, no effect on
cortical localization; when associated
with A-382; A-394; A-395; A-397; A-471
and A-582. {ECO:0000269|PubMed:23509069}.
MUTAGEN 586 586 S->D: No effect on cortical localization;
when associated with D-394; D-395; D-397;
D-471 and D-582.
{ECO:0000269|PubMed:23509069}.
SEQUENCE 679 AA; 75357 MW; D2881CF5087E61F8 CRC64;
MDRVTRYPIL GIPQAHRGTG LVLDGDTSYT YHLVCMGPEA SGWGQDEPQT WPTDHRAQQG
VQRQGVSYSV HAYTGQPSPR GLHSENREDE GWQVYRLGAR DAHQGRPTWA LRPEDGEDKE
MKTYRLDAGD ADPRRLCDLE RERWAVIQGQ AVRKSSTVAT LQGTPDHGDP RTPGPPRSTP
LEENVVDREQ IDFLAARQQF LSLEQANKGA PHSSPARGTP AGTTPGASQA PKAFNKPHLA
NGHVVPIKPQ VKGVVREENK VRAVPTWASV QVVDDPGSLA SVESPGTPKE TPIEREIRLA
QEREADLREQ RGLRQATDHQ ELVEIPTRPL LTKLSLITAP RRERGRPSLY VQRDIVQETQ
REEDHRREGL HVGRASTPDW VSEGPQPGLR RALSSDSILS PAPDARAADP APEVRKVNRI
PPDAYQPYLS PGTPQLEFSA FGAFGKPSSL STAEAKAATS PKATMSPRHL SESSGKPLST
KQEASKPPRG CPQANRGVVR WEYFRLRPLR FRAPDEPQQA QVPHVWGWEV AGAPALRLQK
SQSSDLLERE RESVLRREQE VAEERRNALF PEVFSPTPDE NSDQNSRSSS QASGITGSYS
VSESPFFSPI HLHSNVAWTV EDPVDSAPPG QRKKEQWYAG INPSDGINSE VLEAIRVTRH
KNAMAERWES RIYASEEDD


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EIAAB26172 Bos taurus,Bovine,FAM128,Mitotic-spindle organizing protein 2,Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 2,MOZART2,MZT2
EIAAB26171 Fam128b,Mitotic-spindle organizing protein 2,Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 2B,Mouse,Mozart2,Mus musculus,Mzt2
EIAAB26170 Mitotic-spindle organizing protein 1,Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1,Mouse,Mozart1,Mus musculus,Mzt1
HDAC3_HUMAN Mouse ELISA Kit FOR Mitotic-spindle organizing protein 2 96T
E3652h Human Mitotic Spindle Organizing Protein 1 ELISA K 96T
ODO2_BOVIN Human ELISA Kit FOR Mitotic-spindle organizing protein 1 96T
E0205h Mouse ELISA Kit FOR Mitotic-spindle organizing protein 2 96T
CNOT3_HUMAN Human ELISA Kit FOR Mitotic-spindle organizing protein 1 96T
MZT1_MOUSE Mouse ELISA Kit FOR Mitotic-spindle organizing protein 1 96T
ZNT6_MOUSE Mouse ELISA Kit FOR Mitotic-spindle organizing protein 2 96T
E0250m Human ELISA Kit FOR Mitotic-spindle organizing protein 1 96T
E4302h Human Mitotic Spindle Organizing Protein 2B ELISA 96T
E3635h Human Mitotic Spindle Organizing Protein 2A ELISA 96T
CSB-EL003125HU Human Mitotic-spindle organizing protein 1(C13orf37) ELISA kit 96T
CSB-EL008047HU Human Mitotic-spindle organizing protein 2A(FAM128A) ELISA kit 96T
CSB-EL008048HU Human Mitotic-spindle organizing protein 2B(FAM128B) ELISA kit 96T
CC160_BOVIN Mouse ELISA Kit FOR Mitotic spindle assembly checkpoint protein MAD1 96T
MD2L2_BOVIN Bovine ELISA Kit FOR Mitotic spindle assembly checkpoint protein MAD2B 96T
CSB-EL008047HU Human Mitotic-spindle organizing protein 2A(FAM128A) ELISA kit SpeciesHuman 96T
E0274r Mouse ELISA Kit FOR Mitotic spindle assembly checkpoint protein MAD1 96T
CSB-EL008048HU Human Mitotic-spindle organizing protein 2B(FAM128B) ELISA kit SpeciesHuman 96T


 

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