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Centrosome-associated protein CEP250 (250 kDa centrosomal protein) (Cep250) (Centrosomal Nek2-associated protein 1) (C-Nap1) (Centrosomal protein 2)

 CP250_HUMAN             Reviewed;        2442 AA.
Q9BV73; E1P5Q3; O14812; O60588; Q9H450;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
09-MAY-2003, sequence version 2.
18-JUL-2018, entry version 156.
RecName: Full=Centrosome-associated protein CEP250;
AltName: Full=250 kDa centrosomal protein;
Short=Cep250;
AltName: Full=Centrosomal Nek2-associated protein 1;
Short=C-Nap1;
AltName: Full=Centrosomal protein 2;
Name=CEP250; Synonyms=CEP2, CNAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION AS
AUTOANTIGEN IN AUTOIMMUNE DISEASES.
TISSUE=Cervix carcinoma;
PubMed=9506584;
DOI=10.1002/1529-0131(199803)41:3<551::AID-ART22>3.0.CO;2-X;
Mack G.J., Rees J., Sandblom O., Balczon R., Fritzler M.J.,
Rattner J.B.;
"Autoantibodies to a group of centrosomal proteins in human autoimmune
sera reactive with the centrosome.";
Arthritis Rheum. 41:551-558(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH NEK2,
AND SUBCELLULAR LOCATION DURING THE CELL CYCLE.
TISSUE=Placenta;
PubMed=9647649; DOI=10.1083/jcb.141.7.1563;
Fry A.M., Mayor T., Meraldi P., Stierhof Y.-D., Tanaka K., Nigg E.A.;
"C-Nap1, a novel centrosomal coiled-coil protein and candidate
substrate of the cell cycle-regulated protein kinase Nek2.";
J. Cell Biol. 141:1563-1574(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION, AND INTERACTION WITH NEK2 AND PPP1CA.
PubMed=10880350; DOI=10.1042/0264-6021:3490509;
Helps N.R., Luo X., Barker H.M., Cohen P.T.W.;
"NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase
localized to centrosomes, is complexed to protein phosphatase 1.";
Biochem. J. 349:509-518(2000).
[6]
PHOSPHORYLATION DURING CELL CYCLE.
PubMed=12140259;
Mayor T., Hacker U., Stierhof Y.-D., Nigg E.A.;
"The mechanism regulating the dissociation of the centrosomal protein
C-Nap1 from mitotic spindle poles.";
J. Cell Sci. 115:3275-3284(2002).
[7]
INTERACTION WITH CEP135.
PubMed=18851962; DOI=10.1016/j.yexcr.2008.09.016;
Kim K., Lee S., Chang J., Rhee K.;
"A novel function of CEP135 as a platform protein of C-NAP1 for its
centriolar localization.";
Exp. Cell Res. 314:3692-3700(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2229 AND SER-2252, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
PHOSPHORYLATION AT SER-2417 AND SER-2421.
PubMed=21076410; DOI=10.1038/ncb2120;
Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M.,
Schiebel E.;
"Components of the Hippo pathway cooperate with Nek2 kinase to
regulate centrosome disjunction.";
Nat. Cell Biol. 12:1166-1176(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138; THR-2218; SER-2229
AND SER-2322, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[11]
INTERACTION WITH CNTLN.
PubMed=24554434; DOI=10.1242/jcs.139451;
Fang G., Zhang D., Yin H., Zheng L., Bi X., Yuan L.;
"Centlein mediates an interaction between C-Nap1 and Cep68 to maintain
centrosome cohesion.";
J. Cell Sci. 127:1631-1639(2014).
[12]
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: Probably plays an important role in centrosome cohesion
during interphase.
-!- SUBUNIT: Monomer and homodimer (Probable). Forms a complex in
vitro with both NEK2 kinase and the PPP1CC catalytic subunit of
protein phosphatase 1 (PP1) (PubMed:9647649, PubMed:10880350).
Interacts with CEP135 (PubMed:18851962). Interacts with
CROCC/rootletin (By similarity). Interacts with CNTLN
(PubMed:24554434). Interacts with NIN (via C-terminus) (By
similarity). {ECO:0000250|UniProtKB:Q60952,
ECO:0000269|PubMed:10880350, ECO:0000269|PubMed:18851962,
ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:9647649,
ECO:0000305}.
-!- INTERACTION:
O88566:Axin2 (xeno); NbExp=3; IntAct=EBI-1053100, EBI-7690990;
Q9H0K1:SIK2; NbExp=5; IntAct=EBI-1053100, EBI-1181664;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9647649}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000269|PubMed:9647649}. Note=Component of the core
centrosome. In interphase cells, it specifically associates with
the proximal ends of both mother and daughter centrioles.
Associates with the centrosome in interphase cells. In mitotic
cells, it dissociates from the mitotic spindle poles. At the end
of cell division, it reaccumulates at centrosomes. In
photoreceptors, found at the proximal ends of basal bodies.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BV73-1; Sequence=Displayed;
Name=2;
IsoId=Q9BV73-2; Sequence=VSP_007372;
-!- TISSUE SPECIFICITY: Ubiquitously and weakly expressed.
-!- PTM: Differentially phosphorylated during cell cycle.
Phosphorylation may regulate association/dissociation from
centrosome. During M phase of mitosis, C-terminal part is
phosphorylated by NEK2, suggesting that it may trigger the
dissociation from the mitotic centrosome. Dephosphorylated in
vitro by the PP1 phosphatase. {ECO:0000269|PubMed:10880350,
ECO:0000269|PubMed:12140259, ECO:0000269|PubMed:21076410}.
-!- MISCELLANEOUS: Antibodies against CEP2 are present in sera from
patients with autoimmune diseases that developed autoantibodies
against centrosomal proteins.
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EMBL; AF022655; AAC06349.1; -; mRNA.
EMBL; AF049105; AAC07988.1; -; mRNA.
EMBL; AL121586; CAB89415.1; -; Genomic_DNA.
EMBL; CH471077; EAW76206.1; -; Genomic_DNA.
EMBL; CH471077; EAW76207.1; -; Genomic_DNA.
CCDS; CCDS13255.1; -. [Q9BV73-1]
PIR; T08621; T08621.
RefSeq; NP_001305148.1; NM_001318219.1.
RefSeq; NP_009117.2; NM_007186.5. [Q9BV73-1]
RefSeq; XP_005260319.1; XM_005260262.4. [Q9BV73-1]
RefSeq; XP_006723753.1; XM_006723690.3. [Q9BV73-1]
RefSeq; XP_006723754.1; XM_006723691.1. [Q9BV73-1]
RefSeq; XP_006723755.1; XM_006723692.3. [Q9BV73-1]
RefSeq; XP_006723756.1; XM_006723693.3. [Q9BV73-1]
UniGene; Hs.443976; -.
ProteinModelPortal; Q9BV73; -.
SMR; Q9BV73; -.
BioGrid; 116360; 244.
DIP; DIP-39406N; -.
IntAct; Q9BV73; 15.
MINT; Q9BV73; -.
STRING; 9606.ENSP00000380661; -.
iPTMnet; Q9BV73; -.
PhosphoSitePlus; Q9BV73; -.
BioMuta; CEP250; -.
DMDM; 30580364; -.
EPD; Q9BV73; -.
MaxQB; Q9BV73; -.
PaxDb; Q9BV73; -.
PeptideAtlas; Q9BV73; -.
PRIDE; Q9BV73; -.
ProteomicsDB; 79175; -.
ProteomicsDB; 79176; -. [Q9BV73-2]
DNASU; 11190; -.
Ensembl; ENST00000397527; ENSP00000380661; ENSG00000126001. [Q9BV73-1]
GeneID; 11190; -.
KEGG; hsa:11190; -.
UCSC; uc032pib.2; human. [Q9BV73-1]
CTD; 11190; -.
DisGeNET; 11190; -.
EuPathDB; HostDB:ENSG00000126001.15; -.
GeneCards; CEP250; -.
H-InvDB; HIX0015764; -.
HGNC; HGNC:1859; CEP250.
HPA; HPA064875; -.
MIM; 609689; gene.
neXtProt; NX_Q9BV73; -.
OpenTargets; ENSG00000126001; -.
PharmGKB; PA26415; -.
eggNOG; ENOG410IFAN; Eukaryota.
eggNOG; ENOG410XPG3; LUCA.
GeneTree; ENSGT00730000110800; -.
HOGENOM; HOG000246955; -.
HOVERGEN; HBG081320; -.
InParanoid; Q9BV73; -.
KO; K16464; -.
OMA; QKERIQV; -.
OrthoDB; EOG091G034H; -.
PhylomeDB; Q9BV73; -.
TreeFam; TF101138; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; Q9BV73; -.
ChiTaRS; CEP250; human.
GeneWiki; CEP250; -.
GenomeRNAi; 11190; -.
PRO; PR:Q9BV73; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000126001; -.
CleanEx; HS_CEP250; -.
ExpressionAtlas; Q9BV73; baseline and differential.
Genevisible; Q9BV73; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; NAS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
GO; GO:1905515; P:non-motile cilium assembly; IMP:GO_Central.
GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
GO; GO:0030997; P:regulation of centriole-centriole cohesion; IDA:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
InterPro; IPR026048; CEP250.
PANTHER; PTHR23159:SF1; PTHR23159:SF1; 2.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell projection; Cilium;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 2442 Centrosome-associated protein CEP250.
/FTId=PRO_0000089487.
COILED 95 158 {ECO:0000255}.
COILED 244 352 {ECO:0000255}.
COILED 395 1172 {ECO:0000255}.
COILED 1243 2227 {ECO:0000255}.
COILED 2262 2376 {ECO:0000255}.
COMPBIAS 246 250 Poly-Leu.
COMPBIAS 464 2171 Gln/Glu-rich.
MOD_RES 2138 2138 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2218 2218 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2229 2229 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2252 2252 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2322 2322 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2417 2417 Phosphoserine; by NEK2.
{ECO:0000269|PubMed:21076410}.
MOD_RES 2421 2421 Phosphoserine; by NEK2.
{ECO:0000269|PubMed:21076410}.
VAR_SEQ 863 918 Missing (in isoform 2).
{ECO:0000303|PubMed:9647649}.
/FTId=VSP_007372.
VARIANT 995 995 Q -> H (in dbSNP:rs2296403).
/FTId=VAR_015649.
VARIANT 1072 1072 Q -> E (in dbSNP:rs17092706).
/FTId=VAR_050898.
VARIANT 1441 1441 R -> Q (in dbSNP:rs3748433).
/FTId=VAR_021858.
CONFLICT 120 120 L -> I (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 136 136 E -> A (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 365 365 H -> L (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 372 372 D -> E (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 509 509 E -> D (in Ref. 2; AAC07988).
{ECO:0000305}.
CONFLICT 552 552 S -> I (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 757 757 E -> A (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 784 787 EVTK -> DEPQ (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 1153 1153 Q -> H (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 1246 1246 H -> L (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 1513 1513 L -> P (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 2082 2082 Q -> L (in Ref. 1; AAC06349).
{ECO:0000305}.
CONFLICT 2345 2345 D -> N (in Ref. 1; AAC06349).
{ECO:0000305}.
SEQUENCE 2442 AA; 281137 MW; BC2B8A36E07B8272 CRC64;
METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ RQATLVRKLQ
AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL VRLEEEQQRC ESLAEVNTQL
RLHMEKADVV NKALREDVEK LTVDWSRARD ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL
WREVVTFRRH FLEMKSATDR DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG
REPAQLLLLL AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE
DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ VMVEEGDNIA
QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ AVQDLRQQLA GCQEAVNLLQ
QQHDQWEEEG KALRQRLQKL TGERDTLAGQ TVDLQGEVDS LSKERELLQK AREELRQQLE
VLEQEAWRLR RVNVELQLQG DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS
ELITLREALE SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK
LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA EKRREALWEK
NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR HQQEAATTQL EQLHQEAKRQ
EEVLARAVQE KEALVREKAA LEVRLQAVER DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN
SVIEVTKGQL EVQIQTVTQA KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG
KTALEQQKAA HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA
IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER LRQDMKVQKL
KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS LLQDKMDLQK QVEDLKSQLV
AQDDSQRLVE QEVQEKLRET QEYNRIQKEL EREKASLTLS LMEKEQRLLV LQEADSIRQQ
ELSALRQDMQ EAQGEQKELS AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA
SLWAQEAKAA QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR
PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ DLWKTQQTRD
VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE KSKWEGKQNS LESELMELHE
TMASLQSRLR RAELQRMEAQ GERELLQAAK ENLTAQVEHL QAAVVEARAQ ASAAGILEED
LRTARSALKL KNEEVESERE RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL
RGQIQELEKQ REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE
QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK QLVTLECLAL
ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER SQELQAQSSQ IHDLESHSTV
LARELQERDQ EVKSQREQIE ELQRQKEHLT QDLERRDQEL MLQKERIQVL EDQRTRQTKI
LEEDLEQIKL SLRERGRELT TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC
QQEHIHELQE LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS
LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA HMTLKERHGE
LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE KALLALQQQC AEQAQEHEVE
TRALQDSWLQ AQAVLKERDQ ELEALRAESQ SSRHQEEAAR ARAEALQEAL GKAHAALQGK
EQHLLEQAEL SRSLEASTAT LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL
QQALAQRDEE LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ
LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR ELERLQAALR
QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS VLERDSEQQR LQDELELTRR
ALEKERLHSP GATSTAELGS RGEQGVQLGE VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA
RLEIDRSRLQ RHNVQLRSTL EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG
QKNSDAKCVA ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ
APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR


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EIAAB08871 250 kDa centrosomal protein,Centrosomal Nek2-associated protein 1,Centrosomal protein 2,Centrosome-associated protein CEP250,Cep2,Cep250,Cep250,C-Nap1,Inmp,Intranuclear matrix protein,Mouse,Mus muscul
EIAAB08872 250 kDa centrosomal protein,Centrosomal Nek2-associated protein 1,Centrosomal protein 2,Centrosome-associated protein CEP250,CEP2,Cep250,CEP250,CNAP1,C-Nap1,Homo sapiens,Human
CEP250 CEP170 Gene centrosomal protein 170kDa
CEP350 CEP250 Gene centrosomal protein 250kDa
201-20-1021 CEP250{Homo sapiens centrosomal protein 250kDa}rabbit.pAb 0.1ml
EIAAB06679 C6orf182,Centrosomal protein 57kDa-like protein 1,Centrosomal protein CEP57L1,Centrosomal protein of 57 kDa-related protein,CEP57L1,Cep57R,CEP57R,Cep57-related protein,Homo sapiens,Human
EIAAB06681 Centrosomal protein 57kDa-like protein 1,Centrosomal protein CEP57L1,Centrosomal protein of 57 kDa-related protein,Cep57l1,Cep57R,Cep57r,Cep57-related protein,Rat,Rattus norvegicus
EIAAB06680 Centrosomal protein 57kDa-like protein 1,Centrosomal protein CEP57L1,Centrosomal protein of 57 kDa-related protein,Cep57l1,Cep57R,Cep57r,Cep57-related protein,Mouse,Mus musculus
CSB-EL005239MO Mouse centrosomal protein 250kDa (CEP250) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL005239HU Human centrosomal protein 250kDa (CEP250) ELISA kit, Species Human, Sample Type serum, plasma 96T
CP250_HUMAN ELISA Kit FOR Centrosome-associated protein CEP250; organism: Human; gene name: CEP250 96T
CP250_MOUSE ELISA Kit FOR Centrosome-associated protein CEP250; organism: Mouse; gene name: Cep250 96T
CSB-EL005239MO Mouse Centrosome-associated protein CEP250(CEP250) ELISA kit SpeciesMouse 96T
CSB-EL005239HU Human Centrosome-associated protein CEP250(CEP250) ELISA kit SpeciesHuman 96T
CSB-EL005239MO Mouse Centrosome-associated protein CEP250(CEP250) ELISA kit 96T
CSB-EL005239HU Human Centrosome-associated protein CEP250(CEP250) ELISA kit 96T
EIAAB08340 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,CEP1,Cep110,CEP110,CNTRL,Homo sapiens,Human
EIAAB08838 Centrosomal protein 4,Centrosomal protein of 135 kDa,Cep135,CEP135,CEP4,Homo sapiens,Human,KIAA0635
EIAAB08339 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,Cep1,Cep110,Cep110,Cntrl,Mouse,Mus musculus
EIAAB08839 Centrosomal protein 4,Centrosomal protein of 135 kDa,Cep135,Cep135,Cep4,Kiaa0635,Mouse,Mus musculus
EIAAB06777 CENPJ,CENP-J,Centromere protein J,Centrosomal P4.1-associated protein,CPAP,Homo sapiens,Human,LAG-3-associated protein,LAP,LIP1,LYST-interacting protein 1
CP250_MOUSE Mouse ELISA Kit FOR Centrosome-associated protein CEP250 96T
CP250_HUMAN Human ELISA Kit FOR Centrosome-associated protein CEP250 96T
EIAAB06867 Ccdc45,Centrosomal protein of 95 kDa,Cep95,Coiled-coil domain-containing protein 45,Rat,Rattus norvegicus
EIAAB06861 Ccdc21,Centrosomal protein of 85 kDa,Cep85,Coiled-coil domain-containing protein 21,Mouse,Mus musculus


 

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