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Centriolin (Centrosomal protein 1) (Centrosomal protein of 110 kDa) (Cep110)

 CNTRL_HUMAN             Reviewed;        2325 AA.
Q7Z7A1; A2A2Y1; B2RP67; Q3MN79; Q5FWF8; Q5JVD0; Q6MZR3; Q6PKC1;
Q8TEP3; Q9Y489;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
22-NOV-2017, entry version 130.
RecName: Full=Centriolin;
AltName: Full=Centrosomal protein 1;
AltName: Full=Centrosomal protein of 110 kDa;
Short=Cep110;
Name=CNTRL; Synonyms=CEP1, CEP110;
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 3), TISSUE SPECIFICITY,
CHROMOSOMAL TRANSLOCATION WITH FGFR1, AND SUBCELLULAR LOCATION.
PubMed=10688839;
Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D.,
Rattner J.B., Pebusque M.-J.;
"FGFR1 is fused to the centrosome-associated protein CEP110 in the
8p12 stem cell myeloproliferative disorder with t(8;9)(p12;q33).";
Blood 95:1788-1796(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-56, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=12732615; DOI=10.1083/jcb.200301105;
Gromley A., Jurczyk A., Sillibourne J., Halilovic E., Mogensen M.,
Groisman I., Blomberg M., Doxsey S.J.;
"A novel human protein of the maternal centriole is required for the
final stages of cytokinesis and entry into S phase.";
J. Cell Biol. 161:535-545(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1513 (ISOFORM 2).
TISSUE=Lymph, and Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 434-1677 (ISOFORM 1).
PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
Wells J.W., Banham A.H., Mufti G.J.;
"Humoral detection of leukaemia-associated antigens in presentation
acute myeloid leukaemia.";
Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-2325 (ISOFORM 5).
TISSUE=Spleen;
PubMed=12693554; DOI=10.1093/dnares/10.1.49;
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
Ohara O.;
"Characterization of long cDNA clones from human adult spleen. II. The
complete sequences of 81 cDNA clones.";
DNA Res. 10:49-57(2003).
[8]
SUBCELLULAR LOCATION.
PubMed=11956314;
Ou Y.Y., Mack G.J., Zhang M., Rattner J.B.;
"CEP110 and ninein are located in a specific domain of the centrosome
associated with centrosome maturation.";
J. Cell Sci. 115:1825-1835(2002).
[9]
FUNCTION, INTERACTION WITH EXOC6 AND SNAPIN, AND SUBCELLULAR LOCATION.
PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
Guha M., Sillibourne J., Doxsey S.J.;
"Centriolin anchoring of exocyst and SNARE complexes at the midbody is
required for secretory-vesicle-mediated abscission.";
Cell 123:75-87(2005).
[10]
INTERACTION WITH HOOK2.
PubMed=17140400; DOI=10.1111/j.1600-0854.2006.00511.x;
Szebenyi G., Hall B., Yu R., Hashim A.I., Kraemer H.;
"Hook2 localizes to the centrosome, binds directly to
centriolin/CEP110 and contributes to centrosomal function.";
Traffic 8:32-46(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831 AND SER-1475, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
-!- FUNCTION: Involved in cell cycle progression and cytokinesis.
During the late steps of cytokinesis, anchors exocyst and SNARE
complexes at the midbody, thereby allowing secretory vesicle-
mediated abscission. {ECO:0000269|PubMed:12732615,
ECO:0000269|PubMed:16213214}.
-!- SUBUNIT: Interacts with HOOK2. Interacts with EXOC6 and SNAPIN.
Associates with the exocyst complex. {ECO:0000269|PubMed:16213214,
ECO:0000269|PubMed:17140400}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:10688839,
ECO:0000269|PubMed:11956314, ECO:0000269|PubMed:12732615}.
Midbody, Midbody ring {ECO:0000269|PubMed:12732615,
ECO:0000269|PubMed:16213214}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q7Z7A1-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z7A1-2; Sequence=VSP_032048;
Name=3;
IsoId=Q7Z7A1-3; Sequence=VSP_032047;
Name=4;
IsoId=Q7Z7A1-4; Sequence=VSP_032046, VSP_032050;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q7Z7A1-5; Sequence=VSP_032049;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis
and trachea. {ECO:0000269|PubMed:10688839}.
-!- DISEASE: Note=A chromosomal aberration involving CEP110 may be a
cause of stem cell myeloproliferative disorder (MPD).
Translocation t(8;9)(p12;q33) with FGFR1. MPD is characterized by
myeloid hyperplasia, eosinophilia and T-cell or B-cell
lymphoblastic lymphoma. In general it progresses to acute myeloid
leukemia. The fusion protein CEP110-FGFR1 is found in the
cytoplasm, exhibits constitutive kinase activity and may be
responsible for the transforming activity.
-!- SEQUENCE CAUTION:
Sequence=AAH02932.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH02932.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH89415.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF083322; AAC32373.1; -; mRNA.
EMBL; AF513978; AAP43846.1; -; mRNA.
EMBL; BX640927; CAE45965.1; -; mRNA.
EMBL; AL137068; CAI12358.1; -; Genomic_DNA.
EMBL; AL137068; CAM13285.1; -; Genomic_DNA.
EMBL; BC002932; AAH02932.1; ALT_SEQ; mRNA.
EMBL; BC089415; AAH89415.1; ALT_SEQ; mRNA.
EMBL; BC137286; AAI37287.1; -; mRNA.
EMBL; AY651261; AAX35689.1; -; mRNA.
EMBL; AK074079; BAB84905.1; -; mRNA.
CCDS; CCDS35118.1; -. [Q7Z7A1-1]
CCDS; CCDS83409.1; -. [Q7Z7A1-2]
RefSeq; NP_001317691.1; NM_001330762.1. [Q7Z7A1-2]
RefSeq; NP_008949.4; NM_007018.4. [Q7Z7A1-1]
RefSeq; XP_005251736.1; XM_005251679.3. [Q7Z7A1-1]
UniGene; Hs.653263; -.
ProteinModelPortal; Q7Z7A1; -.
SMR; Q7Z7A1; -.
BioGrid; 116248; 160.
DIP; DIP-47280N; -.
IntAct; Q7Z7A1; 173.
MINT; MINT-4988988; -.
STRING; 9606.ENSP00000238341; -.
iPTMnet; Q7Z7A1; -.
PhosphoSitePlus; Q7Z7A1; -.
BioMuta; CNTRL; -.
DMDM; 172045911; -.
EPD; Q7Z7A1; -.
MaxQB; Q7Z7A1; -.
PaxDb; Q7Z7A1; -.
PeptideAtlas; Q7Z7A1; -.
PRIDE; Q7Z7A1; -.
Ensembl; ENST00000238341; ENSP00000238341; ENSG00000119397. [Q7Z7A1-1]
Ensembl; ENST00000373850; ENSP00000362956; ENSG00000119397. [Q7Z7A1-2]
Ensembl; ENST00000373855; ENSP00000362962; ENSG00000119397. [Q7Z7A1-1]
Ensembl; ENST00000613863; ENSP00000481072; ENSG00000119397. [Q7Z7A1-4]
GeneID; 11064; -.
KEGG; hsa:11064; -.
UCSC; uc004bkx.1; human. [Q7Z7A1-1]
CTD; 11064; -.
DisGeNET; 11064; -.
EuPathDB; HostDB:ENSG00000119397.16; -.
GeneCards; CNTRL; -.
H-InvDB; HIX0008344; -.
HGNC; HGNC:1858; CNTRL.
HPA; HPA020468; -.
HPA; HPA020480; -.
HPA; HPA051583; -.
MIM; 605496; gene.
neXtProt; NX_Q7Z7A1; -.
OpenTargets; ENSG00000119397; -.
PharmGKB; PA26414; -.
eggNOG; ENOG410IJGD; Eukaryota.
eggNOG; ENOG410ZX4Y; LUCA.
GeneTree; ENSGT00900000140836; -.
HOVERGEN; HBG101203; -.
InParanoid; Q7Z7A1; -.
KO; K16770; -.
OMA; DESPYIG; -.
OrthoDB; EOG091G0066; -.
PhylomeDB; Q7Z7A1; -.
TreeFam; TF101135; -.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
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-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; Q7Z7A1; -.
ChiTaRS; CNTRL; human.
GeneWiki; CNTRL; -.
GenomeRNAi; 11064; -.
PRO; PR:Q7Z7A1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119397; -.
CleanEx; HS_CEP110; -.
ExpressionAtlas; Q7Z7A1; baseline and differential.
Genevisible; Q7Z7A1; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR028640; CEP110.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
PANTHER; PTHR44555; PTHR44555; 1.
SMART; SM00369; LRR_TYP; 3.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 5.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division;
Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Leucine-rich repeat; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 2325 Centriolin.
/FTId=PRO_0000323675.
REPEAT 126 147 LRR 1.
REPEAT 148 169 LRR 2.
REPEAT 170 191 LRR 3.
REPEAT 194 215 LRR 4.
DOMAIN 228 266 LRRCT.
REGION 1948 2118 Required for centrosome localization.
REGION 1985 2325 Sufficient for interaction with HOOK2.
{ECO:0000269|PubMed:17140400}.
COILED 267 343 {ECO:0000255}.
COILED 435 799 {ECO:0000255}.
COILED 851 1101 {ECO:0000255}.
COILED 1317 2255 {ECO:0000255}.
COMPBIAS 956 959 Poly-Lys.
COMPBIAS 1147 1150 Poly-Pro.
COMPBIAS 1236 1307 Pro-rich.
SITE 2139 2140 Breakpoint for translocation to form
CEP110-FGFR1.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1475 1475 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1818 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032046.
VAR_SEQ 1 1331 Missing (in isoform 3).
{ECO:0000303|PubMed:10688839}.
/FTId=VSP_032047.
VAR_SEQ 1 552 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032048.
VAR_SEQ 1291 1296 Missing (in isoform 5).
{ECO:0000303|PubMed:12693554}.
/FTId=VSP_032049.
VAR_SEQ 1962 1986 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_032050.
VARIANT 56 56 V -> I (in dbSNP:rs10818503).
{ECO:0000269|PubMed:12732615}.
/FTId=VAR_039559.
VARIANT 216 216 P -> L (in dbSNP:rs10818504).
/FTId=VAR_039560.
VARIANT 889 889 A -> T (in dbSNP:rs17292952).
/FTId=VAR_039561.
VARIANT 1146 1146 M -> V (in dbSNP:rs35342437).
/FTId=VAR_061622.
CONFLICT 1389 1389 Q -> R (in Ref. 1; AAC32373).
{ECO:0000305}.
CONFLICT 1699 1699 K -> Q (in Ref. 1; AAC32373).
{ECO:0000305}.
CONFLICT 1828 1828 E -> D (in Ref. 1; AAC32373).
{ECO:0000305}.
SEQUENCE 2325 AA; 268886 MW; 93DD4CA08B5BD4AF CRC64;
MKKGSQQKIF SKAKIPSSSH SPIPSSMSNM RSRSLSPLIG SETLPFHSGG QWCEQVEIAD
ENNMLLDYQD HKGADSHAGV RYITEALIKK LTKQDNLALI KSLNLSLSKD GGKKFKYIEN
LEKCVKLEVL NLSYNLIGKI EKLDKLLKLR ELNLSYNKIS KIEGIENMCN LQKLNLAGNE
IEHIPVWLGK KLKSLRVLNL KGNKISSLQD ISKLKPLQDL ISLILVENPV VTLPHYLQFT
IFHLRSLESL EGQPVTTQDR QEAFERFSLE EVERLERDLE KKMIETEELK SKQTRFLEEI
KNQDKLNKSL KEEAMLQKQS CEELKSDLNT KNELLKQKTI ELTRACQKQY ELEQELAFYK
IDAKFEPLNY YPSEYAEIDK APDESPYIGK SRYKRNMFAT ESYIIDSAQA VQIKKMEPDE
QLRNDHMNLR GHTPLDTQLE DKEKKISAAQ TRLSELHDEI EKAEQQILRA TEEFKQLEEA
IQLKKISEAG KDLLYKQLSG RLQLVNKLRQ EALDLELQME KQKQEIAGKQ KEIKDLQIAI
DSLDSKDPKH SHMKAQKSGK EQQLDIMNKQ YQQLESRLDE ILSRIAKETE EIKDLEEQLT
EGQIAANEAL KKDLEGVISG LQEYLGTIKG QATQAQNECR KLRDEKETLL QRLTEVEQER
DQLEIVAMDA ENMRKELAEL ESALQEQHEV NASLQQTQGD LSAYEAELEA RLNLRDAEAN
QLKEELEKVT RLTQLEQSAL QAELEKERQA LKNALGKAQF SEEKEQENSE LHAKLKHLQD
DNNLLKQQLK DFQNHLNHVV DGLVRPEEVA ARVDELRRKL KLGTGEMNIH SPSDVLGKSL
ADLQKQFSEI LARSKWERDE AQVRERKLQE EMALQQEKLA TGQEEFRQAC ERALEARMNF
DKRQHEARIQ QMENEIHYLQ ENLKSMEEIQ GLTDLQLQEA DEEKERILAQ LRELEKKKKL
EDAKSQEQVF GLDKELKKLK KAVATSDKLA TAELTIAKDQ LKSLHGTVMK INQERAEELQ
EAERFSRKAA QAARDLTRAE AEIELLQNLL RQKGEQFRLE MEKTGVGTGA NSQVLEIEKL
NETMERQRTE IARLQNVLDL TGSDNKGGFE NVLEEIAELR REVSYQNDYI SSMADPFKRR
GYWYFMPPPP SSKVSSHSSQ ATKDSGVGLK YSASTPVRKP RPGQQDGKEG SQPPPASGYW
VYSPIRSGLH KLFPSRDADS GGDSQEESEL DDQEEPPFVP PPGYMMYTVL PDGSPVPQGM
ALYAPPPPLP NNSRPLTPGT VVYGPPPAGA PMVYGPPPPN FSIPFIPMGV LHCNVPEHHN
LENEVSRLED IMQHLKSKKR EERWMRASKR QSEKEMEELH HNIDDLLQEK KSLECEVEEL
HRTVQKRQQQ KDFIDGNVES LMTELEIEKS LKHHEDIVDE IECIEKTLLK RRSELREADR
LLAEAESELS CTKEKTKNAV EKFTDAKRSL LQTESDAEEL ERRAQETAVN LVKADQQLRS
LQADAKDLEQ HKIKQEEILK EINKIVAAKD SDFQCLSKKK EKLTEELQKL QKDIEMAERN
EDHHLQVLKE SEVLLQAKRA ELEKLKSQVT SQQQEMAVLD RQLGHKKEEL HLLQGSMVQA
KADLQEALRL GETEVTEKCN HIREVKSLLE ELSFQKGELN VQISERKTQL TLIKQEIEKE
EENLQVVLRQ MSKHKTELKN ILDMLQLENH ELQGLKLQHD QRVSELEKTQ VAVLEEKLEL
ENLQQISQQQ KGEIEWQKQL LERDKREIER MTAESRALQS CVECLSKEKE DLQEKCDIWE
KKLAQTKRVL AAAEENSKME QSNLEKLELN VRKLQQELDQ LNRDKLSLHN DISAMQQQLQ
EKREAVNSLQ EELANVQDHL NLAKQDLLHT TKHQDVLLSE QTRLQKDISE WANRFEDCQK
EEETKQQQLQ VLQNEIEENK LKLVQQEMMF QRLQKERESE ESKLETSKVT LKEQQHQLEK
ELTDQKSKLD QVLSKVLAAE ERVRTLQEEE RWCESLEKTL SQTKRQLSER EQQLVEKSGE
LLALQKEADS MRADFSLLRN QFLTERKKAE KQVASLKEAL KIQRSQLEKN LLEQKQENSC
IQKEMATIEL VAQDNHERAR RLMKELNQMQ YEYTELKKQM ANQKDLERRQ MEISDAMRTL
KSEVKDEIRT SLKNLNQFLP ELPADLEAIL ERNENLEGEL ESLKENLPFT MNEGPFEEKL
NFSQVHIMDE HWRGEALREK LRHREDRLKA QLRHCMSKQA EVLIKGKRQT EGTLHSLRRQ
VDALGELVTS TSADSASSPS LSQLESSLTE DSQLGQNQEK NASAR


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E04C0641 Rabbit Centrosomal Protein 110kDa ELISA , CEP110 96 Tests/kit
E14C0641 Sheep Centrosomal Protein 110kDa ELISA , CEP110
E07C0641 Porcine Centrosomal Protein 110kDa Elisa Kit (CEP110) 96 Tests/kit
E06C0641 Goat Centrosomal Protein 110kDa ELISA , CEP110
E03C0641 Mouse Centrosomal Protein 110kDa ELISA , CEP110
E04C0641 Rabbit Centrosomal Protein 110kDa ELISA , CEP110
E07C0641 Porcine Centrosomal Protein 110kDa ELISA , CEP110
E11C0641 Bovine Centrosomal Protein 110kDa ELISA , CEP110 96 Tests/kit
E03C0641 Mouse Centrosomal Protein 110kDa ELISA ,CEP110 96 Tests/kit
E07C0641 Porcine Centrosomal Protein 110kDa ELISA , CEP110 96 Tests/kit
E13C0641 Anserine Centrosomal Protein 110kDa Elisa Kit (CEP110) 96 Tests/kit
E06C0641 Goat Centrosomal Protein 110kDa ELISA , CEP110 96 Tests/kit
E06C0641 Goat Centrosomal Protein 110kDa Elisa Kit (CEP110) 96 Tests/kit


 

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