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

Centrosomal protein of 192 kDa (Cep192)

 CE192_HUMAN             Reviewed;        2537 AA.
Q8TEP8; A0A060A9S4; B7ZMF0; E9PF99; Q8WYT8; Q9H0F4; Q9NW27;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
18-JUL-2018, sequence version 3.
18-JUL-2018, entry version 122.
RecName: Full=Centrosomal protein of 192 kDa;
Short=Cep192;
Short=Cep192/SPD-2 {ECO:0000303|PubMed:25042804};
Name=CEP192; Synonyms=KIAA1569; ORFNames=PP8407;
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), AND FUNCTION.
PubMed=25042804; DOI=10.1016/j.molcel.2014.06.016;
Joukov V., Walter J.C., De Nicolo A.;
"The Cep192-organized aurora A-Plk1 cascade is essential for
centrosome cycle and bipolar spindle assembly.";
Mol. Cell 55:578-591(2014).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 757-2537 (ISOFORM 1), AND
VARIANTS MET-1365; HIS-1544; PRO-1552; PHE-1701; PRO-2121 AND
LEU-2449.
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 797-2537 (ISOFORM 1), AND
VARIANTS PRO-1552; PHE-1701; ASN-2051; PRO-2121; GLU-2271 AND
LEU-2449.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1453-2537 (ISOFORM 2), AND
VARIANTS HIS-1544; PRO-1552 AND PHE-1701.
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1958-2537 (ISOFORM 1), AND
VARIANTS PRO-2121 AND LEU-2449.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND
VARIANTS PRO-1552; PHE-1701; PRO-2121 AND LEU-2449.
TISSUE=Brain;
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).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[9]
INTERACTION WITH SHBG.
PubMed=15862967; DOI=10.1016/j.jsbmb.2005.01.007;
Pope S.N., Lee I.R.;
"Yeast two-hybrid identification of prostatic proteins interacting
with human sex hormone-binding globulin.";
J. Steroid Biochem. Mol. Biol. 94:203-208(2005).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17980596; DOI=10.1016/j.cub.2007.10.019;
Gomez-Ferreria M.A., Rath U., Buster D.W., Chanda S.K., Caldwell J.S.,
Rines D.R., Sharp D.J.;
"Human Cep192 is required for mitotic centrosome and spindle
assembly.";
Curr. Biol. 17:1960-1966(2007).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18207742; DOI=10.1016/j.cub.2007.12.055;
Zhu F., Lawo S., Bird A., Pinchev D., Ralph A., Richter C.,
Mueller-Reichert T., Kittler R., Hyman A.A., Pelletier L.;
"The mammalian SPD-2 ortholog Cep192 regulates centrosome
biogenesis.";
Curr. Biol. 18:136-141(2008).
[12]
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-812; SER-1755; SER-2098
AND SER-2110, 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).
[15]
HYDROXYLATION AT PRO-2313, UBIQUITINATION, AND MUTAGENESIS OF
PRO-2313.
PubMed=23932902; DOI=10.1016/j.devcel.2013.06.014;
Moser S.C., Bensaddek D., Ortmann B., Maure J.F., Mudie S., Blow J.J.,
Lamond A.I., Swedlow J.R., Rocha S.;
"PHD1 links cell-cycle progression to oxygen sensing through
hydroxylation of the centrosomal protein Cep192.";
Dev. Cell 26:381-392(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1755 AND SER-2110, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Required for mitotic centrosome maturation and bipolar
spindle assembly (PubMed:25042804, PubMed:17980596,
PubMed:18207742). Appears to be a major regulator of
pericentriolar material (PCM) recruitment, centrosome maturation,
and centriole duplication (PubMed:25042804, PubMed:17980596,
PubMed:18207742). Centrosome-specific activating scaffold for
AURKA and PLK1 (PubMed:25042804). {ECO:0000269|PubMed:17980596,
ECO:0000269|PubMed:18207742, ECO:0000269|PubMed:25042804}.
-!- SUBUNIT: Interacts with SHBG. {ECO:0000269|PubMed:15862967}.
-!- INTERACTION:
O00444:PLK4; NbExp=13; IntAct=EBI-16111881, EBI-746202;
P62136:PPP1CA; NbExp=2; IntAct=EBI-2339778, EBI-357253;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:17980596,
ECO:0000269|PubMed:18207742}. Note=Pericentriolar location in
mitotic centrosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3;
IsoId=Q8TEP8-3; Sequence=Displayed;
Name=1;
IsoId=Q8TEP8-1; Sequence=VSP_059657;
Name=2;
IsoId=Q8TEP8-2; Sequence=VSP_059657, VSP_059658, VSP_059659;
-!- PTM: Hydroxylation by PHD1/EGLN2 at Pro-2313 promotes
ubiquitination. {ECO:0000269|PubMed:23932902}.
-!- PTM: Ubiquitinated by a SCF(SKP2) complex following proline
hydroxylation. {ECO:0000269|PubMed:23932902}.
-!- SEQUENCE CAUTION:
Sequence=AAL55870.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA91559.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB66752.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB66752.1; Type=Frameshift; Positions=1792, 1835; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; KJ567064; AIA61642.1; -; mRNA.
EMBL; AP001357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136818; CAB66752.1; ALT_SEQ; mRNA.
EMBL; AK074074; BAB84900.1; -; mRNA.
EMBL; AF318363; AAL55870.1; ALT_INIT; mRNA.
EMBL; AK001214; BAA91559.1; ALT_INIT; mRNA.
EMBL; BC144481; AAI44482.1; -; mRNA.
CCDS; CCDS32792.2; -. [Q8TEP8-3]
RefSeq; NP_115518.3; NM_032142.3. [Q8TEP8-3]
UniGene; Hs.100914; -.
PDB; 4N7Z; X-ray; 2.85 A; B=1134-1191.
PDBsum; 4N7Z; -.
ProteinModelPortal; Q8TEP8; -.
SMR; Q8TEP8; -.
ComplexPortal; CPX-1161; CEP192-PLK4 complex.
DIP; DIP-52779N; -.
IntAct; Q8TEP8; 44.
STRING; 9606.ENSP00000427550; -.
iPTMnet; Q8TEP8; -.
PhosphoSitePlus; Q8TEP8; -.
DMDM; 162416230; -.
EPD; Q8TEP8; -.
MaxQB; Q8TEP8; -.
PaxDb; Q8TEP8; -.
PeptideAtlas; Q8TEP8; -.
PRIDE; Q8TEP8; -.
ProteomicsDB; 74474; -.
ProteomicsDB; 74475; -. [Q8TEP8-2]
Ensembl; ENST00000506447; ENSP00000427550; ENSG00000101639. [Q8TEP8-3]
GeneID; 55125; -.
KEGG; hsa:55125; -.
UCSC; uc010xac.3; human. [Q8TEP8-1]
CTD; 55125; -.
DisGeNET; 55125; -.
EuPathDB; HostDB:ENSG00000101639.18; -.
GeneCards; CEP192; -.
HGNC; HGNC:25515; CEP192.
HPA; HPA039392; -.
HPA; HPA040503; -.
MIM; 616426; gene.
neXtProt; NX_Q8TEP8; -.
OpenTargets; ENSG00000101639; -.
PharmGKB; PA142672129; -.
eggNOG; ENOG410IG8G; Eukaryota.
eggNOG; ENOG4110RMB; LUCA.
GeneTree; ENSGT00510000048187; -.
HOGENOM; HOG000111525; -.
HOVERGEN; HBG106621; -.
InParanoid; Q8TEP8; -.
KO; K16725; -.
OMA; EPHMKHT; -.
OrthoDB; EOG091G00BY; -.
PhylomeDB; Q8TEP8; -.
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.
ChiTaRS; CEP192; human.
PRO; PR:Q8TEP8; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000101639; -.
CleanEx; HS_CEP192; -.
ExpressionAtlas; Q8TEP8; baseline and differential.
Genevisible; Q8TEP8; HS.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000242; C:pericentriolar material; IEA:Ensembl.
GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
GO; GO:0090222; P:centrosome-templated microtubule nucleation; 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:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR039103; Spd-2/CEP192.
PANTHER; PTHR16029; PTHR16029; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Hydroxylation; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 2537 Centrosomal protein of 192 kDa.
/FTId=PRO_0000312495.
MOD_RES 812 812 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1755 1755 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2098 2098 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2110 2110 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2313 2313 Hydroxyproline.
{ECO:0000269|PubMed:23932902}.
VAR_SEQ 1 603 MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVA
VSTLARDRSSTDNRYPDIQASYLVEGRFSVPSGSSPGSQSD
AEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQM
ETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQ
SWMNNKEPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLIL
PTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEG
PEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDS
HSSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFS
SGTWGTEKEIENLKGIVPDLNSECASKDVLVKTLRAIDVKL
NSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHMDGCL
DTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRT
CECHESIEKNKDKTDLPQSVVYQNEEGRWVTDLAYYTSFNS
KQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEEFNKEHQFIQ
EENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDA
SYLRLSLGEFFAQRSEALGCLGGGNNVKR -> MKTSDLV
(in isoform 1 and isoform 2).
/FTId=VSP_059657.
VAR_SEQ 1999 2003 ALLHK -> QGPAT (in isoform 2).
/FTId=VSP_059658.
VAR_SEQ 2004 2537 Missing (in isoform 2).
/FTId=VSP_059659.
VARIANT 1053 1053 T -> A (in dbSNP:rs10048340).
/FTId=VAR_037514.
VARIANT 1109 1109 Q -> P (in dbSNP:rs11080623).
/FTId=VAR_050782.
VARIANT 1365 1365 V -> M (in dbSNP:rs2282542).
{ECO:0000269|PubMed:11230166}.
/FTId=VAR_037515.
VARIANT 1544 1544 R -> H (in dbSNP:rs7228940).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:15498874}.
/FTId=VAR_050783.
VARIANT 1552 1552 S -> P (in dbSNP:rs578208).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15498874}.
/FTId=VAR_050784.
VARIANT 1701 1701 L -> F (in dbSNP:rs6505780).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15498874}.
/FTId=VAR_050785.
VARIANT 2051 2051 S -> N (in dbSNP:rs2027698).
{ECO:0000269|PubMed:12693554}.
/FTId=VAR_050786.
VARIANT 2121 2121 L -> P (in dbSNP:rs474337).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_050787.
VARIANT 2271 2271 K -> E (in dbSNP:rs3737379).
{ECO:0000269|PubMed:12693554}.
/FTId=VAR_050788.
VARIANT 2449 2449 R -> L (in dbSNP:rs1786263).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:12693554,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_050789.
MUTAGEN 2313 2313 P->A: Increased presence on interphasic
centrosomes, and decreased presence on
mitotic centrosomes; no ubiquitination
and unchanged levels in response to
hypoxia. {ECO:0000269|PubMed:23932902}.
CONFLICT 357 357 V -> I (in Ref. 1; AIA61642).
{ECO:0000305}.
CONFLICT 1402 1402 R -> L (in Ref. 4; BAB84900).
{ECO:0000305}.
CONFLICT 1453 1453 P -> A (in Ref. 5; AAL55870).
{ECO:0000305}.
CONFLICT 2115 2115 R -> Q (in Ref. 3 and 7; AAI44482).
{ECO:0000305}.
SEQUENCE 2537 AA; 279111 MW; CA0A92F264280C3B CRC64;
MEDFRGIAEE SFPSFLTNSL FGNSGILENV TLSSNLGLPV AVSTLARDRS STDNRYPDIQ
ASYLVEGRFS VPSGSSPGSQ SDAEPRERLQ LSFQDDDSIS RKKSYVESQR LSNALSKQSA
LQMETAGPEE EPAGATESLQ GQDLFNRASP LEQAQDSPID FHLQSWMNNK EPKIVVLDAG
KHFEDKTLKS DLSHTSLLEN EKLILPTSLE DSSDDDIDDE MFYDDHLEAY FEQLAIPGMI
YEDLEGPEPP EKGFKLPTNG LRQANENGSL NCKFQSENNS SLISLDSHSS ETTHKESEES
QVICLPGTSN SIGTGDSRRY TDGMLPFSSG TWGTEKEIEN LKGIVPDLNS ECASKDVLVK
TLRAIDVKLN SDNFHDANAN RGGFDLTDPV KQGAECPHQN KTVLHMDGCL DTETPTVSIQ
ENVDVASLKP ISDSGINFTD AIWSPTCERR TCECHESIEK NKDKTDLPQS VVYQNEEGRW
VTDLAYYTSF NSKQNLNVSL SDEMNEDFRS GSEAFDLIAQ DEEEFNKEHQ FIQEENIDAH
NTSVALGDTS WGATINYSLL RKSRSTSDLD KDDASYLRLS LGEFFAQRSE ALGCLGGGNN
VKRPSFGYFI RSPEKREPIA LIRKSDVSRG NLEKEMAHLN HDLYSGDLNE QSQAQLSEGS
ITLQVEAVES TSQVDENDVT LTADKGKTED TFFMSNKPQR YKDKLPDSGD SMLRISTIAS
AIAEASVNTD PSQLAAMIKA LSNKTRDKTF QEDEKQKDYS HVRHFLPNDL EKSNGSNALD
MEKYLKKTEV SRYESALENF SRASMSDTWD LSLPKEQTTQ DIHPVDLSAT SVSVRAPEEN
TAAIVYVENG ESENQESFRT INSSNSVTNR ENNSAVVDVK TCSIDNKLQD VGNDEKATSI
STPSDSYSSV RNPRITSLCL LKDCEEIRDN RENQRQNECV SEISNSEKHV TFENHRIVSP
KNSDLKNTSP EHGGRGSEDE QESFRPSTSP LSHSSPSEIS GTSSSGCALE SFGSAAQQQQ
PPCEQELSPL VCSPAGVSRL TYVSEPESSY PTTATDDALE DRKSDITSEL STTIIQGSPA
ALEERAMEKL REKVPFQNRG KGTLSSIIQN NSDTRKATET TSLSSKPEYV KPDFRWSKDP
SSKSGNLLET SEVGWTSNPE ELDPIRLALL GKSGLSCQVG SATSHPVSCQ EPIDEDQRIS
PKDKSTAGRE FSGQVSHQTT SENQCTPIPS STVHSSVADM QNMPAAVHAL LTQPSLSAAP
FAQRYLGTLP STGSTTLPQC HAGNATVCGF SGGLPYPAVA GEPVQNSVAV GICLGSNIGS
GWMGTSSLCN PYSNTLNQNL LSTTKPFPVP SVGTNCGIEP WDSGVTSGLG SVRVPEELKL
PHACCVGIAS QTLLSVLNPT DRWLQVSIGV LSISVNGEKV DLSTYRCLVF KNKAIIRPHA
TEEIKVLFIP SSPGVFRCTF SVASWPCSTD AETIVQAEAL ASTVTLTAIA ESPVIEVETE
KKDVLDFGDL TYGGWKALPL KLINRTHATV PIRLIINANA VAWRCFTFSK ESVRAPVEVA
PCADVVTRLA GPSVVNHMMP ASYDGQDPEF LMIWVLFHSP KKQISSSDIL DSAEEFSAKV
DIEVDSPNPT PVLRSVSLRA RAGIARIHAP RDLQTMHFLA KVASSRKQHL PLKNAGNIEV
YLDIKVPEQG SHFSVDPKNL LLKPGEEHEV IVSFTPKDPE ACEERILKIF VQPFGPQYEV
VLKGEVISSG SKPLSPGPCL DIPSILSNKQ FLAWGGVPLG RTQLQKLALR NNSASTTQHL
RLLIRGQDQD CFQLQNTFGS EQRLTSNCEI RIHPKEDIFI SVLFAPTRLS CMLARLEIKQ
LGNRSQPGIK FTIPLSGYGG TSNLILEGVK KLSDSYMVTV NGLVPGKESK IVFSVRNTGS
RAAFVKAVGF KDSQKKVLLD PKVLRIFPDK FVLKERTQEN VTLIYNPSDR GINNKTATEL
STVYLFGGDE ISRQQYRRAL LHKPEMIKQI LPEHSVLQNI NFVEAFQDEL LVTEVYDLPQ
RPNDVQLFYG SMCKIILSVI GEFRDCISSR EFLQPSSKAS LESTSDLGAS GKHGGNVSLD
VLPVKGPQGS PLLSRAARPP LDQLASEEPW TVLPEHLILV APSPCDMAKT GRFQIVNNSV
RLLRFELCWP AHCLTVTPQH GCVAPESKLQ ILVSPNSSLS TKQSMFPWSG LIYIHCDDGQ
KKIVKVQIRE DLTQVELLTR LTSKPFGILS PVSEPSVSHL VKPMTKPPST KVEIRNKSIT
FPTTEPGETS ESCLELENHG TTDVKWHLSS LAPPYVKGVD ESGDVFRATY AAFRCSPISG
LLESHGIQKV SITFLPRGRG DYAQFWDVEC HPLKEPHMKH TLRFQLSGQS IEAENEPENA
CLSTDSLIKI DHLVKPRRQA VSEASARIPE QLDVTARGVY APEDVYRFRP TSVGESRTLK
VNLRNNSFIT HSLKFLSPRE PFYVKHSKYS LRAQHYINMP VQFKPKSAGK FEALLVIQTD
EGKSIAIRLI GEALGKN


Related products :

Catalog number Product name Quantity
EIAAB06674 Centrosomal protein of 192 kDa,Cep192,CEP192,Homo sapiens,Human,KIAA1569,PP8407
CEP192 CEP164 Gene centrosomal protein 164kDa
CEP290 CEP192 Gene centrosomal protein 192kDa
CSB-EL005238HU Human Centrosomal protein of 192 kDa(CEP192) ELISA kit 96T
CSB-EL005238HU Human Centrosomal protein of 192 kDa(CEP192) ELISA kit SpeciesHuman 96T
CE192_HUMAN ELISA Kit FOR Centrosomal protein of 192 kDa; organism: Human; gene name: CEP192 96T
CSB-EL005238HU Human centrosomal protein 192kDa (CEP192) ELISA kit, Species Human, Sample Type serum, plasma 96T
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
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
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
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
EIAAB08340 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,CEP1,Cep110,CEP110,CNTRL,Homo sapiens,Human
EIAAB08339 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,Cep1,Cep110,Cep110,Cntrl,Mouse,Mus musculus
EIAAB08838 Centrosomal protein 4,Centrosomal protein of 135 kDa,Cep135,CEP135,CEP4,Homo sapiens,Human,KIAA0635
EIAAB08839 Centrosomal protein 4,Centrosomal protein of 135 kDa,Cep135,Cep135,Cep4,Kiaa0635,Mouse,Mus musculus
005060A CEP192 250ul
049689A Cep192 250ul
i004462d CEP192 siRNA_Lentivectors 500ng
NBP1-28718 CEP192 0.1 mg
i004462b CEP192 siRNA_Lentivectors 500ng
i004462 CEP192-set siRNA_Lentivectors 4x500ng
i004462c CEP192 siRNA_Lentivectors 500ng
i004462a CEP192 siRNA_Lentivectors 500ng
BP302-324 CEP192 Blocking Peptide 50 ug


 

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