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Centrosomal protein of 55 kDa (Cep55) (Up-regulated in colon cancer 6)

 CEP55_HUMAN             Reviewed;         464 AA.
Q53EZ4; B2RDG8; D3DR37; Q32WF5; Q3MV20; Q5VY28; Q6N034; Q96H32;
Q9NVS7;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
30-AUG-2017, entry version 128.
RecName: Full=Centrosomal protein of 55 kDa;
Short=Cep55;
AltName: Full=Up-regulated in colon cancer 6;
Name=CEP55; Synonyms=C10orf3, URCC6;
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), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, HOMODIMERIZATION, AND VARIANTS GLN-57 AND ALA-99.
PubMed=16406728; DOI=10.1016/j.ygeno.2005.11.006;
Martinez-Garay I., Rustom A., Gerdes H.-H., Kutsche K.;
"The novel centrosomal associated protein CEP55 is present in the
spindle midzone and the midbody.";
Genomics 87:243-253(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-99.
Shimokawa T., Furukawa Y., Sakai M., Nakamura Y.;
"Cloning and characterization of URCC6, a novel gene up-regulated in
colon cancer.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 33-464 (ISOFORM 2), AND VARIANTS
GLN-57; ALA-99 AND LEU-378.
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-99 AND LEU-378.
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-99.
TISSUE=Esophageal carcinoma;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-99 AND
LEU-378.
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-99 AND LEU-378.
TISSUE=Muscle;
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).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH
PLK1; AKAP9 AND PCNT, PHOSPHORYLATION AT SER-425; SER-428 AND SER-436,
MUTAGENESIS OF SER-396; SER-425; SER-428 AND SER-436, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16198290; DOI=10.1016/j.devcel.2005.09.003;
Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E.,
Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.;
"Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome
protein, Cep55, is required for its recruitment to midbody and
cytokinesis.";
Dev. Cell 9:477-488(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND 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).
[11]
FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, AND INTERACTION WITH
PDCD6IP; TSG101; MVB12A; VPS37B; VPS37C AND VPS28.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[12]
SELF-ASSOCIATION, INTERACTION WITH PDCD6IP AND TSG101, AND SUBCELLULAR
LOCATION.
PubMed=17556548; DOI=10.1126/science.1143422;
Carlton J.G., Martin-Serrano J.;
"Parallels between cytokinesis and retroviral budding: a role for the
ESCRT machinery.";
Science 316:1908-1912(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, 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).
[14]
INTERACTION WITH PDCD6IP, AND SUBCELLULAR LOCATION.
PubMed=18641129; DOI=10.1073/pnas.0802008105;
Carlton J.G., Agromayor M., Martin-Serrano J.;
"Differential requirements for Alix and ESCRT-III in cytokinesis and
HIV-1 release.";
Proc. Natl. Acad. Sci. U.S.A. 105:10541-10546(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-428; THR-430
AND SER-436, 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).
[16]
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).
[17]
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).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
SUBCELLULAR LOCATION.
PubMed=21310966; DOI=10.1126/science.1201847;
Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I.,
Leonhardt H., Mueller-Reichert T., Gerlich D.W.;
"Cortical constriction during abscission involves helices of ESCRT-
III-dependent filaments.";
Science 331:1616-1620(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-436, 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).
[21]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 160-217 IN COMPLEX WITH
PDCD6IP, INTERACTION WITH TSG101, AND MUTAGENESIS OF TRP-184; TYR-187;
ASP-188; ARG-191 AND GLU-192.
PubMed=18948538; DOI=10.1126/science.1162042;
Lee H.H., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J.H.;
"Midbody targeting of the ESCRT machinery by a noncanonical coiled
coil in CEP55.";
Science 322:576-580(2008).
[22]
VARIANT [LARGE SCALE ANALYSIS] ALA-99, 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).
[23]
VARIANT [LARGE SCALE ANALYSIS] ALA-99, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Plays a role in mitotic exit and cytokinesis. Recruits
PDCD6IP and TSG101 to midbody during cytokinesis. Required for
successful completion of cytokinesis. Not required for microtubule
nucleation. {ECO:0000269|PubMed:16198290,
ECO:0000269|PubMed:17853893}.
-!- SUBUNIT: Homodimer (PubMed:16406728). Interacts (phosphorylated on
Ser-425 and Ser-428) with PLK1 (PubMed:16198290). Interacts with
AKAP9/CG-NAP; the interaction occurs in interphase and is lost
upon mitotic entry (PubMed:16198290). Interacts with PCNT/Kendrin;
the interaction occurs in interphase and is lost upon mitotic
entry (PubMed:16198290). Directly interacts with PDCD6IP; this
interaction is required for PDCD6IP targeting to the midbody;
CEP55 binds PDCD6IP in a 2:1 stoichiometry; PDCD6IP competes with
TSG101 for the same binding site (PubMed:17853893,
PubMed:17556548, PubMed:18641129, PubMed:18948538). Interacts with
TSG101; TSG101 competes with PDCD6IP for the same binding site;
interaction is required for cytokinesis but not for viral budding
(PubMed:17853893, PubMed:17556548, PubMed:18948538). Interacts
with MVB12A, VPS37B, VPS37C and VPS28 (PubMed:17853893).
{ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16406728,
ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:18948538}.
-!- INTERACTION:
A8K9C1:-; NbExp=3; IntAct=EBI-747776, EBI-10174800;
P50995:ANXA11; NbExp=5; IntAct=EBI-747776, EBI-715243;
Q5T0G8:ANXA11; NbExp=3; IntAct=EBI-747776, EBI-10245225;
D3DTR7:ARHGEF15; NbExp=3; IntAct=EBI-747776, EBI-10176602;
Q9NX04:C1orf109; NbExp=5; IntAct=EBI-747776, EBI-8643161;
Q6UXH8:CCBE1; NbExp=3; IntAct=EBI-747776, EBI-3923278;
Q8TD31-3:CCHCR1; NbExp=5; IntAct=EBI-747776, EBI-10175300;
O75419:CDC45; NbExp=5; IntAct=EBI-747776, EBI-374969;
Q8IYX8:CEP57L1; NbExp=4; IntAct=EBI-747776, EBI-1104570;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-747776, EBI-10181988;
O60941:DTNB; NbExp=3; IntAct=EBI-747776, EBI-740402;
Q8N9N8:EIF1AD; NbExp=3; IntAct=EBI-747776, EBI-750700;
Q86YD7:FAM90A1; NbExp=5; IntAct=EBI-747776, EBI-6658203;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-747776, EBI-10244131;
P51116:FXR2; NbExp=3; IntAct=EBI-747776, EBI-740459;
Q0D2H9:GOLGA8DP; NbExp=5; IntAct=EBI-747776, EBI-10181276;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-747776, EBI-2514791;
O14964:HGS; NbExp=4; IntAct=EBI-747776, EBI-740220;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-747776, EBI-2125614;
Q8NDC0:MAPK1IP1L; NbExp=3; IntAct=EBI-747776, EBI-741424;
P55081:MFAP1; NbExp=5; IntAct=EBI-747776, EBI-1048159;
Q5JRA6-2:MIA3; NbExp=4; IntAct=EBI-747776, EBI-10244342;
Q15014:MORF4L2; NbExp=5; IntAct=EBI-747776, EBI-399257;
Q2TAK8-2:MUM1; NbExp=3; IntAct=EBI-747776, EBI-10239402;
Q8WUM4:PDCD6IP; NbExp=12; IntAct=EBI-747776, EBI-310624;
Q9UBV8:PEF1; NbExp=5; IntAct=EBI-747776, EBI-724639;
Q13526:PIN1; NbExp=3; IntAct=EBI-747776, EBI-714158;
Q3KR16:PLEKHG6; NbExp=5; IntAct=EBI-747776, EBI-10240979;
Q6PIY2:POLM; NbExp=7; IntAct=EBI-747776, EBI-10253863;
Q96T49:PPP1R16B; NbExp=5; IntAct=EBI-747776, EBI-10293968;
Q9H3S7:PTPN23; NbExp=3; IntAct=EBI-747776, EBI-724478;
Q96I25:RBM17; NbExp=5; IntAct=EBI-747776, EBI-740272;
Q9NW64:RBM22; NbExp=5; IntAct=EBI-747776, EBI-2602260;
Q9P2K3:RCOR3; NbExp=3; IntAct=EBI-747776, EBI-743428;
O00560:SDCBP; NbExp=5; IntAct=EBI-747776, EBI-727004;
P14678-2:SNRPB; NbExp=3; IntAct=EBI-747776, EBI-372475;
Q13573:SNW1; NbExp=3; IntAct=EBI-747776, EBI-632715;
Q9Y2D8:SSX2IP; NbExp=5; IntAct=EBI-747776, EBI-2212028;
P56279:TCL1A; NbExp=6; IntAct=EBI-747776, EBI-749995;
D3DUQ6:TEAD4; NbExp=3; IntAct=EBI-747776, EBI-10176734;
Q15561:TEAD4; NbExp=3; IntAct=EBI-747776, EBI-747736;
Q8IWB6:TEX14; NbExp=3; IntAct=EBI-747776, EBI-6674697;
Q92734:TFG; NbExp=5; IntAct=EBI-747776, EBI-357061;
Q99816:TSG101; NbExp=23; IntAct=EBI-747776, EBI-346882;
A5D8V6:VPS37C; NbExp=7; IntAct=EBI-747776, EBI-2559305;
Q9Y3C0:WASHC3; NbExp=5; IntAct=EBI-747776, EBI-712969;
Q96HA8:WDYHV1; NbExp=4; IntAct=EBI-747776, EBI-741158;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:16198290}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:16198290}. Cleavage furrow
{ECO:0000269|PubMed:16198290}. Midbody, Midbody ring
{ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:21310966}.
Note=Present at the centrosomes at interphase. A small portion is
associated preferentially with the mother centriole, whereas the
majority localizes to the pericentriolar material. During mitosis,
loses affinity for the centrosome at the onset of prophase and
diffuses throughout the cell. This dissociation from the
centrosome is phosphorylation-dependent. May remain localized at
the centrosome during mitosis in certain cell types. Appears at
the cleavage furrow in late anaphase and in the midbody in
cytokinesis. {ECO:0000269|PubMed:16198290}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q53EZ4-1; Sequence=Displayed;
Name=2;
IsoId=Q53EZ4-2; Sequence=VSP_014750, VSP_014751;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, mostly in proliferative
tissues. Highly expressed in testis. Intermediate levels in adult
and fetal thymus, as well as in various cancer cell lines. Low
levels in different parts of the digestive tract, bone marrow,
lymph nodes, placenta, fetal heart and fetal spleen. Hardly
detected in brain. {ECO:0000269|PubMed:16198290,
ECO:0000269|PubMed:16406728}.
-!- PTM: There is a hierachy of phosphorylation, where both Ser-425
and Ser-428 are phosphorylated at the onset of mitosis, prior to
Ser-436. Phosphorylation at Ser-425 and Ser-428 is required for
dissociation from the centrosome at the G2/M boundary.
Phosphorylation at the 3 sites, Ser-425, Ser-428 and Ser-436, is
required for protein function at the final stages of cell division
to complete cytokinesis successfully.
{ECO:0000269|PubMed:16198290}.
-!- SEQUENCE CAUTION:
Sequence=BAA91670.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY788918; AAX14687.1; -; mRNA.
EMBL; AB091343; BAE45243.1; -; mRNA.
EMBL; AK001402; BAA91670.1; ALT_INIT; mRNA.
EMBL; AK315536; BAG37915.1; -; mRNA.
EMBL; AK223495; BAD97215.1; -; mRNA.
EMBL; BX640718; CAE45837.1; -; mRNA.
EMBL; AL356214; CAH72324.1; -; Genomic_DNA.
EMBL; CH471066; EAW50071.1; -; Genomic_DNA.
EMBL; CH471066; EAW50072.1; -; Genomic_DNA.
EMBL; BC008947; AAH08947.1; -; mRNA.
CCDS; CCDS7428.1; -. [Q53EZ4-1]
RefSeq; NP_001120654.1; NM_001127182.1.
RefSeq; NP_060601.3; NM_018131.4.
UniGene; Hs.14559; -.
PDB; 3E1R; X-ray; 2.00 A; A/B=160-217.
PDB; 3WUT; X-ray; 2.30 A; A/B/D/E/G/H/J/K=160-217.
PDB; 3WUU; X-ray; 2.90 A; A/B/D/E/G/H/J/K=160-217.
PDB; 3WUV; X-ray; 2.79 A; A/B/D/E/G/H/J/K/M/N/P/Q=160-217.
PDBsum; 3E1R; -.
PDBsum; 3WUT; -.
PDBsum; 3WUU; -.
PDBsum; 3WUV; -.
ProteinModelPortal; Q53EZ4; -.
SMR; Q53EZ4; -.
BioGrid; 120465; 104.
DIP; DIP-44581N; -.
ELM; Q53EZ4; -.
IntAct; Q53EZ4; 99.
MINT; MINT-4994059; -.
STRING; 9606.ENSP00000360540; -.
iPTMnet; Q53EZ4; -.
PhosphoSitePlus; Q53EZ4; -.
BioMuta; CEP55; -.
DMDM; 296439403; -.
EPD; Q53EZ4; -.
MaxQB; Q53EZ4; -.
PaxDb; Q53EZ4; -.
PeptideAtlas; Q53EZ4; -.
PRIDE; Q53EZ4; -.
DNASU; 55165; -.
Ensembl; ENST00000371485; ENSP00000360540; ENSG00000138180. [Q53EZ4-1]
GeneID; 55165; -.
KEGG; hsa:55165; -.
UCSC; uc001kiq.4; human. [Q53EZ4-1]
CTD; 55165; -.
DisGeNET; 55165; -.
GeneCards; CEP55; -.
HGNC; HGNC:1161; CEP55.
HPA; HPA023430; -.
MIM; 610000; gene.
neXtProt; NX_Q53EZ4; -.
OpenTargets; ENSG00000138180; -.
PharmGKB; PA25475; -.
eggNOG; ENOG410IFBZ; Eukaryota.
eggNOG; ENOG41120Y2; LUCA.
GeneTree; ENSGT00510000047961; -.
HOVERGEN; HBG081092; -.
InParanoid; Q53EZ4; -.
KO; K16456; -.
OMA; YDQQREV; -.
OrthoDB; EOG091G065Y; -.
PhylomeDB; Q53EZ4; -.
TreeFam; TF331107; -.
SIGNOR; Q53EZ4; -.
EvolutionaryTrace; Q53EZ4; -.
GeneWiki; CEP55; -.
GenomeRNAi; 55165; -.
PRO; PR:Q53EZ4; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138180; -.
CleanEx; HS_CEP55; -.
ExpressionAtlas; Q53EZ4; baseline and differential.
Genevisible; Q53EZ4; HS.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IGI:MGI.
InterPro; IPR022008; EABR.
Pfam; PF12180; EABR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Mitosis;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 464 Centrosomal protein of 55 kDa.
/FTId=PRO_0000089777.
REGION 157 236 Interaction with TSG101.
REGION 160 214 Interaction with PDCD6IP.
REGION 355 464 Required for localization to the
interphase centrosome and to the midbody
during cytokinesis.
{ECO:0000269|PubMed:16198290}.
COILED 22 186 {ECO:0000255}.
COILED 238 337 {ECO:0000255}.
COILED 374 403 {ECO:0000255}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BT07}.
MOD_RES 425 425 Phosphoserine; by CDK1 and MAPK1.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:16198290}.
MOD_RES 428 428 Phosphoserine; by CDK1 and MAPK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16198290}.
MOD_RES 430 430 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 436 436 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16198290}.
VAR_SEQ 389 400 NQITQLESLKQL -> KNNTVGILETAS (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_014750.
VAR_SEQ 401 464 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014751.
VARIANT 57 57 H -> Q (in dbSNP:rs3740370).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:16406728}.
/FTId=VAR_026559.
VARIANT 99 99 T -> A (in dbSNP:rs7080916).
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16406728,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.2, ECO:0000269|Ref.4,
ECO:0000269|Ref.7}.
/FTId=VAR_022996.
VARIANT 236 236 C -> R (in dbSNP:rs7072484).
/FTId=VAR_056791.
VARIANT 378 378 H -> L (in dbSNP:rs2293277).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4, ECO:0000269|Ref.7}.
/FTId=VAR_022997.
MUTAGEN 184 184 W->A: Abolishes interaction with PDCD6IP.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 187 187 Y->A: Abolishes interaction with PDCD6IP.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 188 188 D->A: Diminishes interaction with
PDCD6IP. {ECO:0000269|PubMed:18948538}.
MUTAGEN 191 191 R->A: Abolishes interaction with PDCD6IP.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 192 192 E->A: Abolishes interaction with PDCD6IP.
{ECO:0000269|PubMed:18948538}.
MUTAGEN 396 396 S->A: No effect on phosphorylation in
mitotic cells.
{ECO:0000269|PubMed:16198290}.
MUTAGEN 425 425 S->A: Partial loss of phosphorylation in
mitotic cells. Complete loss of
phosphorylation in mitotic cells; when
associated with A-428. Remains associated
with the centrosome throughout mitosis;
when associated with A-428. Arrests
mitotic cells at the midbody stage; when
associated with A-428 and A-436.
{ECO:0000269|PubMed:16198290}.
MUTAGEN 428 428 S->A: Partial loss of phosphorylation in
mitotic cells. Complete loss of
phosphorylation in mitotic cells; when
associated with A-425. Remains associated
with the centrosome throughout mitosis;
when associated with A-425. Arrests
mitotic cells at the midbody stage; when
associated with A-425 and A-436.
{ECO:0000269|PubMed:16198290}.
MUTAGEN 436 436 S->A: No effect on phosphorylation in
mitotic cells. Arrests mitotic cells at
the midbody stage; when associated with
A-425 and A-428.
{ECO:0000269|PubMed:16198290}.
CONFLICT 155 155 V -> A (in Ref. 4; BAD97215).
{ECO:0000305}.
CONFLICT 204 204 E -> G (in Ref. 4; BAD97215).
{ECO:0000305}.
CONFLICT 298 298 R -> G (in Ref. 5; CAE45837).
{ECO:0000305}.
CONFLICT 334 334 F -> S (in Ref. 1; AAX14687 and 3;
BAA91670). {ECO:0000305}.
CONFLICT 435 435 E -> G (in Ref. 1; AAX14687).
{ECO:0000305}.
HELIX 166 209 {ECO:0000244|PDB:3E1R}.
SEQUENCE 464 AA; 54178 MW; A652F86EBCE46A51 CRC64;
MSSRSTKDLI KSKWGSKPSN SKSETTLEKL KGEIAHLKTS VDEITSGKGK LTDKERHRLL
EKIRVLEAEK EKNAYQLTEK DKEIQRLRDQ LKARYSTTTL LEQLEETTRE GERREQVLKA
LSEEKDVLKQ QLSAATSRIA ELESKTNTLR LSQTVAPNCF NSSINNIHEM EIQLKDALEK
NQQWLVYDQQ REVYVKGLLA KIFELEKKTE TAAHSLPQQT KKPESEGYLQ EEKQKCYNDL
LASAKKDLEV ERQTITQLSF ELSEFRRKYE ETQKEVHNLN QLLYSQRRAD VQHLEDDRHK
TEKIQKLREE NDIARGKLEE EKKRSEELLS QVQFLYTSLL KQQEEQTRVA LLEQQMQACT
LDFENEKLDR QHVQHQLHVI LKELRKARNQ ITQLESLKQL HEFAITEPLV TFQGETENRE
KVAASPKSPT AALNESLVEC PKCNIQYPAT EHRDLLVHVE YCSK


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