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Centrosomal protein of 192 kDa (Cep192)

 CE192_HUMAN             Reviewed;        1941 AA.
Q8TEP8; A0A060A9S4; B7ZMF0; E9PF99; Q8WYT8; Q9H0F4; Q9NW27;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
28-FEB-2018, entry version 119.
RecName: Full=Centrosomal protein of 192 kDa;
Short=Cep192;
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).
Joukov V., Walter J.C., De Nicolo A.;
"The Cep192-organized Aurora A-Plk1 cascade is essential for
centrosome cycle and bipolar spindle assembly.";
Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
[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 161-1941 (ISOFORM 1), AND
VARIANTS MET-769; HIS-948; PRO-956; PHE-1105; PRO-1525 AND LEU-1853.
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 201-1941 (ISOFORM 1), AND
VARIANTS PRO-956; PHE-1105; ASN-1455; PRO-1525; GLU-1675 AND LEU-1853.
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 857-1941 (ISOFORM 2), AND
VARIANTS HIS-948; PRO-956 AND PHE-1105.
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 1362-1941 (ISOFORM 1), AND
VARIANTS PRO-1525 AND LEU-1853.
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-956; PHE-1105; PRO-1525 AND LEU-1853.
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-216; SER-1159; SER-1502
AND SER-1514, 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-1717, UBIQUITINATION, AND MUTAGENESIS OF
PRO-1717.
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-1159 AND SER-1514, 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 and spindle assembly.
Appears to be a major regulator of pericentriolar material (PCM)
recruitment, centrosome maturation, and centriole duplication.
{ECO:0000269|PubMed:17980596, ECO:0000269|PubMed:18207742}.
-!- 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=1;
IsoId=Q8TEP8-1; Sequence=Displayed;
Name=2;
IsoId=Q8TEP8-2; Sequence=VSP_029845, VSP_029846;
Name=3;
IsoId=Q8TEP8-3; Sequence=VSP_055678;
Note=Ref.1 (AIA61642) sequence is in conflict in position:
357:V->I. {ECO:0000305};
-!- PTM: Hydroxylation by PHD1/EGLN2 at Pro-1717 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=1196, 1239; Evidence={ECO:0000305};
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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=538-595.
PDBsum; 4N7Z; -.
ProteinModelPortal; Q8TEP8; -.
SMR; Q8TEP8; -.
DIP; DIP-52779N; -.
IntAct; Q8TEP8; 43.
STRING; 9606.ENSP00000427550; -.
iPTMnet; Q8TEP8; -.
PhosphoSitePlus; Q8TEP8; -.
DMDM; 162416230; -.
EPD; Q8TEP8; -.
MaxQB; Q8TEP8; -.
PaxDb; Q8TEP8; -.
PeptideAtlas; Q8TEP8; -.
PRIDE; Q8TEP8; -.
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.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013783; Ig-like_fold.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Hydroxylation; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 1941 Centrosomal protein of 192 kDa.
/FTId=PRO_0000312495.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1502 1502 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1514 1514 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1717 1717 Hydroxyproline.
{ECO:0000269|PubMed:23932902}.
VAR_SEQ 1 7 MKTSDLV -> MEDFRGIAEESFPSFLTNSLFGNSGILENV
TLSSNLGLPVAVSTLARDRSSTDNRYPDIQASYLVEGRFSV
PSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLS
NALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQ
AQDSPIDFHLQSWMNNKEPKIVVLDAGKHFEDKTLKSDLSH
TSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLA
IPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQS
ENNSSLISLDSHSSETTHKESEESQVICLPGTSNSIGTGDS
RRYTDGMLPFSSGTWGTEKEIENLKGIVPDLNSECASKDVL
VKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQ
NKTVLHMDGCLDTETPTVSIQENVDVASLKPISDSGINFTD
AIWSPTCERRTCECHESIEKNKDKTDLPQSVVYQNEEGRWV
TDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDE
EEFNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKS
RSTSDLDKDDASYLRLSLGEFFAQRSEALGCLGGGNNVKR
(in isoform 3). {ECO:0000303|Ref.1}.
/FTId=VSP_055678.
VAR_SEQ 1403 1407 ALLHK -> QGPAT (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_029845.
VAR_SEQ 1408 1941 Missing (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_029846.
VARIANT 457 457 T -> A (in dbSNP:rs10048340).
/FTId=VAR_037514.
VARIANT 513 513 Q -> P (in dbSNP:rs11080623).
/FTId=VAR_050782.
VARIANT 769 769 V -> M (in dbSNP:rs2282542).
{ECO:0000269|PubMed:11230166}.
/FTId=VAR_037515.
VARIANT 948 948 R -> H (in dbSNP:rs7228940).
{ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:15498874}.
/FTId=VAR_050783.
VARIANT 956 956 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 1105 1105 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 1455 1455 S -> N (in dbSNP:rs2027698).
{ECO:0000269|PubMed:12693554}.
/FTId=VAR_050786.
VARIANT 1525 1525 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 1675 1675 K -> E (in dbSNP:rs3737379).
{ECO:0000269|PubMed:12693554}.
/FTId=VAR_050788.
VARIANT 1853 1853 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 1717 1717 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 806 806 R -> L (in Ref. 4; BAB84900).
{ECO:0000305}.
CONFLICT 857 857 P -> A (in Ref. 5; AAL55870).
{ECO:0000305}.
CONFLICT 1519 1519 R -> Q (in Ref. 3 and 7; AAI44482).
{ECO:0000305}.
SEQUENCE 1941 AA; 213146 MW; 0DA715D1FAABA8D4 CRC64;
MKTSDLVPSF GYFIRSPEKR EPIALIRKSD VSRGNLEKEM AHLNHDLYSG DLNEQSQAQL
SEGSITLQVE AVESTSQVDE NDVTLTADKG KTEDTFFMSN KPQRYKDKLP DSGDSMLRIS
TIASAIAEAS VNTDPSQLAA MIKALSNKTR DKTFQEDEKQ KDYSHVRHFL PNDLEKSNGS
NALDMEKYLK KTEVSRYESA LENFSRASMS DTWDLSLPKE QTTQDIHPVD LSATSVSVRA
PEENTAAIVY VENGESENQE SFRTINSSNS VTNRENNSAV VDVKTCSIDN KLQDVGNDEK
ATSISTPSDS YSSVRNPRIT SLCLLKDCEE IRDNRENQRQ NECVSEISNS EKHVTFENHR
IVSPKNSDLK NTSPEHGGRG SEDEQESFRP STSPLSHSSP SEISGTSSSG CALESFGSAA
QQQQPPCEQE LSPLVCSPAG VSRLTYVSEP ESSYPTTATD DALEDRKSDI TSELSTTIIQ
GSPAALEERA MEKLREKVPF QNRGKGTLSS IIQNNSDTRK ATETTSLSSK PEYVKPDFRW
SKDPSSKSGN LLETSEVGWT SNPEELDPIR LALLGKSGLS CQVGSATSHP VSCQEPIDED
QRISPKDKST AGREFSGQVS HQTTSENQCT PIPSSTVHSS VADMQNMPAA VHALLTQPSL
SAAPFAQRYL GTLPSTGSTT LPQCHAGNAT VCGFSGGLPY PAVAGEPVQN SVAVGICLGS
NIGSGWMGTS SLCNPYSNTL NQNLLSTTKP FPVPSVGTNC GIEPWDSGVT SGLGSVRVPE
ELKLPHACCV GIASQTLLSV LNPTDRWLQV SIGVLSISVN GEKVDLSTYR CLVFKNKAII
RPHATEEIKV LFIPSSPGVF RCTFSVASWP CSTDAETIVQ AEALASTVTL TAIAESPVIE
VETEKKDVLD FGDLTYGGWK ALPLKLINRT HATVPIRLII NANAVAWRCF TFSKESVRAP
VEVAPCADVV TRLAGPSVVN HMMPASYDGQ DPEFLMIWVL FHSPKKQISS SDILDSAEEF
SAKVDIEVDS PNPTPVLRSV SLRARAGIAR IHAPRDLQTM HFLAKVASSR KQHLPLKNAG
NIEVYLDIKV PEQGSHFSVD PKNLLLKPGE EHEVIVSFTP KDPEACEERI LKIFVQPFGP
QYEVVLKGEV ISSGSKPLSP GPCLDIPSIL SNKQFLAWGG VPLGRTQLQK LALRNNSAST
TQHLRLLIRG QDQDCFQLQN TFGSEQRLTS NCEIRIHPKE DIFISVLFAP TRLSCMLARL
EIKQLGNRSQ PGIKFTIPLS GYGGTSNLIL EGVKKLSDSY MVTVNGLVPG KESKIVFSVR
NTGSRAAFVK AVGFKDSQKK VLLDPKVLRI FPDKFVLKER TQENVTLIYN PSDRGINNKT
ATELSTVYLF GGDEISRQQY RRALLHKPEM IKQILPEHSV LQNINFVEAF QDELLVTEVY
DLPQRPNDVQ LFYGSMCKII LSVIGEFRDC ISSREFLQPS SKASLESTSD LGASGKHGGN
VSLDVLPVKG PQGSPLLSRA ARPPLDQLAS EEPWTVLPEH LILVAPSPCD MAKTGRFQIV
NNSVRLLRFE LCWPAHCLTV TPQHGCVAPE SKLQILVSPN SSLSTKQSMF PWSGLIYIHC
DDGQKKIVKV QIREDLTQVE LLTRLTSKPF GILSPVSEPS VSHLVKPMTK PPSTKVEIRN
KSITFPTTEP GETSESCLEL ENHGTTDVKW HLSSLAPPYV KGVDESGDVF RATYAAFRCS
PISGLLESHG IQKVSITFLP RGRGDYAQFW DVECHPLKEP HMKHTLRFQL SGQSIEAENE
PENACLSTDS LIKIDHLVKP RRQAVSEASA RIPEQLDVTA RGVYAPEDVY RFRPTSVGES
RTLKVNLRNN SFITHSLKFL SPREPFYVKH SKYSLRAQHY INMPVQFKPK SAGKFEALLV
IQTDEGKSIA IRLIGEALGK N


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