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Centromere protein U (CENP-U) (Centromere protein of 50 kDa) (CENP-50) (Interphase centromere complex protein 24) (KSHV latent nuclear antigen-interacting protein 1) (MLF1-interacting protein) (Polo-box-interacting protein 1)

 CENPU_HUMAN             Reviewed;         418 AA.
Q71F23; A2RRD9; Q09GN2; Q32Q71; Q9H5G1;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Centromere protein U;
Short=CENP-U;
AltName: Full=Centromere protein of 50 kDa;
Short=CENP-50;
AltName: Full=Interphase centromere complex protein 24;
AltName: Full=KSHV latent nuclear antigen-interacting protein 1;
AltName: Full=MLF1-interacting protein;
AltName: Full=Polo-box-interacting protein 1;
Name=CENPU; Synonyms=ICEN24, KLIP1, MLF1IP, PBIP1;
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), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH KAPOSI'S
SARCOMA-ASSOCIATED HERPESVIRUS LATENT NUCLEAR ANTIGEN.
PubMed=12941884; DOI=10.1128/JVI.77.18.9758-9768.2003;
Pan H.-Y., Zhang Y.-J., Wang X.-P., Deng J.-H., Zhou F.-C., Gao S.-J.;
"Identification of a novel cellular transcriptional repressor
interacting with the latent nuclear antigen of Kaposi's sarcoma-
associated herpesvirus.";
J. Virol. 77:9758-9768(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH MLF1.
PubMed=15116101; DOI=10.1038/sj.onc.1207448;
Hanissian S.H., Akbar U., Teng B., Janjetovic Z., Hoffmann A.,
Hitzler J.K., Iscove N., Hamre K., Du X., Tong Y., Mukatira S.,
Robertson J.H., Morris S.W.;
"cDNA cloning and characterization of a novel gene encoding the MLF1-
interacting protein MLF1IP.";
Oncogene 23:3700-3707(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Small intestine;
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 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Glioblastoma;
Hanissian S.H.;
"Role of alternatively spliced MLF1IP isoforms in brain tumor
pathogenesis.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Adrenal cortex, and Testis;
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]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15893739; DOI=10.1016/j.brainres.2005.04.017;
Hanissian S.H., Teng B., Akbar U., Janjetovic Z., Zhou Q., Duntsch C.,
Robertson J.H.;
"Regulation of myeloid leukemia factor-1 interacting protein (MLF1IP)
expression in glioblastoma.";
Brain Res. 1047:56-64(2005).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C.,
Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K.;
"Comprehensive analysis of the ICEN (Interphase Centromere Complex)
components enriched in the CENP-A chromatin of human cells.";
Genes Cells 11:673-684(2006).
[11]
IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPN; CENPO;
CENPP; CENPQ AND CENPR.
PubMed=16622420; DOI=10.1038/ncb1396;
Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X.,
Yates J.R. III, Desai A., Fukagawa T.;
"The CENP-H-I complex is required for the efficient incorporation of
newly synthesized CENP-A into centromeres.";
Nat. Cell Biol. 8:446-457(2006).
[12]
IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH;
CENPM; CENPN AND CENPT.
PubMed=16622419; DOI=10.1038/ncb1397;
Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
Cleveland D.W.;
"The human CENP-A centromeric nucleosome-associated complex.";
Nat. Cell Biol. 8:458-469(2006).
[13]
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1,
PHOSPHORYLATION AT THR-78, AND MUTAGENESIS OF SER-77 AND THR-78.
PubMed=17081991; DOI=10.1016/j.molcel.2006.10.016;
Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K.,
Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S.;
"Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1
interaction is critical for proper chromosome segregation.";
Mol. Cell 24:409-422(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-111; SER-136;
SER-139 AND SER-141, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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).
[17]
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).
[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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-98; SER-108; SER-111;
SER-139; SER-141; SER-194 AND SER-232, 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).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated)
complex, a complex that plays a central role in assembly of
kinetochore proteins, mitotic progression and chromosome
segregation. The CENPA-NAC complex recruits the CENPA-CAD
(nucleosome distal) complex and may be involved in incorporation
of newly synthesized CENPA into centromeres. Plays an important
role in the correct PLK1 localization to the mitotic kinetochores.
A scaffold protein responsible for the initial recruitment and
maintenance of the kinetochore PLK1 population until its
degradation. Involved in transcriptional repression.
{ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:16716197,
ECO:0000269|PubMed:17081991}.
-!- SUBUNIT: Component of the CENPA-NAC complex, at least composed of
CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC
complex interacts with the CENPA-CAD complex, composed of CENPI,
CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts with
the N-terminal domain of Kaposi's sarcoma-associated herpesvirus
latent nuclear antigen (LNA). Interacts with MLF1. Interacts with
PLK1. {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:15116101,
ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16622420,
ECO:0000269|PubMed:17081991}.
-!- INTERACTION:
P37198:NUP62; NbExp=3; IntAct=EBI-2515234, EBI-347978;
P53350:PLK1; NbExp=5; IntAct=EBI-15793375, EBI-476768;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-2515234, EBI-1105213;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
kinetochore. Note=Localizes in the kinetochore domain of
centromeres. Colocalizes with PLK1 at the interzone between the
inner and the outer kinetochore plates.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q71F23-1; Sequence=Displayed;
Name=2;
IsoId=Q71F23-2; Sequence=VSP_020030;
Name=3;
IsoId=Q71F23-3; Sequence=VSP_053526, VSP_053527;
-!- TISSUE SPECIFICITY: Expressed at high levels in the testis, fetal
liver, thymus, bone marrow and at lower levels in the lymph nodes,
placenta, colon and spleen. Present in all cell lines examined,
including B-cells, T-cells, epithelial cells and fibroblast cells.
Expressed at high levels in glioblastoma cell lines.
{ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:15116101,
ECO:0000269|PubMed:15893739}.
-!- PTM: Phosphorylated by PLK1 at Thr-78, creating a self-tethering
site that specifically interacts with the polo-box domain of PLK1.
{ECO:0000269|PubMed:17081991}.
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EMBL; AF469667; AAQ05290.1; -; mRNA.
EMBL; AF516710; AAQ08228.1; -; mRNA.
EMBL; AK027121; BAB15665.1; -; mRNA.
EMBL; CR457376; CAG33657.1; -; mRNA.
EMBL; DQ907910; ABI49142.1; -; mRNA.
EMBL; AC079257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04666.1; -; Genomic_DNA.
EMBL; BC107744; AAI07745.1; -; mRNA.
EMBL; BC031520; AAH31520.1; -; mRNA.
EMBL; BC131556; AAI31557.1; -; mRNA.
CCDS; CCDS3838.1; -. [Q71F23-1]
RefSeq; NP_078905.2; NM_024629.3. [Q71F23-1]
UniGene; Hs.575032; -.
ProteinModelPortal; Q71F23; -.
SMR; Q71F23; -.
BioGrid; 122805; 66.
CORUM; Q71F23; -.
DIP; DIP-48539N; -.
IntAct; Q71F23; 43.
MINT; MINT-4992596; -.
STRING; 9606.ENSP00000281453; -.
iPTMnet; Q71F23; -.
PhosphoSitePlus; Q71F23; -.
BioMuta; MLF1IP; -.
DMDM; 74712714; -.
EPD; Q71F23; -.
MaxQB; Q71F23; -.
PaxDb; Q71F23; -.
PeptideAtlas; Q71F23; -.
PRIDE; Q71F23; -.
Ensembl; ENST00000281453; ENSP00000281453; ENSG00000151725. [Q71F23-1]
GeneID; 79682; -.
KEGG; hsa:79682; -.
UCSC; uc003iwq.4; human. [Q71F23-1]
CTD; 79682; -.
DisGeNET; 79682; -.
EuPathDB; HostDB:ENSG00000151725.11; -.
GeneCards; CENPU; -.
HGNC; HGNC:21348; CENPU.
HPA; HPA022048; -.
MIM; 611511; gene.
neXtProt; NX_Q71F23; -.
OpenTargets; ENSG00000151725; -.
PharmGKB; PA134893791; -.
eggNOG; ENOG410J00R; Eukaryota.
eggNOG; ENOG410Z48V; LUCA.
GeneTree; ENSGT00390000015511; -.
HOGENOM; HOG000236255; -.
HOVERGEN; HBG081090; -.
InParanoid; Q71F23; -.
KO; K11513; -.
OMA; KQLHQDY; -.
OrthoDB; EOG091G09Q1; -.
PhylomeDB; Q71F23; -.
TreeFam; TF330780; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SIGNOR; Q71F23; -.
GeneWiki; MLF1IP; -.
GenomeRNAi; 79682; -.
PRO; PR:Q71F23; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000151725; -.
CleanEx; HS_MLF1IP; -.
ExpressionAtlas; Q71F23; baseline and differential.
Genevisible; Q71F23; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0043009; P:chordate embryonic development; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR025214; CENP-U.
Pfam; PF13097; CENP-U; 1.
1: Evidence at protein level;
Alternative splicing; Centromere; Chromosome; Coiled coil;
Complete proteome; Cytoplasm; Host-virus interaction; Isopeptide bond;
Kinetochore; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 418 Centromere protein U.
/FTId=PRO_0000247672.
COILED 297 356 {ECO:0000255}.
COILED 397 417 {ECO:0000255}.
MOTIF 6 23 Nuclear localization signal.
{ECO:0000255}.
MOTIF 303 320 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 78 78 Phosphothreonine; by PLK1.
{ECO:0000269|PubMed:17081991}.
MOD_RES 98 98 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C4M7}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C4M7}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C4M7}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 185 185 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 242 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_020030.
VAR_SEQ 331 337 EPQLKQL -> WTGAGLW (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_053526.
VAR_SEQ 338 418 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_053527.
VARIANT 16 16 G -> R (in dbSNP:rs902174).
/FTId=VAR_048692.
VARIANT 16 16 G -> S (in dbSNP:rs902174).
/FTId=VAR_027144.
VARIANT 157 157 I -> T (in dbSNP:rs6552804).
/FTId=VAR_027145.
VARIANT 214 214 I -> M (in dbSNP:rs4616798).
/FTId=VAR_027146.
VARIANT 279 279 A -> T (in dbSNP:rs34007339).
/FTId=VAR_048693.
MUTAGEN 77 77 S->A: Insensitive to PLK1-induced
degradation.
{ECO:0000269|PubMed:17081991}.
MUTAGEN 78 78 T->A: Insensitive to PLK1-induced
degradation.
{ECO:0000269|PubMed:17081991}.
MUTAGEN 78 78 T->D: Failed to enhance the PLK1-
dependent degradation.
{ECO:0000269|PubMed:17081991}.
MUTAGEN 78 78 T->E: Failed to enhance the PLK1-
dependent degradation.
{ECO:0000269|PubMed:17081991}.
CONFLICT 163 163 E -> G (in Ref. 8; AAI07745).
{ECO:0000305}.
SEQUENCE 418 AA; 47522 MW; A99BC012EF7188F9 CRC64;
MAPRGRRRPR PHRSEGARRS KNTLERTHSM KDKAGQKCKP IDVFDFPDNS DVSSIGRLGE
NEKDEETYET FDPPLHSTAI YADEEEFSKH CGLSLSSTPP GKEAKRSSDT SGNEASEIES
VKISAKKPGR KLRPISDDSE SIEESDTRRK VKSAEKISTQ RHEVIRTTAS SELSEKPAES
VTSKKTGPLS AQPSVEKENL AIESQSKTQK KGKISHDKRK KSRSKAIGSD TSDIVHIWCP
EGMKTSDIKE LNIVLPEFEK THLEHQQRIE SKVCKAAIAT FYVNVKEQFI KMLKESQMLT
NLKRKNAKMI SDIEKKRQRM IEVQDELLRL EPQLKQLQTK YDELKERKSS LRNAAYFLSN
LKQLYQDYSD VQAQEPNVKE TYDSSSLPAL LFKARTLLGA ESHLRNINHQ LEKLLDQG


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