CENPU_HUMAN
ID CENPU_HUMAN Reviewed; 418 AA.
AC Q71F23; A2RRD9; Q09GN2; Q32Q71; Q9H5G1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Centromere protein U;
DE Short=CENP-U;
DE AltName: Full=Centromere protein of 50 kDa;
DE Short=CENP-50;
DE AltName: Full=Interphase centromere complex protein 24;
DE AltName: Full=KSHV latent nuclear antigen-interacting protein 1;
DE AltName: Full=MLF1-interacting protein;
DE AltName: Full=Polo-box-interacting protein 1;
GN Name=CENPU; Synonyms=ICEN24, KLIP1, MLF1IP, PBIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH KAPOSI'S SARCOMA-ASSOCIATED
RP HERPESVIRUS LATENT NUCLEAR ANTIGEN (MICROBIAL INFECTION).
RX PubMed=12941884; DOI=10.1128/jvi.77.18.9758-9768.2003;
RA Pan H.-Y., Zhang Y.-J., Wang X.-P., Deng J.-H., Zhou F.-C., Gao S.-J.;
RT "Identification of a novel cellular transcriptional repressor interacting
RT with the latent nuclear antigen of Kaposi's sarcoma-associated
RT herpesvirus.";
RL J. Virol. 77:9758-9768(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH MLF1.
RX PubMed=15116101; DOI=10.1038/sj.onc.1207448;
RA Hanissian S.H., Akbar U., Teng B., Janjetovic Z., Hoffmann A.,
RA Hitzler J.K., Iscove N., Hamre K., Du X., Tong Y., Mukatira S.,
RA Robertson J.H., Morris S.W.;
RT "cDNA cloning and characterization of a novel gene encoding the MLF1-
RT interacting protein MLF1IP.";
RL Oncogene 23:3700-3707(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Glioblastoma;
RA Hanissian S.H.;
RT "Role of alternatively spliced MLF1IP isoforms in brain tumor
RT pathogenesis.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adrenal cortex, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15893739; DOI=10.1016/j.brainres.2005.04.017;
RA Hanissian S.H., Teng B., Akbar U., Janjetovic Z., Zhou Q., Duntsch C.,
RA Robertson J.H.;
RT "Regulation of myeloid leukemia factor-1 interacting protein (MLF1IP)
RT expression in glioblastoma.";
RL Brain Res. 1047:56-64(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y.,
RA Goshima N., Nomura F., Nomura N., Yoda K.;
RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex)
RT components enriched in the CENP-A chromatin of human cells.";
RL Genes Cells 11:673-684(2006).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPN; CENPO; CENPP;
RP CENPQ AND CENPR.
RX PubMed=16622420; DOI=10.1038/ncb1396;
RA Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III,
RA Desai A., Fukagawa T.;
RT "The CENP-H-I complex is required for the efficient incorporation of newly
RT synthesized CENP-A into centromeres.";
RL Nat. Cell Biol. 8:446-457(2006).
RN [12]
RP IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM;
RP CENPN AND CENPT.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [13]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1,
RP PHOSPHORYLATION AT THR-78, AND MUTAGENESIS OF SER-77 AND THR-78.
RX PubMed=17081991; DOI=10.1016/j.molcel.2006.10.016;
RA Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K.,
RA Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S.;
RT "Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1
RT interaction is critical for proper chromosome segregation.";
RL Mol. Cell 24:409-422(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-111; SER-136;
RP SER-139 AND SER-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-98; SER-108; SER-111;
RP SER-139; SER-141; SER-194 AND SER-232, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation. The CENPA-NAC complex
CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved
CC in incorporation of newly synthesized CENPA into centromeres. Plays an
CC important role in the correct PLK1 localization to the mitotic
CC kinetochores. A scaffold protein responsible for the initial
CC recruitment and maintenance of the kinetochore PLK1 population until
CC its degradation. Involved in transcriptional repression.
CC {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:16716197,
CC ECO:0000269|PubMed:17081991}.
CC -!- SUBUNIT: Component of the CENPA-NAC complex, at least composed of
CC CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC
CC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK,
CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Interacts with MLF1.
CC Interacts with PLK1. {ECO:0000269|PubMed:15116101,
CC ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16622420,
CC ECO:0000269|PubMed:17081991}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the N-terminal domain of
CC Kaposi's sarcoma-associated herpesvirus latent nuclear antigen (LNA).
CC {ECO:0000269|PubMed:12941884}.
CC -!- INTERACTION:
CC Q71F23; P37198: NUP62; NbExp=3; IntAct=EBI-2515234, EBI-347978;
CC Q71F23; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-2515234, EBI-1105213;
CC Q71F23-1; P53350: PLK1; NbExp=5; IntAct=EBI-15793375, EBI-476768;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
CC kinetochore. Note=Localizes in the kinetochore domain of centromeres.
CC Colocalizes with PLK1 at the interzone between the inner and the outer
CC kinetochore plates.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q71F23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71F23-2; Sequence=VSP_020030;
CC Name=3;
CC IsoId=Q71F23-3; Sequence=VSP_053526, VSP_053527;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the testis, fetal
CC liver, thymus, bone marrow and at lower levels in the lymph nodes,
CC placenta, colon and spleen. Present in all cell lines examined,
CC including B-cells, T-cells, epithelial cells and fibroblast cells.
CC Expressed at high levels in glioblastoma cell lines.
CC {ECO:0000269|PubMed:12941884, ECO:0000269|PubMed:15116101,
CC ECO:0000269|PubMed:15893739}.
CC -!- PTM: Phosphorylated by PLK1 at Thr-78, creating a self-tethering site
CC that specifically interacts with the polo-box domain of PLK1.
CC {ECO:0000269|PubMed:17081991}.
CC -!- SIMILARITY: Belongs to the CENP-U/AME1 family. {ECO:0000305}.
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DR EMBL; AF469667; AAQ05290.1; -; mRNA.
DR EMBL; AF516710; AAQ08228.1; -; mRNA.
DR EMBL; AK027121; BAB15665.1; -; mRNA.
DR EMBL; CR457376; CAG33657.1; -; mRNA.
DR EMBL; DQ907910; ABI49142.1; -; mRNA.
DR EMBL; AC079257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04666.1; -; Genomic_DNA.
DR EMBL; BC107744; AAI07745.1; -; mRNA.
DR EMBL; BC031520; AAH31520.1; -; mRNA.
DR EMBL; BC131556; AAI31557.1; -; mRNA.
DR CCDS; CCDS3838.1; -. [Q71F23-1]
DR RefSeq; NP_078905.2; NM_024629.3. [Q71F23-1]
DR AlphaFoldDB; Q71F23; -.
DR SMR; Q71F23; -.
DR BioGRID; 122805; 104.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR CORUM; Q71F23; -.
DR DIP; DIP-48539N; -.
DR IntAct; Q71F23; 61.
DR MINT; Q71F23; -.
DR STRING; 9606.ENSP00000281453; -.
DR iPTMnet; Q71F23; -.
DR PhosphoSitePlus; Q71F23; -.
DR BioMuta; CENPU; -.
DR DMDM; 74712714; -.
DR EPD; Q71F23; -.
DR jPOST; Q71F23; -.
DR MassIVE; Q71F23; -.
DR MaxQB; Q71F23; -.
DR PaxDb; Q71F23; -.
DR PeptideAtlas; Q71F23; -.
DR PRIDE; Q71F23; -.
DR ProteomicsDB; 58731; -.
DR ProteomicsDB; 68598; -. [Q71F23-1]
DR ProteomicsDB; 68599; -. [Q71F23-2]
DR Antibodypedia; 17397; 313 antibodies from 31 providers.
DR DNASU; 79682; -.
DR Ensembl; ENST00000281453.10; ENSP00000281453.5; ENSG00000151725.12. [Q71F23-1]
DR GeneID; 79682; -.
DR KEGG; hsa:79682; -.
DR MANE-Select; ENST00000281453.10; ENSP00000281453.5; NM_024629.4; NP_078905.2.
DR UCSC; uc003iwq.4; human. [Q71F23-1]
DR CTD; 79682; -.
DR DisGeNET; 79682; -.
DR GeneCards; CENPU; -.
DR HGNC; HGNC:21348; CENPU.
DR HPA; ENSG00000151725; Tissue enhanced (bone marrow, testis).
DR MIM; 611511; gene.
DR neXtProt; NX_Q71F23; -.
DR OpenTargets; ENSG00000151725; -.
DR PharmGKB; PA134893791; -.
DR VEuPathDB; HostDB:ENSG00000151725; -.
DR eggNOG; ENOG502S1IM; Eukaryota.
DR GeneTree; ENSGT00390000015511; -.
DR HOGENOM; CLU_057340_1_0_1; -.
DR InParanoid; Q71F23; -.
DR OMA; HQDYSDI; -.
DR OrthoDB; 970617at2759; -.
DR PhylomeDB; Q71F23; -.
DR TreeFam; TF330780; -.
DR PathwayCommons; Q71F23; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q71F23; -.
DR SIGNOR; Q71F23; -.
DR BioGRID-ORCS; 79682; 49 hits in 1075 CRISPR screens.
DR ChiTaRS; CENPU; human.
DR GeneWiki; MLF1IP; -.
DR GenomeRNAi; 79682; -.
DR Pharos; Q71F23; Tbio.
DR PRO; PR:Q71F23; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q71F23; protein.
DR Bgee; ENSG00000151725; Expressed in sperm and 164 other tissues.
DR ExpressionAtlas; Q71F23; baseline and differential.
DR Genevisible; Q71F23; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043009; P:chordate embryonic development; IEA:Ensembl.
DR InterPro; IPR025214; CENP-U.
DR Pfam; PF13097; CENP-U; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Host-virus interaction; Isopeptide bond; Kinetochore; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..418
FT /note="Centromere protein U"
FT /id="PRO_0000247672"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 297..356
FT /evidence="ECO:0000255"
FT COILED 397..417
FT /evidence="ECO:0000255"
FT MOTIF 6..23
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 303..320
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000269|PubMed:17081991"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_020030"
FT VAR_SEQ 331..337
FT /note="EPQLKQL -> WTGAGLW (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_053526"
FT VAR_SEQ 338..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_053527"
FT VARIANT 16
FT /note="G -> R (in dbSNP:rs902174)"
FT /id="VAR_048692"
FT VARIANT 16
FT /note="G -> S (in dbSNP:rs902174)"
FT /id="VAR_027144"
FT VARIANT 157
FT /note="I -> T (in dbSNP:rs6552804)"
FT /id="VAR_027145"
FT VARIANT 214
FT /note="I -> M (in dbSNP:rs4616798)"
FT /id="VAR_027146"
FT VARIANT 279
FT /note="A -> T (in dbSNP:rs34007339)"
FT /id="VAR_048693"
FT MUTAGEN 77
FT /note="S->A: Insensitive to PLK1-induced degradation."
FT /evidence="ECO:0000269|PubMed:17081991"
FT MUTAGEN 78
FT /note="T->A: Insensitive to PLK1-induced degradation."
FT /evidence="ECO:0000269|PubMed:17081991"
FT MUTAGEN 78
FT /note="T->D: Failed to enhance the PLK1-dependent
FT degradation."
FT /evidence="ECO:0000269|PubMed:17081991"
FT MUTAGEN 78
FT /note="T->E: Failed to enhance the PLK1-dependent
FT degradation."
FT /evidence="ECO:0000269|PubMed:17081991"
FT CONFLICT 163
FT /note="E -> G (in Ref. 8; AAI07745)"
FT /evidence="ECO:0000305"
SQ 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
