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 24-JAN-2024, entry version 151. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7PB8; X-ray; 3.68 A; U=1-418. DR PDB; 7PKN; EM; 3.20 A; U=1-418. DR PDB; 7QOO; EM; 4.60 A; U=1-418. DR PDB; 7R5S; EM; 2.83 A; U=1-418. DR PDB; 7R5V; EM; 4.55 A; U=1-418. DR PDB; 7XHN; EM; 3.71 A; U=1-418. DR PDB; 7XHO; EM; 3.29 A; U=1-418. DR PDB; 7YWX; EM; 12.00 A; U=1-418. DR PDB; 7YYH; EM; 8.90 A; U=1-418. DR PDBsum; 7PB8; -. DR PDBsum; 7PKN; -. DR PDBsum; 7QOO; -. DR PDBsum; 7R5S; -. DR PDBsum; 7R5V; -. DR PDBsum; 7XHN; -. DR PDBsum; 7XHO; -. DR PDBsum; 7YWX; -. DR PDBsum; 7YYH; -. DR AlphaFoldDB; Q71F23; -. DR EMDB; EMD-13473; -. DR EMDB; EMD-14098; -. DR EMDB; EMD-14336; -. DR EMDB; EMD-14341; -. DR EMDB; EMD-14351; -. DR EMDB; EMD-14375; -. DR EMDB; EMD-33196; -. DR EMDB; EMD-33197; -. DR SMR; Q71F23; -. DR BioGRID; 122805; 107. 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 GlyGen; Q71F23; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000281453; -. DR PeptideAtlas; Q71F23; -. DR ProteomicsDB; 58731; -. DR ProteomicsDB; 68598; -. [Q71F23-1] DR ProteomicsDB; 68599; -. [Q71F23-2] DR Pumba; Q71F23; -. DR Antibodypedia; 17397; 350 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 AGR; HGNC:21348; -. 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; NTVGRTH; -. DR OrthoDB; 5323626at2759; -. 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; 57 hits in 1156 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 166 other cell types or tissues. DR ExpressionAtlas; Q71F23; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000939; C:inner kinetochore; IPI:ComplexPortal. 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 GO; GO:0007059; P:chromosome segregation; NAS:ComplexPortal. DR InterPro; IPR025214; CENP-U. DR PANTHER; PTHR32222; CENTROMERE PROTEIN U; 1. DR PANTHER; PTHR32222:SF1; CENTROMERE PROTEIN U; 1. DR Pfam; PF13097; CENP-U; 1. DR Genevisible; Q71F23; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Centromere; Chromosome; Coiled coil; KW Cytoplasm; 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" FT HELIX 254..266 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 272..368 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 371..374 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 387..398 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 400..414 FT /evidence="ECO:0007829|PDB:7R5S" 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 //