CENPU_MOUSE
ID CENPU_MOUSE Reviewed; 410 AA.
AC Q8C4M7; Q6UNA2; Q9D9U1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Centromere protein U;
DE Short=CENP-U;
DE AltName: Full=MLF1-interacting protein;
GN Name=Cenpu; Synonyms=Mlf1ip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, Liver, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-111; SER-115;
RP SER-182; SER-186 AND THR-191, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes in
CC the kinetochore domain of centromeres. Colocalizes with PLK1 at the
CC interzone between the inner and the outer kinetochore plates (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q8C4M7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C4M7-2; Sequence=VSP_020031, VSP_020032;
CC -!- TISSUE SPECIFICITY: Testis, spleen, heart, kidney, liver, lung, brain
CC and CFU-E erythroid precursor cells. {ECO:0000269|PubMed:15116101}.
CC -!- DEVELOPMENTAL STAGE: Expressed at different stages of development
CC between 7 dpc and 17 dpc, and highest expression seen at 11 dpc.
CC Detected in the liver at 13.5 dpc and strongly expressed in the
CC cephalic mesenchyme and roof of the hindbrain, lining of the
CC pericardial cavity and atrial chamber of the heart and lumen of the
CC stomach in 11.5-day embryos. {ECO:0000269|PubMed:15116101}.
CC -!- PTM: Phosphorylated by PLK1 at Thr-74, creating a self-tethering site
CC that specifically interacts with the polo-box domain of PLK1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CENP-U/AME1 family. {ECO:0000305}.
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DR EMBL; AY366362; AAR13082.1; -; mRNA.
DR EMBL; AK006479; BAB24609.1; -; mRNA.
DR EMBL; AK050386; BAC34227.1; -; mRNA.
DR EMBL; AK081703; BAC38300.1; -; mRNA.
DR CCDS; CCDS22292.1; -. [Q8C4M7-1]
DR RefSeq; NP_082249.1; NM_027973.3. [Q8C4M7-1]
DR AlphaFoldDB; Q8C4M7; -.
DR SMR; Q8C4M7; -.
DR BioGRID; 214999; 11.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR CORUM; Q8C4M7; -.
DR STRING; 10090.ENSMUSP00000034045; -.
DR iPTMnet; Q8C4M7; -.
DR PhosphoSitePlus; Q8C4M7; -.
DR EPD; Q8C4M7; -.
DR jPOST; Q8C4M7; -.
DR MaxQB; Q8C4M7; -.
DR PaxDb; Q8C4M7; -.
DR PeptideAtlas; Q8C4M7; -.
DR PRIDE; Q8C4M7; -.
DR ProteomicsDB; 281192; -. [Q8C4M7-1]
DR ProteomicsDB; 281193; -. [Q8C4M7-2]
DR Antibodypedia; 17397; 313 antibodies from 31 providers.
DR DNASU; 71876; -.
DR Ensembl; ENSMUST00000034045; ENSMUSP00000034045; ENSMUSG00000031629. [Q8C4M7-1]
DR Ensembl; ENSMUST00000093518; ENSMUSP00000091239; ENSMUSG00000031629. [Q8C4M7-2]
DR GeneID; 71876; -.
DR KEGG; mmu:71876; -.
DR UCSC; uc009lqg.1; mouse. [Q8C4M7-1]
DR UCSC; uc009lqh.1; mouse. [Q8C4M7-2]
DR CTD; 79682; -.
DR MGI; MGI:1919126; Cenpu.
DR VEuPathDB; HostDB:ENSMUSG00000031629; -.
DR eggNOG; ENOG502S1IM; Eukaryota.
DR GeneTree; ENSGT00390000015511; -.
DR HOGENOM; CLU_057340_1_0_1; -.
DR InParanoid; Q8C4M7; -.
DR OMA; HQDYSDI; -.
DR OrthoDB; 970617at2759; -.
DR PhylomeDB; Q8C4M7; -.
DR TreeFam; TF330780; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 71876; 18 hits in 75 CRISPR screens.
DR PRO; PR:Q8C4M7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8C4M7; protein.
DR Bgee; ENSMUSG00000031629; Expressed in spermatocyte and 165 other tissues.
DR ExpressionAtlas; Q8C4M7; baseline and differential.
DR Genevisible; Q8C4M7; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025214; CENP-U.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13097; CENP-U; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Kinetochore; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..410
FT /note="Centromere protein U"
FT /id="PRO_0000247673"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..352
FT /evidence="ECO:0000255"
FT MOTIF 4..21
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 295..312
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT VAR_SEQ 15..48
FT /note="AKHSKNTLRSTYSRKQKAGPKPRPKDVFDFSNNS -> PPSAQYGYLRRRRA
FT VQTLCVLQFPGHPQREGEQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15116101"
FT /id="VSP_020031"
FT VAR_SEQ 49..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15116101"
FT /id="VSP_020032"
FT CONFLICT 327
FT /note="K -> E (in Ref. 1; BAC38300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46370 MW; F2E8677FB373F75D CRC64;
MAARRSLRYS GNPGAKHSKN TLRSTYSRKQ KAGPKPRPKD VFDFSNNSDA SSIPGALEEE
EETYETFDPP LHSTAIYAED ELSKHCVSSS SLATHRGKAS RNLDPSEDEA SGNESIKVST
KKPRRKLEPI SGESDSSADD VRRRVASAEG PRSQQRQAAP AAPSPPERPA EPVTPRRTRL
HSAQLSPVDE TPATQSQLKT QKKVRPSPGR RKRPRRGHTD TDGSESMHIW CLEGKRQSDI
TELDVILSVF EKTFLEYKQR VESESCNQAI NKFYFKMKGE LIRMLKEAQM LKALKMKNTK
IIANMEKKRQ RLIEVQDELI RLEPQLKQLQ TKYDDLKERK SSLKKSKHFL SNLKQLCQDY
SNVQEKGPKG TGKYDSSSLP ALLFKARSIL GAENHLRTIN YQLGKLLELD
