CENPU_RAT
ID CENPU_RAT Reviewed; 410 AA.
AC Q4V8G7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Centromere protein U;
DE Short=CENP-U;
DE AltName: Full=MLF1-interacting protein;
GN Name=Cenpu; Synonyms=Mlf1ip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [2]
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).
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:0000269|PubMed:15893739}. Nucleus
CC {ECO:0000269|PubMed:15893739}. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Note=Localizes in the kinetochore domain of centromeres.
CC Colocalizes with PLK1 at the interzone between the inner and the outer
CC kinetochore plates (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in glioblastoma cell
CC lines. Up-regulated in GBM (glioblastoma multiforme) tumors.
CC Significantly increased in both the tumor core as well as the
CC contralateral striatum and cortex in gliomas.
CC {ECO:0000269|PubMed:15893739}.
CC -!- PTM: Phosphorylated by PLK1 at Thr-73, 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; BC097399; AAH97399.1; -; mRNA.
DR RefSeq; NP_001020844.1; NM_001025673.1.
DR AlphaFoldDB; Q4V8G7; -.
DR SMR; Q4V8G7; -.
DR STRING; 10116.ENSRNOP00000046417; -.
DR iPTMnet; Q4V8G7; -.
DR PhosphoSitePlus; Q4V8G7; -.
DR PaxDb; Q4V8G7; -.
DR PRIDE; Q4V8G7; -.
DR Ensembl; ENSRNOT00000041596; ENSRNOP00000046417; ENSRNOG00000022261.
DR GeneID; 306464; -.
DR KEGG; rno:306464; -.
DR CTD; 79682; -.
DR RGD; 1562566; Cenpu.
DR eggNOG; ENOG502S1IM; Eukaryota.
DR GeneTree; ENSGT00390000015511; -.
DR HOGENOM; CLU_057340_1_0_1; -.
DR InParanoid; Q4V8G7; -.
DR OMA; HQDYSDI; -.
DR OrthoDB; 970617at2759; -.
DR PhylomeDB; Q4V8G7; -.
DR TreeFam; TF330780; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q4V8G7; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000022261; Expressed in testis and 17 other tissues.
DR Genevisible; Q4V8G7; RN.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043009; P:chordate embryonic development; ISO:RGD.
DR InterPro; IPR025214; CENP-U.
DR Pfam; PF13097; CENP-U; 1.
PE 2: Evidence at transcript level;
KW Centromere; Chromosome; Coiled coil; Cytoplasm; Isopeptide bond;
KW Kinetochore; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..410
FT /note="Centromere protein U"
FT /id="PRO_0000247674"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..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 87..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
SQ SEQUENCE 410 AA; 46801 MW; 0B6EB7DE22C2100A CRC64;
MAARRSLRYS GDPGAKRSRN TLGSTNSRKQ KAGQKPKRKD VFDFPNTSDV SSMLRELEEE
EPYETFDPPL HSTAIYTDDE LYKHCVSSTS PATHRGKESR NLNPSENEAS GNDSIKLSAK
KPRRKLEPIS DESDSSEDNV RRSVSIERPR ARKPPAAPAA ASSSSSPSER PAEQVTPRKT
SFPQPSAVEE TPAAQSQLKT QKKVRPSPGR RKRPRRGSTH SDASESMHIL CLEGKRQSDV
MELDVVLSAF ERTFLDYKQR VESESCNQAI SKFYFKIKGE LIRMLKEVQM LKALKRKNTK
IISNMEKKRQ RLIDVQDELI RLEPQLKQLQ TKYDDLKKRK SALKNSKHFL SNLKQLYQDY
SNVREEEPKE KEKYDSSSLP ALLFKARSIL GAEKHLKTIN YHLGKLLKQD
