CENPU_BOVIN
ID CENPU_BOVIN Reviewed; 408 AA.
AC Q2KIW5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Centromere protein U;
DE Short=CENP-U;
DE AltName: Full=MLF1-interacting protein;
DE Flags: Fragment;
GN Name=CENPU; Synonyms=MLF1IP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Phosphorylated by PLK1 at Thr-72, 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; BC112483; AAI12484.1; -; mRNA.
DR AlphaFoldDB; Q2KIW5; -.
DR SMR; Q2KIW5; -.
DR STRING; 9913.ENSBTAP00000025113; -.
DR PRIDE; Q2KIW5; -.
DR eggNOG; ENOG502S1IM; Eukaryota.
DR InParanoid; Q2KIW5; -.
DR OrthoDB; 970617at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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..408
FT /note="Centromere protein U"
FT /id="PRO_0000247671"
FT REGION 1..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 273..350
FT /evidence="ECO:0000255"
FT MOTIF 293..310
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 19..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 104
FT /note="Phosphothreonine"
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 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4M7"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q71F23"
FT NON_TER 1
SQ SEQUENCE 408 AA; 46674 MW; 0C4EC86A75C44D58 CRC64;
DRPRPARLSH ARFSKNHSGR THSMKDKAGR KHRPLDVFDF PDHSQLSSFS RLGENEKDEE
SYETFDPPLH STAIYADEEE FSKQCGSHLP STPQEKEAKR SSDTSEIEAS ENESVKISAK
KPRRKLKPIS DESESPEESD VRRKVKPTEN ISTQHEAVSA TALPGLSEKP AEAVTPQKTG
PQSAESSAEK ATLATEHQLE TQKNKMLPGK RKKPRSYTTD TSDCAPVWCL KEKKASEIME
LDVFLSAFEN ILLEYEQKID SRVCKAAINK FHSNLKEELI KMVQEIQMLK TLKRKNAKII
SNIEKKRQRL IEVQDELLQV EPELKQLQIK YEELQERKAS LRKAAYFLSN LKQLHQDYSD
VQEEEPSVKE TYDSSSLPAL LFKARPLLGA EHHLQNINYQ LENLLDQK
