CEP55_RAT
ID CEP55_RAT Reviewed; 462 AA.
AC Q4V7C8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Centrosomal protein of 55 kDa {ECO:0000312|RGD:1305340};
DE Short=Cep55;
GN Name=Cep55 {ECO:0000312|RGD:1305340};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in mitotic exit and cytokinesis. Recruits
CC PDCD6IP and TSG101 to midbody during cytokinesis. Required for
CC successful completion of cytokinesis. Not required for microtubule
CC nucleation. Plays a role in the development of the brain and kidney.
CC {ECO:0000250|UniProtKB:Q53EZ4}.
CC -!- SUBUNIT: Homodimer. Interacts (phosphorylated on Ser-423 and Ser-426)
CC with PLK1. Interacts with AKAP9/CG-NAP; the interaction occurs in
CC interphase and is lost upon mitotic entry. Interacts with PCNT/Kendrin;
CC the interaction occurs in interphase and is lost upon mitotic entry.
CC Directly interacts with PDCD6IP; this interaction is required for
CC PDCD6IP targeting to the midbody; CEP55 binds PDCD6IP in a 2:1
CC stoichiometry; PDCD6IP competes with TSG101 for the same binding site.
CC Interacts with TSG101; TSG101 competes with PDCD6IP for the same
CC binding site; interaction is required for cytokinesis. Interacts with
CC MVB12A, VPS37B, VPS37C and VPS28 (By similarity).
CC {ECO:0000250|UniProtKB:Q53EZ4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q53EZ4}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:Q53EZ4}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q53EZ4}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q53EZ4}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q53EZ4}. Note=Present at the centrosomes at
CC interphase. A small portion is associated preferentially with the
CC mother centriole, whereas the majority localizes to the pericentriolar
CC material. During mitosis, loses affinity for the centrosome at the
CC onset of prophase and diffuses throughout the cell. This dissociation
CC from the centrosome is phosphorylation-dependent. May remain localized
CC at the centrosome during mitosis in certain cell types. Appears at the
CC cleavage furrow in late anaphase and in the midbody in cytokinesis.
CC {ECO:0000250|UniProtKB:Q53EZ4}.
CC -!- PTM: There is a hierachy of phosphorylation, where both Ser-423 and
CC Ser-426 are phosphorylated at the onset of mitosis, prior to Ser-434.
CC Phosphorylation at Ser-423 and Ser-426 is required for dissociation
CC from the centrosome at the G2/M boundary. Phosphorylation at the 3
CC sites, Ser-423, Ser-426 and Ser-434, is required for protein function
CC at the final stages of cell division to complete cytokinesis
CC successfully (By similarity). {ECO:0000250}.
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DR EMBL; BC098013; AAH98013.1; -; mRNA.
DR RefSeq; NP_001020817.1; NM_001025646.1.
DR RefSeq; XP_006231380.1; XM_006231318.3.
DR RefSeq; XP_006231381.1; XM_006231319.2.
DR RefSeq; XP_006231382.1; XM_006231320.2.
DR AlphaFoldDB; Q4V7C8; -.
DR SMR; Q4V7C8; -.
DR STRING; 10116.ENSRNOP00000022133; -.
DR iPTMnet; Q4V7C8; -.
DR PhosphoSitePlus; Q4V7C8; -.
DR PaxDb; Q4V7C8; -.
DR PRIDE; Q4V7C8; -.
DR Ensembl; ENSRNOT00000022133; ENSRNOP00000022133; ENSRNOG00000016377.
DR GeneID; 294074; -.
DR KEGG; rno:294074; -.
DR UCSC; RGD:1305340; rat.
DR CTD; 55165; -.
DR RGD; 1305340; Cep55.
DR eggNOG; ENOG502QTDI; Eukaryota.
DR GeneTree; ENSGT00510000047961; -.
DR HOGENOM; CLU_047132_0_0_1; -.
DR InParanoid; Q4V7C8; -.
DR OMA; QWLIYDQ; -.
DR OrthoDB; 850483at2759; -.
DR PhylomeDB; Q4V7C8; -.
DR TreeFam; TF331107; -.
DR PRO; PR:Q4V7C8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016377; Expressed in thymus and 17 other tissues.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0090543; C:Flemming body; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:1904888; P:cranial skeletal system development; ISS:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0061952; P:midbody abscission; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IEA:InterPro.
DR InterPro; IPR038926; CEP55.
DR InterPro; IPR022008; EABR.
DR PANTHER; PTHR31838; PTHR31838; 1.
DR Pfam; PF12180; EABR; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..462
FT /note="Centrosomal protein of 55 kDa"
FT /id="PRO_0000238666"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..235
FT /note="Interaction with TSG101"
FT /evidence="ECO:0000250"
FT REGION 160..214
FT /note="Interaction with PDCD6IP"
FT /evidence="ECO:0000250"
FT REGION 354..462
FT /note="Required for localization to the interphase
FT centrosome and to the midbody during cytokinesis"
FT /evidence="ECO:0000250"
FT COILED 50..185
FT /evidence="ECO:0000255"
FT COILED 228..400
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BT07"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EZ4"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53EZ4"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53EZ4"
FT MOD_RES 434
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q53EZ4"
SQ SEQUENCE 462 AA; 53995 MW; 81F79EA1C4F49FB9 CRC64;
MSSRSPKDLI KSKWGSRPSS SKSDTALEKF KGEIAAFKTS LDEITNGKGK VANKDRSKLL
EKIQVLEAER EKNVYYLMEK DKEIQRLKDH LRSRYSSSSL LEQLEEKTKE CEKKQQLLES
LSRETDILKK QLSATTKRLS ELESKASTLH LSQSVPANCF NSSMNSIHEK EMQLKDALEK
NQQWLVYDQQ REAYVKGLLA KIFELEKRTE TAAASLPQQM KKTESEGYLQ EEKQKYDHLL
ENAKKDLEVE RQTVTQLRLE LDEFRRKYEE TQKEVEDLNQ LLSSQRKADI QHLEEDKHKT
EKIQKLREES SVFKGKLEEE RKKSEELLSQ VRILYDSLLK HQEEQSRVAL LERQMQACTL
DFENEKLDRQ NMQHQLYVIL KELRKAKSQI TQLESLKQLH GFTFTEQPFP LQGEPENRVK
ATSPKSPTAV LNESLVECPK CSVQYPATEH RDLLVHVEYC MK
