CEP85_MOUSE
ID CEP85_MOUSE Reviewed; 761 AA.
AC Q8BMK0; Q8BUF1; Q8K0E6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Centrosomal protein of 85 kDa;
DE Short=Cep85;
DE AltName: Full=Coiled-coil domain-containing protein 21;
GN Name=Cep85; Synonyms=Ccdc21;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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: Acts as a negative regulator of NEK2 to maintain the
CC centrosome integrity in interphase. Suppresses centrosome disjunction
CC by inhibiting NEK2 kinase activity. {ECO:0000250|UniProtKB:Q6P2H3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q6P2H3}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q6P2H3}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q6P2H3}. Note=Localizes to centrosomes
CC and nucleolus in interphase. Upon entry into mitosis, relocates from
CC nucleolus and accumulates at spindle poles. Associated with the
CC pericentriolar material. Localizes to centrosomes at a low level in G1
CC phase and a slightly increased level in S phase, with gradually
CC elevated levels during G2 phase. The levels at centrosomes further
CC increase at G2/M, reaching a peak at spindle poles at early mitotic
CC stages and remain high until the end of anaphase.
CC {ECO:0000250|UniProtKB:Q6P2H3}.
CC -!- SIMILARITY: Belongs to the CEP85 family. {ECO:0000305}.
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DR EMBL; AK030742; BAC27110.1; -; mRNA.
DR EMBL; AK085545; BAC39468.1; -; mRNA.
DR EMBL; BC031729; AAH31729.1; -; mRNA.
DR CCDS; CCDS18765.1; -.
DR RefSeq; NP_653110.3; NM_144527.3.
DR RefSeq; XP_011248632.1; XM_011250330.2.
DR AlphaFoldDB; Q8BMK0; -.
DR SMR; Q8BMK0; -.
DR BioGRID; 213817; 6.
DR IntAct; Q8BMK0; 5.
DR MINT; Q8BMK0; -.
DR STRING; 10090.ENSMUSP00000039889; -.
DR iPTMnet; Q8BMK0; -.
DR PhosphoSitePlus; Q8BMK0; -.
DR EPD; Q8BMK0; -.
DR jPOST; Q8BMK0; -.
DR MaxQB; Q8BMK0; -.
DR PaxDb; Q8BMK0; -.
DR PRIDE; Q8BMK0; -.
DR ProteomicsDB; 283886; -.
DR Antibodypedia; 16049; 71 antibodies from 15 providers.
DR Ensembl; ENSMUST00000040271; ENSMUSP00000039889; ENSMUSG00000037443.
DR GeneID; 70012; -.
DR KEGG; mmu:70012; -.
DR UCSC; uc008ved.2; mouse.
DR CTD; 64793; -.
DR MGI; MGI:1917262; Cep85.
DR VEuPathDB; HostDB:ENSMUSG00000037443; -.
DR eggNOG; ENOG502QR5U; Eukaryota.
DR GeneTree; ENSGT00620000087993; -.
DR HOGENOM; CLU_020103_0_0_1; -.
DR InParanoid; Q8BMK0; -.
DR OMA; DWKTPML; -.
DR OrthoDB; 489645at2759; -.
DR PhylomeDB; Q8BMK0; -.
DR TreeFam; TF331041; -.
DR BioGRID-ORCS; 70012; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Cep85; mouse.
DR PRO; PR:Q8BMK0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BMK0; protein.
DR Bgee; ENSMUSG00000037443; Expressed in right kidney and 166 other tissues.
DR ExpressionAtlas; Q8BMK0; baseline and differential.
DR Genevisible; Q8BMK0; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; ISS:UniProtKB.
DR InterPro; IPR029777; Cep85.
DR InterPro; IPR040210; Cep85/Cep85L.
DR PANTHER; PTHR31075; PTHR31075; 1.
DR PANTHER; PTHR31075:SF3; PTHR31075:SF3; 1.
PE 1: Evidence at protein level;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..761
FT /note="Centrosomal protein of 85 kDa"
FT /id="PRO_0000233661"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..432
FT /note="Mediates interaction with NEK2 and is required for
FT its function in the suppression of centrosome disjunction"
FT /evidence="ECO:0000250|UniProtKB:Q6P2H3"
FT REGION 433..475
FT /note="Required for centrosome localization and for its
FT function in the suppression of centrosome disjunction"
FT /evidence="ECO:0000250|UniProtKB:Q6P2H3"
FT REGION 435..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..656
FT /evidence="ECO:0000255"
FT COILED 723..749
FT /evidence="ECO:0000255"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2H3"
FT CONFLICT 68
FT /note="E -> G (in Ref. 1; BAC27110)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..302
FT /note="Missing (in Ref. 2; AAH31729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 85340 MW; 43504973E2F620DF CRC64;
MAMQEKYPND RSHATSPGSN VIQKGSSLGT EWQTPVISET FRSRFSRCSS IADSGDTAIG
TSCSDIAEDF CSSSGSPSFQ PIKSHITIPT AHVMPSTLGA SPAKPNSAPS GPSSAKLPLS
GLTEGVGMTR NGDFGAVKRS PGLARDFMYL PSAAGENGSQ QSWFPAVGHE REGEMRKFDV
PSMESTLNQP AMLETLYSDP HYRAHFPNPR PDTNKDVYKV LPESKKAPGS GAVFERNGPH
ASSSGVLPLG LQPAPGLSKS LSSQVWQPSP DPWHPGEQSC ELSTCRQQLE LIRLQMEQMQ
LQNGAMCHHP AAFAPLLPTL EPAQWLSILN SNEHLLKEKE LLIDKQRKHI SQLEQKVRES
ELQVHSALLG RPAPFGDVCL LRLQELQREN TFLRAQFAQK TEALSKEKME LEKKLSASEV
EIQLIRESLK VTLQKHSEEG KKQEERVKGR DKHINNLKKK CQKESEQNRE KQQRIETLER
YLADLPTLED HQKQTEQLKD AELKNTELQE RVAELETLLE DTQATCREKE VQLESLRQRE
ADLSSARHSF QDKQSVEEAN GENLRVDMES QQKECDSLRK MVERQQLKME QLHSQVQSQK
QELAQEEGIN QALREEAQRR ETALQQMRTA VKELSVQNQD LIEKNLTLQE HLRQAQPGSS
SSPDSAQLAC ELHQELASCL QDLQAVCSIV TQRAQGHNPN LSLLLGIHST QHPGTQLDLQ
KPDVIRRKLE EVQQLRHDIE DLRTSLSDRY AQDMGENCAT Q
