CP135_MOUSE
ID CP135_MOUSE Reviewed; 1140 AA.
AC Q6P5D4; Q6A030;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Centrosomal protein of 135 kDa;
DE Short=Cep135;
DE AltName: Full=Centrosomal protein 4;
GN Name=Cep135; Synonyms=Cep4, Kiaa0635;
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=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-1140.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11781336; DOI=10.1083/jcb.200108088;
RA Ohta T., Essner R., Ryu J.-H., Palazzo R.E., Uetake Y., Kuriyama R.;
RT "Characterization of Cep135, a novel coiled-coil centrosomal protein
RT involved in microtubule organization in mammalian cells.";
RL J. Cell Biol. 156:87-99(2002).
RN [4]
RP INTERACTION WITH DCTN2.
RX PubMed=14983524; DOI=10.1002/cm.10175;
RA Uetake Y., Terada Y., Matuliene J., Kuriyama R.;
RT "Interaction of Cep135 with a p50 dynactin subunit in mammalian
RT centrosomes.";
RL Cell Motil. Cytoskeleton 58:53-66(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1130 AND THR-1134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, and Spleen;
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: Centrosomal protein involved in centriole biogenesis. Acts as
CC a scaffolding protein during early centriole biogenesis. Required for
CC the targeting of centriole satellite proteins to centrosomes such as of
CC PCM1, SSX2IP and CEP290 and recruitment of WRAP73 to centrioles. Also
CC required for centriole-centriole cohesion during interphase by acting
CC as a platform protein for CEP250 at the centriole. Required for the
CC recruitment of CEP295 to the proximal end of new-born centrioles at the
CC centriolar microtubule wall during early S phase in a PLK4-dependent
CC manner (By similarity). {ECO:0000250|UniProtKB:Q66GS9}.
CC -!- SUBUNIT: Interacts with CEP250 (By similarity). Interacts with DCTN2.
CC {ECO:0000250|UniProtKB:Q66GS9, ECO:0000269|PubMed:14983524}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:11781336}.
CC Note=During centriole biogenesis, it is concentrated within the
CC proximal lumen of both parental centrioles and procentrioles.
CC {ECO:0000250|UniProtKB:Q66GS9}.
CC -!- SIMILARITY: Belongs to the CEP135/TSGA10 family. {ECO:0000305}.
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DR EMBL; BC062951; AAH62951.1; -; mRNA.
DR EMBL; AK172988; BAD32266.1; -; mRNA.
DR CCDS; CCDS19365.1; -.
DR RefSeq; NP_950197.1; NM_199032.2.
DR RefSeq; XP_006535086.1; XM_006535023.3.
DR AlphaFoldDB; Q6P5D4; -.
DR SMR; Q6P5D4; -.
DR BioGRID; 238025; 73.
DR IntAct; Q6P5D4; 68.
DR STRING; 10090.ENSMUSP00000112602; -.
DR iPTMnet; Q6P5D4; -.
DR PhosphoSitePlus; Q6P5D4; -.
DR EPD; Q6P5D4; -.
DR jPOST; Q6P5D4; -.
DR MaxQB; Q6P5D4; -.
DR PaxDb; Q6P5D4; -.
DR PRIDE; Q6P5D4; -.
DR ProteomicsDB; 283435; -.
DR Antibodypedia; 23978; 155 antibodies from 23 providers.
DR DNASU; 381644; -.
DR Ensembl; ENSMUST00000049060; ENSMUSP00000038674; ENSMUSG00000036403.
DR Ensembl; ENSMUST00000121979; ENSMUSP00000112602; ENSMUSG00000036403.
DR GeneID; 381644; -.
DR KEGG; mmu:381644; -.
DR UCSC; uc008xvc.1; mouse.
DR CTD; 9662; -.
DR MGI; MGI:2681869; Cep135.
DR VEuPathDB; HostDB:ENSMUSG00000036403; -.
DR eggNOG; ENOG502QT27; Eukaryota.
DR GeneTree; ENSGT00940000159453; -.
DR HOGENOM; CLU_008607_0_0_1; -.
DR InParanoid; Q6P5D4; -.
DR OMA; QGRENTM; -.
DR OrthoDB; 139407at2759; -.
DR PhylomeDB; Q6P5D4; -.
DR TreeFam; TF326518; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 381644; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cep135; mouse.
DR PRO; PR:Q6P5D4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P5D4; protein.
DR Bgee; ENSMUSG00000036403; Expressed in animal zygote and 94 other tissues.
DR Genevisible; Q6P5D4; MM.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0007099; P:centriole replication; ISO:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISS:UniProtKB.
DR InterPro; IPR026732; Cep135.
DR PANTHER; PTHR23159:SF18; PTHR23159:SF18; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disulfide bond; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1140
FT /note="Centrosomal protein of 135 kDa"
FT /id="PRO_0000089492"
FT REGION 1117..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..153
FT /evidence="ECO:0000255"
FT COILED 194..420
FT /evidence="ECO:0000255"
FT COILED 447..647
FT /evidence="ECO:0000255"
FT COILED 674..1117
FT /evidence="ECO:0000255"
FT COMPBIAS 1119..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66GS9"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66GS9"
FT MOD_RES 1121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66GS9"
FT MOD_RES 1130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1134
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 110
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q66GS9"
SQ SEQUENCE 1140 AA; 133345 MW; F04798C298E6C4A9 CRC64;
MTTAAERKYI NIRKRLDQLG YRQTLSVDSL PLVEKLFSDL VHTTESLRQC RLSSGKAEKE
SANLDFVLEP YKLENTRLNK ENNELYLELM KLRECSDKHI KDLKTTLKKC SRETADLKFL
NNQYVHKVKV LEKESKAKDE KIQQLQEKNL RAVVQTPGGR KRNIAFRRQR MQIDEPAPPS
EVSAYPVPQP EDPYIADLLQ VADNRIQELQ EEVQQLQEKL AQMEKGVLDY SKQIELRERE
IQRLSLALDG GCSPDVLSLE TRNKTNEKLI AHLNVQVDFL QQANKELEKH IQELMETKET
VTTEVVNLSN RNEKLCQELT EIDQLAQRLE RHKEQVLETA DKELGEAKKE IKRNLCEMRN
LEEKMSKLQW ELDLSHKEKE RLNSELLLKS DLETVVHQLE QEKQRLSKKL QSFAVTEREL
TLEVERMRLE HGIKRRDKSP SRLDTFLKGI EEERDYYKKE LEKLQHLIQR RSCAINYSAR
EKPPVVKCSE KGDCSTDVHL ITRERDELQR MLERFEKYME DIQSNVKLLT AERDKLNVLY
KEAKEELSTL RKESTNSTSP NHLVSCVEKE KERALSELRR ITAEKEALRE KLKNIQERNA
VGKSDLEKTI EHLTYINHQL ENEKYELQSK MLMMKETVES LENKSKLQAQ KLSHVTGDSS
HQKTEMTSLR IVSEQLQRSL DDCQHRLSIK RGELESAQEQ IKMLEQKLEN LSHRMTVQSE
ETHAMKKTIG VMDKEKDFLQ ETVDEKTEKI ANLQESLLSK EKVIAQLKVT VAEYETSLNQ
LQETLTTRDR EINSLRRQLD ASHKELDDVG KSREISFKEN RRLQDDLATM ARENQEISLE
LEAAVQEKEE MKSRVHKYIT EVSRWESLMA AKEKENKDLL DRFQMLHSRA EDWEVKAQQA
EGENSSVRLE LLSIDTERRH LRERVDLLEK EIQEHINAHH AYESQISSMA KAMSQLEEEL
RRHESEKATM LGDVSSLREL CIKLDSGKDV MTQQLNSKSL ELERAVAELE NVKSESELLK
KQLTNERQTI KNLESLLATN RDKEFQSHLT SHEKDTEIQL LKEKLNLSES KLTTQSRETS
MLRTKVTQLQ TDYDNLKRQM SNEKYERERA IQEMRRLGLP TSPLSSTLKS PVQTPDHINA
