CCD69_HUMAN
ID CCD69_HUMAN Reviewed; 296 AA.
AC A6NI79; A8K9X6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Coiled-coil domain-containing protein 69 {ECO:0000305};
GN Name=CCDC69 {ECO:0000312|HGNC:HGNC:24487};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-197.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20962590; DOI=10.4161/cc.9.20.13387;
RA Pal D., Wu D., Haruta A., Matsumura F., Wei Q.;
RT "Role of a novel coiled-coil domain-containing protein CCDC69 in regulating
RT central spindle assembly.";
RL Cell Cycle 9:4117-4129(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May act as a scaffold to regulate the recruitment and
CC assembly of spindle midzone components. Required for the localization
CC of AURKB and PLK1 to the spindle midzone.
CC {ECO:0000305|PubMed:20962590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:20962590}. Midbody {ECO:0000269|PubMed:20962590}.
CC Note=During early anaphase, localizes along overlapping interpolar
CC microtubules between the separating chromosomes. During late anaphase,
CC localizes to the center of spindle midzone. Concentrated at the midbody
CC during telophase. {ECO:0000269|PubMed:20962590}.
CC -!- TISSUE SPECIFICITY: Highly expressed in duodenum, esophagus, pancreas,
CC prostate, salivary gland, thymus and urinary bladder.
CC {ECO:0000269|PubMed:20962590}.
CC -!- SIMILARITY: Belongs to the CCDC69 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK292841; BAF85530.1; -; mRNA.
DR EMBL; AC011342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4312.1; -.
DR RefSeq; NP_056436.2; NM_015621.2.
DR AlphaFoldDB; A6NI79; -.
DR SMR; A6NI79; -.
DR BioGRID; 117558; 29.
DR IntAct; A6NI79; 6.
DR MINT; A6NI79; -.
DR STRING; 9606.ENSP00000347586; -.
DR iPTMnet; A6NI79; -.
DR PhosphoSitePlus; A6NI79; -.
DR SwissPalm; A6NI79; -.
DR BioMuta; CCDC69; -.
DR EPD; A6NI79; -.
DR jPOST; A6NI79; -.
DR MassIVE; A6NI79; -.
DR MaxQB; A6NI79; -.
DR PaxDb; A6NI79; -.
DR PeptideAtlas; A6NI79; -.
DR PRIDE; A6NI79; -.
DR ProteomicsDB; 1255; -.
DR TopDownProteomics; A6NI79; -.
DR Antibodypedia; 28179; 145 antibodies from 23 providers.
DR DNASU; 26112; -.
DR Ensembl; ENST00000355417.7; ENSP00000347586.2; ENSG00000198624.13.
DR GeneID; 26112; -.
DR KEGG; hsa:26112; -.
DR MANE-Select; ENST00000355417.7; ENSP00000347586.2; NM_015621.3; NP_056436.2.
DR UCSC; uc003ltq.4; human.
DR CTD; 26112; -.
DR DisGeNET; 26112; -.
DR GeneCards; CCDC69; -.
DR HGNC; HGNC:24487; CCDC69.
DR HPA; ENSG00000198624; Tissue enhanced (skeletal).
DR MIM; 619288; gene.
DR neXtProt; NX_A6NI79; -.
DR OpenTargets; ENSG00000198624; -.
DR PharmGKB; PA128394640; -.
DR VEuPathDB; HostDB:ENSG00000198624; -.
DR eggNOG; ENOG502RYPP; Eukaryota.
DR GeneTree; ENSGT00950000183026; -.
DR HOGENOM; CLU_079661_0_0_1; -.
DR InParanoid; A6NI79; -.
DR OMA; FEWQLRI; -.
DR OrthoDB; 1278490at2759; -.
DR PhylomeDB; A6NI79; -.
DR PathwayCommons; A6NI79; -.
DR SignaLink; A6NI79; -.
DR BioGRID-ORCS; 26112; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; CCDC69; human.
DR GenomeRNAi; 26112; -.
DR Pharos; A6NI79; Tdark.
DR PRO; PR:A6NI79; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; A6NI79; protein.
DR Bgee; ENSG00000198624; Expressed in mucosa of stomach and 186 other tissues.
DR ExpressionAtlas; A6NI79; baseline and differential.
DR Genevisible; A6NI79; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051255; P:spindle midzone assembly; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Lipoprotein; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..296
FT /note="Coiled-coil domain-containing protein 69"
FT /id="PRO_0000328962"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..272
FT /evidence="ECO:0000255"
FT COMPBIAS 13..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TCJ8"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VARIANT 197
FT /note="R -> K (in dbSNP:rs248427)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_042584"
SQ SEQUENCE 296 AA; 34796 MW; 083A804AFAE45C8E CRC64;
MGCRHSRLSS CKPPKKKRQE PEPEQPPRPE PHELGPLNGD TAITVQLCAS EEAERHQKDI
TRILQQHEEE KKKWAQQVEK ERELELRDRL DEQQRVLEGK NEEALQVLRA SYEQEKEALT
HSFREASSTQ QETIDRLTSQ LEAFQAKMKR VEESILSRNY KKHIQDYGSP SQFWEQELES
LHFVIEMKNE RIHELDRRLI LMETVKEKNL ILEEKITTLQ QENEDLHVRS RNQVVLSRQL
SEDLLLTREA LEKEVQLRRQ LQQEKEELLY RVLGANASPA FPLAPVTPTE VSFLAT
