CC28B_MOUSE
ID CC28B_MOUSE Reviewed; 200 AA.
AC Q8CEG5; A2ADZ9; Q8K132;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Coiled-coil domain-containing protein 28B;
GN Name=Ccdc28b;
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=Head;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16327777; DOI=10.1038/nature04370;
RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S.,
RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.;
RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome.";
RL Nature 439:326-330(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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).
RN [6]
RP FUNCTION IN AKT1 PHOSPHORYLATION.
RX PubMed=23727834; DOI=10.1093/hmg/ddt253;
RA Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N.,
RA Beales P.L., Badano J.L.;
RT "The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2
RT function and interacts with SIN1 to control cilia length independently of
RT the mTOR complex.";
RL Hum. Mol. Genet. 22:4031-4042(2013).
CC -!- FUNCTION: Involved in ciliogenesis. Regulates cilia length through its
CC interaction with MAPKAP1/SIN1 but independently of mTORC2 complex.
CC Modulates mTORC2 complex assembly and function, possibly enhances AKT1
CC phosphorylation. Does not seem to modulate assembly and function of
CC mTORC1 complex. {ECO:0000269|PubMed:23727834}.
CC -!- SUBUNIT: Interacts with BBS1, BBS2, BBS4, BBS5, BBS6, BBS7 and
CC TTC8/BBS8. Interacts with MAPKAP1/SIN1 isoform 1 and RICTOR (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Note=It localizes near centrosomes
CC and basal bodies. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina, pericardium and limb
CC epithelium. {ECO:0000269|PubMed:16327777}.
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DR EMBL; AK028262; BAC25848.1; -; mRNA.
DR EMBL; AK158016; BAE34319.1; -; mRNA.
DR EMBL; AL671759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028873; AAH28873.1; -; mRNA.
DR CCDS; CCDS18700.1; -.
DR RefSeq; NP_079731.2; NM_025455.2.
DR AlphaFoldDB; Q8CEG5; -.
DR SMR; Q8CEG5; -.
DR STRING; 10090.ENSMUSP00000030586; -.
DR iPTMnet; Q8CEG5; -.
DR PhosphoSitePlus; Q8CEG5; -.
DR jPOST; Q8CEG5; -.
DR MaxQB; Q8CEG5; -.
DR PaxDb; Q8CEG5; -.
DR PeptideAtlas; Q8CEG5; -.
DR PRIDE; Q8CEG5; -.
DR ProteomicsDB; 265701; -.
DR Antibodypedia; 31247; 88 antibodies from 20 providers.
DR DNASU; 66264; -.
DR Ensembl; ENSMUST00000030586; ENSMUSP00000030586; ENSMUSG00000028795.
DR GeneID; 66264; -.
DR KEGG; mmu:66264; -.
DR UCSC; uc008uxt.1; mouse.
DR CTD; 79140; -.
DR MGI; MGI:1913514; Ccdc28b.
DR VEuPathDB; HostDB:ENSMUSG00000028795; -.
DR eggNOG; ENOG502RYUK; Eukaryota.
DR GeneTree; ENSGT00500000044870; -.
DR HOGENOM; CLU_089059_1_0_1; -.
DR InParanoid; Q8CEG5; -.
DR OMA; RRSPKPC; -.
DR OrthoDB; 1460268at2759; -.
DR TreeFam; TF323549; -.
DR BioGRID-ORCS; 66264; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc28b; mouse.
DR PRO; PR:Q8CEG5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CEG5; protein.
DR Bgee; ENSMUSG00000028795; Expressed in retinal neural layer and 229 other tissues.
DR ExpressionAtlas; Q8CEG5; baseline and differential.
DR Genevisible; Q8CEG5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR InterPro; IPR025271; CCDC28.
DR PANTHER; PTHR13400; PTHR13400; 1.
DR Pfam; PF13270; DUF4061; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..200
FT /note="Coiled-coil domain-containing protein 28B"
FT /id="PRO_0000234095"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..189
FT /evidence="ECO:0000255"
FT COMPBIAS 140..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN5"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUN5"
FT CONFLICT 17
FT /note="P -> Q (in Ref. 1; BAE34319 and 3; AAH28873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22033 MW; 0D05C62109FC290A CRC64;
MEDKKKKRSP KPCLTQPAQA PGTLRRVPVP TSHSGSLALG LPHLPSPKQR AKFKRAGKEK
CRPVLAGGGG GSAGTPLQHS FLTEVTDVYE MEGGLLNLLN DFHSGRLQAF GKECSFEQLE
HVREMQEKLA RLHFSLDVCG EEEDEEEEED GVTEGLPEEQ KKTMADRNLD QLLSNLEDLS
NSIQKLHLAE NAEPEDQPAA
