CCSAP_MOUSE
ID CCSAP_MOUSE Reviewed; 252 AA.
AC Q8QZT2; Q8C3E1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Centriole, cilia and spindle-associated protein;
GN Name=Ccsap;
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 MRNA].
RC TISSUE=Eye, and Mammary tumor;
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-65 AND SER-191, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Plays a role in microtubule (MT) stabilization and this
CC stabilization involves the maintenance of NUMA1 at the spindle poles.
CC Colocalizes with polyglutamylated MTs to promote MT stabilization and
CC regulate bipolar spindle formation in mitosis. Binding of CCSAP to
CC centrosomes and the spindle around centrosomes during mitosis inhibits
CC MT depolymerization, thereby stabilizing the mitotic spindle. May play
CC a role in embryonic development. May be required for proper cilia
CC beating (By similarity). {ECO:0000250|UniProtKB:Q6IQ19,
CC ECO:0000250|UniProtKB:Q6P3G4}.
CC -!- SUBUNIT: Associates with microtubules; the association occurs on
CC polyglutamylated tubulin. {ECO:0000250|UniProtKB:Q6IQ19}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q6IQ19}.
CC Cell projection, axon {ECO:0000250|UniProtKB:Q6IQ19}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:Q6IQ19}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q6IQ19}. Note=Localizes to two to four
CC centrioles throughout the cell cycle. Localizes to mitotic spindle
CC microtubules during prometaphase and throughout the remainder of
CC mitosis. Localizes to cytoskeleton on interphase. Localizes at the
CC ciliary transition zone which connects the basal bodies to ciliary
CC microtubules. Colocalizes with polyglutamylated tubulin (By
CC similarity). {ECO:0000250|UniProtKB:Q6IQ19}.
CC -!- SIMILARITY: Belongs to the CCSAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39624.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK086180; BAC39624.1; ALT_FRAME; mRNA.
DR EMBL; BC024705; AAH24705.1; -; mRNA.
DR EMBL; BC036300; AAH36300.1; -; mRNA.
DR CCDS; CCDS22763.1; -.
DR RefSeq; NP_082812.1; NM_028536.1.
DR AlphaFoldDB; Q8QZT2; -.
DR SMR; Q8QZT2; -.
DR BioGRID; 216002; 3.
DR STRING; 10090.ENSMUSP00000113319; -.
DR iPTMnet; Q8QZT2; -.
DR PhosphoSitePlus; Q8QZT2; -.
DR EPD; Q8QZT2; -.
DR jPOST; Q8QZT2; -.
DR MaxQB; Q8QZT2; -.
DR PaxDb; Q8QZT2; -.
DR PeptideAtlas; Q8QZT2; -.
DR PRIDE; Q8QZT2; -.
DR ProteomicsDB; 279952; -.
DR Antibodypedia; 34675; 93 antibodies from 16 providers.
DR Ensembl; ENSMUST00000034452; ENSMUSP00000034452; ENSMUSG00000031971.
DR Ensembl; ENSMUST00000122421; ENSMUSP00000113319; ENSMUSG00000031971.
DR GeneID; 73420; -.
DR KEGG; mmu:73420; -.
DR UCSC; uc009nwp.1; mouse.
DR CTD; 126731; -.
DR MGI; MGI:1920670; Ccsap.
DR VEuPathDB; HostDB:ENSMUSG00000031971; -.
DR eggNOG; ENOG502S0N0; Eukaryota.
DR GeneTree; ENSGT00390000003512; -.
DR HOGENOM; CLU_054214_0_0_1; -.
DR InParanoid; Q8QZT2; -.
DR OMA; WLWDGWE; -.
DR OrthoDB; 1131280at2759; -.
DR PhylomeDB; Q8QZT2; -.
DR TreeFam; TF332378; -.
DR BioGRID-ORCS; 73420; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ccsap; mouse.
DR PRO; PR:Q8QZT2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8QZT2; protein.
DR Bgee; ENSMUSG00000031971; Expressed in superior frontal gyrus and 101 other tissues.
DR Genevisible; Q8QZT2; MM.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990755; P:mitotic spindle microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR InterPro; IPR029774; CSAP.
DR PANTHER; PTHR31022; PTHR31022; 1.
DR Pfam; PF15748; CCSAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Developmental protein; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..252
FT /note="Centriole, cilia and spindle-associated protein"
FT /id="PRO_0000284644"
FT REGION 49..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..15
FT /note="ST]-E-Y-X(3)-Y motif 1; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 242..248
FT /note="ST]-E-Y-X(3)-Y motif 2; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT COMPBIAS 83..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ19"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 129
FT /note="S -> I (in Ref. 1; BAC39624)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Q -> K (in Ref. 1; BAC39624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 28379 MW; 0392B8050ECFBE6C CRC64;
MSPGSGVKSE YMKRYREPRW DEYAPCYREL LRYRLGRRLL EQAHAPWLWD AWGPDSPSDS
SASPSPAPRG ALGEPSAPSA REEEQPVGER GAELRDAEEQ DTVLPAPPKK DTEEKPEEHK
TKETDGAPSG PGPRQQPSAL CARGSKKATR SPQRSTSKIK ENKHPFALYG WGERQMDMGS
QKTHNVCASA SVHEIHESAL RAKNRRQVEK RKLAAQRQRA HSVDVEKNQR VKPASAENPW
LTEYMRCYSA RA
