CCSAP_HUMAN
ID CCSAP_HUMAN Reviewed; 270 AA.
AC Q6IQ19; A8K5X2; Q6P9G2; Q6ZW85; Q8IXU1; Q96BM2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Centriole, cilia and spindle-associated protein;
GN Name=CCSAP; Synonyms=C1orf96, CSAP;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Thalamus;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Duodenum, and Placenta;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP ASSOCIATION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=22493317; DOI=10.1091/mbc.e11-11-0931;
RA Backer C.B., Gutzman J.H., Pearson C.G., Cheeseman I.M.;
RT "CSAP localizes to polyglutamylated microtubules and promotes proper cilia
RT function and zebrafish development.";
RL Mol. Biol. Cell 23:2122-2130(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
RX PubMed=26562023; DOI=10.1371/journal.pone.0142798;
RA Ohta S., Hamada M., Sato N., Toramoto I.;
RT "Polyglutamylated tubulin binding protein C1orf96/CSAP is involved in
RT microtubule stabilization in mitotic spindles.";
RL PLoS ONE 10:E0142798-E0142798(2015).
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
CC (PubMed:26562023). May play a role in embryonic development. May be
CC required for proper cilia beating (By similarity).
CC {ECO:0000250|UniProtKB:Q6P3G4, ECO:0000269|PubMed:26562023}.
CC -!- SUBUNIT: Associates with microtubules; the association occurs on
CC polyglutamylated tubulin (PubMed:22493317, PubMed:26562023).
CC {ECO:0000269|PubMed:22493317, ECO:0000269|PubMed:26562023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:22493317}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:22493317,
CC ECO:0000269|PubMed:26562023}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, cilium
CC axoneme {ECO:0000269|PubMed:22493317}. Cell projection, axon
CC {ECO:0000269|PubMed:22493317}. Cell projection, cilium
CC {ECO:0000269|PubMed:22493317}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:26562023}. Note=Localizes to two to four centrioles
CC throughout the cell cycle. Localizes to mitotic spindle microtubules
CC during prometaphase and throughout the remainder of mitosis. Localizes
CC to cytoskeleton on interphase. Localizes at the ciliary transition zone
CC which connects the basal bodies to ciliary microtubules. Colocalizes
CC with polyglutamylated tubulin. {ECO:0000269|PubMed:22493317,
CC ECO:0000269|PubMed:26562023}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6IQ19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IQ19-2; Sequence=VSP_024582, VSP_024583;
CC Name=3;
CC IsoId=Q6IQ19-3; Sequence=VSP_024585, VSP_024586;
CC Name=4;
CC IsoId=Q6IQ19-4; Sequence=VSP_024584, VSP_024587;
CC -!- SIMILARITY: Belongs to the CCSAP family. {ECO:0000305}.
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DR EMBL; AK123465; BAC85619.1; -; mRNA.
DR EMBL; AK291437; BAF84126.1; -; mRNA.
DR EMBL; AL117350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW69897.1; -; Genomic_DNA.
DR EMBL; BC015419; AAH15419.1; -; mRNA.
DR EMBL; BC039241; AAH39241.1; -; mRNA.
DR EMBL; BC060777; AAH60777.1; -; mRNA.
DR EMBL; BC071609; AAH71609.1; -; mRNA.
DR CCDS; CCDS1577.1; -. [Q6IQ19-1]
DR RefSeq; NP_660300.3; NM_145257.4. [Q6IQ19-1]
DR AlphaFoldDB; Q6IQ19; -.
DR SMR; Q6IQ19; -.
DR BioGRID; 126011; 3.
DR IntAct; Q6IQ19; 3.
DR MINT; Q6IQ19; -.
DR STRING; 9606.ENSP00000284617; -.
DR iPTMnet; Q6IQ19; -.
DR PhosphoSitePlus; Q6IQ19; -.
DR BioMuta; CCSAP; -.
DR DMDM; 145558871; -.
DR EPD; Q6IQ19; -.
DR jPOST; Q6IQ19; -.
DR MassIVE; Q6IQ19; -.
DR MaxQB; Q6IQ19; -.
DR PaxDb; Q6IQ19; -.
DR PeptideAtlas; Q6IQ19; -.
DR PRIDE; Q6IQ19; -.
DR ProteomicsDB; 66472; -. [Q6IQ19-1]
DR ProteomicsDB; 66473; -. [Q6IQ19-2]
DR ProteomicsDB; 66474; -. [Q6IQ19-3]
DR ProteomicsDB; 66475; -. [Q6IQ19-4]
DR Antibodypedia; 34675; 93 antibodies from 16 providers.
DR DNASU; 126731; -.
DR Ensembl; ENST00000284617.7; ENSP00000284617.2; ENSG00000154429.11. [Q6IQ19-1]
DR Ensembl; ENST00000366686.1; ENSP00000355647.1; ENSG00000154429.11. [Q6IQ19-2]
DR Ensembl; ENST00000366687.5; ENSP00000355648.1; ENSG00000154429.11. [Q6IQ19-1]
DR GeneID; 126731; -.
DR KEGG; hsa:126731; -.
DR MANE-Select; ENST00000284617.7; ENSP00000284617.2; NM_145257.5; NP_660300.3.
DR UCSC; uc001htl.4; human. [Q6IQ19-1]
DR CTD; 126731; -.
DR GeneCards; CCSAP; -.
DR HGNC; HGNC:29578; CCSAP.
DR HPA; ENSG00000154429; Tissue enhanced (brain, retina).
DR neXtProt; NX_Q6IQ19; -.
DR OpenTargets; ENSG00000154429; -.
DR PharmGKB; PA142672480; -.
DR VEuPathDB; HostDB:ENSG00000154429; -.
DR eggNOG; ENOG502S0N0; Eukaryota.
DR GeneTree; ENSGT00390000003512; -.
DR HOGENOM; CLU_054214_0_0_1; -.
DR InParanoid; Q6IQ19; -.
DR OMA; WLWDGWE; -.
DR OrthoDB; 1131280at2759; -.
DR PhylomeDB; Q6IQ19; -.
DR TreeFam; TF332378; -.
DR PathwayCommons; Q6IQ19; -.
DR SignaLink; Q6IQ19; -.
DR BioGRID-ORCS; 126731; 16 hits in 1070 CRISPR screens.
DR GenomeRNAi; 126731; -.
DR Pharos; Q6IQ19; Tbio.
DR PRO; PR:Q6IQ19; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6IQ19; protein.
DR Bgee; ENSG00000154429; Expressed in Brodmann (1909) area 46 and 184 other tissues.
DR Genevisible; Q6IQ19; HS.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA: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; IDA: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; IMP:UniProtKB.
DR InterPro; IPR029774; CSAP.
DR PANTHER; PTHR31022; PTHR31022; 1.
DR Pfam; PF15748; CCSAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell projection; Cilium; Cytoplasm; Cytoskeleton; Developmental protein;
KW Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..270
FT /note="Centriole, cilia and spindle-associated protein"
FT /id="PRO_0000284643"
FT REGION 50..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..255
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 260..266
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 74..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024582"
FT VAR_SEQ 115..122
FT /note="DAEDAALP -> MVPVFTSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024583"
FT VAR_SEQ 123..140
FT /note="ALPVKDVEDKPEQQTRTR -> GTRPGGEREGPARRDGLL (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024584"
FT VAR_SEQ 123..129
FT /note="ALPVKDV -> GNAWLRT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024585"
FT VAR_SEQ 130..270
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024586"
FT VAR_SEQ 141..270
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024587"
FT VARIANT 123
FT /note="A -> V (in dbSNP:rs6587326)"
FT /id="VAR_059594"
FT CONFLICT 28
FT /note="R -> G (in Ref. 4; AAH71609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 30216 MW; DA40F8593A5354EC CRC64;
MSPGSGVKSE YMKRYQEPRW EEYGPCYREL LHYRLGRRLL EQAHAPWLWD DWGPAGSSED
SASSESSGAG GPAPRCAPPS PPPPVEPATQ EEAERRARGA PEEQDAEAGD AEAEDAEDAA
LPALPVKDVE DKPEQQTRTR ETDKSPTSTE PRQQPSALFA RGNRKAVKSP QRSSSKIKEN
KHPFALYGWG EKQTDTGSQK THNVCASAPV HEIHESALRA KNRRQVEKRK LVAQRQRAHS
VDVEKNRKMK ASSSENPWMT EYMRCYSARA
