CEP44_HUMAN
ID CEP44_HUMAN Reviewed; 390 AA.
AC Q9C0F1; A8K8W9; A8MW11; B3KT53; D3DP42; Q8IXZ4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Centrosomal protein of 44 kDa;
DE Short=Cep44;
DE AltName: Full=HBV PreS1-transactivated protein 3;
DE Short=PS1TP3;
GN Name=CEP44; Synonyms=KIAA1712;
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 [MRNA] (ISOFORM 1).
RA Ji D., Cheng J., Dong J., Wang J., Liu Y., Yang Q., Dang X.;
RT "Screening and cloning of the target genes transactivated by hepatitis B
RT virus PreS1 protein using suppression subtractive hybridization
RT technique.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-147.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-147.
RC TISSUE=Hippocampus, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-346, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21399614; DOI=10.1038/emboj.2011.63;
RA Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
RA Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
RA Hyman A.A., Andersen J.S.;
RT "Novel asymmetrically localizing components of human centrosomes identified
RT by complementary proteomics methods.";
RL EMBO J. 30:1520-1535(2011).
RN [9]
RP IDENTIFICATION BY MASS 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-345, AND
RP IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY 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).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CROCC, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=31974111; DOI=10.1242/jcs.239616;
RA Hossain D., Shih S.Y., Xiao X., White J., Tsang W.Y.;
RT "Cep44 functions in centrosome cohesion by stabilizing rootletin.";
RL J. Cell Sci. 133:0-0(2020).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POC1B, AND MUTAGENESIS OF
RP 68-LYS--LYS-88.
RX PubMed=32060285; DOI=10.1038/s41467-020-14767-2;
RA Atorino E.S., Hata S., Funaya C., Neuner A., Schiebel E.;
RT "CEP44 ensures the formation of bona fide centriole wall, a requirement for
RT the centriole-to-centrosome conversion.";
RL Nat. Commun. 11:903-903(2020).
CC -!- FUNCTION: Centriole-enriched microtubule-binding protein involved in
CC centriole biogenesis. In collaboration with CEP295 and POC1B, is
CC required for the centriole-to-centrosome conversion by ensuring the
CC formation of bona fide centriole wall (PubMed:32060285). Functions as a
CC linker component that maintains centrosome cohesion. Associates with
CC CROCC and regulates its stability and localization to the centrosome
CC (PubMed:31974111). {ECO:0000269|PubMed:31974111,
CC ECO:0000269|PubMed:32060285}.
CC -!- SUBUNIT: Interacts with CROCC (PubMed:31974111). Interacts with POC1B;
CC the interaction is direct and recruits POC1B to centriolar microtubules
CC (PubMed:32060285). Binds to centriolar microtubules (PubMed:32060285).
CC {ECO:0000269|PubMed:31974111, ECO:0000269|PubMed:32060285}.
CC -!- INTERACTION:
CC Q9C0F1; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-744115, EBI-11096309;
CC Q9C0F1; Q9P2A4: ABI3; NbExp=9; IntAct=EBI-744115, EBI-742038;
CC Q9C0F1; P29972: AQP1; NbExp=3; IntAct=EBI-744115, EBI-745213;
CC Q9C0F1; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-744115, EBI-10181188;
CC Q9C0F1; Q13515: BFSP2; NbExp=3; IntAct=EBI-744115, EBI-10229433;
CC Q9C0F1; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-744115, EBI-465781;
CC Q9C0F1; Q13895: BYSL; NbExp=5; IntAct=EBI-744115, EBI-358049;
CC Q9C0F1; Q9Y376: CAB39; NbExp=3; IntAct=EBI-744115, EBI-306905;
CC Q9C0F1; Q8NA61: CBY2; NbExp=4; IntAct=EBI-744115, EBI-741724;
CC Q9C0F1; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-744115, EBI-10749669;
CC Q9C0F1; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-744115, EBI-10247802;
CC Q9C0F1; Q8N715: CCDC185; NbExp=5; IntAct=EBI-744115, EBI-740814;
CC Q9C0F1; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-744115, EBI-396137;
CC Q9C0F1; Q6IPU0: CENPP; NbExp=5; IntAct=EBI-744115, EBI-10250303;
CC Q9C0F1; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-744115, EBI-10181988;
CC Q9C0F1; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-744115, EBI-741528;
CC Q9C0F1; Q13561: DCTN2; NbExp=4; IntAct=EBI-744115, EBI-715074;
CC Q9C0F1; Q6P158: DHX57; NbExp=3; IntAct=EBI-744115, EBI-1051531;
CC Q9C0F1; Q14689: DIP2A; NbExp=3; IntAct=EBI-744115, EBI-2564275;
CC Q9C0F1; O75616: ERAL1; NbExp=3; IntAct=EBI-744115, EBI-6393536;
CC Q9C0F1; Q3B820: FAM161A; NbExp=3; IntAct=EBI-744115, EBI-719941;
CC Q9C0F1; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-744115, EBI-10247271;
CC Q9C0F1; P51116: FXR2; NbExp=3; IntAct=EBI-744115, EBI-740459;
CC Q9C0F1; P61952: GNG11; NbExp=3; IntAct=EBI-744115, EBI-720198;
CC Q9C0F1; Q53Y01: GNG11; NbExp=3; IntAct=EBI-744115, EBI-10243023;
CC Q9C0F1; O75409: H2AP; NbExp=6; IntAct=EBI-744115, EBI-6447217;
CC Q9C0F1; Q96CS2: HAUS1; NbExp=4; IntAct=EBI-744115, EBI-2514791;
CC Q9C0F1; Q8WYH8: ING5; NbExp=3; IntAct=EBI-744115, EBI-488533;
CC Q9C0F1; Q6ICG6-3: KIAA0930; NbExp=3; IntAct=EBI-744115, EBI-12401561;
CC Q9C0F1; P25800: LMO1; NbExp=3; IntAct=EBI-744115, EBI-8639312;
CC Q9C0F1; Q32MZ4-4: LRRFIP1; NbExp=3; IntAct=EBI-744115, EBI-10240044;
CC Q9C0F1; P45984: MAPK9; NbExp=9; IntAct=EBI-744115, EBI-713568;
CC Q9C0F1; Q96EZ8: MCRS1; NbExp=6; IntAct=EBI-744115, EBI-348259;
CC Q9C0F1; Q8NEQ2: MGC24125; NbExp=3; IntAct=EBI-744115, EBI-10270788;
CC Q9C0F1; Q6P2C6: MLLT6; NbExp=3; IntAct=EBI-744115, EBI-5773143;
CC Q9C0F1; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-744115, EBI-748896;
CC Q9C0F1; P41227: NAA10; NbExp=3; IntAct=EBI-744115, EBI-747693;
CC Q9C0F1; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-744115, EBI-742388;
CC Q9C0F1; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-744115, EBI-5452779;
CC Q9C0F1; Q969H6: POP5; NbExp=6; IntAct=EBI-744115, EBI-366525;
CC Q9C0F1; O43242: PSMD3; NbExp=3; IntAct=EBI-744115, EBI-357622;
CC Q9C0F1; Q96T37: RBM15; NbExp=3; IntAct=EBI-744115, EBI-2514922;
CC Q9C0F1; O76064: RNF8; NbExp=4; IntAct=EBI-744115, EBI-373337;
CC Q9C0F1; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-744115, EBI-748391;
CC Q9C0F1; Q15560: TCEA2; NbExp=3; IntAct=EBI-744115, EBI-710310;
CC Q9C0F1; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-744115, EBI-725997;
CC Q9C0F1; Q9BZW7: TSGA10; NbExp=6; IntAct=EBI-744115, EBI-744794;
CC Q9C0F1; P40222: TXLNA; NbExp=6; IntAct=EBI-744115, EBI-359793;
CC Q9C0F1; Q68DK2-5: ZFYVE26; NbExp=6; IntAct=EBI-744115, EBI-8656416;
CC Q9C0F1; Q8TAU3: ZNF417; NbExp=4; IntAct=EBI-744115, EBI-740727;
CC Q9C0F1; Q96SQ5: ZNF587; NbExp=6; IntAct=EBI-744115, EBI-6427977;
CC Q9C0F1; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-744115, EBI-16429014;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:31974111}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:31974111,
CC ECO:0000269|PubMed:32060285}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:21399614}. Midbody {ECO:0000269|PubMed:21399614}.
CC Note=Localizes to the proximal end of mother and daughter centrioles.
CC {ECO:0000269|PubMed:31974111, ECO:0000269|PubMed:32060285}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0F1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0F1-2; Sequence=VSP_041378;
CC -!- DEVELOPMENTAL STAGE: Moderate expression in G0 and G1, increasing in S
CC and G2, and dropping in prophase, metaphase and anaphase (at protein
CC level). {ECO:0000269|PubMed:31974111}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21803.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY426674; AAR88428.1; -; mRNA.
DR EMBL; AB051499; BAB21803.1; ALT_INIT; mRNA.
DR EMBL; AK094961; BAG52965.1; -; mRNA.
DR EMBL; AK292484; BAF85173.1; -; mRNA.
DR EMBL; AC097653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04738.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04739.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04740.1; -; Genomic_DNA.
DR EMBL; BC038667; AAH38667.1; -; mRNA.
DR CCDS; CCDS34106.1; -. [Q9C0F1-1]
DR CCDS; CCDS47163.1; -. [Q9C0F1-2]
DR RefSeq; NP_001035247.1; NM_001040157.2. [Q9C0F1-1]
DR RefSeq; NP_001138786.1; NM_001145314.1. [Q9C0F1-2]
DR RefSeq; XP_011530587.1; XM_011532285.2. [Q9C0F1-2]
DR RefSeq; XP_011530588.1; XM_011532286.2. [Q9C0F1-2]
DR RefSeq; XP_011530589.1; XM_011532287.2. [Q9C0F1-2]
DR RefSeq; XP_016864143.1; XM_017008654.1. [Q9C0F1-1]
DR RefSeq; XP_016864144.1; XM_017008655.1. [Q9C0F1-1]
DR PDB; 7PT5; X-ray; 2.30 A; A=1-140.
DR PDBsum; 7PT5; -.
DR AlphaFoldDB; Q9C0F1; -.
DR SMR; Q9C0F1; -.
DR BioGRID; 123315; 195.
DR IntAct; Q9C0F1; 152.
DR MINT; Q9C0F1; -.
DR STRING; 9606.ENSP00000389427; -.
DR GlyGen; Q9C0F1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9C0F1; -.
DR PhosphoSitePlus; Q9C0F1; -.
DR BioMuta; CEP44; -.
DR DMDM; 152032537; -.
DR EPD; Q9C0F1; -.
DR jPOST; Q9C0F1; -.
DR MassIVE; Q9C0F1; -.
DR MaxQB; Q9C0F1; -.
DR PaxDb; Q9C0F1; -.
DR PeptideAtlas; Q9C0F1; -.
DR PRIDE; Q9C0F1; -.
DR ProteomicsDB; 80028; -. [Q9C0F1-1]
DR ProteomicsDB; 80029; -. [Q9C0F1-2]
DR Antibodypedia; 50770; 115 antibodies from 22 providers.
DR DNASU; 80817; -.
DR Ensembl; ENST00000296519.6; ENSP00000296519.4; ENSG00000164118.13. [Q9C0F1-1]
DR Ensembl; ENST00000396791.7; ENSP00000380009.3; ENSG00000164118.13. [Q9C0F1-1]
DR Ensembl; ENST00000426172.3; ENSP00000408221.1; ENSG00000164118.13. [Q9C0F1-2]
DR Ensembl; ENST00000457424.6; ENSP00000389427.2; ENSG00000164118.13. [Q9C0F1-2]
DR Ensembl; ENST00000503780.6; ENSP00000423153.1; ENSG00000164118.13. [Q9C0F1-1]
DR GeneID; 80817; -.
DR KEGG; hsa:80817; -.
DR MANE-Select; ENST00000503780.6; ENSP00000423153.1; NM_001040157.3; NP_001035247.1.
DR UCSC; uc003itr.4; human. [Q9C0F1-1]
DR CTD; 80817; -.
DR GeneCards; CEP44; -.
DR HGNC; HGNC:29356; CEP44.
DR HPA; ENSG00000164118; Low tissue specificity.
DR neXtProt; NX_Q9C0F1; -.
DR OpenTargets; ENSG00000164118; -.
DR PharmGKB; PA134933992; -.
DR VEuPathDB; HostDB:ENSG00000164118; -.
DR eggNOG; ENOG502R3RQ; Eukaryota.
DR GeneTree; ENSGT00390000009873; -.
DR HOGENOM; CLU_060541_0_0_1; -.
DR InParanoid; Q9C0F1; -.
DR OMA; YCGLKEN; -.
DR OrthoDB; 1589624at2759; -.
DR PhylomeDB; Q9C0F1; -.
DR TreeFam; TF332994; -.
DR PathwayCommons; Q9C0F1; -.
DR SignaLink; Q9C0F1; -.
DR BioGRID-ORCS; 80817; 43 hits in 1078 CRISPR screens.
DR ChiTaRS; CEP44; human.
DR GenomeRNAi; 80817; -.
DR Pharos; Q9C0F1; Tdark.
DR PRO; PR:Q9C0F1; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9C0F1; protein.
DR Bgee; ENSG00000164118; Expressed in bronchial epithelial cell and 177 other tissues.
DR ExpressionAtlas; Q9C0F1; baseline and differential.
DR Genevisible; Q9C0F1; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; TAS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IDA:UniProtKB.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR InterPro; IPR033603; CEP44.
DR InterPro; IPR029157; CEP44_CC.
DR PANTHER; PTHR31477; PTHR31477; 2.
DR Pfam; PF15007; CEP44; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..390
FT /note="Centrosomal protein of 44 kDa"
FT /id="PRO_0000293722"
FT REGION 11..195
FT /note="Binds with microtubules and centrioles"
FT /evidence="ECO:0000269|PubMed:31974111"
FT REGION 322..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 233..269
FT /evidence="ECO:0000255"
FT COILED 361..385
FT /evidence="ECO:0000255"
FT COMPBIAS 333..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 363..390
FT /note="ETTIQKMERMKKMFEETAELLKCPNHYL -> NFPAWSATSSCSSLSWLLRG
FT HTSYLSSQSFAWPLSCV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041378"
FT VARIANT 147
FT /note="G -> S (in dbSNP:rs4695918)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_033116"
FT MUTAGEN 68..88
FT /note="KNDLRFIDAVYKLLRDQFNYK->DNDLEFIDAVYDLLDQFNYD: Loss of
FT binding to microtubules and location to centrioles."
FT /evidence="ECO:0000269|PubMed:32060285"
SQ SEQUENCE 390 AA; 44140 MW; 5B917C1159B1B7E2 CRC64;
MATGDLKRSL RNLEQVLRLL NYPEEVDCVG LIKGDPAASL PIISYSFTSY SPYVTELIME
SNVELIAKND LRFIDAVYKL LRDQFNYKPI LTKKQFIQCG FAEWKIQIVC DILNCVMKKH
KELSSLQKIP SQQRKKISSG KSEPPLGNEK ISAEAVGVDI SGRFMTSGKK KAVVIRHLYN
EDNVDISEDT LSPITDVNEA VDVSDLNATE IKMPEVKVPE IKAEQQDVNV NPEITALQTM
LAECQENLKK LTSIEKRLDC LEQKMKGKVM VDENTWTNLL SRVTLLETEM LLSKKNDEFI
EFNEVSEDYA SCSDMDLLNP HRKSEVERPA SIPLSSGYST ASSDSTPRAS TVNYCGLNEI
SEETTIQKME RMKKMFEETA ELLKCPNHYL
