CE164_HUMAN
ID CE164_HUMAN Reviewed; 1460 AA.
AC Q9UPV0; Q6PKH9; Q7Z2X9; Q9NVS0; Q9UFJ6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Centrosomal protein of 164 kDa;
DE Short=Cep164;
GN Name=CEP164; Synonyms=KIAA1052, NPHP15;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=17954613; DOI=10.1083/jcb.200707181;
RA Graser S., Stierhof Y.-D., Lavoie S.B., Gassner O.S., Lamla S.,
RA Le Clech M., Nigg E.A.;
RT "Cep164, a novel centriole appendage protein required for primary cilium
RT formation.";
RL J. Cell Biol. 179:321-330(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH ATM;
RP ATR; ATRIP AND MDC1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-186, AND
RP MUTAGENESIS OF SER-186.
RX PubMed=18283122; DOI=10.1101/gad.1627708;
RA Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.;
RT "Cep164 is a mediator protein required for the maintenance of genomic
RT stability through modulation of MDC1, RPA, and CHK1.";
RL Genes Dev. 22:587-600(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116 (ISOFORMS 1/2).
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-1460 (ISOFORM 1), AND
RP VARIANTS SER-988 AND ARG-1119.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1038-1460 (ISOFORM 1), AND
RP VARIANT ARG-1119.
RC TISSUE=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 [8]
RP INTERACTION WITH XPA, AND SUBCELLULAR LOCATION.
RX PubMed=19197159; DOI=10.4161/cc.8.4.7844;
RA Pan Y.R., Lee E.Y.;
RT "UV-dependent interaction between Cep164 and XPA mediates localization of
RT Cep164 at sites of DNA damage and UV sensitivity.";
RL Cell Cycle 8:655-664(2009).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21976302; DOI=10.1002/cm.20536;
RA Sillibourne J.E., Specht C.G., Izeddin I., Hurbain I., Tran P., Triller A.,
RA Darzacq X., Dahan M., Bornens M.;
RT "Assessing the localization of centrosomal proteins by PALM/STORM
RT nanoscopy.";
RL Cytoskeleton 68:619-627(2011).
RN [10]
RP SUBCELLULAR LOCATION, INTERACTION WITH CCDC92; TTBK2; NPHP3; NPHP4 AND
RP DVL3, AND VARIANTS NPHP15 PRO-11 AND TRP-93.
RX PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
RA Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H.,
RA Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J.,
RA Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.,
RA van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H.,
RA Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A.,
RA Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S.,
RA Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S.,
RA Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C.,
RA Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G.,
RA Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A.,
RA Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
RA Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
RA Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
RA Hildebrandt F.;
RT "Exome capture reveals ZNF423 and CEP164 mutations, linking renal
RT ciliopathies to DNA damage response signaling.";
RL Cell 150:533-548(2012).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23348840; DOI=10.1101/gad.207043.112;
RA Tanos B.E., Yang H.J., Soni R., Wang W.J., Macaluso F.P., Asara J.M.,
RA Tsou M.F.;
RT "Centriole distal appendages promote membrane docking, leading to cilia
RT initiation.";
RL Genes Dev. 27:163-168(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-566; SER-1386;
RP SER-1388 AND SER-1443, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [13]
RP INTERACTION WITH CEP83, AND SUBCELLULAR LOCATION.
RX PubMed=23530209; DOI=10.1073/pnas.1220927110;
RA Joo K., Kim C.G., Lee M.S., Moon H.Y., Lee S.H., Kim M.J., Kweon H.S.,
RA Park W.Y., Kim C.H., Gleeson J.G., Kim J.;
RT "CCDC41 is required for ciliary vesicle docking to the mother centriole.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5987-5992(2013).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT duplication.";
RL Mol. Biol. Cell 26:3788-3802(2015).
CC -!- FUNCTION: Plays a role in microtubule organization and/or maintenance
CC for the formation of primary cilia (PC), a microtubule-based structure
CC that protrudes from the surface of epithelial cells. Plays a critical
CC role in G2/M checkpoint and nuclear divisions. A key player in the DNA
CC damage-activated ATR/ATM signaling cascade since it is required for the
CC proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical
CC role in chromosome segregation, acting as a mediator required for the
CC maintenance of genomic stability through modulation of MDC1, RPA and
CC CHEK1. {ECO:0000269|PubMed:17954613, ECO:0000269|PubMed:18283122,
CC ECO:0000269|PubMed:23348840}.
CC -!- SUBUNIT: Interacts (via N-terminus) with ATRIP. Interacts with ATM, ATR
CC and MDC1. Interacts with XPA (via N-terminus) upon UV irradiation.
CC Interacts with CEP83, CCDC92, TTBK2, DVL3, NPHP3 and weakly with NPHP4.
CC Interacts with DZIP1 (By similarity). {ECO:0000250|UniProtKB:Q5DU05,
CC ECO:0000269|PubMed:18283122, ECO:0000269|PubMed:19197159,
CC ECO:0000269|PubMed:22863007, ECO:0000269|PubMed:23530209}.
CC -!- INTERACTION:
CC Q9UPV0; Q53HC0: CCDC92; NbExp=5; IntAct=EBI-3937015, EBI-719994;
CC Q9UPV0; Q92989: CLP1; NbExp=3; IntAct=EBI-3937015, EBI-2559831;
CC Q9UPV0; Q92997: DVL3; NbExp=5; IntAct=EBI-3937015, EBI-739789;
CC Q9UPV0; Q7Z494: NPHP3; NbExp=2; IntAct=EBI-3937015, EBI-2804263;
CC Q9UPV0; Q6IQ55: TTBK2; NbExp=4; IntAct=EBI-3937015, EBI-1050303;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:26337392}. Nucleus.
CC Note=Localizes specifically to very distally located appendage
CC structures on the mature centriole from which initiate PC formation
CC (PubMed:26337392). Persisted at centrioles throughout mitosis.
CC Expressed in chromatin-enriched nuclear fraction of HeLa cells. In
CC response to DNA damage, it translocates to nuclear foci that contain
CC the DNA damage response proteins KAT5/TIP60 and CHEK1.
CC {ECO:0000269|PubMed:26337392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPV0-2; Sequence=VSP_029843, VSP_029844;
CC -!- TISSUE SPECIFICITY: Expressed in several cell lines.
CC {ECO:0000269|PubMed:17954613}.
CC -!- PTM: Phosphorylation at Ser-186 is induced upon DNA-damage caused by
CC treatment with IR irradiation, UV irradiation, hydroxyurea or
CC amphidicolin. Also MDC1-mediated chromatin remodeling is critical for
CC DNA damage-induced phosphorylation. {ECO:0000269|PubMed:18283122}.
CC -!- DISEASE: Nephronophthisis 15 (NPHP15) [MIM:614845]: An autosomal
CC recessive disorder characterized by the association of nephronophthisis
CC with Leber congenital amaurosis and retinal degeneration, often
CC resulting in blindness during childhood. Additional features include
CC seizures, cerebellar vermis hypoplasia, facial dysmorphism,
CC bronchiectasis and liver failure. Nephronophthisis is a chronic tubulo-
CC interstitial nephritis that progresses to end-stage renal failure.
CC {ECO:0000269|PubMed:22863007}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00602.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH54015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA83004.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB56023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB028975; BAA83004.2; ALT_INIT; mRNA.
DR EMBL; AP000892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000602; AAH00602.1; ALT_SEQ; mRNA.
DR EMBL; BC054015; AAH54015.1; ALT_SEQ; mRNA.
DR EMBL; AL117632; CAB56023.1; ALT_INIT; mRNA.
DR EMBL; AK001412; BAA91677.1; ALT_INIT; mRNA.
DR CCDS; CCDS31683.1; -. [Q9UPV0-1]
DR PIR; T17333; T17333.
DR RefSeq; NP_001258862.1; NM_001271933.1. [Q9UPV0-2]
DR RefSeq; NP_055771.4; NM_014956.4. [Q9UPV0-1]
DR RefSeq; XP_005271513.1; XM_005271456.1. [Q9UPV0-1]
DR RefSeq; XP_005271514.1; XM_005271457.1. [Q9UPV0-2]
DR PDB; 7NWJ; NMR; -; A=1-109.
DR PDB; 7O06; X-ray; 1.60 A; C/D=1-109.
DR PDB; 7O0S; X-ray; 1.70 A; B=1-109.
DR PDB; 7O3B; X-ray; 2.40 A; G/H/I=1-109.
DR PDBsum; 7NWJ; -.
DR PDBsum; 7O06; -.
DR PDBsum; 7O0S; -.
DR PDBsum; 7O3B; -.
DR AlphaFoldDB; Q9UPV0; -.
DR SMR; Q9UPV0; -.
DR BioGRID; 116561; 126.
DR CORUM; Q9UPV0; -.
DR IntAct; Q9UPV0; 89.
DR STRING; 9606.ENSP00000278935; -.
DR CarbonylDB; Q9UPV0; -.
DR iPTMnet; Q9UPV0; -.
DR PhosphoSitePlus; Q9UPV0; -.
DR BioMuta; CEP164; -.
DR DMDM; 162416241; -.
DR EPD; Q9UPV0; -.
DR jPOST; Q9UPV0; -.
DR MassIVE; Q9UPV0; -.
DR MaxQB; Q9UPV0; -.
DR PaxDb; Q9UPV0; -.
DR PeptideAtlas; Q9UPV0; -.
DR PRIDE; Q9UPV0; -.
DR ProteomicsDB; 85453; -. [Q9UPV0-1]
DR ProteomicsDB; 85454; -. [Q9UPV0-2]
DR Antibodypedia; 32367; 216 antibodies from 29 providers.
DR DNASU; 22897; -.
DR Ensembl; ENST00000278935.8; ENSP00000278935.3; ENSG00000110274.16. [Q9UPV0-1]
DR GeneID; 22897; -.
DR KEGG; hsa:22897; -.
DR MANE-Select; ENST00000278935.8; ENSP00000278935.3; NM_014956.5; NP_055771.4.
DR UCSC; uc001prc.4; human. [Q9UPV0-1]
DR CTD; 22897; -.
DR DisGeNET; 22897; -.
DR GeneCards; CEP164; -.
DR GeneReviews; CEP164; -.
DR HGNC; HGNC:29182; CEP164.
DR HPA; ENSG00000110274; Low tissue specificity.
DR MalaCards; CEP164; -.
DR MIM; 614845; phenotype.
DR MIM; 614848; gene.
DR neXtProt; NX_Q9UPV0; -.
DR OpenTargets; ENSG00000110274; -.
DR Orphanet; 3156; Senior-Loken syndrome.
DR PharmGKB; PA142672127; -.
DR VEuPathDB; HostDB:ENSG00000110274; -.
DR eggNOG; ENOG502QR4A; Eukaryota.
DR GeneTree; ENSGT00950000183078; -.
DR HOGENOM; CLU_002153_0_0_1; -.
DR InParanoid; Q9UPV0; -.
DR OMA; LPHCEWW; -.
DR PhylomeDB; Q9UPV0; -.
DR TreeFam; TF333034; -.
DR PathwayCommons; Q9UPV0; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9UPV0; -.
DR BioGRID-ORCS; 22897; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; CEP164; human.
DR GeneWiki; CEP164; -.
DR GenomeRNAi; 22897; -.
DR Pharos; Q9UPV0; Tbio.
DR PRO; PR:Q9UPV0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UPV0; protein.
DR Bgee; ENSG00000110274; Expressed in sperm and 172 other tissues.
DR ExpressionAtlas; Q9UPV0; baseline and differential.
DR Genevisible; Q9UPV0; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00201; WW; 1.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Ciliopathy;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; DNA damage; DNA repair; Mitosis; Nephronophthisis;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1460
FT /note="Centrosomal protein of 164 kDa"
FT /id="PRO_0000312494"
FT DOMAIN 56..89
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..194
FT /note="Interaction with ATRIP"
FT /evidence="ECO:0000269|PubMed:18283122"
FT REGION 107..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1154..1206
FT /evidence="ECO:0000255"
FT COMPBIAS 257..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine; by ATR and ATM"
FT /evidence="ECO:0000269|PubMed:18283122"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 469
FT /note="E -> ERYH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:18283122"
FT /id="VSP_029843"
FT VAR_SEQ 1242..1250
FT /note="REWWRQQRI -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:18283122"
FT /id="VSP_029844"
FT VARIANT 11
FT /note="Q -> P (in NPHP15; dbSNP:rs387907309)"
FT /evidence="ECO:0000269|PubMed:22863007"
FT /id="VAR_068503"
FT VARIANT 93
FT /note="R -> W (in NPHP15; dbSNP:rs387907310)"
FT /evidence="ECO:0000269|PubMed:22863007"
FT /id="VAR_068504"
FT VARIANT 94
FT /note="S -> N (in dbSNP:rs490262)"
FT /id="VAR_037511"
FT VARIANT 988
FT /note="T -> S (in dbSNP:rs2305830)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_037512"
FT VARIANT 1119
FT /note="Q -> R (in dbSNP:rs573455)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_037513"
FT MUTAGEN 186
FT /note="S->A: Prevents phosphorylation."
FT /evidence="ECO:0000269|PubMed:18283122"
FT CONFLICT 110
FT /note="K -> N (in Ref. 5; AAH54015)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7O3B"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7O0S"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:7O06"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:7O06"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:7O06"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:7O06"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7O06"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:7NWJ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:7O06"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:7O06"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:7O06"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:7O06"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7NWJ"
SQ SEQUENCE 1460 AA; 164314 MW; 7A4F91E1CB7D1E43 CRC64;
MAGRPLRIGD QLVLEEDYDE TYIPSEQEIL EFAREIGIDP IKEPELMWLA REGIVAPLPG
EWKPCQDITG DIYYFNFANG QSMWDHPCDE HYRSLVIQER AKLSTSGAIK KKKKKKEKKD
KKDRDPPKSS LALGSSLAPV HVPLGGLAPL RGLVDTPPSA LRGSQSVSLG SSVESGRQLG
ELMLPSQGLK TSAYTKGLLG SIYEDKTALS LLGLGEETNE EDEEESDNQS VHSSSEPLRN
LHLDIGALGG DFEYEESLRT SQPEEKKDVS LDSDAAGPPT PCKPSSPGAD SSLSSAVGKG
RQGSGARPGL PEKEENEKSE PKICRNLVTP KADPTGSEPA KASEKEAPED TVDAGEEGSR
REEAAKEPKK KASALEEGSS DASQELEISE HMKEPQLSDS IASDPKSFHG LDFGFRSRIS
EHLLDVDVLS PVLGGACRQA QQPLGIEDKD DSQSSQDELQ SKQSKGLEER LSPPLPHEER
AQSPPRSLAT EEEPPQGPEG QPEWKEAEEL GEDSAASLSL QLSLQREQAP SPPAACEKGK
EQHSQAEELG PGQEEAEDPE EKVAVSPTPP VSPEVRSTEP VAPPEQLSEA ALKAMEEAVA
QVLEQDQRHL LESKQEKMQQ LREKLCQEEE EEILRLHQQK EQSLSSLRER LQKAIEEEEA
RMREEESQRL SWLRAQVQSS TQADEDQIRA EQEASLQKLR EELESQQKAE RASLEQKNRQ
MLEQLKEEIE ASEKSEQAAL NAAKEKALQQ LREQLEGERK EAVATLEKEH SAELERLCSS
LEAKHREVVS SLQKKIQEAQ QKEEAQLQKC LGQVEHRVHQ KSYHVAGYEH ELSSLLREKR
QEVEGEHERR LDKMKEEHQQ VMAKAREQYE AEERKQRAEL LGHLTGELER LQRAHERELE
TVRQEQHKRL EDLRRRHREQ ERKLQDLELD LETRAKDVKA RLALLEVQEE TARREKQQLL
DVQRQVALKS EEATATHQQL EEAQKEHTHL LQSNQQLREI LDELQARKLK LESQVDLLQA
QSQQLQKHFS SLEAEAQKKQ HLLREVTVEE NNASPHFEPD LHIEDLRKSL GTNQTKEVSS
SLSQSKEDLY LDSLSSHNVW HLLSAEGVAL RSAKEFLVQQ TRSMRRRQTA LKAAQQHWRH
ELASAQEVAK DPPGIKALED MRKNLEKETR HLDEMKSAMR KGHNLLKKKE EKLNQLESSL
WEEASDEGTL GGSPTKKAVT FDLSDMDSLS SESSESFSPP HREWWRQQRI DSTPSLTSRK
IHGLSHSLRQ ISSQLSSVLS ILDSLNPQSP PPLLASMPAQ LPPRDPKSTP TPTYYGSLAR
FSALSSATPT STQWAWDSGQ GPRLPSSVAQ TVDDFLLEKW RKYFPSGIPL LSNSPTPLES
RLGYMSASEQ LRLLQHSHSQ VPEAGSTTFQ GIIEANRRWL ERVKNDPRLP LFSSTPKPKA
TLSLLQLGLD EHNRVKVYRF
