ID PPR35_HUMAN Reviewed; 253 AA. AC Q8TAP8; A4D2C5; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 24-JAN-2024, entry version 134. DE RecName: Full=Protein phosphatase 1 regulatory subunit 35 {ECO:0000305}; GN Name=PPP1R35 {ECO:0000312|HGNC:HGNC:28320}; GN Synonyms=C7orf47 {ECO:0000312|HGNC:HGNC:28320}; 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 GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [6] RP IDENTIFICATION BY 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 [7] RP FUNCTION, AND INTERACTION WITH PPP1CA. RX PubMed=19389623; DOI=10.1016/j.chembiol.2009.02.012; RA Hendrickx A., Beullens M., Ceulemans H., Den Abt T., Van Eynde A., RA Nicolaescu E., Lesage B., Bollen M.; RT "Docking motif-guided mapping of the interactome of protein RT phosphatase-1."; RL Chem. Biol. 16:365-371(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-52, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [11] RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH RTTN, AND MUTAGENESIS OF RP SER-45; SER-47; SER-52; VAL-79 AND PHE-81. RX PubMed=30168418; DOI=10.7554/elife.37846; RA Sydor A.M., Coyaud E., Rovelli C., Laurent E., Liu H., Raught B., RA Mennella V.; RT "PPP1R35 is a novel centrosomal protein that regulates centriole length in RT concert with the microcephaly protein RTTN."; RL Elife 7:0-0(2018). RN [12] RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH PPP1CA. RX PubMed=30230954; DOI=10.1091/mbc.e18-08-0525; RA Fong C.S., Ozaki K., Tsou M.B.; RT "PPP1R35 ensures centriole homeostasis by promoting centriole-to-centrosome RT conversion."; RL Mol. Biol. Cell 29:2801-2808(2018). CC -!- FUNCTION: During centriole duplication, plays a role in the centriole CC elongation by promoting the recruitment of the microtubule-binding CC elongation machinery through its interaction with RTTN, leading to the CC centriole to centrosome conversion (PubMed:30168418, PubMed:30230954). CC In addition, may play a role in the primary cilia assembly (By CC similarity). {ECO:0000250|UniProtKB:Q9D8C8, CC ECO:0000269|PubMed:30168418, ECO:0000269|PubMed:30230954}. CC -!- SUBUNIT: Interacts with PPP1CA; this interaction mediates the PPP1CA CC phosphatase activity inhibition (PubMed:19389623, PubMed:30230954). CC Interacts with RTTN; this interaction allows the mutual recruitment to CC the centriole (PubMed:30168418). {ECO:0000269|PubMed:19389623, CC ECO:0000269|PubMed:30168418, ECO:0000269|PubMed:30230954}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:30168418}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome, centriole CC {ECO:0000269|PubMed:30168418, ECO:0000269|PubMed:30230954}. CC Note=Recruited to the nascent daughter centriole early in the CC duplication cycle and localizes to the proximal centriolar lumen just CC above the cartwheel (PubMed:30168418, PubMed:30230954). Co-localizes CC with RTTN at the centriole (PubMed:30168418). CC {ECO:0000269|PubMed:30168418, ECO:0000269|PubMed:30230954}. CC -!- SIMILARITY: Belongs to the PPP1R35 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC092849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236956; EAL23833.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76532.1; -; Genomic_DNA. DR EMBL; BC026269; AAH26269.1; -; mRNA. DR CCDS; CCDS5694.1; -. DR RefSeq; NP_659467.1; NM_145030.3. DR AlphaFoldDB; Q8TAP8; -. DR BioGRID; 128765; 11. DR IntAct; Q8TAP8; 10. DR STRING; 9606.ENSP00000292330; -. DR iPTMnet; Q8TAP8; -. DR PhosphoSitePlus; Q8TAP8; -. DR BioMuta; PPP1R35; -. DR DMDM; 74730374; -. DR EPD; Q8TAP8; -. DR jPOST; Q8TAP8; -. DR MassIVE; Q8TAP8; -. DR MaxQB; Q8TAP8; -. DR PaxDb; 9606-ENSP00000292330; -. DR PeptideAtlas; Q8TAP8; -. DR ProteomicsDB; 73904; -. DR Pumba; Q8TAP8; -. DR Antibodypedia; 55003; 71 antibodies from 15 providers. DR DNASU; 221908; -. DR Ensembl; ENST00000292330.3; ENSP00000292330.2; ENSG00000160813.7. DR GeneID; 221908; -. DR KEGG; hsa:221908; -. DR MANE-Select; ENST00000292330.3; ENSP00000292330.2; NM_145030.4; NP_659467.1. DR UCSC; uc003uuy.2; human. DR AGR; HGNC:28320; -. DR CTD; 221908; -. DR GeneCards; PPP1R35; -. DR HGNC; HGNC:28320; PPP1R35. DR HPA; ENSG00000160813; Tissue enhanced (testis). DR MIM; 618937; gene. DR neXtProt; NX_Q8TAP8; -. DR OpenTargets; ENSG00000160813; -. DR PharmGKB; PA162380520; -. DR VEuPathDB; HostDB:ENSG00000160813; -. DR eggNOG; ENOG502S5MS; Eukaryota. DR GeneTree; ENSGT00390000004198; -. DR HOGENOM; CLU_096528_0_0_1; -. DR InParanoid; Q8TAP8; -. DR OMA; RCEMEEN; -. DR OrthoDB; 5305819at2759; -. DR PhylomeDB; Q8TAP8; -. DR TreeFam; TF337101; -. DR PathwayCommons; Q8TAP8; -. DR SignaLink; Q8TAP8; -. DR BioGRID-ORCS; 221908; 97 hits in 1151 CRISPR screens. DR ChiTaRS; PPP1R35; human. DR GenomeRNAi; 221908; -. DR Pharos; Q8TAP8; Tdark. DR PRO; PR:Q8TAP8; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q8TAP8; Protein. DR Bgee; ENSG00000160813; Expressed in oocyte and 173 other cell types or tissues. 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:0019902; F:phosphatase binding; IEA:InterPro. DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0048570; P:notochord morphogenesis; ISS:UniProtKB. DR GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB. DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB. DR InterPro; IPR033590; PPP1R35. DR InterPro; IPR029135; PPP1R35_C. DR PANTHER; PTHR28625; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 35; 1. DR PANTHER; PTHR28625:SF1; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 35; 1. DR Pfam; PF15503; PPP1R35_C; 1. DR Genevisible; Q8TAP8; HS. PE 1: Evidence at protein level; KW Cytoplasm; Cytoskeleton; Phosphoprotein; Protein phosphatase inhibitor; KW Reference proteome. FT CHAIN 1..253 FT /note="Protein phosphatase 1 regulatory subunit 35" FT /id="PRO_0000271356" FT REGION 1..98 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..35 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..77 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MUTAGEN 45 FT /note="S->A: Does not affect centrosome localization; when FT associated with A-47 and A-52. Does not affect interaction FT with RTTN; when associated with A-47 and A-52." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 45 FT /note="S->D: Does not affect centrosome localization; when FT associated with D-47 and D-52. Does not affect interaction FT with RTTN; when associated with D-47 and D-52." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 47 FT /note="S->A: Does not affect centrosome localization; when FT associated with A-45 and A-52. Does not affect interaction FT with RTTN; when associated with A-45 and A-52." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 47 FT /note="S->D: Does not affect centrosome localization; when FT associated with D-45 and D-52. Does not affect interaction FT with RTTN; when associated with D-45 and D-52." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 52 FT /note="S->A: Does not affect centrosome localization; when FT associated with A-45 and A-47. Does not affect interaction FT with RTTN; when associated with A-45 and A-47." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 52 FT /note="S->D: Does not affect centrosome localization; when FT associated with D-45 and D-47. Does not affect interaction FT with RTTN; when associated with D-45 and D-47." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 79 FT /note="V->A: Does not affect centriole localization; when FT associated with A-81. Does not affect interaction with FT RTTN; when associated with A-81." FT /evidence="ECO:0000269|PubMed:30168418" FT MUTAGEN 81 FT /note="F->A: Does not affect centriole localization; when FT associated with A-79. Does not affect interaction with FT RTTN; when associated with A-79." FT /evidence="ECO:0000269|PubMed:30168418" SQ SEQUENCE 253 AA; 27953 MW; 9DE5142EDD2150B2 CRC64; MMMGCGESEL KSADGEEAAA VPGPPPEPQV PQLRAPVPEP GLDLSLSPRP DSPQPRHGSP GRRKGRAERR GAARQRRQVR FRLTPPSPVR SEPQPAVPQE LEMPVLKSSL ALGLELRAAA GSHFDAAKAV EEQLRKSFQI RCGLEESVSE GLNVPRSKRL FRDLVSLQVP EEQVLNAALR EKLALLPPQA RAPHPKEPPG PGPDMTILCD PETLFYESPH LTLDGLPPLR LQLRPRPSED TFLMHRTLRR WEA //