PPR35_HUMAN
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 03-AUG-2022, entry version 128.
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 phosphatase-
RT 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}.
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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; 10.
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; Q8TAP8; -.
DR PeptideAtlas; Q8TAP8; -.
DR PRIDE; Q8TAP8; -.
DR ProteomicsDB; 73904; -.
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 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; 1390072at2759; -.
DR PhylomeDB; Q8TAP8; -.
DR TreeFam; TF337101; -.
DR PathwayCommons; Q8TAP8; -.
DR SignaLink; Q8TAP8; -.
DR BioGRID-ORCS; 221908; 76 hits in 1075 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 171 other tissues.
DR Genevisible; Q8TAP8; 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:0019902; F:phosphatase binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IEA:InterPro.
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; PTHR28625; 2.
DR Pfam; PF15503; PPP1R35_C; 1.
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
