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PPR35_MOUSE
ID   PPR35_MOUSE             Reviewed;         260 AA.
AC   Q9D8C8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 35 {ECO:0000305};
GN   Name=Ppp1r35 {ECO:0000312|MGI:MGI:1922853};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=16926269; DOI=10.1152/physiolgenomics.00284.2005;
RA   Wilson M.D., Cheung J., Martindale D.W., Scherer S.W., Koop B.F.;
RT   "Comparative analysis of the paired immunoglobulin-like receptor (PILR)
RT   locus in six mammalian genomes: duplication, conversion, and the birth of
RT   new genes.";
RL   Physiol. Genomics 27:201-218(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
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-46 AND SER-53, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
RX   PubMed=32628936; DOI=10.1016/j.ydbio.2020.06.011;
RA   Archambault D., Cheong A., Iverson E., Tremblay K.D., Mager J.;
RT   "Protein phosphatase 1 regulatory subunit 35 is required for ciliogenesis,
RT   notochord morphogenesis, and cell-cycle progression during murine
RT   development.";
RL   Dev. Biol. 465:1-10(2020).
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 TTTN, leading to the
CC       centriole to centrosome conversion (By similarity). In addition may
CC       play a role in the primary cilia assembly (PubMed:32628936).
CC       {ECO:0000250|UniProtKB:Q8TAP8, ECO:0000269|PubMed:32628936}.
CC   -!- SUBUNIT: Interacts with PPP1CA; this interaction mediates the PPP1CA
CC       phosphatase activity inhibition. Interacts with RTTN; this interaction
CC       allows the mutual recruitment to the centriole.
CC       {ECO:0000250|UniProtKB:Q8TAP8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q8TAP8}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q8TAP8}. Note=Recruited to the nascent daughter
CC       centriole early in the duplication cycle and localizes to the proximal
CC       centriolar lumen just above the cartwheel. Co-localizes with RTTN at
CC       the centriole. {ECO:0000250|UniProtKB:Q8TAP8}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout much of the embryo at E7.5,
CC       in mesoderm and ectoderm-derived structures at E8.5, and throughout
CC       much of the embryo at E9.5 but is absent in the extra-embryonic
CC       visceral endoderm (VE) at all stages. {ECO:0000269|PubMed:32628936}.
CC   -!- DISRUPTION PHENOTYPE: Mice homozygous embryos for the Ppp1r35 gene are
CC       lethal during early embryogenesis (PubMed:32628936). Homozygous embryos
CC       are capable of initiating and completing gastrulation as well as
CC       specifying the anterior/posterior and the dorsal/ventral axis, but
CC       exhibit a developmental delays which are the result in the failure to
CC       progress past E8.5-9.0 (PubMed:32628936).
CC       {ECO:0000269|PubMed:32628936}.
CC   -!- SIMILARITY: Belongs to the PPP1R35 family. {ECO:0000305}.
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DR   EMBL; AY823670; AAX39498.1; -; Genomic_DNA.
DR   EMBL; AK008148; BAB25495.1; -; mRNA.
DR   EMBL; AC125063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052497; AAH52497.1; -; mRNA.
DR   CCDS; CCDS19777.1; -.
DR   RefSeq; NP_081518.1; NM_027242.4.
DR   AlphaFoldDB; Q9D8C8; -.
DR   SMR; Q9D8C8; -.
DR   BioGRID; 213727; 1.
DR   STRING; 10090.ENSMUSP00000031739; -.
DR   iPTMnet; Q9D8C8; -.
DR   PhosphoSitePlus; Q9D8C8; -.
DR   EPD; Q9D8C8; -.
DR   jPOST; Q9D8C8; -.
DR   MaxQB; Q9D8C8; -.
DR   PaxDb; Q9D8C8; -.
DR   PeptideAtlas; Q9D8C8; -.
DR   PRIDE; Q9D8C8; -.
DR   ProteomicsDB; 289386; -.
DR   Antibodypedia; 55003; 71 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000031739; ENSMUSP00000031739; ENSMUSG00000029725.
DR   GeneID; 69871; -.
DR   KEGG; mmu:69871; -.
DR   UCSC; uc009adx.1; mouse.
DR   CTD; 221908; -.
DR   MGI; MGI:1922853; Ppp1r35.
DR   VEuPathDB; HostDB:ENSMUSG00000029725; -.
DR   eggNOG; ENOG502S5MS; Eukaryota.
DR   GeneTree; ENSGT00390000004198; -.
DR   HOGENOM; CLU_096528_0_0_1; -.
DR   InParanoid; Q9D8C8; -.
DR   OMA; RCEMEEN; -.
DR   OrthoDB; 1390072at2759; -.
DR   PhylomeDB; Q9D8C8; -.
DR   TreeFam; TF337101; -.
DR   BioGRID-ORCS; 69871; 7 hits in 76 CRISPR screens.
DR   ChiTaRS; Ppp1r35; mouse.
DR   PRO; PR:Q9D8C8; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9D8C8; protein.
DR   Bgee; ENSMUSG00000029725; Expressed in spermatocyte and 146 other tissues.
DR   ExpressionAtlas; Q9D8C8; baseline and differential.
DR   Genevisible; Q9D8C8; MM.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS: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; IMP:UniProtKB.
DR   GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR   InterPro; IPR033590; PPP1R35.
DR   InterPro; IPR029135; PPP1R35_C.
DR   PANTHER; PTHR28625; PTHR28625; 1.
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..260
FT                   /note="Protein phosphatase 1 regulatory subunit 35"
FT                   /id="PRO_0000358929"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   260 AA;  28355 MW;  9BCB161E56D7317D CRC64;
     MMGFGASALE SIEGEEALEV PGPPPEPRAP EPRAPEPEPG LDLSLSPSPL PESPKARKSS
     PGQRKGRRGG SRRGRQVRFQ LAPPSPVRSE PLLVAGAPGD DHELEAPALQ SSLALSLELQ
     NARAAVASGQ FDASKAVEEQ LRKSFRTRCA LEETVAEGLN VPRSKRLYRD LVSLQVPEEQ
     VLNAALREKL AMLPPQPRAP PLKEVLGPGP DMTMLCNPDS LWSESPHLTV DGLPPLRLQA
     RPRPSEDTFL MHRMLRRWEA
 
 
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