P4R3B_MOUSE
ID P4R3B_MOUSE Reviewed; 820 AA.
AC Q922R5; Q3V0E4; Q5M6V9; Q5RJC0; Q5RJC1; Q6ZPS5; Q8BTK2; Q8BY94; Q8BYY0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3B {ECO:0000250|UniProtKB:Q5MIZ7};
DE AltName: Full=SMEK homolog 2;
GN Name=Ppp4r3b {ECO:0000250|UniProtKB:Q5MIZ7};
GN Synonyms=Kiaa1387, Pp4r3b, Smek2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=B-cell, Skin, Testis, and Thymus;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, Spleen, 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).
CC -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4
CC (PP4). May regulate the activity of PPP4C at centrosomal microtubule
CC organizing centers (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Component of the PP4 complex PPP4C-PPP4R2-PPP4R3B.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Nucleus. Note=In interphase localized in
CC the cytoplasm and (with higher levels) the nucleus. During metaphase
CC located in pericentriolar regions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q922R5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q922R5-2; Sequence=VSP_021264, VSP_021265;
CC -!- SIMILARITY: Belongs to the SMEK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98154.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129344; BAC98154.1; ALT_INIT; mRNA.
DR EMBL; AK037253; BAC29779.2; -; mRNA.
DR EMBL; AK041513; BAC30967.1; -; mRNA.
DR EMBL; AK090014; BAC41046.1; -; mRNA.
DR EMBL; AK133211; BAE21560.1; -; mRNA.
DR EMBL; BX000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX294116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006870; AAH06870.1; -; mRNA.
DR CCDS; CCDS24492.1; -. [Q922R5-1]
DR RefSeq; NP_598795.2; NM_134034.2. [Q922R5-1]
DR AlphaFoldDB; Q922R5; -.
DR ComplexPortal; CPX-164; PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex.
DR STRING; 10090.ENSMUSP00000020755; -.
DR iPTMnet; Q922R5; -.
DR PhosphoSitePlus; Q922R5; -.
DR EPD; Q922R5; -.
DR MaxQB; Q922R5; -.
DR PaxDb; Q922R5; -.
DR PeptideAtlas; Q922R5; -.
DR PRIDE; Q922R5; -.
DR ProteomicsDB; 294366; -. [Q922R5-1]
DR ProteomicsDB; 294367; -. [Q922R5-2]
DR Antibodypedia; 73190; 164 antibodies from 25 providers.
DR DNASU; 104570; -.
DR Ensembl; ENSMUST00000020755; ENSMUSP00000020755; ENSMUSG00000020463. [Q922R5-1]
DR Ensembl; ENSMUST00000102856; ENSMUSP00000099920; ENSMUSG00000020463. [Q922R5-2]
DR GeneID; 104570; -.
DR KEGG; mmu:104570; -.
DR UCSC; uc007igq.2; mouse. [Q922R5-2]
DR UCSC; uc007igs.2; mouse. [Q922R5-1]
DR CTD; 57223; -.
DR MGI; MGI:2144474; Ppp4r3b.
DR VEuPathDB; HostDB:ENSMUSG00000020463; -.
DR eggNOG; KOG2175; Eukaryota.
DR GeneTree; ENSGT00390000018199; -.
DR HOGENOM; CLU_004909_3_1_1; -.
DR InParanoid; Q922R5; -.
DR OMA; YHRYMIS; -.
DR OrthoDB; 388216at2759; -.
DR PhylomeDB; Q922R5; -.
DR TreeFam; TF315190; -.
DR BioGRID-ORCS; 104570; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Smek2; mouse.
DR PRO; PR:Q922R5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q922R5; protein.
DR Bgee; ENSMUSG00000020463; Expressed in saccule of membranous labyrinth and 252 other tissues.
DR ExpressionAtlas; Q922R5; baseline and differential.
DR Genevisible; Q922R5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:MGI.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..820
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 3B"
FT /id="PRO_0000254604"
FT DOMAIN 1..100
FT /note="WH1"
FT REGION 687..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5MIZ7"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5MIZ7"
FT VAR_SEQ 614..616
FT /note="EDI -> VSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021264"
FT VAR_SEQ 617..820
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021265"
FT CONFLICT 110
FT /note="T -> I (in Ref. 2; BAC30967)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="A -> T (in Ref. 3; BAC41046 and 4; AAH06870)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="Q -> P (in Ref. 3; BAC41046)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="L -> W (in Ref. 3; BAC41046)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="K -> Q (in Ref. 3; BAC41046)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="M -> V (in Ref. 3; BAC41046 and 4; AAH06870)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="N -> D (in Ref. 3; BAC41046)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="I -> V (in Ref. 3; BAC41046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 93934 MW; 7B5A35D71663AB91 CRC64;
MSDTRRRVKV YTLNEDRQWD DRGTGHVSST YVEELKGMSL LVRAESDGSL LLESKINPNT
AYQKQQDTLI VWSEAENYDL ALSFQEKAGC DEIWEKICQV QGKDPSVEVT QDLIDESEEE
RFEEMPETSH LIDLPACELS KLEEIADLVT SVLSSPIRRE KLALALENEG YIKKLLQLFQ
ACENLENTEG LHHLYEIIRG ILFLNKATLF EVMFSDECIM DVVGCLEYDP ALAQPKRHRE
FLTKTAKFKE VIPITDSELR QKIHQTYRVQ YIQDIILPTP SVFEENFLST LTSFIFFNKV
EIVSMLQEDE KFLSEVFAQL TDEATDDDKR RELVNFFKEF CAFSQTLQPQ NRDAFFKTLA
KLGILPALEI VMGMDDLQVR SAATDIFSYL VEFSPSMVRE FVMQEAQQSD DDVLLINVVI
EQMICDTDPE LGGAVQLMGL LRTLIDPENM LATTNKTEKS EFLNFFYNHC MHVLTAPLLT
NTSEDKCEKD NMLGSNTTNT ICPDNYQTAQ LLALILELLT FCVEHHTYHI KNYIMNKDLL
RRVLVLMNSK HTFLALCALR FMRRIIGLKD EFYNRYITKG NLFEPVINAL LDNGTRYNLL
NSAVIELFEF IRVEDIKSLT AHIVENFYKA LESIEYVQTF KGLKTKYEQE KDRQNQKLNS
VPSILRSNRF RRDAKALEED EEMWFNEDDD EEGKAVITPV EKSKTEDDFP DSYEKFMETK
KAKESEDKEN LPKRASSGGF KFTFSHSPSA TNGTNSTNSK SVVSQTTPAS SNVASSKTTS
LATSVTATKG NLVGLVDYPD DEEEDEEEES SPRKRPRLGS
