PPR37_HUMAN
ID PPR37_HUMAN Reviewed; 691 AA.
AC O75864; B5MDA4; Q8IWK3; Q8TF16;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 37;
DE AltName: Full=Leucine-rich repeat-containing protein 68;
GN Name=PPP1R37; Synonyms=KIAA1986, LRRC68;
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 MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-180 (ISOFORM 1).
RC TISSUE=Duodenum;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 254-460.
RX PubMed=12107411;
RA Wistow G., Berstein S.L., Wyatt M.K., Ray S., Behal A., Touchman J.W.,
RA Bouffard G., Smith D., Peterson K.;
RT "Expressed sequence tag analysis of human retina for the NEIBank project:
RT retbindin, an abundant, novel retinal cDNA and alternative splicing of
RT other retina-preferred gene transcripts.";
RL Mol. Vis. 8:196-204(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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).
CC -!- FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1)
CC complexes. {ECO:0000269|PubMed:19389623}.
CC -!- SUBUNIT: Interacts with PPP1CA. {ECO:0000269|PubMed:19389623}.
CC -!- INTERACTION:
CC O75864; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-5235692, EBI-10181188;
CC O75864; O75593: FOXH1; NbExp=3; IntAct=EBI-5235692, EBI-1759806;
CC O75864; B2RXH8: HNRNPCL2; NbExp=3; IntAct=EBI-5235692, EBI-9512317;
CC O75864; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-5235692, EBI-11022007;
CC O75864; P62136: PPP1CA; NbExp=5; IntAct=EBI-5235692, EBI-357253;
CC O75864; Q15415: RBMY1J; NbExp=3; IntAct=EBI-5235692, EBI-8642021;
CC O75864; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-5235692, EBI-11987469;
CC O75864; Q96H86: ZNF764; NbExp=3; IntAct=EBI-5235692, EBI-745775;
CC O75864; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-5235692, EBI-11962574;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75864-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75864-2; Sequence=VSP_031754, VSP_031755;
CC -!- MISCELLANEOUS: [Isoform 2]: Due to an intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PPP1R37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62258.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB85572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB075866; BAB85572.1; ALT_INIT; mRNA.
DR EMBL; AC011489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005757; AAC62258.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC035704; AAH35704.1; -; mRNA.
DR EMBL; BQ638089; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS56096.1; -. [O75864-1]
DR RefSeq; NP_061994.1; NM_019121.1. [O75864-1]
DR AlphaFoldDB; O75864; -.
DR SMR; O75864; -.
DR BioGRID; 129838; 36.
DR IntAct; O75864; 14.
DR MINT; O75864; -.
DR STRING; 9606.ENSP00000221462; -.
DR iPTMnet; O75864; -.
DR PhosphoSitePlus; O75864; -.
DR BioMuta; PPP1R37; -.
DR EPD; O75864; -.
DR jPOST; O75864; -.
DR MassIVE; O75864; -.
DR MaxQB; O75864; -.
DR PaxDb; O75864; -.
DR PeptideAtlas; O75864; -.
DR PRIDE; O75864; -.
DR ProteomicsDB; 50229; -. [O75864-1]
DR ProteomicsDB; 50230; -. [O75864-2]
DR Antibodypedia; 49146; 50 antibodies from 12 providers.
DR DNASU; 284352; -.
DR Ensembl; ENST00000221462.9; ENSP00000221462.3; ENSG00000104866.11. [O75864-1]
DR GeneID; 284352; -.
DR KEGG; hsa:284352; -.
DR MANE-Select; ENST00000221462.9; ENSP00000221462.3; NM_019121.2; NP_061994.1.
DR UCSC; uc021uvs.2; human. [O75864-1]
DR CTD; 284352; -.
DR DisGeNET; 284352; -.
DR GeneCards; PPP1R37; -.
DR HGNC; HGNC:27607; PPP1R37.
DR HPA; ENSG00000104866; Low tissue specificity.
DR neXtProt; NX_O75864; -.
DR OpenTargets; ENSG00000104866; -.
DR VEuPathDB; HostDB:ENSG00000104866; -.
DR eggNOG; KOG1908; Eukaryota.
DR GeneTree; ENSGT00940000157454; -.
DR HOGENOM; CLU_014302_0_0_1; -.
DR InParanoid; O75864; -.
DR OMA; EHELRCP; -.
DR OrthoDB; 1186874at2759; -.
DR PhylomeDB; O75864; -.
DR TreeFam; TF328391; -.
DR PathwayCommons; O75864; -.
DR SignaLink; O75864; -.
DR BioGRID-ORCS; 284352; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; PPP1R37; human.
DR GenomeRNAi; 284352; -.
DR Pharos; O75864; Tdark.
DR PRO; PR:O75864; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75864; protein.
DR Bgee; ENSG00000104866; Expressed in adenohypophysis and 116 other tissues.
DR ExpressionAtlas; O75864; baseline and differential.
DR Genevisible; O75864; HS.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13516; LRR_6; 3.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Leucine-rich repeat; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat.
FT CHAIN 1..691
FT /note="Protein phosphatase 1 regulatory subunit 37"
FT /id="PRO_0000320939"
FT REPEAT 220..240
FT /note="LRR 1"
FT REPEAT 248..269
FT /note="LRR 2"
FT REPEAT 277..297
FT /note="LRR 3"
FT REPEAT 306..326
FT /note="LRR 4"
FT REPEAT 334..354
FT /note="LRR 5"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RYF1"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..473
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_031754"
FT VAR_SEQ 665..691
FT /note="ELSCSKNEKELEELLLEASQESGQETL -> GERGPRAGVEGPWVLYVTPGK
FT PLPVVGLSFPLFKMVLAGASKVGLSSHLHPASLGSWELFLGWGGM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_031755"
SQ SEQUENCE 691 AA; 74767 MW; 45578CC726B2063F CRC64;
MEIAPQEAPP VPGADGDIEE APAEAGSPSP ASPPADGRLK AAAKRVTFPS DEDIVSGAVE
PKDPWRHAQN VTVDEVIGAY KQACQKLNCR QIPKLLRQLQ EFTDLGHRLD CLDLKGEKLD
YKTCEALEEV FKRLQFKVVD LEQTNLDEDG ASALFDMIEY YESATHLNIS FNKHIGTRGW
QAAAHMMRKT SCLQYLDARN TPLLDHSAPF VARALRIRSS LAVLHLENAS LSGRPLMLLA
TALKMNMNLR ELYLADNKLN GLQDSAQLGN LLKFNCSLQI LDLRNNHVLD SGLAYICEGL
KEQRKGLVTL VLWNNQLTHT GMAFLGMTLP HTQSLETLNL GHNPIGNEGV RHLKNGLISN
RSVLRLGLAS TKLTCEGAVA VAEFIAESPR LLRLDLRENE IKTGGLMALS LALKVNHSLL
RLDLDREPKK EAVKSFIETQ KALLAEIQNG CKRNLVLARE REEKEQPPQL SASMPETTAT
EPQPDDEPAA GVQNGAPSPA PSPDSDSDSD SDGEEEEEEE GERDETPCPA LVPPTDSLGP
GDRSPPGSPS TPTEQRISVS SPGRGHKVFV VTRVESPPER AEPPASPTPP SPPPPPSPPA
SPSLPPAGAI DTRDTGSSEP QPPPEPPRSG PPLPNGLKPE FALALPPEPP PGPEVKGGSC
GLEHELSCSK NEKELEELLL EASQESGQET L
