PP6R1_HUMAN
ID PP6R1_HUMAN Reviewed; 881 AA.
AC Q9UPN7; Q2M2H3; Q504V2; Q6NVJ6; Q9BU97;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 5.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 1;
DE AltName: Full=SAPS domain family member 1;
GN Name=PPP6R1; Synonyms=KIAA1115, PP6R1, SAPS1;
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].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, Skin, and 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP FUNCTION, INTERACTION WITH PPP6C AND NFKBIE, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16769727; DOI=10.1074/jbc.m601772200;
RA Stefansson B., Brautigan D.L.;
RT "Protein phosphatase 6 subunit with conserved Sit4-associated protein
RT domain targets IkappaBepsilon.";
RL J. Biol. Chem. 281:22624-22634(2006).
RN [6]
RP INTERACTION WITH PPP6C; ANKRD28; ANKRD44 AND ANKRD52, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18186651; DOI=10.1021/bi7022877;
RA Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.;
RT "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat
RT domains.";
RL Biochemistry 47:1442-1451(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638 AND SER-759, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-638; SER-702;
RP SER-726 AND SER-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-524; SER-635 AND SER-638, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-530 AND SER-531, AND
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. Involved in the PP6-mediated
CC dephosphorylation of NFKBIE opposing its degradation in response to
CC TNF-alpha. {ECO:0000269|PubMed:16769727}.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
CC heterotrimeric complex formed of the catalytic subunit, a SAPS domain-
CC containing subunit (PP6R) and an ankyrin repeat-domain containing
CC regulatory subunit (ARS). Interacts with PPP6C and NFKBIE. Interacts
CC with ANKRD28, ANKRD44 and ANKRD52. {ECO:0000269|PubMed:16769727,
CC ECO:0000269|PubMed:18186651}.
CC -!- INTERACTION:
CC Q9UPN7; O15084: ANKRD28; NbExp=10; IntAct=EBI-359745, EBI-359567;
CC Q9UPN7; Q8N8A2: ANKRD44; NbExp=4; IntAct=EBI-359745, EBI-1245329;
CC Q9UPN7; Q8NB46: ANKRD52; NbExp=4; IntAct=EBI-359745, EBI-1996119;
CC Q9UPN7; O00221: NFKBIE; NbExp=2; IntAct=EBI-359745, EBI-355098;
CC Q9UPN7; O00743: PPP6C; NbExp=12; IntAct=EBI-359745, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727,
CC ECO:0000269|PubMed:18186651}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in testis.
CC {ECO:0000269|PubMed:16769727}.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83067.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB029038; BAA83067.3; ALT_INIT; mRNA.
DR EMBL; BC002799; AAH02799.2; -; mRNA.
DR EMBL; BC068014; AAH68014.1; -; mRNA.
DR EMBL; BC094753; AAH94753.2; -; mRNA.
DR CCDS; CCDS46186.1; -.
DR RefSeq; NP_055746.3; NM_014931.3.
DR AlphaFoldDB; Q9UPN7; -.
DR SMR; Q9UPN7; -.
DR BioGRID; 116537; 169.
DR CORUM; Q9UPN7; -.
DR DIP; DIP-27589N; -.
DR IntAct; Q9UPN7; 86.
DR MINT; Q9UPN7; -.
DR STRING; 9606.ENSP00000414202; -.
DR ChEMBL; CHEMBL4105774; -.
DR GlyGen; Q9UPN7; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPN7; -.
DR PhosphoSitePlus; Q9UPN7; -.
DR BioMuta; PPP6R1; -.
DR DMDM; 261260102; -.
DR EPD; Q9UPN7; -.
DR jPOST; Q9UPN7; -.
DR MassIVE; Q9UPN7; -.
DR MaxQB; Q9UPN7; -.
DR PaxDb; Q9UPN7; -.
DR PeptideAtlas; Q9UPN7; -.
DR PRIDE; Q9UPN7; -.
DR ProteomicsDB; 85391; -.
DR Antibodypedia; 33046; 67 antibodies from 20 providers.
DR DNASU; 22870; -.
DR Ensembl; ENST00000412770.7; ENSP00000414202.1; ENSG00000105063.19.
DR Ensembl; ENST00000587283.5; ENSP00000467521.1; ENSG00000105063.19.
DR GeneID; 22870; -.
DR KEGG; hsa:22870; -.
DR MANE-Select; ENST00000412770.7; ENSP00000414202.1; NM_014931.4; NP_055746.3.
DR UCSC; uc002qjw.5; human.
DR CTD; 22870; -.
DR DisGeNET; 22870; -.
DR GeneCards; PPP6R1; -.
DR HGNC; HGNC:29195; PPP6R1.
DR HPA; ENSG00000105063; Low tissue specificity.
DR MIM; 610875; gene.
DR neXtProt; NX_Q9UPN7; -.
DR OpenTargets; ENSG00000105063; -.
DR PharmGKB; PA165394108; -.
DR VEuPathDB; HostDB:ENSG00000105063; -.
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR HOGENOM; CLU_012598_0_0_1; -.
DR InParanoid; Q9UPN7; -.
DR OMA; NAEQGPN; -.
DR OrthoDB; 329232at2759; -.
DR PhylomeDB; Q9UPN7; -.
DR TreeFam; TF313227; -.
DR PathwayCommons; Q9UPN7; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR SignaLink; Q9UPN7; -.
DR BioGRID-ORCS; 22870; 19 hits in 1080 CRISPR screens.
DR ChiTaRS; PPP6R1; human.
DR GenomeRNAi; 22870; -.
DR Pharos; Q9UPN7; Tbio.
DR PRO; PR:Q9UPN7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UPN7; protein.
DR Bgee; ENSG00000105063; Expressed in left testis and 96 other tissues.
DR ExpressionAtlas; Q9UPN7; baseline and differential.
DR Genevisible; Q9UPN7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..881
FT /note="Serine/threonine-protein phosphatase 6 regulatory
FT subunit 1"
FT /id="PRO_0000046096"
FT REGION 10..403
FT /note="Interaction with PPP6C"
FT REGION 621..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..686
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TSI3"
FT MOD_RES 524
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TSI3"
SQ SEQUENCE 881 AA; 96724 MW; 36DDA2E945ED599A CRC64;
MFWKFDLHTS SHLDTLLERE DLSLPELLDE EDVLQECKVV NRKLLDFLLQ PPHLQAMVAW
VTQEPPDSGE ERLRYKYPSV ACEILTSDVP QINDALGADE SLLNRLYGFL QSTGSLNPLL
ASFFSKVMGI LINRKTDQLV SFLRKKDDFV DLLLQHIGTS AIMDLLLRLL TCVERPQLRQ
DVVNWLNEEK IVQRLIEQIH PSKDENQHSN ASQSLCDIIR LSREQMIQVQ DSPEPDQLLA
TLEKQETIEQ LLSNMFEGEQ SQSVIVSGIQ VLLTLLEPRR PRSESVTVNS FFSSVDGQLE
LLAQGALEST VSSVGALHAL RPRLSCFHQL LLEPPKLEPL QMTWGMLAPP LGNTRLHVVK
LLASALSAND AALTHELLAL DVPNTMLDLF FHYVFNNFLH AQVEGCVSTM LSLGPPPDSS
PETPIQNPVV KHLLQQCRLV ERILTSWEEN DRVQCAGGPR KGYMGHLTRV AGALVQNTEK
GPNAEQLRQL LKELPSEQQE QWEAFVSGPL AETNKKNMVD LVNTHHLHSS SDDEDDRLKE
FNFPEEAVLQ QAFMDFQMQR MTSAFIDHFG FNDEEFGEQE ESVNAPFDKT ANITFSLNAD
DENPNANLLE ICYKDRIQQF DDDEEEEDEE EAQGSGESDG EDGAWQGSQL ARGARLGQPP
GVRSGGSTDS EDEEEEDEEE EEDEEGIGCA ARGGATPLSY PSPGPQPPGP SWTATFDPVP
TDAPTSPRVS GEEELHTGPP APQGPLSVPQ GLPTQSLASP PARDALQLRS QDPTPPSAPQ
EATEGSKVTE PSAPCQALVS IGDLQATFHG IRSAPSSSDS ATRDPSTSVP ASGAHQPPQT
TEGEKSPEPL GLPQSQSAQA LTPPPIPNGS APEGPASPGS Q
