PP16B_HUMAN
ID PP16B_HUMAN Reviewed; 567 AA.
AC Q96T49; A2RRR6; E9PFS8; O94912; Q5W9G4; Q9NQG4;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein phosphatase 1 regulatory inhibitor subunit 16B;
DE AltName: Full=Ankyrin repeat domain-containing protein 4;
DE AltName: Full=CAAX box protein TIMAP;
DE AltName: Full=TGF-beta-inhibited membrane-associated protein;
DE Short=hTIMAP;
DE Flags: Precursor;
GN Name=PPP1R16B; Synonyms=ANKRD4, KIAA0823;
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 [MRNA] (ISOFORM 1).
RX PubMed=12055102; DOI=10.1152/ajpcell.00442.2001;
RA Cao W., Mattagajasingh S.N., Xu H., Kim K., Fierlbeck W., Deng J.,
RA Lowenstein C.J., Ballermann B.J.;
RT "TIMAP, a novel CAAX box protein regulated by TGF-beta1 and expressed in
RT endothelial cells.";
RL Am. J. Physiol. 283:C327-C337(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-525 (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT "Alternative splice variants encoding unstable protein domains exist in the
RT human brain.";
RL J. Mol. Biol. 343:1207-1220(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1CA AND RPSA.
RX PubMed=16263087; DOI=10.1016/j.bbrc.2005.10.089;
RA Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.;
RT "The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 338:1327-1334(2005).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP PPP1CB AND MSN.
RX PubMed=18586956; DOI=10.1152/ajplung.00325.2007;
RA Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G.,
RA Verin A.D.;
RT "TIMAP is a positive regulator of pulmonary endothelial barrier function.";
RL Am. J. Physiol. 295:L440-L450(2008).
RN [10]
RP INDUCTION BY LPS.
RX PubMed=21907835; DOI=10.1016/j.resp.2011.08.012;
RA Poirier C., Gorshkov B.A., Zemskova M.A., Bogatcheva N.V., Verin A.D.;
RT "TIMAP protects endothelial barrier from LPS-induced vascular leakage and
RT is down-regulated by LPS.";
RL Respir. Physiol. Neurobiol. 179:334-337(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-476, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTEN.
RX PubMed=25007873; DOI=10.1152/ajprenal.00070.2014;
RA Obeidat M., Li L., Ballermann B.J.;
RT "TIMAP promotes angiogenesis by suppressing PTEN-mediated Akt inhibition in
RT human glomerular endothelial cells.";
RL Am. J. Physiol. 307:F623-F633(2014).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EEF1A1, AND MUTAGENESIS OF
RP GLY-252.
RX PubMed=26497934; DOI=10.1016/j.biocel.2015.10.021;
RA Boratko A., Peter M., Thalwieser Z., Kovacs E., Csortos C.;
RT "Elongation factor-1A1 is a novel substrate of the protein phosphatase 1-
RT TIMAP complex.";
RL Int. J. Biochem. Cell Biol. 69:105-113(2015).
CC -!- FUNCTION: Regulator of protein phosphatase 1 (PP1) that acts as a
CC positive regulator of pulmonary endothelial cell (EC) barrier function
CC (PubMed:18586956). Involved in the regulation of the PI3K/AKT signaling
CC pathway, angiogenesis and endothelial cell proliferation
CC (PubMed:25007873). Regulates angiogenesis and endothelial cell
CC proliferation through the control of ECE1 dephosphorylation,
CC trafficking and activity (By similarity). Protects the endothelial
CC barrier from lipopolysaccharide (LPS)-induced vascular leakage (By
CC similarity). Involved in the regulation of endothelial cell filopodia
CC extension (By similarity). May be a downstream target for TGF-beta1
CC signaling cascade in endothelial cells (PubMed:16263087,
CC PubMed:18586956). Involved in PKA-mediated moesin dephosphorylation
CC which is important in EC barrier protection against thrombin
CC stimulation (PubMed:18586956). Promotes the interaction of PPP1CA with
CC RPSA/LAMR1 and in turn facilitates the dephosphorylation of RPSA/LAMR1
CC (PubMed:16263087). Involved in the dephosphorylation of EEF1A1
CC (PubMed:26497934). {ECO:0000250|UniProtKB:Q8VHQ3,
CC ECO:0000250|UniProtKB:Q95N27, ECO:0000269|PubMed:16263087,
CC ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:25007873,
CC ECO:0000269|PubMed:26497934}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and MSN. Interacts (via its
CC fourth ankyrin repeat) with the mature dimeric form of RPSA/LAMR1
CC (PubMed:16263087, PubMed:18586956). Interacts with EEF1A1
CC (PubMed:26497934). Interacts with PTEN (PubMed:25007873). Interacts
CC with ECE1 (By similarity). {ECO:0000250|UniProtKB:Q95N27,
CC ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:18586956,
CC ECO:0000269|PubMed:25007873, ECO:0000269|PubMed:26497934}.
CC -!- INTERACTION:
CC Q96T49; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-10293968, EBI-1166928;
CC Q96T49; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-10293968, EBI-5278764;
CC Q96T49; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-10293968, EBI-747776;
CC Q96T49; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10293968, EBI-739624;
CC Q96T49; O43186: CRX; NbExp=4; IntAct=EBI-10293968, EBI-748171;
CC Q96T49; Q92997: DVL3; NbExp=3; IntAct=EBI-10293968, EBI-739789;
CC Q96T49; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-10293968, EBI-1384254;
CC Q96T49; O95363: FARS2; NbExp=3; IntAct=EBI-10293968, EBI-2513774;
CC Q96T49; Q4VC44: FLYWCH1; NbExp=3; IntAct=EBI-10293968, EBI-719415;
CC Q96T49; P14136: GFAP; NbExp=3; IntAct=EBI-10293968, EBI-744302;
CC Q96T49; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10293968, EBI-618309;
CC Q96T49; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-10293968, EBI-11956675;
CC Q96T49; O43464: HTRA2; NbExp=3; IntAct=EBI-10293968, EBI-517086;
CC Q96T49; P42858: HTT; NbExp=3; IntAct=EBI-10293968, EBI-466029;
CC Q96T49; Q9UKT9: IKZF3; NbExp=7; IntAct=EBI-10293968, EBI-747204;
CC Q96T49; Q7L273: KCTD9; NbExp=3; IntAct=EBI-10293968, EBI-4397613;
CC Q96T49; P61326: MAGOH; NbExp=3; IntAct=EBI-10293968, EBI-299134;
CC Q96T49; Q8IVT2: MISP; NbExp=3; IntAct=EBI-10293968, EBI-2555085;
CC Q96T49; I6L9F6: NEFL; NbExp=3; IntAct=EBI-10293968, EBI-10178578;
CC Q96T49; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-10293968, EBI-11022007;
CC Q96T49; Q8IXK0: PHC2; NbExp=4; IntAct=EBI-10293968, EBI-713786;
CC Q96T49; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-10293968, EBI-12014286;
CC Q96T49; P62136: PPP1CA; NbExp=4; IntAct=EBI-10293968, EBI-357253;
CC Q96T49; P62140: PPP1CB; NbExp=5; IntAct=EBI-10293968, EBI-352350;
CC Q96T49; P41219: PRPH; NbExp=3; IntAct=EBI-10293968, EBI-752074;
CC Q96T49; P40937: RFC5; NbExp=3; IntAct=EBI-10293968, EBI-712376;
CC Q96T49; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-10293968, EBI-748391;
CC Q96T49; Q15427: SF3B4; NbExp=4; IntAct=EBI-10293968, EBI-348469;
CC Q96T49; Q92529: SHC3; NbExp=3; IntAct=EBI-10293968, EBI-79084;
CC Q96T49; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-10293968, EBI-747797;
CC Q96T49; O75478: TADA2A; NbExp=3; IntAct=EBI-10293968, EBI-742268;
CC Q96T49; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-10293968, EBI-10172380;
CC Q96T49; Q99757: TXN2; NbExp=3; IntAct=EBI-10293968, EBI-2932492;
CC Q96T49; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-10293968, EBI-11741890;
CC Q96T49; Q8TBZ8: ZNF564; NbExp=4; IntAct=EBI-10293968, EBI-10273713;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18586956,
CC ECO:0000269|PubMed:26497934}. Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Nucleus {ECO:0000269|PubMed:18586956}. Cell projection
CC {ECO:0000269|PubMed:25007873}. Note=Colocalizes with RPSA/LAMR1 in the
CC cell membrane (PubMed:16263087). Localizes to the perinuclear region
CC (By similarity). Colocalizes with PTEN at the tip of EC projections
CC (PubMed:25007873). {ECO:0000250|UniProtKB:Q95N27,
CC ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:25007873}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96T49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96T49-2; Sequence=VSP_047508;
CC -!- INDUCTION: Inhibited by TGFB1 (Probable). Down-regulated by LPS
CC (PubMed:21907835). {ECO:0000269|PubMed:21907835, ECO:0000305}.
CC -!- PTM: Phosphorylated by PKA and, after PKA priming, by GSK3B.
CC Phosphorylation by GSK3B reduces its association with PP1C and enhances
CC PP1C activity. Dephosphorylation by its associated PP1C results in
CC enhanced association with PP1C, but reduced PP1C activity (By
CC similarity). {ECO:0000250|UniProtKB:Q95N27}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74846.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF362910; AAK52796.1; -; mRNA.
DR EMBL; AB020630; BAA74846.2; ALT_INIT; mRNA.
DR EMBL; AL023803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76009.1; -; Genomic_DNA.
DR EMBL; BC131801; AAI31802.1; -; mRNA.
DR EMBL; BC152467; AAI52468.1; -; mRNA.
DR EMBL; AB177855; BAD66833.1; -; mRNA.
DR CCDS; CCDS13309.1; -. [Q96T49-1]
DR CCDS; CCDS54462.1; -. [Q96T49-2]
DR RefSeq; NP_001166206.1; NM_001172735.2. [Q96T49-2]
DR RefSeq; NP_056383.1; NM_015568.3. [Q96T49-1]
DR AlphaFoldDB; Q96T49; -.
DR SMR; Q96T49; -.
DR BioGRID; 117514; 65.
DR ELM; Q96T49; -.
DR IntAct; Q96T49; 59.
DR MINT; Q96T49; -.
DR STRING; 9606.ENSP00000299824; -.
DR iPTMnet; Q96T49; -.
DR PhosphoSitePlus; Q96T49; -.
DR SwissPalm; Q96T49; -.
DR BioMuta; PPP1R16B; -.
DR DMDM; 22256977; -.
DR MassIVE; Q96T49; -.
DR MaxQB; Q96T49; -.
DR PaxDb; Q96T49; -.
DR PeptideAtlas; Q96T49; -.
DR PRIDE; Q96T49; -.
DR ProteomicsDB; 20168; -.
DR ProteomicsDB; 78183; -. [Q96T49-1]
DR Antibodypedia; 26914; 157 antibodies from 23 providers.
DR DNASU; 26051; -.
DR Ensembl; ENST00000299824.6; ENSP00000299824.1; ENSG00000101445.10. [Q96T49-1]
DR Ensembl; ENST00000373331.2; ENSP00000362428.1; ENSG00000101445.10. [Q96T49-2]
DR GeneID; 26051; -.
DR KEGG; hsa:26051; -.
DR MANE-Select; ENST00000299824.6; ENSP00000299824.1; NM_015568.4; NP_056383.1.
DR UCSC; uc002xje.3; human. [Q96T49-1]
DR CTD; 26051; -.
DR DisGeNET; 26051; -.
DR GeneCards; PPP1R16B; -.
DR HGNC; HGNC:15850; PPP1R16B.
DR HPA; ENSG00000101445; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 613275; gene.
DR neXtProt; NX_Q96T49; -.
DR OpenTargets; ENSG00000101445; -.
DR PharmGKB; PA33635; -.
DR VEuPathDB; HostDB:ENSG00000101445; -.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000154090; -.
DR HOGENOM; CLU_000134_54_2_1; -.
DR InParanoid; Q96T49; -.
DR OMA; ISPDLCN; -.
DR OrthoDB; 564568at2759; -.
DR PhylomeDB; Q96T49; -.
DR TreeFam; TF316803; -.
DR PathwayCommons; Q96T49; -.
DR SignaLink; Q96T49; -.
DR BioGRID-ORCS; 26051; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; PPP1R16B; human.
DR GenomeRNAi; 26051; -.
DR Pharos; Q96T49; Tbio.
DR PRO; PR:Q96T49; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96T49; protein.
DR Bgee; ENSG00000101445; Expressed in CA1 field of hippocampus and 177 other tissues.
DR Genevisible; Q96T49; HS.
DR GO; GO:0042995; C:cell projection; IDA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0017020; F:myosin phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:GO_Central.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:GO_Central.
DR GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IMP:GO_Central.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:GO_Central.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:GO_Central.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:GO_Central.
DR GO; GO:0035304; P:regulation of protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017417; Pase-1_reg_su_16AB.
DR Pfam; PF12796; Ank_2; 2.
DR PIRSF; PIRSF038159; PP1_16AB_vert; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Cell projection;
KW Coiled coil; Lipoprotein; Membrane; Methylation; Nucleus; Palmitate;
KW Phosphoprotein; Prenylation; Reference proteome; Repeat.
FT CHAIN 1..564
FT /note="Protein phosphatase 1 regulatory inhibitor subunit
FT 16B"
FT /id="PRO_0000067043"
FT PROPEP 565..567
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000396710"
FT REPEAT 100..129
FT /note="ANK 1"
FT REPEAT 133..162
FT /note="ANK 2"
FT REPEAT 228..257
FT /note="ANK 3"
FT REPEAT 261..290
FT /note="ANK 4"
FT REPEAT 530..559
FT /note="ANK 5"
FT REGION 378..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..55
FT /evidence="ECO:0000255"
FT COMPBIAS 381..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHQ3"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q95N27"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q95N27"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 564
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q923M0"
FT LIPID 563
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q923M0"
FT LIPID 564
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q923M0"
FT VAR_SEQ 233..274
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15491607"
FT /id="VSP_047508"
FT MUTAGEN 252
FT /note="G->A: Strongly decreased interaction with EEF1A1."
FT /evidence="ECO:0000269|PubMed:26497934"
SQ SEQUENCE 567 AA; 63551 MW; 8418CE26D0035CF1 CRC64;
MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLQHRKRK HERKRSTGGR
RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL
LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL
DVIETCMAYQ GITQEKINEM RVAPEQQMIA DIHCMIAAGQ DLDWIDAQGA TLLHIAGANG
YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMQMAEL LVSHGASLSA RTSMDEMPID
LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK
EYEGEAILWQ RSAAEDQRTS TYNGDIRETR TDQENKDPNP RLEKPVLLSE FPTKIPRGEL
DMPVENGLRA PVSAYQYALA NGDVWKVHEV PDYSMAYGNP GVADATPPWS SYKEQSPQTL
LELKRQRAAA KLLSHPFLST HLGSSMARTG ESSSEGKAPL IGGRTSPYSS NGTSVYYTVT
SGDPPLLKFK APIEEMEEKV HGCCRIS
