PHAR3_HUMAN
ID PHAR3_HUMAN Reviewed; 559 AA.
AC Q96KR7; B1AKX0; B1AN68; B1AN69; B2RB46; Q32P33; Q707P6; Q9H4T4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phosphatase and actin regulator 3;
DE AltName: Full=Scaffold-associated PP1-inhibiting protein;
DE Short=Scapinin;
GN Name=PHACTR3; Synonyms=C20orf101, SCAPIN1;
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] (ISOFORMS 2 AND 3), AND INTERACTION WITH PP1CA.
RC TISSUE=Promyelocytic leukemia;
RX PubMed=12925532; DOI=10.1074/jbc.m305227200;
RA Sagara J., Higuchi T., Hattori Y., Moriya M., Sarvotham H., Shima H.,
RA Shirato H., Kikuchi K., Taniguchi S.;
RT "Scapinin, a putative protein phosphatase-1 regulatory subunit associated
RT with the nuclear nonchromatin structure.";
RL J. Biol. Chem. 278:45611-45619(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RA Worch S., Kussmann S., Hansmann I., Schlote D.;
RT "Structure and expression of scapinin in mouse and human.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, Hippocampus, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
CC -!- SUBUNIT: Binds actin and PPP1CA; thus inhibiting the protein
CC phosphatase 1 (PP1) activity.
CC -!- INTERACTION:
CC Q96KR7; Q96L46: CAPNS2; NbExp=3; IntAct=EBI-717068, EBI-12188723;
CC Q96KR7; O43169: CYB5B; NbExp=3; IntAct=EBI-717068, EBI-1058710;
CC Q96KR7; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-717068, EBI-11721828;
CC Q96KR7; P62140: PPP1CB; NbExp=3; IntAct=EBI-717068, EBI-352350;
CC Q96KR7; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-717068, EBI-2819725;
CC Q96KR7; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-717068, EBI-607755;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Note=Localized to the nuclear
CC matrix-intermediate filament scaffold. Isoform 2 is also found in some
CC cytoplasmic extensions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Scapinin 1B;
CC IsoId=Q96KR7-1; Sequence=Displayed;
CC Name=2; Synonyms=Scapinin-L, Scapinin 1C;
CC IsoId=Q96KR7-2; Sequence=VSP_009091;
CC Name=3; Synonyms=Scapinin-S;
CC IsoId=Q96KR7-3; Sequence=VSP_009091, VSP_009092;
CC Name=4;
CC IsoId=Q96KR7-4; Sequence=VSP_044546;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain. Also found in
CC several tumors such as lung carcinomas, nervous tumors and HL-60
CC leukemia cells. Isoform 3 is the major form in U-937, GOTO and HL-60
CC leukemia cells.
CC -!- INDUCTION: Down-regulated in HL-60 leukemia cells by RA, PMA and
CC dimethyl sulfoxide.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC67489.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB098521; BAC82348.1; -; mRNA.
DR EMBL; AB098522; BAC82349.1; -; mRNA.
DR EMBL; AJ311122; CAC67489.2; ALT_INIT; mRNA.
DR EMBL; AJ617581; CAF04087.1; -; mRNA.
DR EMBL; AK098788; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK314493; BAG37093.1; -; mRNA.
DR EMBL; AK316047; BAH14418.1; -; mRNA.
DR EMBL; AL121908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75428.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75429.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75430.1; -; Genomic_DNA.
DR EMBL; BC108303; AAI08304.1; -; mRNA.
DR EMBL; BC117362; AAI17363.1; -; mRNA.
DR EMBL; BC117364; AAI17365.1; -; mRNA.
DR CCDS; CCDS13480.1; -. [Q96KR7-1]
DR CCDS; CCDS13481.1; -. [Q96KR7-3]
DR CCDS; CCDS42895.1; -. [Q96KR7-2]
DR CCDS; CCDS56202.1; -. [Q96KR7-4]
DR RefSeq; NP_001186434.1; NM_001199505.1. [Q96KR7-4]
DR RefSeq; NP_001186435.1; NM_001199506.1. [Q96KR7-2]
DR RefSeq; NP_001268436.1; NM_001281507.1. [Q96KR7-2]
DR RefSeq; NP_542403.1; NM_080672.4. [Q96KR7-1]
DR RefSeq; NP_899067.1; NM_183244.1. [Q96KR7-2]
DR RefSeq; NP_899069.1; NM_183246.1. [Q96KR7-3]
DR RefSeq; XP_011526827.1; XM_011528525.2. [Q96KR7-2]
DR RefSeq; XP_016883115.1; XM_017027626.1. [Q96KR7-2]
DR RefSeq; XP_016883116.1; XM_017027627.1. [Q96KR7-2]
DR RefSeq; XP_016883118.1; XM_017027629.1. [Q96KR7-3]
DR RefSeq; XP_016883119.1; XM_017027630.1. [Q96KR7-3]
DR RefSeq; XP_016883120.1; XM_017027631.1. [Q96KR7-2]
DR AlphaFoldDB; Q96KR7; -.
DR SMR; Q96KR7; -.
DR BioGRID; 125483; 35.
DR IntAct; Q96KR7; 34.
DR MINT; Q96KR7; -.
DR STRING; 9606.ENSP00000360054; -.
DR iPTMnet; Q96KR7; -.
DR PhosphoSitePlus; Q96KR7; -.
DR BioMuta; PHACTR3; -.
DR DMDM; 38605426; -.
DR EPD; Q96KR7; -.
DR MassIVE; Q96KR7; -.
DR PaxDb; Q96KR7; -.
DR PeptideAtlas; Q96KR7; -.
DR PRIDE; Q96KR7; -.
DR ProteomicsDB; 3118; -.
DR ProteomicsDB; 77109; -. [Q96KR7-1]
DR ProteomicsDB; 77110; -. [Q96KR7-2]
DR ProteomicsDB; 77111; -. [Q96KR7-3]
DR Antibodypedia; 29289; 112 antibodies from 22 providers.
DR DNASU; 116154; -.
DR Ensembl; ENST00000355648.8; ENSP00000347866.4; ENSG00000087495.17. [Q96KR7-2]
DR Ensembl; ENST00000359926.7; ENSP00000353002.3; ENSG00000087495.17. [Q96KR7-4]
DR Ensembl; ENST00000361300.4; ENSP00000354555.4; ENSG00000087495.17. [Q96KR7-3]
DR Ensembl; ENST00000371015.6; ENSP00000360054.1; ENSG00000087495.17. [Q96KR7-1]
DR Ensembl; ENST00000395636.6; ENSP00000378998.2; ENSG00000087495.17. [Q96KR7-2]
DR Ensembl; ENST00000541461.5; ENSP00000442483.1; ENSG00000087495.17. [Q96KR7-2]
DR GeneID; 116154; -.
DR KEGG; hsa:116154; -.
DR MANE-Select; ENST00000371015.6; ENSP00000360054.1; NM_080672.5; NP_542403.1.
DR UCSC; uc002yat.3; human. [Q96KR7-1]
DR CTD; 116154; -.
DR DisGeNET; 116154; -.
DR GeneCards; PHACTR3; -.
DR HGNC; HGNC:15833; PHACTR3.
DR HPA; ENSG00000087495; Group enriched (brain, choroid plexus).
DR MIM; 608725; gene.
DR neXtProt; NX_Q96KR7; -.
DR OpenTargets; ENSG00000087495; -.
DR PharmGKB; PA128394750; -.
DR VEuPathDB; HostDB:ENSG00000087495; -.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000157562; -.
DR HOGENOM; CLU_015753_3_1_1; -.
DR InParanoid; Q96KR7; -.
DR OMA; SRPADEM; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; Q96KR7; -.
DR TreeFam; TF316316; -.
DR PathwayCommons; Q96KR7; -.
DR SignaLink; Q96KR7; -.
DR BioGRID-ORCS; 116154; 18 hits in 1073 CRISPR screens.
DR ChiTaRS; PHACTR3; human.
DR GeneWiki; PHACTR3; -.
DR GenomeRNAi; 116154; -.
DR Pharos; Q96KR7; Tbio.
DR PRO; PR:Q96KR7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96KR7; protein.
DR Bgee; ENSG00000087495; Expressed in cortical plate and 132 other tissues.
DR ExpressionAtlas; Q96KR7; baseline and differential.
DR Genevisible; Q96KR7; HS.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR029990; Phactr3.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF7; PTHR12751:SF7; 1.
DR Pfam; PF02755; RPEL; 1.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat.
FT CHAIN 1..559
FT /note="Phosphatase and actin regulator 3"
FT /id="PRO_0000126638"
FT REPEAT 93..118
FT /note="RPEL 1"
FT REPEAT 401..426
FT /note="RPEL 2"
FT REPEAT 439..464
FT /note="RPEL 3"
FT REPEAT 477..502
FT /note="RPEL 4"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..518
FT /note="Required for PP1CA binding and inhibition of PP1
FT activity"
FT COILED 346..369
FT /evidence="ECO:0000255"
FT COILED 450..486
FT /evidence="ECO:0000255"
FT COMPBIAS 11..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17693683"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYK5"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYK5"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12925532,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_009091"
FT VAR_SEQ 1..39
FT /note="MAASEDGSGCLVSRGRSQSDPSVLTDSSATSSADAGENP -> MRGRGGGRA
FT RCPAPLRSLLGAFGARDAAAAARDPAQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044546"
FT VAR_SEQ 181..250
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12925532"
FT /id="VSP_009092"
FT VARIANT 154
FT /note="P -> L (in dbSNP:rs2277759)"
FT /id="VAR_021969"
FT CONFLICT 62
FT /note="V -> M (in Ref. 3; AK098788)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="E -> G (in Ref. 3; AK098788)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="K -> R (in Ref. 2; CAF04087)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="K -> R (in Ref. 2; CAF04087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 62552 MW; E98182FBE3D25D37 CRC64;
MAASEDGSGC LVSRGRSQSD PSVLTDSSAT SSADAGENPD EMDQTPPARP EYLVSGIRTP
PVRRNSKLAT LGRIFKPWKW RKKKNEKLKQ TTSALEKKMA GRQGREELIK KGLLEMMEQD
AESKTCNPDG GPRSVQSEPP TPKSETLTSE DAQPGSPLAT GTDQVSLDKP LSSAAHLDDA
AKMPSASSGE EADAGSLLPT TNELSQALAG ADSLDSPPRP LERSVGQLPS PPLLPTPPPK
ASSKTTKNVT GQATLFQASS MKSADPSLRG QLSTPTGSPH LTTVHRPLPP SRVIEELHRA
LATKHRQDSF QGRESKGSPK KRLDVRLSRT SSVERGKERE EAWSFDGALE NKRTAAKESE
ENKENLIINS ELKDDLLLYQ DEEALNDSII SGTLPRKCKK ELLAVKLRNR PSKQELEDRN
IFPRRTDEER QEIRQQIEMK LSKRLSQRPA VEELERRNIL KQRNDQTEQE ERREIKQRLT
RKLNQRPTVD ELRDRKILIR FSDYVEVAKA QDYDRRADKP WTRLSAADKA AIRKELNEYK
SNEMEVHASS KHLTRFHRP
