ID PHAR4_HUMAN Reviewed; 702 AA. AC Q8IZ21; A2APK6; B9ZVW0; D3DPM3; Q68DD4; Q6NUN6; Q8N384; Q9H395; Q9H6X0; AC Q9H8W6; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Phosphatase and actin regulator 4; GN Name=PHACTR4; ORFNames=PRO2963; 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 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 271-702 (ISOFORM 1). 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Adrenal cortex, 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 365-702 (ISOFORM 1). RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., RA Gao F., Liu M., He F.; RT "Functional prediction of the coding sequences of 75 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, AND IDENTIFICATION BY RP 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-342; SER-344; RP THR-358; SER-427; THR-432 AND SER-628, AND IDENTIFICATION BY MASS RP 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, AND IDENTIFICATION BY RP 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-464 AND SER-628, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-131; SER-147; RP SER-291; SER-443; SER-464; SER-590 AND SER-628, AND IDENTIFICATION BY MASS RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, 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: Regulator of protein phosphatase 1 (PP1) required for neural CC tube and optic fissure closure, and enteric neural crest cell (ENCCs) CC migration during development. Acts as an activator of PP1 by CC interacting with PPP1CA and preventing phosphorylation of PPP1CA at CC 'Thr-320'. During neural tube closure, localizes to the ventral neural CC tube and activates PP1, leading to down-regulate cell proliferation CC within cranial neural tissue and the neural retina. Also acts as a CC regulator of migration of enteric neural crest cells (ENCCs) by CC activating PP1, leading to dephosphorylation and subsequent activation CC of cofilin (COF1 or COF2) and repression of the integrin signaling CC through the RHO/ROCK pathway (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Binds PPP1CA and actin. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, CC lamellipodium {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8IZ21-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IZ21-2; Sequence=VSP_025437; CC Name=3; CC IsoId=Q8IZ21-3; Sequence=VSP_025436; CC Name=4; CC IsoId=Q8IZ21-4; Sequence=VSP_039730, VSP_039731; CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG35507.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH68508.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC Sequence=BAB14483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15130.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAH18286.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK023233; BAB14483.1; ALT_INIT; mRNA. DR EMBL; AK025436; BAB15130.1; ALT_FRAME; mRNA. DR EMBL; CR749449; CAH18286.1; ALT_FRAME; mRNA. DR EMBL; AL360012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL670471; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR391992; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR589951; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07696.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07698.1; -; Genomic_DNA. DR EMBL; BC021247; AAH21247.3; -; mRNA. DR EMBL; BC029266; AAH29266.1; -; mRNA. DR EMBL; BC068508; AAH68508.1; ALT_SEQ; mRNA. DR EMBL; AF130081; AAG35507.1; ALT_INIT; mRNA. DR CCDS; CCDS41293.1; -. [Q8IZ21-1] DR CCDS; CCDS41294.1; -. [Q8IZ21-2] DR RefSeq; NP_001041648.1; NM_001048183.1. [Q8IZ21-1] DR RefSeq; NP_076412.3; NM_023923.3. [Q8IZ21-2] DR RefSeq; XP_016857657.1; XM_017002168.1. DR RefSeq; XP_016857662.1; XM_017002173.1. DR AlphaFoldDB; Q8IZ21; -. DR SMR; Q8IZ21; -. DR BioGRID; 122429; 113. DR DIP; DIP-47323N; -. DR IntAct; Q8IZ21; 44. DR MINT; Q8IZ21; -. DR STRING; 9606.ENSP00000362942; -. DR GlyCosmos; Q8IZ21; 5 sites, 1 glycan. DR GlyGen; Q8IZ21; 12 sites, 1 O-linked glycan (12 sites). DR iPTMnet; Q8IZ21; -. DR PhosphoSitePlus; Q8IZ21; -. DR BioMuta; PHACTR4; -. DR DMDM; 74728415; -. DR EPD; Q8IZ21; -. DR jPOST; Q8IZ21; -. DR MassIVE; Q8IZ21; -. DR MaxQB; Q8IZ21; -. DR PaxDb; 9606-ENSP00000362942; -. DR PeptideAtlas; Q8IZ21; -. DR ProteomicsDB; 71271; -. [Q8IZ21-1] DR ProteomicsDB; 71272; -. [Q8IZ21-2] DR ProteomicsDB; 71273; -. [Q8IZ21-3] DR ProteomicsDB; 71274; -. [Q8IZ21-4] DR Pumba; Q8IZ21; -. DR Antibodypedia; 30935; 133 antibodies from 27 providers. DR DNASU; 65979; -. DR Ensembl; ENST00000373836.4; ENSP00000362942.3; ENSG00000204138.13. [Q8IZ21-2] DR Ensembl; ENST00000373839.8; ENSP00000362945.3; ENSG00000204138.13. [Q8IZ21-1] DR Ensembl; ENST00000493669.2; ENSP00000488359.1; ENSG00000204138.13. [Q8IZ21-4] DR GeneID; 65979; -. DR KEGG; hsa:65979; -. DR MANE-Select; ENST00000373839.8; ENSP00000362945.3; NM_001048183.3; NP_001041648.1. DR UCSC; uc001bpw.4; human. [Q8IZ21-1] DR AGR; HGNC:25793; -. DR CTD; 65979; -. DR DisGeNET; 65979; -. DR GeneCards; PHACTR4; -. DR HGNC; HGNC:25793; PHACTR4. DR HPA; ENSG00000204138; Low tissue specificity. DR MIM; 608726; gene. DR neXtProt; NX_Q8IZ21; -. DR OpenTargets; ENSG00000204138; -. DR PharmGKB; PA134959472; -. DR VEuPathDB; HostDB:ENSG00000204138; -. DR eggNOG; KOG4339; Eukaryota. DR GeneTree; ENSGT00940000157582; -. DR HOGENOM; CLU_015753_1_1_1; -. DR InParanoid; Q8IZ21; -. DR OMA; XKNEADR; -. DR OrthoDB; 2882458at2759; -. DR PhylomeDB; Q8IZ21; -. DR TreeFam; TF316316; -. DR PathwayCommons; Q8IZ21; -. DR SignaLink; Q8IZ21; -. DR BioGRID-ORCS; 65979; 17 hits in 1156 CRISPR screens. DR ChiTaRS; PHACTR4; human. DR GenomeRNAi; 65979; -. DR Pharos; Q8IZ21; Tbio. DR PRO; PR:Q8IZ21; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8IZ21; Protein. DR Bgee; ENSG00000204138; Expressed in pharyngeal mucosa and 196 other cell types or tissues. DR ExpressionAtlas; Q8IZ21; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0008157; F:protein phosphatase 1 binding; ISS:UniProtKB. DR GO; GO:0072542; F:protein phosphatase activator activity; ISS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0061386; P:closure of optic fissure; ISS:UniProtKB. DR GO; GO:0048484; P:enteric nervous system development; ISS:UniProtKB. DR GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB. DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB. DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB. DR Gene3D; 6.10.140.1750; -; 1. DR Gene3D; 6.10.140.2130; -; 1. DR InterPro; IPR004018; RPEL_repeat. DR PANTHER; PTHR12751:SF4; PHOSPHATASE AND ACTIN REGULATOR 4; 1. DR PANTHER; PTHR12751; PHOSPHATASE AND ACTIN REGULATOR PHACTR; 1. DR Pfam; PF02755; RPEL; 3. DR SMART; SM00707; RPEL; 3. DR PROSITE; PS51073; RPEL; 3. DR Genevisible; Q8IZ21; HS. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Cell projection; Cytoplasm; KW Developmental protein; Neurogenesis; Phosphoprotein; Reference proteome; KW Repeat. FT CHAIN 1..702 FT /note="Phosphatase and actin regulator 4" FT /id="PRO_0000287306" FT REPEAT 63..88 FT /note="RPEL 1" FT REPEAT 583..608 FT /note="RPEL 2" FT REPEAT 621..646 FT /note="RPEL 3" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 72..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 222..363 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 592..615 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..94 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 127..145 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 178..194 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..251 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 254..268 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..288 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 303..317 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..363 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 504..521 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501J7" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 270 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501J7" FT MOD_RES 291 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 358 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 432 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 453 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501J7" FT MOD_RES 464 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 514 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501J7" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501J7" FT MOD_RES 557 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 590 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 628 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..16 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_025436" FT VAR_SEQ 1..5 FT /note="MEDPF -> MGQADVSRPVNPDAV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_025437" FT VAR_SEQ 6 FT /note="E -> DFSREPWNSRGSRPAHYRARHGPGQCGSRRHNTSYQKEEQVLRLWQD FT LQALEMEEKKK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_039730" FT VAR_SEQ 7..702 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_039731" FT CONFLICT 183 FT /note="E -> G (in Ref. 2; CAH18286)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="L -> P (in Ref. 1; BAB14483)" FT /evidence="ECO:0000305" SQ SEQUENCE 702 AA; 78211 MW; 89AC6A1D08411948 CRC64; MEDPFEEADQ PTTEPGMVLD SVEAGDTTPP TKRKSKFSGF GKIFKPWKWR KKKSSDKFKE TSEVLERKIS MRKPREELVK RGVLLEDPEQ GGEDPGKPSD AMLKNGHTTP IGNARSSSPV QVEEEPVRLA SLRKAIPEED LKKRLGSTGS QPNSEAESVP ENVPKPPLLP PKRPLSSSHE ASEGQAKDAT SSGGTARFII STSITTAPAA TTAATSLAKT VNLSVTPSPA PRTLPAAPAS TNTTATPSLT HMVPAKQPPI PPPKPAHRNS NPVIAELSQA INSGTLLSKP SPPLPPKRGI PSTSVPTLES AAAITTKTPS DEREKSTCSM GSELLPMISP RSPSPPLPTH IPPEPPRTPP FPAKTFQVVP EIEFPPSLDL HQEIPQQEDQ KKEVPKRILD QNFGEPHIPS RLPPLPLHIR IQQALTSPLP MTPILEGSHR AHSLLFENSD SFSEDSSTLG RTRSLPITIE MLKVPDDEEE EEQTCPSTFS EEMTPTSVIP KLPQCLREEE EKESDSDSEG PIQYRDEEDE DESYQSALAN KVKRKDTLAM KLNHRPSEPE LNLNSWPCKS KEEWNEIRHQ IGNTLIRRLS QRPTPEELEQ RNILQPKNEA DRQAEKREIK RRLTRKLSQR PTVAELLARK ILRFNEYVEV TDAQDYDRRA DKPWTKLTPA DKAAIRKELN EFKSSEMEVH EESKHFTRYH RP //