PHAR1_HUMAN
ID PHAR1_HUMAN Reviewed; 580 AA.
AC Q9C0D0; A8K1V2; Q3MJ93; Q5JSJ2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatase and actin regulator 1;
GN Name=PHACTR1; Synonyms=KIAA1733, RPEL1;
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=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, and Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=21798305; DOI=10.1016/j.biochi.2011.07.010;
RA Jarray R., Allain B., Borriello L., Biard D., Loukaci A., Larghero J.,
RA Hadj-Slimane R., Garbay C., Lepelletier Y., Raynaud F.;
RT "Depletion of the novel protein PHACTR-1 from human endothelial cells
RT abolishes tube formation and induces cell death receptor apoptosis.";
RL Biochimie 93:1668-1675(2011).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21939755; DOI=10.1016/j.cellsig.2011.09.003;
RA Allain B., Jarray R., Borriello L., Leforban B., Dufour S., Liu W.Q.,
RA Pamonsinlapatham P., Bianco S., Larghero J., Hadj-Slimane R., Garbay C.,
RA Raynaud F., Lepelletier Y.;
RT "Neuropilin-1 regulates a new VEGF-induced gene, Phactr-1, which controls
RT tubulogenesis and modulates lamellipodial dynamics in human endothelial
RT cells.";
RL Cell. Signal. 24:214-223(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 AND SER-505, 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 [8]
RP INVOLVEMENT IN DEE70, VARIANTS DEE70 ILE-479 AND PRO-500, AND
RP CHARACTERIZATION OF VARIANTS DEE70 ILE-479; PRO-500 AND CYS-521.
RX PubMed=30256902; DOI=10.1093/brain/awy246;
RA Hamada N., Ogaya S., Nakashima M., Nishijo T., Sugawara Y., Iwamoto I.,
RA Ito H., Maki Y., Shirai K., Baba S., Maruyama K., Saitsu H., Kato M.,
RA Matsumoto N., Momiyama T., Nagata K.I.;
RT "De novo PHACTR1 mutations in West syndrome and their pathophysiological
RT effects.";
RL Brain 141:3098-3114(2018).
RN [9]
RP VARIANT DEE70 CYS-521.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Binds actin monomers (G actin) and plays a role in multiple
CC processes including the regulation of actin cytoskeleton dynamics,
CC actin stress fibers formation, cell motility and survival, formation of
CC tubules by endothelial cells, and regulation of PPP1CA activity
CC (PubMed:21798305, PubMed:21939755). Involved in the regulation of
CC cortical neuron migration and dendrite arborization (By similarity).
CC {ECO:0000250|UniProtKB:Q2M3X8, ECO:0000269|PubMed:21798305,
CC ECO:0000269|PubMed:21939755}.
CC -!- SUBUNIT: Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and
CC PPP1CA compete for the same binding site.
CC -!- INTERACTION:
CC Q9C0D0; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-7971325, EBI-725606;
CC Q9C0D0; Q9HC52: CBX8; NbExp=3; IntAct=EBI-7971325, EBI-712912;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}.
CC Nucleus {ECO:0000250}. Note=Enriched at synapses (By similarity).
CC Cytoplasmic in resting cells, and is imported into the nucleus upon
CC serum stimulation. Interaction with actin prevents nuclear import (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0D0-2; Sequence=VSP_018529, VSP_018530;
CC -!- TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells.
CC {ECO:0000269|PubMed:21939755}.
CC -!- INDUCTION: Up-regulated by VEGFA. {ECO:0000269|PubMed:21798305,
CC ECO:0000269|PubMed:21939755}.
CC -!- DOMAIN: Binds three actin monomers via the three C-terminal RPEL
CC repeats. {ECO:0000250}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 70 (DEE70)
CC [MIM:618298]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE70 is an autosomal dominant form with onset in
CC first months of life and variable severity.
CC {ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:30256902}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21824.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051520; BAB21824.1; ALT_INIT; mRNA.
DR EMBL; AK090769; BAG52223.1; -; mRNA.
DR EMBL; AK290017; BAF82706.1; -; mRNA.
DR EMBL; AL008729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101526; AAI01527.1; -; mRNA.
DR EMBL; BC101528; AAI01529.1; -; mRNA.
DR CCDS; CCDS75401.1; -. [Q9C0D0-1]
DR RefSeq; NP_001229577.1; NM_001242648.2. [Q9C0D0-1]
DR RefSeq; NP_001309237.1; NM_001322308.1. [Q9C0D0-1]
DR RefSeq; NP_001309238.1; NM_001322309.1. [Q9C0D0-1]
DR RefSeq; NP_001309239.1; NM_001322310.1.
DR RefSeq; NP_001309240.1; NM_001322311.1.
DR RefSeq; NP_001309241.1; NM_001322312.1.
DR RefSeq; NP_001309242.1; NM_001322313.1.
DR RefSeq; NP_001309243.1; NM_001322314.1.
DR RefSeq; NP_112210.1; NM_030948.3. [Q9C0D0-1]
DR PDB; 6ZEE; X-ray; 1.90 A; C/D/U/V/W/X=508-580.
DR PDB; 6ZEF; X-ray; 1.94 A; C/D=516-580.
DR PDB; 6ZEG; X-ray; 1.09 A; C/D=516-580.
DR PDB; 6ZEH; X-ray; 1.30 A; C/D=516-580.
DR PDB; 6ZEI; X-ray; 1.39 A; C/D=516-580.
DR PDB; 6ZEJ; X-ray; 1.78 A; A/D/F/I/L/O=526-580.
DR PDBsum; 6ZEE; -.
DR PDBsum; 6ZEF; -.
DR PDBsum; 6ZEG; -.
DR PDBsum; 6ZEH; -.
DR PDBsum; 6ZEI; -.
DR PDBsum; 6ZEJ; -.
DR AlphaFoldDB; Q9C0D0; -.
DR SMR; Q9C0D0; -.
DR BioGRID; 128746; 8.
DR IntAct; Q9C0D0; 5.
DR MINT; Q9C0D0; -.
DR STRING; 9606.ENSP00000329880; -.
DR iPTMnet; Q9C0D0; -.
DR PhosphoSitePlus; Q9C0D0; -.
DR BioMuta; PHACTR1; -.
DR DMDM; 97536946; -.
DR EPD; Q9C0D0; -.
DR jPOST; Q9C0D0; -.
DR MassIVE; Q9C0D0; -.
DR MaxQB; Q9C0D0; -.
DR PaxDb; Q9C0D0; -.
DR PeptideAtlas; Q9C0D0; -.
DR PRIDE; Q9C0D0; -.
DR ProteomicsDB; 80005; -. [Q9C0D0-1]
DR ProteomicsDB; 80006; -. [Q9C0D0-2]
DR TopDownProteomics; Q9C0D0-2; -. [Q9C0D0-2]
DR Antibodypedia; 24916; 66 antibodies from 20 providers.
DR DNASU; 221692; -.
DR Ensembl; ENST00000332995.12; ENSP00000329880.8; ENSG00000112137.19. [Q9C0D0-1]
DR Ensembl; ENST00000674637.1; ENSP00000501634.1; ENSG00000112137.19. [Q9C0D0-1]
DR Ensembl; ENST00000676159.1; ENSP00000501921.1; ENSG00000112137.19. [Q9C0D0-1]
DR GeneID; 221692; -.
DR KEGG; hsa:221692; -.
DR MANE-Select; ENST00000332995.12; ENSP00000329880.8; NM_030948.6; NP_112210.1.
DR UCSC; uc003nag.3; human. [Q9C0D0-1]
DR CTD; 221692; -.
DR DisGeNET; 221692; -.
DR GeneCards; PHACTR1; -.
DR HGNC; HGNC:20990; PHACTR1.
DR HPA; ENSG00000112137; Tissue enhanced (bone marrow, brain, lymphoid tissue).
DR MalaCards; PHACTR1; -.
DR MIM; 608723; gene.
DR MIM; 618298; phenotype.
DR neXtProt; NX_Q9C0D0; -.
DR OpenTargets; ENSG00000112137; -.
DR Orphanet; 3451; Infantile spasms syndrome.
DR PharmGKB; PA134923900; -.
DR VEuPathDB; HostDB:ENSG00000112137; -.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000155842; -.
DR InParanoid; Q9C0D0; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; Q9C0D0; -.
DR PathwayCommons; Q9C0D0; -.
DR SignaLink; Q9C0D0; -.
DR SIGNOR; Q9C0D0; -.
DR BioGRID-ORCS; 221692; 6 hits in 322 CRISPR screens.
DR ChiTaRS; PHACTR1; human.
DR GenomeRNAi; 221692; -.
DR Pharos; Q9C0D0; Tbio.
DR PRO; PR:Q9C0D0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9C0D0; protein.
DR Bgee; ENSG00000112137; Expressed in cortical plate and 133 other tissues.
DR ExpressionAtlas; Q9C0D0; baseline and differential.
DR Genevisible; Q9C0D0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
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 GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR InterPro; IPR029987; Phactr1.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF6; PTHR12751:SF6; 2.
DR Pfam; PF02755; RPEL; 4.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Epilepsy;
KW Nucleus; Phosphoprotein; Protein phosphatase inhibitor; Reference proteome;
KW Repeat; Synapse.
FT CHAIN 1..580
FT /note="Phosphatase and actin regulator 1"
FT /id="PRO_0000126634"
FT REPEAT 138..163
FT /note="RPEL 1"
FT REPEAT 422..447
FT /note="RPEL 2"
FT REPEAT 460..484
FT /note="RPEL 3"
FT REPEAT 498..523
FT /note="RPEL 4"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..129
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 331..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3X8"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3X8"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3X8"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 483..484
FT /note="PR -> RK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214970"
FT /id="VSP_018529"
FT VAR_SEQ 485..580
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214970"
FT /id="VSP_018530"
FT VARIANT 247
FT /note="I -> M (in dbSNP:rs17602409)"
FT /id="VAR_053645"
FT VARIANT 479
FT /note="N -> I (in DEE70; severely impaired interaction with
FT actin; dbSNP:rs1562103192)"
FT /evidence="ECO:0000269|PubMed:30256902"
FT /id="VAR_081810"
FT VARIANT 500
FT /note="L -> P (in DEE70; severely impaired interaction with
FT actin; dbSNP:rs1562114406)"
FT /evidence="ECO:0000269|PubMed:30256902"
FT /id="VAR_081811"
FT VARIANT 521
FT /note="R -> C (in DEE70; loss of interaction with PP1
FT complex; dbSNP:rs748743403)"
FT /evidence="ECO:0000269|PubMed:23033978,
FT ECO:0000269|PubMed:30256902"
FT /id="VAR_069379"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:6ZEG"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:6ZEG"
FT HELIX 547..563
FT /evidence="ECO:0007829|PDB:6ZEG"
FT HELIX 569..574
FT /evidence="ECO:0007829|PDB:6ZEG"
SQ SEQUENCE 580 AA; 66308 MW; 5111973836BBEA39 CRC64;
MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS SEDDIDRRPI
RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP GTHTPPIRRR SKFANLGRIF
KPWKWRKKKS EKFKHTSAAL ERKISMRQSR EELIKRGVLK EIYDKDGELS ISNEEDSLEN
GQSLSSSQLS LPALSEMEPV PMPRDPCSYE VLQPSDIMDG PDPGAPVKLP CLPVKLSPPL
PPKKVMICMP VGGPDLSLVS YTAQKSGQQG VAQHHHTVLP SQIQHQLQYG SHGQHLPSTT
GSLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSGDG VTKAGPMGLP
EIRQVPTVVI ECDDNKENVP HESDYEDSSC LYTREEEEEE EDEDDDSSLY TSSLAMKVCR
KDSLAIKLSN RPSKRELEEK NILPRQTDEE RLELRQQIGT KLTRRLSQRP TAEELEQRNI
LKPRNEQEEQ EEKREIKRRL TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK
PWTRLTAADK AAIRKELNEF KSTEMEVHEL SRHLTRFHRP
