DCAF8_HUMAN
ID DCAF8_HUMAN Reviewed; 597 AA.
AC Q5TAQ9; D3DVE6; Q12839; Q4QQI6; Q53F14; Q66K50; Q68CS7; Q96E00;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DDB1- and CUL4-associated factor 8;
DE AltName: Full=WD repeat-containing protein 42A;
GN Name=DCAF8; Synonyms=H326, WDR42A;
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).
RC TISSUE=Myeloma;
RA Bergsagel P.L., Kuehl W.;
RT "H326 is a human gene homologous to murine PC326 that is ubiquitously
RT expressed, and has a murine homologue that is also ubiquitously
RT expressed.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
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 [4]
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 [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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Skin;
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 FUNCTION, INTERACTION WITH DDB1; CUL4A AND CUL4B, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF ARG-314 AND ARG-362.
RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is
RT required for S phase destruction of the replication factor Cdt1.";
RL Mol. Cell 23:709-721(2006).
RN [8]
RP FUNCTION.
RX PubMed=16964240; DOI=10.1038/nature05175;
RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase
RT machinery.";
RL Nature 443:590-593(2006).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH KPNA1; KPNB1 AND XPO1, AND
RP MUTAGENESIS OF 39-ILE--LEU-50 AND 115-ARG--ARG-122.
RX PubMed=22500989; DOI=10.1016/j.febslet.2012.02.053;
RA Wu F., Wang S., Xing J., Li M., Zheng C.;
RT "Characterization of nuclear import and export signals determining the
RT subcellular localization of WD repeat-containing protein 42A (WDR42A).";
RL FEBS Lett. 586:1079-1085(2012).
RN [10]
RP METHYLATION AT ARG-204 BY PRMT1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23455924; DOI=10.1038/nmeth.2397;
RA Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D.,
RA Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U.;
RT "A Y2H-seq approach defines the human protein methyltransferase
RT interactome.";
RL Nat. Methods 10:339-342(2013).
RN [11]
RP VARIANT GAN2 CYS-317, INTERACTION WITH DDB1, AND CHARACTERIZATION OF
RP VARIANT GAN2 CYS-317.
RX PubMed=24500646; DOI=10.1212/wnl.0000000000000206;
RA Klein C.J., Wu Y., Vogel P., Goebel H.H., Bonnemann C., Zukosky K.,
RA Botuyan M.V., Duan X., Middha S., Atkinson E.J., Mer G., Dyck P.J.;
RT "Ubiquitin ligase defect by DCAF8 mutation causes HMSN2 with giant axons.";
RL Neurology 82:873-878(2014).
CC -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:16964240}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DDB1, CUL4A and CUL4B. Interacts with KPNA1,
CC KPNB1 and XPO1. {ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:22500989, ECO:0000269|PubMed:24500646}.
CC -!- INTERACTION:
CC Q5TAQ9; Q16531: DDB1; NbExp=6; IntAct=EBI-740686, EBI-350322;
CC Q5TAQ9; P52294: KPNA1; NbExp=2; IntAct=EBI-740686, EBI-358383;
CC Q5TAQ9; Q99750: MDFI; NbExp=6; IntAct=EBI-740686, EBI-724076;
CC Q5TAQ9; Q99873: PRMT1; NbExp=2; IntAct=EBI-740686, EBI-78738;
CC Q5TAQ9; Q93062: RBPMS; NbExp=3; IntAct=EBI-740686, EBI-740322;
CC Q5TAQ9; O43463: SUV39H1; NbExp=2; IntAct=EBI-740686, EBI-349968;
CC Q5TAQ9; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-740686, EBI-741515;
CC Q5TAQ9; Q9BYV2: TRIM54; NbExp=2; IntAct=EBI-740686, EBI-2130429;
CC Q5TAQ9; Q969Q1: TRIM63; NbExp=3; IntAct=EBI-740686, EBI-5661333;
CC Q5TAQ9; P12520: vpr; Xeno; NbExp=2; IntAct=EBI-740686, EBI-6164519;
CC Q5TAQ9-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25842815, EBI-10976677;
CC Q5TAQ9-2; Q01658: DR1; NbExp=3; IntAct=EBI-25842815, EBI-750300;
CC Q5TAQ9-2; P28799: GRN; NbExp=3; IntAct=EBI-25842815, EBI-747754;
CC Q5TAQ9-2; Q00403: GTF2B; NbExp=3; IntAct=EBI-25842815, EBI-389564;
CC Q5TAQ9-2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-25842815, EBI-1054873;
CC Q5TAQ9-2; P04792: HSPB1; NbExp=3; IntAct=EBI-25842815, EBI-352682;
CC Q5TAQ9-2; O43464: HTRA2; NbExp=3; IntAct=EBI-25842815, EBI-517086;
CC Q5TAQ9-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25842815, EBI-1055254;
CC Q5TAQ9-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25842815, EBI-10975473;
CC Q5TAQ9-2; P07196: NEFL; NbExp=3; IntAct=EBI-25842815, EBI-475646;
CC Q5TAQ9-2; P35240: NF2; NbExp=3; IntAct=EBI-25842815, EBI-1014472;
CC Q5TAQ9-2; O43933: PEX1; NbExp=3; IntAct=EBI-25842815, EBI-988601;
CC Q5TAQ9-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-25842815, EBI-21251460;
CC Q5TAQ9-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25842815, EBI-396669;
CC Q5TAQ9-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25842815, EBI-5235340;
CC Q5TAQ9-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-25842815, EBI-372899;
CC Q5TAQ9-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-25842815, EBI-12806590;
CC Q5TAQ9-2; P40337-2: VHL; NbExp=3; IntAct=EBI-25842815, EBI-12157263;
CC Q5TAQ9-2; O76024: WFS1; NbExp=3; IntAct=EBI-25842815, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22500989}. Cytoplasm
CC {ECO:0000269|PubMed:22500989}. Note=It shuttles between the nucleus and
CC the cytoplasm. Nuclear import is mediated by KPNA1 and KPNB1 under the
CC regulation of nuclear GTPase RAN. Nuclear export to the cytoplasm is
CC XPO1 dependent. {ECO:0000269|PubMed:22500989}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5TAQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TAQ9-2; Sequence=VSP_027264, VSP_027265;
CC -!- DISEASE: Giant axonal neuropathy 2, autosomal dominant (GAN2)
CC [MIM:610100]: An autosomal dominant peripheral axonal neuropathy
CC characterized by onset of distal sensory impairment with lower
CC extremity muscle weakness and atrophy after the second decade. Clinical
CC features include foot deformities apparent in childhood, and
CC cardiomyopathy in severely affected individuals. Sural nerve biopsy
CC shows giant axonal swelling with neurofilament accumulation.
CC {ECO:0000269|PubMed:24500646}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat DCAF8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16607.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U06631; AAA16607.1; ALT_FRAME; mRNA.
DR EMBL; AK223475; BAD97195.1; -; mRNA.
DR EMBL; CR749801; CAH18661.1; -; mRNA.
DR EMBL; AL139011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52731.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52732.1; -; Genomic_DNA.
DR EMBL; BC013107; AAH13107.1; -; mRNA.
DR EMBL; BC080597; AAH80597.1; -; mRNA.
DR EMBL; BC098271; AAH98271.1; -; mRNA.
DR EMBL; BC099709; AAH99709.1; -; mRNA.
DR EMBL; BC099846; AAH99846.1; -; mRNA.
DR EMBL; BC111063; AAI11064.1; -; mRNA.
DR CCDS; CCDS1200.1; -. [Q5TAQ9-1]
DR RefSeq; NP_056541.2; NM_015726.3. [Q5TAQ9-1]
DR PDB; 3I8E; X-ray; 3.40 A; C/D=153-165.
DR PDBsum; 3I8E; -.
DR AlphaFoldDB; Q5TAQ9; -.
DR SMR; Q5TAQ9; -.
DR BioGRID; 119121; 123.
DR DIP; DIP-48762N; -.
DR IntAct; Q5TAQ9; 77.
DR MINT; Q5TAQ9; -.
DR STRING; 9606.ENSP00000357052; -.
DR GlyGen; Q5TAQ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5TAQ9; -.
DR PhosphoSitePlus; Q5TAQ9; -.
DR BioMuta; DCAF8; -.
DR DMDM; 74756455; -.
DR EPD; Q5TAQ9; -.
DR jPOST; Q5TAQ9; -.
DR MassIVE; Q5TAQ9; -.
DR MaxQB; Q5TAQ9; -.
DR PaxDb; Q5TAQ9; -.
DR PeptideAtlas; Q5TAQ9; -.
DR PRIDE; Q5TAQ9; -.
DR ProteomicsDB; 64861; -. [Q5TAQ9-1]
DR ProteomicsDB; 64862; -. [Q5TAQ9-2]
DR Antibodypedia; 20487; 89 antibodies from 17 providers.
DR DNASU; 50717; -.
DR Ensembl; ENST00000326837.6; ENSP00000318227.2; ENSG00000132716.19. [Q5TAQ9-1]
DR Ensembl; ENST00000368073.7; ENSP00000357052.3; ENSG00000132716.19. [Q5TAQ9-1]
DR Ensembl; ENST00000368074.6; ENSP00000357053.1; ENSG00000132716.19. [Q5TAQ9-1]
DR Ensembl; ENST00000475733.5; ENSP00000476351.1; ENSG00000132716.19. [Q5TAQ9-2]
DR Ensembl; ENST00000610139.5; ENSP00000477464.1; ENSG00000132716.19. [Q5TAQ9-2]
DR GeneID; 50717; -.
DR KEGG; hsa:50717; -.
DR MANE-Select; ENST00000368074.6; ENSP00000357053.1; NM_015726.4; NP_056541.2.
DR UCSC; uc001fvn.3; human. [Q5TAQ9-1]
DR CTD; 50717; -.
DR DisGeNET; 50717; -.
DR GeneCards; DCAF8; -.
DR HGNC; HGNC:24891; DCAF8.
DR HPA; ENSG00000132716; Low tissue specificity.
DR MalaCards; DCAF8; -.
DR MIM; 610100; phenotype.
DR MIM; 615820; gene.
DR neXtProt; NX_Q5TAQ9; -.
DR OpenTargets; ENSG00000132716; -.
DR Orphanet; 401964; Autosomal dominant Charcot-Marie-Tooth disease type 2 with giant axons.
DR PharmGKB; PA165751195; -.
DR VEuPathDB; HostDB:ENSG00000132716; -.
DR eggNOG; KOG1334; Eukaryota.
DR eggNOG; KOG3133; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR HOGENOM; CLU_012381_4_1_1; -.
DR InParanoid; Q5TAQ9; -.
DR OMA; IFQTKIM; -.
DR PhylomeDB; Q5TAQ9; -.
DR TreeFam; TF326071; -.
DR PathwayCommons; Q5TAQ9; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q5TAQ9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 50717; 9 hits in 1108 CRISPR screens.
DR ChiTaRS; DCAF8; human.
DR EvolutionaryTrace; Q5TAQ9; -.
DR GenomeRNAi; 50717; -.
DR Pharos; Q5TAQ9; Tbio.
DR PRO; PR:Q5TAQ9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TAQ9; protein.
DR Bgee; ENSG00000132716; Expressed in right uterine tube and 93 other tissues.
DR ExpressionAtlas; Q5TAQ9; baseline and differential.
DR Genevisible; Q5TAQ9; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15574; PTHR15574; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW Methylation; Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..597
FT /note="DDB1- and CUL4-associated factor 8"
FT /id="PRO_0000296957"
FT REPEAT 191..230
FT /note="WD 1"
FT REPEAT 234..275
FT /note="WD 2"
FT REPEAT 281..321
FT /note="WD 3"
FT REPEAT 329..369
FT /note="WD 4"
FT REPEAT 385..424
FT /note="WD 5"
FT REPEAT 432..472
FT /note="WD 6"
FT REPEAT 476..515
FT /note="WD 7"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..50
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:22500989"
FT MOTIF 114..122
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22500989"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N7N5"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N7N5"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N7N5"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N7N5"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N7N5"
FT MOD_RES 204
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:23455924"
FT VAR_SEQ 242..273
FT /note="AKFLPNSGDSTLAMCARDGQVRVAELSATQCC -> VRQGSIIATERIRHEL
FT EKSELQHGLGADSELL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027264"
FT VAR_SEQ 274..597
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027265"
FT VARIANT 317
FT /note="R -> C (in GAN2; interaction with DDB1 is decreased;
FT dbSNP:rs587777425)"
FT /evidence="ECO:0000269|PubMed:24500646"
FT /id="VAR_071265"
FT MUTAGEN 39..50
FT /note="IEVEASDLSLSL->AEVEASDASASA: Abrogates cytoplasmic
FT localization."
FT /evidence="ECO:0000269|PubMed:22500989"
FT MUTAGEN 115..122
FT /note="RRRVQRKR->AAAVQAKA: Abrogates nuclear localization."
FT /evidence="ECO:0000269|PubMed:22500989"
FT MUTAGEN 314
FT /note="R->A: Reduces association with DDB1."
FT /evidence="ECO:0000269|PubMed:16949367"
FT MUTAGEN 362
FT /note="R->A: Reduces association with DDB1."
FT /evidence="ECO:0000269|PubMed:16949367"
FT CONFLICT 68
FT /note="D -> E (in Ref. 6; AAH13107)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> T (in Ref. 6; AAH98271)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="L -> F (in Ref. 3; CAH18661)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="QR -> HG (in Ref. 1; AAA16607)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="S -> G (in Ref. 2; BAD97195)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="K -> E (in Ref. 3; CAH18661)"
FT /evidence="ECO:0000305"
FT TURN 156..163
FT /evidence="ECO:0007829|PDB:3I8E"
SQ SEQUENCE 597 AA; 66852 MW; 3F3396C77EA1E3AD CRC64;
MSSKGSSTDG RTDLANGSLS SSPEEMSGAE EGRETSSGIE VEASDLSLSL TGDDGGPNRT
STESRGTDTE SSGEDKDSDS MEDTGHYSIN DENRVHDRSE EEEEEEEEEE EEQPRRRVQR
KRANRDQDSS DDERALEDWV SSETSALPRP RWQALPALRE RELGSSARFV YEACGARVFV
QRFRLQHGLE GHTGCVNTLH FNQRGTWLAS GSDDLKVVVW DWVRRQPVLD FESGHKSNVF
QAKFLPNSGD STLAMCARDG QVRVAELSAT QCCKNTKRVA QHKGASHKLA LEPDSPCTFL
SAGEDAVVFT IDLRQDRPAS KLVVTKEKEK KVGLYTIYVN PANTHQFAVG GRDQFVRIYD
QRKIDENENN GVLKKFCPHH LVNSESKANI TCLVYSHDGT ELLASYNDED IYLFNSSHSD
GAQYVKRYKG HRNNATVKGV NFYGPKSEFV VSGSDCGHIF LWEKSSCQII QFMEGDKGGV
VNCLEPHPHL PVLATSGLDH DVKIWAPTAE ASTELTGLKD VIKKNKRERD EDSLHQTDLF
DSHMLWFLMH HLRQRRHHRR WREPGVGATD ADSDESPSSS DTSDEEEGPD RVQCMPS
