PARP4_HUMAN
ID PARP4_HUMAN Reviewed; 1724 AA.
AC Q9UKK3; O75903; Q14682; Q5QNZ9; Q9H1M6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protein mono-ADP-ribosyltransferase PARP4 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000269|PubMed:25043379};
DE AltName: Full=193 kDa vault protein {ECO:0000303|PubMed:10477748};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 4 {ECO:0000303|PubMed:20106667};
DE Short=ARTD4 {ECO:0000303|PubMed:20106667};
DE AltName: Full=PARP-related/IalphaI-related H5/proline-rich {ECO:0000303|PubMed:10100603};
DE Short=PH5P {ECO:0000303|PubMed:10100603};
DE AltName: Full=Poly [ADP-ribose] polymerase 4 {ECO:0000303|PubMed:20106667};
DE Short=PARP-4 {ECO:0000303|PubMed:20106667};
DE AltName: Full=Vault poly(ADP-ribose) polymerase {ECO:0000303|PubMed:10477748};
DE Short=VPARP {ECO:0000303|PubMed:10477748};
GN Name=PARP4 {ECO:0000303|PubMed:20106667, ECO:0000312|HGNC:HGNC:271};
GN Synonyms=ADPRTL1 {ECO:0000303|PubMed:10644454},
GN KIAA0177 {ECO:0000303|PubMed:8724849}, PARPL;
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], PROTEIN SEQUENCE OF 306-319, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND VARIANT THR-899.
RX PubMed=10477748; DOI=10.1083/jcb.146.5.917;
RA Kickhoefer V.A., Siva A.C., Kedersha N.L., Inman E.M., Ruland C.,
RA Streuli M., Rome L.H.;
RT "The 193 kDa vault protein, VPARP, is a novel poly(ADP-ribose)
RT polymerase.";
RL J. Cell Biol. 146:917-928(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-873; ALA-1265 AND ARG-1280.
RC TISSUE=Thymus;
RX PubMed=10644454; DOI=10.1006/geno.1999.6024;
RA Still I.H., Vince P., Cowell J.K.;
RT "Identification of a novel gene (ADPRTL1) encoding a potential poly(ADP-
RT ribosyl)transferase protein.";
RL Genomics 62:533-536(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-873; ALA-1265 AND
RP ARG-1280.
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP DISCUSSION OF SEQUENCE.
RX PubMed=10100603; DOI=10.1016/s0014-5793(99)00173-8;
RA Jean L., Risler J.-L., Nagase T., Coulouarn C., Nomura N., Salier J.-P.;
RT "The nuclear protein PH5P of the inter-alpha-inhibitor superfamily: a
RT missing link between poly(ADP-ribose)polymerase and the inter-alpha-
RT inhibitor family and a novel actor of DNA repair?";
RL FEBS Lett. 446:6-8(1999).
RN [7]
RP ASSOCIATION WITH TEP1.
RX PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
RA Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.;
RT "Vaults and telomerase share a common subunit, TEP1.";
RL J. Biol. Chem. 274:32712-32717(1999).
RN [8]
RP INTERACTION WITH TEP1.
RX PubMed=15169895; DOI=10.1128/mcb.24.12.5314-5323.2004;
RA Liu Y., Snow B.E., Kickhoefer V.A., Erdmann N., Zhou W., Wakeham A.,
RA Gomez M., Rome L.H., Harrington L.;
RT "Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase
RT and is dispensable for telomerase function and vault structure in vivo.";
RL Mol. Cell. Biol. 24:5314-5323(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-1236; SER-1335 AND
RP SER-1504, AND IDENTIFICATION BY MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1335, 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 [11]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; SER-1236 AND SER-1335,
RP AND IDENTIFICATION BY MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101, 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).
RN [15]
RP FUNCTION.
RX PubMed=25043379; DOI=10.1038/ncomms5426;
RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I.,
RA Chang P.;
RT "Family-wide analysis of poly(ADP-ribose) polymerase activity.";
RL Nat. Commun. 5:4426-4426(2014).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1476, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-
CC ribosylation of target proteins. {ECO:0000269|PubMed:25043379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Component of the vault ribonucleoprotein particle, at least
CC composed of MVP, PARP4 and one or more vault RNAs (vRNAs)
CC (PubMed:10477748). Interacts with TEP1 (PubMed:10551828,
CC PubMed:15169895). {ECO:0000269|PubMed:10477748,
CC ECO:0000269|PubMed:10551828, ECO:0000269|PubMed:15169895}.
CC -!- INTERACTION:
CC Q9UKK3; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-2623021, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10477748}. Nucleus
CC {ECO:0000269|PubMed:10477748}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:10477748}. Note=Also found in the nucleus,
CC associated with mitotic spindles. {ECO:0000269|PubMed:10477748}.
CC -!- TISSUE SPECIFICITY: Widely expressed; the highest levels are in the
CC kidney; also detected in heart, placenta, lung, liver, skeletal muscle,
CC spleen, leukocytes and pancreas. {ECO:0000269|PubMed:10477748}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to mediate to mediate poly-ADP-
CC ribosylation of proteins (PubMed:10477748). However, it was later shown
CC to act as a mono-ADP-ribosyltransferase (PubMed:25043379).
CC {ECO:0000269|PubMed:10477748, ECO:0000269|PubMed:25043379}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11494.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF158255; AAD47250.1; -; mRNA.
DR EMBL; AF057160; AAC62491.1; -; mRNA.
DR EMBL; D79999; BAA11494.2; ALT_INIT; mRNA.
DR EMBL; AL359763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS9307.1; -.
DR RefSeq; NP_006428.2; NM_006437.3.
DR RefSeq; XP_011533234.1; XM_011534932.2.
DR AlphaFoldDB; Q9UKK3; -.
DR SMR; Q9UKK3; -.
DR BioGRID; 106653; 41.
DR IntAct; Q9UKK3; 25.
DR MINT; Q9UKK3; -.
DR STRING; 9606.ENSP00000371419; -.
DR BindingDB; Q9UKK3; -.
DR ChEMBL; CHEMBL6142; -.
DR DrugCentral; Q9UKK3; -.
DR CarbonylDB; Q9UKK3; -.
DR GlyGen; Q9UKK3; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9UKK3; -.
DR PhosphoSitePlus; Q9UKK3; -.
DR BioMuta; PARP4; -.
DR DMDM; 308153574; -.
DR EPD; Q9UKK3; -.
DR jPOST; Q9UKK3; -.
DR MassIVE; Q9UKK3; -.
DR MaxQB; Q9UKK3; -.
DR PaxDb; Q9UKK3; -.
DR PeptideAtlas; Q9UKK3; -.
DR PRIDE; Q9UKK3; -.
DR ProteomicsDB; 84811; -.
DR Antibodypedia; 1562; 203 antibodies from 27 providers.
DR DNASU; 143; -.
DR Ensembl; ENST00000381989.4; ENSP00000371419.3; ENSG00000102699.6.
DR GeneID; 143; -.
DR KEGG; hsa:143; -.
DR MANE-Select; ENST00000381989.4; ENSP00000371419.3; NM_006437.4; NP_006428.2.
DR UCSC; uc001upl.4; human.
DR CTD; 143; -.
DR DisGeNET; 143; -.
DR GeneCards; PARP4; -.
DR HGNC; HGNC:271; PARP4.
DR HPA; ENSG00000102699; Low tissue specificity.
DR MIM; 607519; gene.
DR neXtProt; NX_Q9UKK3; -.
DR OpenTargets; ENSG00000102699; -.
DR PharmGKB; PA24591; -.
DR VEuPathDB; HostDB:ENSG00000102699; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000160555; -.
DR HOGENOM; CLU_001437_0_0_1; -.
DR InParanoid; Q9UKK3; -.
DR OMA; HTELEEY; -.
DR OrthoDB; 955432at2759; -.
DR PhylomeDB; Q9UKK3; -.
DR TreeFam; TF329720; -.
DR BRENDA; 2.4.2.30; 2681.
DR PathwayCommons; Q9UKK3; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR Reactome; R-HSA-9683610; Maturation of nucleoprotein.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR SignaLink; Q9UKK3; -.
DR BioGRID-ORCS; 143; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; PARP4; human.
DR GeneWiki; PARP4; -.
DR GenomeRNAi; 143; -.
DR Pharos; Q9UKK3; Tchem.
DR PRO; PR:Q9UKK3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9UKK3; protein.
DR Bgee; ENSG00000102699; Expressed in rectum and 99 other tissues.
DR Genevisible; Q9UKK3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; NAS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0019899; F:enzyme binding; IDA:MGI.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; NAS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; IDA:UniProtKB.
DR GO; GO:0140289; P:protein mono-ADP-ribosylation; IDA:UniProtKB.
DR GO; GO:0051972; P:regulation of telomerase activity; IDA:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; NAS:UniProtKB.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031273; PARP4.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR013694; VIT.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR46530; PTHR46530; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF08487; VIT; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00609; VIT; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51468; VIT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycosyltransferase;
KW Methylation; NAD; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Transferase.
FT CHAIN 1..1724
FT /note="Protein mono-ADP-ribosyltransferase PARP4"
FT /id="PRO_0000211330"
FT DOMAIN 1..94
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 242..370
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 369..573
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DOMAIN 607..735
FT /note="VIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT DOMAIN 876..1046
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 97..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1724
FT /note="Interaction with the major vault protein"
FT /evidence="ECO:0000269|PubMed:10477748"
FT MOTIF 19..25
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1237..1249
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1408..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1476
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 81
FT /note="I -> V (in dbSNP:rs35200240)"
FT /id="VAR_056645"
FT VARIANT 122
FT /note="S -> N (in dbSNP:rs9578751)"
FT /id="VAR_056646"
FT VARIANT 215
FT /note="F -> Y (in dbSNP:rs9318600)"
FT /id="VAR_056647"
FT VARIANT 792
FT /note="P -> L (in dbSNP:rs4986818)"
FT /id="VAR_056648"
FT VARIANT 873
FT /note="S -> N (in dbSNP:rs7140044)"
FT /evidence="ECO:0000269|PubMed:10644454,
FT ECO:0000269|PubMed:8724849"
FT /id="VAR_056649"
FT VARIANT 899
FT /note="A -> T (in dbSNP:rs2275660)"
FT /evidence="ECO:0000269|PubMed:10477748"
FT /id="VAR_056650"
FT VARIANT 991
FT /note="K -> R (in dbSNP:rs34689435)"
FT /id="VAR_056651"
FT VARIANT 1012
FT /note="V -> I (in dbSNP:rs9581043)"
FT /id="VAR_056652"
FT VARIANT 1253
FT /note="S -> T (in dbSNP:rs4986822)"
FT /id="VAR_056653"
FT VARIANT 1265
FT /note="G -> A (in dbSNP:rs1050110)"
FT /evidence="ECO:0000269|PubMed:10644454,
FT ECO:0000269|PubMed:8724849"
FT /id="VAR_016090"
FT VARIANT 1280
FT /note="G -> R (in dbSNP:rs13428)"
FT /evidence="ECO:0000269|PubMed:10644454,
FT ECO:0000269|PubMed:8724849"
FT /id="VAR_016091"
FT CONFLICT 519
FT /note="S -> P (in Ref. 1; AAD47250)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="Q -> E (in Ref. 2; AAC62491 and 3; BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="M -> A (in Ref. 2; AAC62491 and 3; BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="M -> T (in Ref. 1; AAD47250)"
FT /evidence="ECO:0000305"
FT CONFLICT 1065
FT /note="V -> A (in Ref. 1; AAD47250 and 2; AAC62491)"
FT /evidence="ECO:0000305"
FT CONFLICT 1080
FT /note="L -> R (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1108
FT /note="R -> C (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1328
FT /note="P -> T (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="A -> T (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394
FT /note="S -> A (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1459
FT /note="S -> Y (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1550
FT /note="L -> P (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1555
FT /note="V -> L (in Ref. 1; AAD47250)"
FT /evidence="ECO:0000305"
FT CONFLICT 1564
FT /note="I -> T (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
FT CONFLICT 1656
FT /note="A -> P (in Ref. 1; AAD47250, 2; AAC62491 and 3;
FT BAA11494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1724 AA; 192595 MW; DCA1DD4C001EA22F CRC64;
MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL DNADVLSQYQ
LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI TPPPDQKASS SEVKTEGLCP
DSATEEEDTV ELTEFGMQNV EIPHLPQDFE VAKYNTLEKV GMEGGQEAVV VELQCSRDSR
DCPFLISSHF LLDDGMETRR QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL
ASEQLQALLL EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI
LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC QLIRDMVNVC
ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL QNHHSKSPVD VLQIFRVGRV
NETTEFLSKL GNVRPLLHGS PVQNIVGILC RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD
SLSTSIKYSH PGETDGTRLL LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT
TDFEDDEFVV YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL
PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH VPIEAKYIFP
LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG HGAYLMSQDA PDVFTVSVGN
LPPKAKVLIK ITYITELSIL GTVGVFFMPA TVAPWQQDKA LNENLQDTVE KICIKEIGTK
QSFSLTMSIE MPYVIEFIFS DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL
PRMWVEKHPE KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL
HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN TDFWKTLRYL
SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF ACGIGSTANR HVLRILSQCG
AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL
NDRLLVYGFI PHCTQATLCA LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI
LHENETSHEM KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK
EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM ELSQPEVSED
FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP LFKKVSPWET STSSFFPILA
PAVGSYLPPT ARAHSPASLS FASYRQVASF GSAAPPRQFD ASQFSQGPVP GTCADWIPQS
ASCPTGPPQN PPSSPYCGIV FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS
LPTDPDPIRG FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL
LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL CFLEVKEEDE
IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT NGLHSFLKQK GIQSLGVKGR
ECLLDLIATM LVLQFIRTRL EKEGIVFKSL MKMDDASISR NIPWAFEAIK QASEWVRRTE
GQYPSICPRL ELGNDWDSAT KQLLGLQPIS TVSPLHRVLH YSQG
