PHF3_HUMAN
ID PHF3_HUMAN Reviewed; 2039 AA.
AC Q92576; A3KFI8; Q14CR5; Q5CZI1; Q5T1T6; Q9NQ16; Q9UI45;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=PHD finger protein 3;
GN Name=PHF3; Synonyms=KIAA0244;
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), AND TISSUE SPECIFICITY.
RX PubMed=11856869; DOI=10.1159/000048804;
RA Fischer U., Struss A.-K., Hemmer D., Michel A., Henn W., Steudel W.-I.,
RA Meese E.;
RT "PHF3 expression is frequently reduced in glioma.";
RL Cytogenet. Cell Genet. 94:131-136(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
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 [5]
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 [6]
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 [7]
RP IDENTIFICATION BY 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=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-299; SER-680;
RP SER-1133; SER-1178 AND SER-1642, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-125; SER-283;
RP SER-1014; SER-1133; SER-1614; SER-1642 AND SER-1925, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133; SER-1148; SER-1178 AND
RP SER-1898, AND IDENTIFICATION BY 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 [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1867 AND ARG-1877, AND
RP IDENTIFICATION BY MASS 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).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-644; LYS-964 AND LYS-1931, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP STRUCTURE BY NMR OF 923-1029.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the TFIIS domain II of human PHD finger protein 3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92576-2; Sequence=VSP_026434;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression is significantly reduced or
CC lost in glioblastomas, glioblastoma cell lines, anaplastic
CC astrocytomas, and astrocytomas. {ECO:0000269|PubMed:11856869}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13438.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF091622; AAF21292.1; -; mRNA.
DR EMBL; D87685; BAA13438.2; ALT_INIT; mRNA.
DR EMBL; BX648268; CAI56715.1; -; mRNA.
DR EMBL; AL050329; CAM45842.1; -; Genomic_DNA.
DR EMBL; AL354719; CAM45842.1; JOINED; Genomic_DNA.
DR EMBL; BC113650; AAI13651.1; -; mRNA.
DR EMBL; BC113652; AAI13653.1; -; mRNA.
DR CCDS; CCDS4966.1; -. [Q92576-1]
DR RefSeq; NP_001277188.1; NM_001290259.1. [Q92576-2]
DR RefSeq; NP_001277189.1; NM_001290260.1.
DR RefSeq; NP_055968.1; NM_015153.3. [Q92576-1]
DR RefSeq; XP_005248758.1; XM_005248701.3.
DR RefSeq; XP_005248759.1; XM_005248702.3.
DR RefSeq; XP_006715489.1; XM_006715426.3. [Q92576-1]
DR PDB; 2DME; NMR; -; A=923-1029.
DR PDB; 6IC8; X-ray; 1.93 A; A/B=1199-1356.
DR PDB; 6IC9; X-ray; 1.75 A; A/B=1199-1356.
DR PDB; 6Q2V; X-ray; 2.59 A; A/B/C/D/E/F/G/H=1199-1356.
DR PDB; 6Q5Y; X-ray; 2.85 A; A/B/C/D=1199-1356.
DR PDBsum; 2DME; -.
DR PDBsum; 6IC8; -.
DR PDBsum; 6IC9; -.
DR PDBsum; 6Q2V; -.
DR PDBsum; 6Q5Y; -.
DR AlphaFoldDB; Q92576; -.
DR SMR; Q92576; -.
DR BioGRID; 117031; 77.
DR IntAct; Q92576; 26.
DR MINT; Q92576; -.
DR STRING; 9606.ENSP00000262043; -.
DR GlyGen; Q92576; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92576; -.
DR MetOSite; Q92576; -.
DR PhosphoSitePlus; Q92576; -.
DR BioMuta; PHF3; -.
DR DMDM; 34098662; -.
DR EPD; Q92576; -.
DR jPOST; Q92576; -.
DR MassIVE; Q92576; -.
DR MaxQB; Q92576; -.
DR PaxDb; Q92576; -.
DR PeptideAtlas; Q92576; -.
DR PRIDE; Q92576; -.
DR ProteomicsDB; 75337; -. [Q92576-1]
DR ProteomicsDB; 75338; -. [Q92576-2]
DR Antibodypedia; 31168; 76 antibodies from 21 providers.
DR DNASU; 23469; -.
DR Ensembl; ENST00000262043.8; ENSP00000262043.4; ENSG00000118482.12. [Q92576-1]
DR Ensembl; ENST00000393387.5; ENSP00000377048.1; ENSG00000118482.12. [Q92576-1]
DR GeneID; 23469; -.
DR KEGG; hsa:23469; -.
DR MANE-Select; ENST00000262043.8; ENSP00000262043.4; NM_001370348.2; NP_001357277.1.
DR UCSC; uc003pep.2; human. [Q92576-1]
DR CTD; 23469; -.
DR DisGeNET; 23469; -.
DR GeneCards; PHF3; -.
DR HGNC; HGNC:8921; PHF3.
DR HPA; ENSG00000118482; Low tissue specificity.
DR MalaCards; PHF3; -.
DR MIM; 607789; gene.
DR neXtProt; NX_Q92576; -.
DR OpenTargets; ENSG00000118482; -.
DR PharmGKB; PA33261; -.
DR VEuPathDB; HostDB:ENSG00000118482; -.
DR eggNOG; KOG1634; Eukaryota.
DR GeneTree; ENSGT00940000155080; -.
DR HOGENOM; CLU_001663_0_0_1; -.
DR InParanoid; Q92576; -.
DR OMA; QMNVEEK; -.
DR OrthoDB; 174961at2759; -.
DR PhylomeDB; Q92576; -.
DR TreeFam; TF350578; -.
DR PathwayCommons; Q92576; -.
DR SignaLink; Q92576; -.
DR SIGNOR; Q92576; -.
DR BioGRID-ORCS; 23469; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; PHF3; human.
DR EvolutionaryTrace; Q92576; -.
DR GeneWiki; PHF3; -.
DR GenomeRNAi; 23469; -.
DR Pharos; Q92576; Tbio.
DR PRO; PR:Q92576; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92576; protein.
DR Bgee; ENSG00000118482; Expressed in tendon of biceps brachii and 214 other tissues.
DR ExpressionAtlas; Q92576; baseline and differential.
DR Genevisible; Q92576; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF07744; SPOC; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00510; TFS2M; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2039
FT /note="PHD finger protein 3"
FT /id="PRO_0000059292"
FT DOMAIN 927..1046
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 717..772
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 144..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1884..2039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..2039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1867
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1877
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 644
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 964
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1931
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026434"
FT VARIANT 525
FT /note="V -> I (in dbSNP:rs34288820)"
FT /id="VAR_051599"
FT VARIANT 1834
FT /note="H -> Y (in dbSNP:rs3734881)"
FT /id="VAR_022040"
FT CONFLICT 1394
FT /note="E -> G (in Ref. 4; CAI56715)"
FT /evidence="ECO:0000305"
FT HELIX 924..943
FT /evidence="ECO:0007829|PDB:2DME"
FT TURN 944..947
FT /evidence="ECO:0007829|PDB:2DME"
FT HELIX 952..970
FT /evidence="ECO:0007829|PDB:2DME"
FT HELIX 975..984
FT /evidence="ECO:0007829|PDB:2DME"
FT HELIX 986..989
FT /evidence="ECO:0007829|PDB:2DME"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:2DME"
FT HELIX 996..1002
FT /evidence="ECO:0007829|PDB:2DME"
FT STRAND 1003..1005
FT /evidence="ECO:0007829|PDB:2DME"
FT HELIX 1009..1012
FT /evidence="ECO:0007829|PDB:2DME"
FT TURN 1015..1020
FT /evidence="ECO:0007829|PDB:2DME"
FT TURN 1024..1026
FT /evidence="ECO:0007829|PDB:2DME"
FT STRAND 1208..1215
FT /evidence="ECO:0007829|PDB:6IC9"
FT TURN 1216..1218
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1219..1230
FT /evidence="ECO:0007829|PDB:6IC9"
FT HELIX 1235..1238
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1241..1249
FT /evidence="ECO:0007829|PDB:6IC9"
FT HELIX 1251..1264
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1267..1278
FT /evidence="ECO:0007829|PDB:6IC9"
FT HELIX 1279..1295
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1298..1303
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1308..1316
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1318..1320
FT /evidence="ECO:0007829|PDB:6Q2V"
FT HELIX 1324..1326
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1330..1332
FT /evidence="ECO:0007829|PDB:6IC9"
FT STRAND 1341..1349
FT /evidence="ECO:0007829|PDB:6IC9"
SQ SEQUENCE 2039 AA; 229481 MW; FDAFF00576005E9B CRC64;
MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSASQNV LEDSLKNMLS DKDPMLGSAS
NQFCLPVLDS NDPNFQMPCS TVVGLDDIMD EGVVKESGND TIDEEELILP NRNLRDKVEE
NSVRSPRKSP RLMAQEQVRS LRQSTIAKRS NAAPLSNTKK ASGKTVSTAK AGVKQPERSQ
VKEEVCMSLK PEYHKENRRC SRNSGQIEVV PEVSVSSSHS SVSSCLEMKD EDGLDSKHKC
NNPGEIDVPS HELNCSLLSE TCVTIGEKKN EALMECKAKP VGSPLFKFSD KEEHEQNDSI
SGKTGETVVE EMIATRKVEQ DSKETVKLSH EDDHILEDAG SSDISSDAAC TNPNKTENSL
VGLPSCVDEV TECNLELKDT MGIADKTENT LERNKIEPLG YCEDAESNRQ LESTEFNKSN
LEVVDTSTFG PESNILENAI CDVPDQNSKQ LNAIESTKIE SHETANLQDD RNSQSSSVSY
LESKSVKSKH TKPVIHSKQN MTTDAPKKIV AAKYEVIHSK TKVNVKSVKR NTDVPESQQN
FHRPVKVRKK QIDKEPKIQS CNSGVKSVKN QAHSVLKKTL QDQTLVQIFK PLTHSLSDKS
HAHPGCLKEP HHPAQTGHVS HSSQKQCHKP QQQAPAMKTN SHVKEELEHP GVEHFKEEDK
LKLKKPEKNL QPRQRRSSKS FSLDEPPLFI PDNIATIRRE GSDHSSSFES KYMWTPSKQC
GFCKKPHGNR FMVGCGRCDD WFHGDCVGLS LSQAQQMGEE DKEYVCVKCC AEEDKKTEIL
DPDTLENQAT VEFHSGDKTM ECEKLGLSKH TTNDRTKYID DTVKHKVKIL KRESGEGRNS
SDCRDNEIKK WQLAPLRKMG QPVLPRRSSE EKSEKIPKES TTVTCTGEKA SKPGTHEKQE
MKKKKVEKGV LNVHPAASAS KPSADQIRQS VRHSLKDILM KRLTDSNLKV PEEKAAKVAT
KIEKELFSFF RDTDAKYKNK YRSLMFNLKD PKNNILFKKV LKGEVTPDHL IRMSPEELAS
KELAAWRRRE NRHTIEMIEK EQREVERRPI TKITHKGEIE IESDAPMKEQ EAAMEIQEPA
ANKSLEKPEG SEKQKEEVDS MSKDTTSQHR QHLFDLNCKI CIGRMAPPVD DLSPKKVKVV
VGVARKHSDN EAESIADALS STSNILASEF FEEEKQESPK STFSPAPRPE MPGTVEVEST
FLARLNFIWK GFINMPSVAK FVTKAYPVSG SPEYLTEDLP DSIQVGGRIS PQTVWDYVEK
IKASGTKEIC VVRFTPVTEE DQISYTLLFA YFSSRKRYGV AANNMKQVKD MYLIPLGATD
KIPHPLVPFD GPGLELHRPN LLLGLIIRQK LKRQHSACAS TSHIAETPES APPIALPPDK
KSKIEVSTEE APEEENDFFN SFTTVLHKQR NKPQQNLQED LPTAVEPLME VTKQEPPKPL
RFLPGVLIGW ENQPTTLELA NKPLPVDDIL QSLLGTTGQV YDQAQSVMEQ NTVKEIPFLN
EQTNSKIEKT DNVEVTDGEN KEIKVKVDNI SESTDKSAEI ETSVVGSSSI SAGSLTSLSL
RGKPPDVSTE AFLTNLSIQS KQEETVESKE KTLKRQLQED QENNLQDNQT SNSSPCRSNV
GKGNIDGNVS CSENLVANTA RSPQFINLKR DPRQAAGRSQ PVTTSESKDG DSCRNGEKHM
LPGLSHNKEH LTEQINVEEK LCSAEKNSCV QQSDNLKVAQ NSPSVENIQT SQAEQAKPLQ
EDILMQNIET VHPFRRGSAV ATSHFEVGNT CPSEFPSKSI TFTSRSTSPR TSTNFSPMRP
QQPNLQHLKS SPPGFPFPGP PNFPPQSMFG FPPHLPPPLL PPPGFGFAQN PMVPWPPVVH
LPGQPQRMMG PLSQASRYIG PQNFYQVKDI RRPERRHSDP WGRQDQQQLD RPFNRGKGDR
QRFYSDSHHL KRERHEKEWE QESERHRRRD RSQDKDRDRK SREEGHKDKE RARLSHGDRG
TDGKASRDSR NVDKKPDKPK SEDYEKDKER EKSKHREGEK DRDRYHKDRD HTDRTKSKR
