ZN318_HUMAN
ID ZN318_HUMAN Reviewed; 2279 AA.
AC Q5VUA4; O94796; Q4G0E4; Q8NEM6; Q9UNU8; Q9Y2W9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Zinc finger protein 318;
DE AltName: Full=Endocrine regulatory protein;
GN Name=ZNF318; ORFNames=HRIHFB2436;
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), TISSUE SPECIFICITY, AND VARIANT
RP ALA-1797.
RA Lopez-Egido J.R., Oberg K., Gobl A.E.;
RT "A novel cDNA expressed in endocrine tissue.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1213 (ISOFORM 1).
RC TISSUE=Lymph, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2056-2279 (ISOFORM 1), AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-173; SER-214;
RP SER-1896; SER-2189; SER-2192 AND SER-2243, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-214 AND SER-1713,
RP AND 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-527; SER-1243;
RP SER-1420; SER-1896; SER-2101 AND SER-2243, AND IDENTIFICATION BY MASS
RP 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 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-81; SER-136; SER-527;
RP SER-1037; SER-1243 AND SER-2101, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-136; SER-207;
RP SER-472; SER-501; SER-527; THR-842; SER-1010; SER-1243; SER-1267; SER-1420;
RP SER-1856; SER-1896; SER-1971; SER-2030; SER-2035; SER-2091; SER-2101;
RP SER-2189; SER-2192 AND SER-2243, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 SER-173; SER-1037; SER-1267 AND
RP SER-2101, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-578, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-547; LYS-553; LYS-566 AND
RP LYS-578, AND 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 [17]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-812 AND ARG-1274.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: [Isoform 2]: Acts as a transcriptional corepressor for AR-
CC mediated transactivation function. May act as a transcriptional
CC regulator during spermatogenesis and, in particular, during meiotic
CC division. {ECO:0000250|UniProtKB:Q99PP2}.
CC -!- FUNCTION: [Isoform 1]: Acts as a transcriptional coactivator for AR-
CC mediated transactivation function. May act as a transcriptional
CC regulator during spermatogenesis and, in particular, during meiotic
CC division. {ECO:0000250|UniProtKB:Q99PP2}.
CC -!- SUBUNIT: Homodimer. Heterodimer of isoform 1 and isoform 2. Isoform 1
CC and isoform 2 interact with AR. {ECO:0000250|UniProtKB:Q99PP2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VUA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VUA4-2; Sequence=VSP_016592, VSP_016593;
CC -!- TISSUE SPECIFICITY: Expressed in endocrine tissue. {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: [Isoform 2]: 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 -!- SEQUENCE CAUTION:
CC Sequence=AAD17298.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAD47387.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH98434.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH98434.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 1214.; 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; AF090114; AAD47387.1; ALT_FRAME; mRNA.
DR EMBL; AF121141; AAD17298.1; ALT_INIT; mRNA.
DR EMBL; AL590383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030687; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC098434; AAH98434.1; ALT_SEQ; mRNA.
DR EMBL; AB015342; BAA34799.1; -; mRNA.
DR CCDS; CCDS4895.2; -. [Q5VUA4-1]
DR RefSeq; NP_055160.2; NM_014345.2. [Q5VUA4-1]
DR RefSeq; XP_011512754.1; XM_011514452.2.
DR AlphaFoldDB; Q5VUA4; -.
DR SMR; Q5VUA4; -.
DR BioGRID; 117299; 93.
DR IntAct; Q5VUA4; 34.
DR STRING; 9606.ENSP00000354964; -.
DR GlyConnect; 2091; 1 N-Linked glycan (1 site).
DR GlyGen; Q5VUA4; 4 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (3 sites).
DR iPTMnet; Q5VUA4; -.
DR PhosphoSitePlus; Q5VUA4; -.
DR BioMuta; ZNF318; -.
DR DMDM; 166215018; -.
DR EPD; Q5VUA4; -.
DR jPOST; Q5VUA4; -.
DR MassIVE; Q5VUA4; -.
DR MaxQB; Q5VUA4; -.
DR PaxDb; Q5VUA4; -.
DR PeptideAtlas; Q5VUA4; -.
DR PRIDE; Q5VUA4; -.
DR ProteomicsDB; 65403; -. [Q5VUA4-1]
DR ProteomicsDB; 65404; -. [Q5VUA4-2]
DR Antibodypedia; 16456; 94 antibodies from 21 providers.
DR DNASU; 24149; -.
DR Ensembl; ENST00000361428.3; ENSP00000354964.2; ENSG00000171467.16. [Q5VUA4-1]
DR Ensembl; ENST00000605935.5; ENSP00000475748.1; ENSG00000171467.16. [Q5VUA4-2]
DR GeneID; 24149; -.
DR KEGG; hsa:24149; -.
DR MANE-Select; ENST00000361428.3; ENSP00000354964.2; NM_014345.3; NP_055160.2.
DR UCSC; uc003ouw.4; human. [Q5VUA4-1]
DR CTD; 24149; -.
DR DisGeNET; 24149; -.
DR GeneCards; ZNF318; -.
DR HGNC; HGNC:13578; ZNF318.
DR HPA; ENSG00000171467; Low tissue specificity.
DR MIM; 617512; gene.
DR neXtProt; NX_Q5VUA4; -.
DR OpenTargets; ENSG00000171467; -.
DR PharmGKB; PA134923137; -.
DR VEuPathDB; HostDB:ENSG00000171467; -.
DR eggNOG; ENOG502R1ZF; Eukaryota.
DR GeneTree; ENSGT00390000000614; -.
DR HOGENOM; CLU_306659_0_0_1; -.
DR InParanoid; Q5VUA4; -.
DR OMA; CQSRPYE; -.
DR OrthoDB; 44718at2759; -.
DR PhylomeDB; Q5VUA4; -.
DR TreeFam; TF350583; -.
DR PathwayCommons; Q5VUA4; -.
DR SignaLink; Q5VUA4; -.
DR SIGNOR; Q5VUA4; -.
DR BioGRID-ORCS; 24149; 14 hits in 1114 CRISPR screens.
DR ChiTaRS; ZNF318; human.
DR GeneWiki; ZNF318; -.
DR GenomeRNAi; 24149; -.
DR Pharos; Q5VUA4; Tbio.
DR PRO; PR:Q5VUA4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VUA4; protein.
DR Bgee; ENSG00000171467; Expressed in left testis and 192 other tissues.
DR ExpressionAtlas; Q5VUA4; baseline and differential.
DR Genevisible; Q5VUA4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR SMART; SM00451; ZnF_U1; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Isopeptide bond; Meiosis;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2279
FT /note="Zinc finger protein 318"
FT /id="PRO_0000191807"
FT ZN_FING 1063..1097
FT /note="Matrin-type 1"
FT ZN_FING 1136..1166
FT /note="Matrin-type 2"
FT REGION 1..1092
FT /note="Interaction with AR"
FT /evidence="ECO:0000250|UniProtKB:Q99PP2"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2252..2279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..343
FT /evidence="ECO:0000255"
FT COILED 876..980
FT /evidence="ECO:0000255"
FT COILED 1768..1792
FT /evidence="ECO:0000255"
FT COMPBIAS 75..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99PP2"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 842
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2030
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2091
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2101
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 2189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 566
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1093..1117
FT /note="TLDPYNRPWASKTQSEAKQDAIKRT -> GQFQKSSDFQKEGLQQTFLPPER
FT QG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016592"
FT VAR_SEQ 1118..2279
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016593"
FT VARIANT 407
FT /note="S -> I (in dbSNP:rs34541323)"
FT /id="VAR_053759"
FT VARIANT 812
FT /note="N -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs141660717)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036056"
FT VARIANT 870
FT /note="L -> V (in dbSNP:rs9357410)"
FT /id="VAR_053760"
FT VARIANT 1274
FT /note="G -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036057"
FT VARIANT 1292
FT /note="T -> I (in dbSNP:rs10948072)"
FT /id="VAR_053761"
FT VARIANT 1580
FT /note="A -> T (in dbSNP:rs3734684)"
FT /id="VAR_053762"
FT VARIANT 1583
FT /note="T -> I (in dbSNP:rs36107018)"
FT /id="VAR_053763"
FT VARIANT 1797
FT /note="V -> A (in dbSNP:rs1459675)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_053764"
FT CONFLICT 62
FT /note="G -> R (in Ref. 1; AAD47387)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="G -> V (in Ref. 1; AAD47387/AAD17298)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034..1035
FT /note="RT -> CI (in Ref. 1; AAD47387/AAD17298)"
FT /evidence="ECO:0000305"
FT CONFLICT 1259
FT /note="L -> F (in Ref. 1; AAD47387/AAD17298)"
FT /evidence="ECO:0000305"
FT CONFLICT 1349
FT /note="R -> G (in Ref. 1; AAD47387/AAD17298)"
FT /evidence="ECO:0000305"
FT CONFLICT 2160
FT /note="S -> F (in Ref. 1; AAD47387/AAD17298)"
FT /evidence="ECO:0000305"
FT CONFLICT 2173
FT /note="V -> D (in Ref. 4; BAA34799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2279 AA; 251112 MW; CC8F7D54710E2450 CRC64;
MYRSSARSSV SSHRPKDDGG GGPRSGRSSG SSSGPARRSS PPPPPSGSSS RTPARRPRSP
SGHRGRRASP SPPRGRRVSP SPPRARRGSP SPPRGRRLFP PGPAGFRGSS RGESRADYAR
DGRGDHPGDS GSRRRSPGLC SDSLEKSLRI TVGNDHFCVS TPERRRLSDR LGSPVDNLED
MDRDDLTDDS VFTRSSQCSR GLERYISQEE GPLSPFLGQL DEDYRTKETF LHRSDYSPHI
SCHDELLRGT ERNREKLKGY SIRSEERSRE AKRPRYDDTV KINSMGGDHP SFTSGTRNYR
QRRRSPSPRF LDPEFRELDL ARRKREEEEE RSRSLSQELV GVDGGGTGCS IPGLSGVLTA
SEPGYSLHRP EEVSVMPKKS ILKKRIEVDI MEPSMQLESF SSSTSSSQDH PLYSGHPSLP
LSGAIAAFAS EIENKGTMVE TALKEPQGNL YQWGPLPGIP KDNSPLREKF GSFLCHKDNL
DLKAEGPERH TDFLLPHERA SQDGSGFSRI LSMLADSTST QEKRRRSFPD IEDEEKFLYG
DEEEDLKAES VPKPLGSSES EVMRQKASSL PSSAPAVKLE SLEETNPEYA KIHDLLKTIG
LDIGVAEISQ LAARTQERLH GKKPSLRSSA DRRSSVDRYF SADHCSSVDH RFSADRCSSV
DHCFSADRRS SDPHRLESRE AHHSNTHSPE VSHPHPPSPV DPYLLTKNSP PFLKSDHPVG
HISGPEVVGS GFQSSVAVRC MLPSAPSAPI RLPHTAALSQ FHMPRASQFA AARIPPNYQG
PAIPPASFDA YRHYMAYAAS RWPMYPTSQP SNHPVPEPHR IMPITKQATR SRPNLRVIPT
VTPDKPKQKE SLRGSIPAAQ VPVQVSIPSL IRYNPEKISD EKNRASQKQK VIEEREKLKN
DREARQKKMY YLRTELERLH KQQGEMLRKK RREKDGHKDP LLVEVSRLQD NIMKDIAELR
QEAEEAEKKQ SELDKVAQIL GINIFDKSQK SLSDSREPTE KPGKAEKSKS PEKVSSFSNS
SSNKESKVNN EKFRTKSPKP AESPQSATKQ LDQPTAAYEY YDAGNHWCKD CNTICGTMFD
FFTHMHNKKH TQTLDPYNRP WASKTQSEAK QDAIKRTDKI TVPAKGSEFL VPISGFYCQL
CEEFLGDPIS GEQHVKGHQH NEKYKKYVDE NPLYEERRNL DRQAGLAVVL ETERRRQSEL
KRKLSEKPKE EKKEKKAKAV KEVKEDDKVS EKLEDQLSEG RNSPEKAENK RNTGIKLQLK
EEVKKESPTS SSFGKFSWKK PEKEEEKSSL VTPSISKEEI LESSKDKEDG KTEAGKAKPI
KIKLSGKTVV AHTSPWMPVV TTSTQTKIRP NLPIPSTVLR KSCSATMSKP APLNTFLSIK
SSGTTAKPLP VVKESSADLL LPPDIISKAF GGEEVILKGS PEEKVVLAEK SEPSHLPEQI
LPPPPPPPPP PPPPPPVIPH PAAPSAAQAN AILAPVKSNP VVSQTLSPGF VGPNILNPVL
PVAIMASAQP AAIPSDETAP GVSESDRDQT LFSVLVRPPP PLSSVFSEQA KKLEKRNSCL
ATANAKDLYD IFYSSGGKGA PETKGAPETK LSGGPLANGE NSNLSRTKSS DTSSTSPLNS
SASQEELHQD EGLVAAPIVS NSEKPIAKTL VALGKWSVVE HVGPKSTGST YGFLQPLTRL
CQSRPYETIT PKTDTLAIWT SSSFQSDTSR DISPEKSELD LGEPGPPGVE PPPQLLDIQC
KESQKLVEIH LRESVNQDKE SQELRKSEDC RESEIETNTE LKERVKELSE GIVDEGVSTS
IGPHSIDDSN LNHGNRYMWE GEVKQPNLLM IDKEAEQSNK LMTGSETPSK VVIKLSPQAC
SFTKAKLDSF LSEARSLLNP QDTPVKISAP ELLLHSPARS AMCLTGSPQE QGVSVVSEEG
LENSAPESAS RTSRYRSLKL KRERSKDFQV KKIYELAVWD ENKKRPETWE SPEKPKTEAL
ELQDVHPELT VTIESKALED FEATDLKVEE LTALGNLGDM PVDFCTTRVS PAHRSPTVLC
QKVCEENSVS PIGCNSSDPA DFEPIPSFSG FPLDSPKTLV LDFETEGERN SPNPRSVRIP
SPNILKTGLT ENVDRGLGGL EGTHQALDLL AGGMMPEEVK ESSQLDKQES LGLELKTINS
AGLGPSPCLP DLVDFVTRTS GVQKDKLCSP LSEPGDPSKC SSLELGPLQL EISNASTTEV
AILQVDDDSG DPLNLVKAPV SRSPPREQVI EDNMVPQGMP EQETTVGAIQ DHTESSVHN
