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   27-MAR-2024, entry version 163.
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};
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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; 118.
DR   IntAct; Q5VUA4; 37.
DR   MINT; Q5VUA4; -.
DR   STRING; 9606.ENSP00000354964; -.
DR   GlyConnect; 2091; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q5VUA4; 4 sites, 3 glycans.
DR   GlyGen; Q5VUA4; 8 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (7 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; 9606-ENSP00000354964; -.
DR   PeptideAtlas; Q5VUA4; -.
DR   ProteomicsDB; 65403; -. [Q5VUA4-1]
DR   ProteomicsDB; 65404; -. [Q5VUA4-2]
DR   Pumba; Q5VUA4; -.
DR   Antibodypedia; 16456; 116 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   AGR; HGNC:13578; -.
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; DTLAMWT; -.
DR   OrthoDB; 2969966at2759; -.
DR   PhylomeDB; Q5VUA4; -.
DR   TreeFam; TF350583; -.
DR   PathwayCommons; Q5VUA4; -.
DR   SignaLink; Q5VUA4; -.
DR   SIGNOR; Q5VUA4; -.
DR   BioGRID-ORCS; 24149; 14 hits in 1194 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 194 other cell types or tissues.
DR   ExpressionAtlas; Q5VUA4; baseline and differential.
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 DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   PANTHER; PTHR15577; ZINC FINGER CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR15577:SF2; ZINC FINGER PROTEIN 318; 1.
DR   SMART; SM00451; ZnF_U1; 2.
DR   Genevisible; Q5VUA4; HS.
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
//