ID   SUGP2_HUMAN             Reviewed;        1082 AA.
AC   Q8IX01; C9JI71; O15071; O60369; Q5JPH7; Q8WUF7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   02-SEP-2026, entry version 180.
DE   RecName: Full=SURP and G-patch domain-containing protein 2;
DE   AltName: Full=Arginine/serine-rich-splicing factor 14;
DE   AltName: Full=Splicing factor, arginine/serine-rich 14;
GN   Name=SUGP2; Synonyms=KIAA0365, SFRS14;
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), ALTERNATIVE SPLICING, TISSUE
RP   SPECIFICITY, AND VARIANT SER-206.
RX   PubMed=12594045; DOI=10.1016/s0378-1119(02)01230-1;
RA   Sampson N.D., Hewitt J.E.;
RT   "SF4 and SFRS14, two related putative splicing factors on human chromosome
RT   19p13.11.";
RL   Gene 305:91-100(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [3]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R., Nomura N.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP   SER-206.
RC   TISSUE=Endometrial tumor, and Testis;
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=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-206.
RC   TISSUE=Duodenum;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7, AND IDENTIFICATION BY MASS
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275 AND SER-277, AND
RP   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   [9]
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   [10]
RP   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   [11]
RP   IDENTIFICATION BY 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   [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 SER-96; SER-224; SER-315; SER-573
RP   AND SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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-573 AND SER-754, AND
RP   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-228; LYS-305 AND LYS-650, 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   [16]
RP   STRUCTURE BY NMR OF 587-639.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of SURP domain in SFRS14 protein.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May play a role in mRNA splicing. {ECO:0000305}.
CC   -!- INTERACTION:
CC       Q8IX01-3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12317645, EBI-618309;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8IX01-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q8IX01-3; Sequence=VSP_013112, VSP_013113;
CC       Name=4;
CC         IsoId=Q8IX01-4; Sequence=VSP_013112;
CC   -!- TISSUE SPECIFICITY: Detected in adult testis, and in fetal brain and
CC       kidney. {ECO:0000269|PubMed:12594045}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC06129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAH20586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA20820.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF518874; AAN77117.1; -; mRNA.
DR   EMBL; AB002363; BAA20820.2; ALT_INIT; mRNA.
DR   EMBL; BX647813; CAI46012.1; -; mRNA.
DR   EMBL; AL832488; CAI46117.1; -; mRNA.
DR   EMBL; AC004447; AAC06129.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC020586; AAH20586.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12392.1; -. [Q8IX01-1]
DR   PIR; T03030; T03030.
DR   RefSeq; NP_001017392.2; NM_001017392.5. [Q8IX01-1]
DR   RefSeq; NP_001308626.1; NM_001321697.2. [Q8IX01-1]
DR   RefSeq; NP_001339000.1; NM_001352071.2. [Q8IX01-1]
DR   RefSeq; NP_055699.2; NM_014884.5. [Q8IX01-1]
DR   PDB; 1X4P; NMR; -; A=587-639.
DR   AlphaFoldDB; Q8IX01; -.
DR   SMR; Q8IX01; -.
DR   BioGRID; 115449; 245.
DR   FunCoup; Q8IX01; 2706.
DR   IntAct; Q8IX01; 123.
DR   MINT; Q8IX01; -.
DR   STRING; 9606.ENSP00000472914; -.
DR   GlyCosmos; Q8IX01; 3 sites, 1 glycan.
DR   GlyGen; Q8IX01; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q8IX01; -.
DR   PhosphoSitePlus; Q8IX01; -.
DR   SwissPalm; Q8IX01; -.
DR   BioMuta; SUGP2; -.
DR   DMDM; 308153496; -.
DR   jPOST; Q8IX01; -.
DR   MassIVE; Q8IX01; -.
DR   PaxDb; 9606-ENSP00000472914; -.
DR   PeptideAtlas; Q8IX01; -.
DR   ProteomicsDB; 70947; -. [Q8IX01-1]
DR   ProteomicsDB; 70948; -. [Q8IX01-3]
DR   ProteomicsDB; 70949; -. [Q8IX01-4]
DR   Pumba; Q8IX01; -.
DR   Antibodypedia; 28312; 158 antibodies from 27 providers.
DR   DNASU; 10147; -.
DR   Ensembl; ENST00000330854.15; ENSP00000332373.10; ENSG00000064607.18. [Q8IX01-4]
DR   Ensembl; ENST00000337018.10; ENSP00000337926.5; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000452918.7; ENSP00000389380.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000594773.5; ENSP00000470915.1; ENSG00000064607.18. [Q8IX01-3]
DR   Ensembl; ENST00000601879.5; ENSP00000472286.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867061.1; ENSP00000537120.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867062.1; ENSP00000537121.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867063.1; ENSP00000537122.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867064.1; ENSP00000537123.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867065.1; ENSP00000537124.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867066.1; ENSP00000537125.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867067.1; ENSP00000537126.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867068.1; ENSP00000537127.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867069.1; ENSP00000537128.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000867070.1; ENSP00000537129.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000928454.1; ENSP00000598513.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000928456.1; ENSP00000598515.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000928457.1; ENSP00000598516.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000953721.1; ENSP00000623780.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000953724.1; ENSP00000623783.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000953725.1; ENSP00000623784.1; ENSG00000064607.18. [Q8IX01-1]
DR   Ensembl; ENST00000953726.1; ENSP00000623785.1; ENSG00000064607.18. [Q8IX01-1]
DR   GeneID; 10147; -.
DR   KEGG; hsa:10147; -.
DR   MANE-Select; ENST00000452918.7; ENSP00000389380.1; NM_001017392.5; NP_001017392.2.
DR   UCSC; uc002nkx.3; human. [Q8IX01-1]
DR   AGR; HGNC:18641; -.
DR   ClinPGx; PA165394371; -.
DR   CTD; 10147; -.
DR   DisGeNET; 10147; -.
DR   GeneCards; SUGP2; -.
DR   HGNC; HGNC:18641; SUGP2.
DR   HPA; ENSG00000064607; Low tissue specificity.
DR   MIM; 607993; gene.
DR   OpenTargets; ENSG00000064607; -.
DR   VEuPathDB; HostDB:ENSG00000064607; -.
DR   eggNOG; KOG0965; Eukaryota.
DR   GeneTree; ENSGT00410000025695; -.
DR   HOGENOM; CLU_010012_0_0_1; -.
DR   InParanoid; Q8IX01; -.
DR   OMA; KAKRYHI; -.
DR   OrthoDB; 4822at2759; -.
DR   PAN-GO; Q8IX01; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8IX01; -.
DR   PathwayCommons; Q8IX01; -.
DR   SignaLink; Q8IX01; -.
DR   Agora; ENSG00000064607; -.
DR   BioGRID-ORCS; 10147; 29 hits in 1158 CRISPR screens.
DR   CD-CODE; 232F8A39; P-body.
DR   CD-CODE; DEE660B4; Stress granule.
DR   ChiTaRS; SUGP2; human.
DR   EvolutionaryTrace; Q8IX01; -.
DR   GeneWiki; SFRS14; -.
DR   GenomeRNAi; 10147; -.
DR   Pharos; Q8IX01; Tdark.
DR   PRO; PR:Q8IX01; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8IX01; protein.
DR   Bgee; ENSG00000064607; Expressed in left testis and 204 other cell types or tissues.
DR   ExpressionAtlas; Q8IX01; baseline and differential.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   FunFam; 1.10.10.790:FF:000008; SURP and G-patch domain-containing protein 2; 1.
DR   FunFam; 1.10.10.790:FF:000010; SURP and G-patch domain-containing protein 2; 1.
DR   Gene3D; 1.10.10.790; Surp module; 2.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR040169; SUGP1/2.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR035967; SWAP/Surp_sf.
DR   PANTHER; PTHR23340; ARGININE/SERINE RICH SPLICING FACTOR SF4/14; 1.
DR   PANTHER; PTHR23340:SF2; SURP AND G-PATCH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF27652; ARMC6_N; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01805; Surp; 2.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00648; SWAP; 2.
DR   SUPFAM; SSF109905; Surp module (SWAP domain); 2.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50128; SURP; 1.
DR   PDBsum; 1X4P; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Isopeptide bond; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..1082
FT                   /note="SURP and G-patch domain-containing protein 2"
FT                   /id="PRO_0000097708"
FT   REPEAT          590..633
FT                   /note="SURP motif 1"
FT   REPEAT          787..830
FT                   /note="SURP motif 2"
FT   DOMAIN          1011..1057
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           995..1000
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        71..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..708
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..738
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..877
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..904
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..999
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         275
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         573
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         757
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CH09"
FT   MOD_RES         863
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CH09"
FT   CROSSLNK        228
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        305
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        650
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         890..941
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_013112"
FT   VAR_SEQ         1044..1082
FT                   /note="GTPSEGEGLGADGQEHKEDTFDVFRQRMMQMYRHKRANK -> YAAGSLGWE
FT                   WVGPQSFHLQPAAWLLHSQDGLQLAVDFCFLNRRHLQMRS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013113"
FT   VARIANT         206
FT                   /note="G -> S (in dbSNP:rs4808907)"
FT                   /evidence="ECO:0000269|PubMed:12594045,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_023711"
FT   VARIANT         552
FT                   /note="M -> T (in dbSNP:rs10404860)"
FT                   /id="VAR_051341"
FT   VARIANT         649
FT                   /note="Q -> R (in dbSNP:rs10414535)"
FT                   /id="VAR_051342"
FT   VARIANT         722
FT                   /note="Q -> R (in dbSNP:rs34540303)"
FT                   /id="VAR_051343"
FT   VARIANT         881
FT                   /note="R -> Q (in dbSNP:rs35646935)"
FT                   /id="VAR_051344"
FT   HELIX           588..599
FT                   /evidence="ECO:0007829|PDB:1X4P"
FT   HELIX           604..612
FT                   /evidence="ECO:0007829|PDB:1X4P"
FT   HELIX           614..616
FT                   /evidence="ECO:0007829|PDB:1X4P"
FT   TURN            618..620
FT                   /evidence="ECO:0007829|PDB:1X4P"
FT   STRAND          623..625
FT                   /evidence="ECO:0007829|PDB:1X4P"
FT   HELIX           626..639
FT                   /evidence="ECO:0007829|PDB:1X4P"
SQ   SEQUENCE   1082 AA;  120207 MW;  619AE0AC087761BD CRC64;
     MAARRITQET FDAVLQEKAK RYHMDASGEA VSETLQFKAQ DLLRAVPRSR AEMYDDVHSD
     GRYSLSGSVA HSRDAGREGL RSDVFPGPSF RSSNPSISDD SYFRKECGRD LEFSHSDSRD
     QVIGHRKLGH FRSQDWKFAL RGSWEQDFGH PVSQESSWSQ EYSFGPSAVL GDFGSSRLIE
     KECLEKESRD YDVDHPGEAD SVLRGGSQVQ ARGRALNIVD QEGSLLGKGE TQGLLTAKGG
     VGKLVTLRNV STKKIPTVNR ITPKTQGTNQ IQKNTPSPDV TLGTNPGTED IQFPIQKIPL
     GLDLKNLRLP RRKMSFDIID KSDVFSRFGI EIIKWAGFHT IKDDIKFSQL FQTLFELETE
     TCAKMLASFK CSLKPEHRDF CFFTIKFLKH SALKTPRVDN EFLNMLLDKG AVKTKNCFFE
     IIKPFDKYIM RLQDRLLKSV TPLLMACNAY ELSVKMKTLS NPLDLALALE TTNSLCRKSL
     ALLGQTFSLA SSFRQEKILE AVGLQDIAPS PAAFPNFEDS TLFGREYIDH LKAWLVSSGC
     PLQVKKAEPE PMREEEKMIP PTKPEIQAKA PSSLSDAVPQ RADHRVVGTI DQLVKRVIEG
     SLSPKERTLL KEDPAYWFLS DENSLEYKYY KLKLAEMQRM SENLRGADQK PTSADCAVRA
     MLYSRAVRNL KKKLLPWQRR GLLRAQGLRG WKARRATTGT QTLLSSGTRL KHHGRQAPGL
     SQAKPSLPDR NDAAKDCPPD PVGPSPQDPS LEASGPSPKP AGVDISEAPQ TSSPCPSADI
     DMKTMETAEK LARFVAQVGP EIEQFSIENS TDNPDLWFLH DQNSSAFKFY RKKVFELCPS
     ICFTSSPHNL HTGGGDTTGS QESPVDLMEG EAEFEDEPPP REAELESPEV MPEEEDEDDE
     DGGEEAPAPG GAGKSEGSTP ADGLPGEAAE DDLAGAPALS QASSGTCFPR KRISSKSLKV
     GMIPAPKRVC LIQEPKVHEP VRIAYDRPRG RPMSKKKKPK DLDFAQQKLT DKNLGFQMLQ
     KMGWKEGHGL GSLGKGIREP VSVGTPSEGE GLGADGQEHK EDTFDVFRQR MMQMYRHKRA
     NK
//