ID   U2AFM_HUMAN             Reviewed;         482 AA.
AC   Q15696; Q14D69;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2;
DE   AltName: Full=CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2;
DE   AltName: Full=Renal carcinoma antigen NY-REN-20;
DE   AltName: Full=U2(RNU2) small nuclear RNA auxiliary factor 1-like 2;
DE   AltName: Full=U2AF35-related protein;
DE            Short=URP;
GN   Name=ZRSR2; Synonyms=U2AF1-RS2, U2AF1L2, U2AF1RS2, URP;
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].
RC   TISSUE=Brain;
RX   PubMed=8586425; DOI=10.1006/geno.1995.9879;
RA   Kitagawa K., Wang X., Hatada I., Yamaoka T., Nojima H., Inazawa J., Abe T.,
RA   Mitsuya K., Oshimura M., Murata A., Monden M., Mukai T.;
RT   "Isolation and mapping of human homologues of an imprinted mouse gene
RT   U2af1-rs1.";
RL   Genomics 30:257-263(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INTERACTION WITH SRSF1;
RP   SRSF2; SRPK1 AND U2AF2.
RX   PubMed=9237760; DOI=10.1038/41137;
RA   Tronchere H., Wang J., Fu X.D.;
RT   "A protein related to splicing factor U2AF35 that interacts with U2AF65 and
RT   SR proteins in splicing of pre-mRNA.";
RL   Nature 388:397-400(1997).
RN   [5]
RP   IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10508479;
RX   DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA   Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA   Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA   Old L.J.;
RT   "Antigens recognized by autologous antibody in patients with renal-cell
RT   carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [6]
RP   IDENTIFICATION IN THE U11/U12 SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=15146077; DOI=10.1261/rna.7320604;
RA   Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA   Tuschl T., Luehrmann R.;
RT   "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT   the U2-dependent spliceosome.";
RL   RNA 10:929-941(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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   [9]
RP   FUNCTION, IDENTIFICATION IN THE U11/U12 SPLICEOSOME COMPLEX, AND
RP   RNA-BINDING.
RX   PubMed=21041408; DOI=10.1101/gad.1974810;
RA   Shen H., Zheng X., Luecke S., Green M.R.;
RT   "The U2AF35-related protein Urp contacts the 3' splice site to promote U12-
RT   type intron splicing and the second step of U2-type intron splicing.";
RL   Genes Dev. 24:2389-2394(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-45 AND LYS-62, AND IDENTIFICATION
RP   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).
CC   -!- FUNCTION: Pre-mRNA-binding protein required for splicing of both
CC       U2- and U12-type introns. Selectively interacts with the 3'-splice site
CC       of U2- and U12-type pre-mRNAs and promotes different steps in U2 and
CC       U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent
CC       manner and is required for assembly of the prespliceosome, a precursor
CC       to other spliceosomal complexes. For U2-type introns, it is selectively
CC       and specifically required for the second step of splicing.
CC       {ECO:0000269|PubMed:21041408, ECO:0000269|PubMed:9237760}.
CC   -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC       spliceosome. Interacts (via RS domain) with SRSF1 and SRSF2. Interacts
CC       with U2AF2/U2AF65. {ECO:0000269|PubMed:15146077,
CC       ECO:0000269|PubMed:21041408, ECO:0000269|PubMed:9237760}.
CC   -!- INTERACTION:
CC       Q15696; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-6657923, EBI-2836773;
CC       Q15696; P49760: CLK2; NbExp=8; IntAct=EBI-6657923, EBI-750020;
CC       Q15696; Q92997: DVL3; NbExp=3; IntAct=EBI-6657923, EBI-739789;
CC       Q15696; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-6657923, EBI-9089060;
CC       Q15696; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-6657923, EBI-352851;
CC       Q15696; Q6BDI9: REP15; NbExp=3; IntAct=EBI-6657923, EBI-12048237;
CC       Q15696; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-6657923, EBI-742426;
CC       Q15696; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-6657923, EBI-539478;
CC       Q15696; P78362: SRPK2; NbExp=7; IntAct=EBI-6657923, EBI-593303;
CC       Q15696; A7MD48: SRRM4; NbExp=3; IntAct=EBI-6657923, EBI-3867173;
CC       Q15696; Q13243: SRSF5; NbExp=3; IntAct=EBI-6657923, EBI-720503;
CC       Q15696; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-6657923, EBI-2212028;
CC       Q15696; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-6657923, EBI-11139477;
CC       Q15696; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-6657923, EBI-752102;
CC       Q15696; Q15696: ZRSR2; NbExp=3; IntAct=EBI-6657923, EBI-6657923;
CC       Q15696; Q15695: ZRSR2P1; NbExp=4; IntAct=EBI-6657923, EBI-12270264;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15146077}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9237760}.
CC   -!- PTM: Phosphorylated in the RS domain by SRPK1.
CC       {ECO:0000269|PubMed:9237760}.
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DR   EMBL; D49677; BAA08533.1; -; mRNA.
DR   EMBL; AC004106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113454; AAI13455.1; -; mRNA.
DR   EMBL; BC113480; AAI13481.1; -; mRNA.
DR   CCDS; CCDS14172.1; -.
DR   RefSeq; NP_005080.1; NM_005089.3.
DR   AlphaFoldDB; Q15696; -.
DR   SMR; Q15696; -.
DR   BioGRID; 113865; 78.
DR   CORUM; Q15696; -.
DR   DIP; DIP-62117N; -.
DR   IntAct; Q15696; 52.
DR   STRING; 9606.ENSP00000303015; -.
DR   iPTMnet; Q15696; -.
DR   PhosphoSitePlus; Q15696; -.
DR   BioMuta; ZRSR2; -.
DR   DMDM; 2833266; -.
DR   EPD; Q15696; -.
DR   jPOST; Q15696; -.
DR   MassIVE; Q15696; -.
DR   MaxQB; Q15696; -.
DR   PaxDb; 9606-ENSP00000303015; -.
DR   PeptideAtlas; Q15696; -.
DR   ProteomicsDB; 60704; -.
DR   Pumba; Q15696; -.
DR   Antibodypedia; 8950; 125 antibodies from 22 providers.
DR   DNASU; 8233; -.
DR   Ensembl; ENST00000307771.8; ENSP00000303015.7; ENSG00000169249.14.
DR   GeneID; 8233; -.
DR   KEGG; hsa:8233; -.
DR   MANE-Select; ENST00000307771.8; ENSP00000303015.7; NM_005089.4; NP_005080.1.
DR   UCSC; uc004cxg.5; human.
DR   AGR; HGNC:23019; -.
DR   CTD; 8233; -.
DR   DisGeNET; 8233; -.
DR   GeneCards; ZRSR2; -.
DR   HGNC; HGNC:23019; ZRSR2.
DR   HPA; ENSG00000169249; Low tissue specificity.
DR   MIM; 300028; gene.
DR   neXtProt; NX_Q15696; -.
DR   OpenTargets; ENSG00000169249; -.
DR   PharmGKB; PA162410930; -.
DR   VEuPathDB; HostDB:ENSG00000169249; -.
DR   eggNOG; KOG2202; Eukaryota.
DR   GeneTree; ENSGT00950000183152; -.
DR   HOGENOM; CLU_029117_1_0_1; -.
DR   InParanoid; Q15696; -.
DR   OMA; HCEICPV; -.
DR   OrthoDB; 1967949at2759; -.
DR   PhylomeDB; Q15696; -.
DR   TreeFam; TF324447; -.
DR   PathwayCommons; Q15696; -.
DR   Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR   SignaLink; Q15696; -.
DR   SIGNOR; Q15696; -.
DR   BioGRID-ORCS; 8233; 193 hits in 789 CRISPR screens.
DR   ChiTaRS; ZRSR2; human.
DR   GeneWiki; ZRSR2; -.
DR   GenomeRNAi; 8233; -.
DR   Pharos; Q15696; Tbio.
DR   PRO; PR:Q15696; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q15696; Protein.
DR   Bgee; ENSG00000169249; Expressed in sural nerve and 208 other cell types or tissues.
DR   ExpressionAtlas; Q15696; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR   GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IC:HGNC-UCL.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IMP:UniProtKB.
DR   CDD; cd12540; RRM_U2AFBPL; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   InterPro; IPR009145; U2AF_small.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR12620:SF38; U2 SMALL NUCLEAR RIBONUCLEOPROTEIN AUXILIARY FACTOR 35 KDA SUBUNIT-RELATED PROTEIN 2; 1.
DR   PANTHER; PTHR12620; U2 SNRNP AUXILIARY FACTOR, SMALL SUBUNIT; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   PRINTS; PR01848; U2AUXFACTOR.
DR   SMART; SM00361; RRM_1; 1.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
DR   Genevisible; Q15696; HS.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   Spliceosome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..482
FT                   /note="U2 small nuclear ribonucleoprotein auxiliary factor
FT                   35 kDa subunit-related protein 2"
FT                   /id="PRO_0000082001"
FT   DOMAIN          198..304
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   ZN_FING         166..194
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         306..333
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..420
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..469
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:21406692"
FT   CROSSLNK        45
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        62
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
SQ   SEQUENCE   482 AA;  58045 MW;  1DACC8A6CA4727A6 CRC64;
     MAAPEKMTFP EKPSHKKYRA ALKKEKRKKR RQELARLRDS GLSQKEEEED TFIEEQQLEE
     EKLLERERQR LHEEWLLREQ KAQEEFRIKK EKEEAAKKRQ EEQERKLKEQ WEEQQRKERE
     EEEQKRQEKK EKEEALQKML DQAENELENG TTWQNPEPPV DFRVMEKDRA NCPFYSKTGA
     CRFGDRCSRK HNFPTSSPTL LIKSMFTTFG MEQCRRDDYD PDASLEYSEE ETYQQFLDFY
     EDVLPEFKNV GKVIQFKVSC NLEPHLRGNV YVQYQSEEEC QAALSLFNGR WYAGRQLQCE
     FCPVTRWKMA ICGLFEIQQC PRGKHCNFLH VFRNPNNEFW EANRDIYLSP DRTGSSFGKN
     SERRERMGHH DDYYSRLRGR RNPSPDHSYK RNGESERKSS RHRGKKSHKR TSKSRERHNS
     RSRGRNRDRS RDRSRGRGSR SRSRSRSRRS RRSRSQSSSR SRSRGRRRSG NRDRTVQSPK
     SK
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