ID   ZBTB2_HUMAN             Reviewed;         514 AA.
AC   Q8N680; A8K7C7; Q5SZ81; Q9P245;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 2;
GN   Name=ZBTB2; Synonyms=KIAA1483, ZNF437;
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 [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
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 GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Melanoma;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-514.
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
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-341, AND IDENTIFICATION BY
RP   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   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-505, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-505, 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   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-362 AND LYS-505, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-154; LYS-362; LYS-465;
RP   LYS-505 AND LYS-506, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q8N680; Q9UER7: DAXX; NbExp=3; IntAct=EBI-2515601, EBI-77321;
CC       Q8N680; P60520: GABARAPL2; NbExp=3; IntAct=EBI-2515601, EBI-720116;
CC       Q8N680; Q9UHH9: IP6K2; NbExp=3; IntAct=EBI-2515601, EBI-747509;
CC       Q8N680; Q92993: KAT5; NbExp=3; IntAct=EBI-2515601, EBI-399080;
CC       Q8N680; Q969G2: LHX4; NbExp=3; IntAct=EBI-2515601, EBI-2865388;
CC       Q8N680; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2515601, EBI-739832;
CC       Q8N680; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2515601, EBI-16439278;
CC       Q8N680; Q9UL63: MKLN1; NbExp=3; IntAct=EBI-2515601, EBI-1048053;
CC       Q8N680; P00540: MOS; NbExp=3; IntAct=EBI-2515601, EBI-1757866;
CC       Q8N680; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-2515601, EBI-5453723;
CC       Q8N680; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2515601, EBI-79165;
CC       Q8N680; Q13526: PIN1; NbExp=3; IntAct=EBI-2515601, EBI-714158;
CC       Q8N680; Q8NHQ8-2: RASSF8; NbExp=4; IntAct=EBI-2515601, EBI-10976415;
CC       Q8N680; P08047: SP1; NbExp=4; IntAct=EBI-2515601, EBI-298336;
CC       Q8N680; P63165: SUMO1; NbExp=3; IntAct=EBI-2515601, EBI-80140;
CC       Q8N680; O43463: SUV39H1; NbExp=3; IntAct=EBI-2515601, EBI-349968;
CC       Q8N680; Q96A09: TENT5B; NbExp=3; IntAct=EBI-2515601, EBI-752030;
CC       Q8N680; Q7Z403: TMC6; NbExp=3; IntAct=EBI-2515601, EBI-9088037;
CC       Q8N680; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2515601, EBI-10180829;
CC       Q8N680; Q99592: ZBTB18; NbExp=3; IntAct=EBI-2515601, EBI-3232046;
CC       Q8N680; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-2515601, EBI-2515601;
CC       Q8N680; P24278: ZBTB25; NbExp=3; IntAct=EBI-2515601, EBI-739899;
CC       Q8N680; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-2515601, EBI-2859943;
CC       Q8N680; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-2515601, EBI-746595;
CC       Q8N680; Q9UID6: ZNF639; NbExp=5; IntAct=EBI-2515601, EBI-947476;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AK291942; BAF84631.1; -; mRNA.
DR   EMBL; AL590413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47751.1; -; Genomic_DNA.
DR   EMBL; BC020172; AAH20172.1; -; mRNA.
DR   EMBL; AB040916; BAA96007.1; -; mRNA.
DR   CCDS; CCDS5231.1; -.
DR   RefSeq; NP_065912.1; NM_020861.2.
DR   RefSeq; XP_005267133.1; XM_005267076.2.
DR   RefSeq; XP_011534306.1; XM_011536004.2.
DR   AlphaFoldDB; Q8N680; -.
DR   BioGRID; 121667; 461.
DR   DIP; DIP-53681N; -.
DR   IntAct; Q8N680; 46.
DR   MINT; Q8N680; -.
DR   STRING; 9606.ENSP00000323183; -.
DR   ChEMBL; CHEMBL5069373; -.
DR   iPTMnet; Q8N680; -.
DR   PhosphoSitePlus; Q8N680; -.
DR   SwissPalm; Q8N680; -.
DR   BioMuta; ZBTB2; -.
DR   DMDM; 30316315; -.
DR   EPD; Q8N680; -.
DR   jPOST; Q8N680; -.
DR   MassIVE; Q8N680; -.
DR   MaxQB; Q8N680; -.
DR   PaxDb; 9606-ENSP00000323183; -.
DR   PeptideAtlas; Q8N680; -.
DR   ProteomicsDB; 72136; -.
DR   Pumba; Q8N680; -.
DR   Antibodypedia; 19926; 180 antibodies from 29 providers.
DR   DNASU; 57621; -.
DR   Ensembl; ENST00000325144.5; ENSP00000323183.4; ENSG00000181472.5.
DR   GeneID; 57621; -.
DR   KEGG; hsa:57621; -.
DR   MANE-Select; ENST00000325144.5; ENSP00000323183.4; NM_020861.3; NP_065912.1.
DR   UCSC; uc003qoh.4; human.
DR   AGR; HGNC:20868; -.
DR   CTD; 57621; -.
DR   DisGeNET; 57621; -.
DR   GeneCards; ZBTB2; -.
DR   HGNC; HGNC:20868; ZBTB2.
DR   HPA; ENSG00000181472; Low tissue specificity.
DR   MIM; 616595; gene.
DR   neXtProt; NX_Q8N680; -.
DR   OpenTargets; ENSG00000181472; -.
DR   PharmGKB; PA134949885; -.
DR   VEuPathDB; HostDB:ENSG00000181472; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000158401; -.
DR   HOGENOM; CLU_025271_1_0_1; -.
DR   InParanoid; Q8N680; -.
DR   OMA; HLCRSRF; -.
DR   OrthoDB; 5351313at2759; -.
DR   PhylomeDB; Q8N680; -.
DR   TreeFam; TF332229; -.
DR   PathwayCommons; Q8N680; -.
DR   SignaLink; Q8N680; -.
DR   BioGRID-ORCS; 57621; 67 hits in 1217 CRISPR screens.
DR   ChiTaRS; ZBTB2; human.
DR   GenomeRNAi; 57621; -.
DR   Pharos; Q8N680; Tbio.
DR   PRO; PR:Q8N680; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8N680; Protein.
DR   Bgee; ENSG00000181472; Expressed in secondary oocyte and 163 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR   CDD; cd18193; BTB_POZ_ZBTB2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24394:SF41; ZINC FINGER AND BTB DOMAIN CONTAINING 2; 1.
DR   PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
DR   Genevisible; Q8N680; HS.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..514
FT                   /note="Zinc finger and BTB domain-containing protein 2"
FT                   /id="PRO_0000047709"
FT   DOMAIN          24..89
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         254..276
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         363..385
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         390..410
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         448..468
FT                   /note="C2H2-type 4; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          149..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CROSSLNK        147
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        154
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        362
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        465
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        505
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        506
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CONFLICT        466
FT                   /note="H -> L (in Ref. 5; BAA96007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  57337 MW;  2087A104CCA3DD85 CRC64;
     MDLANHGLIL LQQLNAQREF GFLCDCTVAI GDVYFKAHKS VLASFSNYFK MLFVHQTSEC
     VRLKPTDIQP DIFSYLLHLM YTGKMAPQLI DPVRLEQGIK FLHAYPLIQE ASLASQGAFS
     HPDQVFPLAS SLYGIQIADH QLRQATKIAS APEKLGRDPR PQTSRISQEQ VPEASQLSQL
     TSNLAQVNRT NMTPSDPLQT SLSPELVSTP VPPPPPGEET NLEASSSDEQ PASLTIAHVK
     PSIMKRNGSF PKYYACHLCG RRFTLRSSLR EHLQIHTGVP FTSSQQGESR VPLTLCSNAA
     DLGKDAMEVP EAGMISDSEL QHISDSPIID GQQQSETPPP SDIADIDNLE QADQEREVKR
     RKYECTICGR KFIQKSHWRE HMYIHTGKPF KCSTCDKSFC RANQAARHVC LNQSIDTYTM
     VDKQTLELCT FEEGSQMDNM LVQTNKPYKC NLCDKTFSTP NEVVKHSCQN QNSDVFALDE
     GRSILLGSGD SEVTEPDHPV LASIKKEQET VLLD
//