ID ZN33A_HUMAN Reviewed; 810 AA. AC Q06730; A8K9X9; B4E0M8; F6TH33; F8WAJ5; P17013; Q5VZ86; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 09-APR-2025, entry version 213. DE RecName: Full=Zinc finger protein 33A; DE AltName: Full=Zinc finger and ZAK-associated protein with KRAB domain; DE Short=ZZaPK; DE AltName: Full=Zinc finger protein 11A; DE AltName: Full=Zinc finger protein KOX31; GN Name=ZNF33A; Synonyms=KIAA0065, KOX31, ZNF11, ZNF11A, ZNF33; 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), AND INTERACTION WITH MAP3K20. RX PubMed=12535642; DOI=10.1016/s0006-291x(02)02980-7; RA Yang J.-J.; RT "A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the RT ZAK-expressing cells re-entering the cell cycle."; RL Biochem. Biophys. Res. Commun. 301:71-77(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., RA Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. The RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP GLU-549. RC TISSUE=Trachea; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 139-361 AND 629-810 (ISOFORM RP 1). RX PubMed=8464732; DOI=10.1093/nar/21.6.1409; RA Tunnacliffe A., Liu L., Moore J.K., Leversha M.A., Jackson M.S., RA Ferguson-Smith M.A., Thiesen H.-J., Ponder B.A.; RT "Duplicated KOX zinc finger gene clusters flank the centromere of human RT chromosome 10: evidence for a pericentric inversion during primate RT evolution."; RL Nucleic Acids Res. 21:1409-1417(1993). RN [6] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-180, 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 [7] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND IDENTIFICATION BY MASS RP 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 [8] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-180; LYS-237; LYS-312; LYS-456; RP LYS-676 AND LYS-732, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND RP LYS-92 (ISOFORM 2), 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 -!- SUBUNIT: Interacts with MAP3K20/ZAK. {ECO:0000269|PubMed:12535642}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q06730-1; Sequence=Displayed; CC Name=2; CC IsoId=Q06730-2; Sequence=VSP_046420; CC Name=3; CC IsoId=Q06730-3; Sequence=VSP_055165; CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY184389; AAO24702.1; -; mRNA. DR EMBL; D31763; BAA06541.1; -; mRNA. DR EMBL; AK292844; BAF85533.1; -; mRNA. DR EMBL; AK303445; BAG64490.1; -; mRNA. DR EMBL; AL161931; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL117337; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X68686; CAA48645.1; -; Genomic_DNA. DR EMBL; X68687; CAA48646.1; -; mRNA. DR EMBL; X68689; CAA48648.1; -; Genomic_DNA. DR CCDS; CCDS31182.1; -. [Q06730-1] DR CCDS; CCDS44372.1; -. [Q06730-2] DR CCDS; CCDS60514.1; -. [Q06730-3] DR PIR; S33991; S33991. DR PIR; S33992; S33990. DR RefSeq; NP_001265099.1; NM_001278170.2. [Q06730-3] DR RefSeq; NP_001265100.1; NM_001278171.1. DR RefSeq; NP_001265102.1; NM_001278173.1. DR RefSeq; NP_001265103.1; NM_001278174.1. DR RefSeq; NP_001265104.1; NM_001278175.1. DR RefSeq; NP_001265105.1; NM_001278176.1. DR RefSeq; NP_001265106.1; NM_001278177.1. DR RefSeq; NP_001265107.1; NM_001278178.1. DR RefSeq; NP_001265108.1; NM_001278179.1. DR RefSeq; NP_008885.1; NM_006954.2. [Q06730-2] DR RefSeq; NP_008905.1; NM_006974.3. [Q06730-1] DR RefSeq; XP_011517952.1; XM_011519650.3. [Q06730-2] DR RefSeq; XP_011517953.1; XM_011519651.3. [Q06730-1] DR AlphaFoldDB; Q06730; -. DR SMR; Q06730; -. DR BioGRID; 113410; 10. DR IntAct; Q06730; 7. DR STRING; 9606.ENSP00000304268; -. DR GlyGen; Q06730; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q06730; -. DR PhosphoSitePlus; Q06730; -. DR BioMuta; ZNF33A; -. DR DMDM; 11140929; -. DR jPOST; Q06730; -. DR MassIVE; Q06730; -. DR PaxDb; 9606-ENSP00000304268; -. DR PeptideAtlas; Q06730; -. DR ProteomicsDB; 27974; -. DR ProteomicsDB; 30512; -. DR ProteomicsDB; 58475; -. [Q06730-1] DR Pumba; Q06730; -. DR Antibodypedia; 26733; 111 antibodies from 17 providers. DR DNASU; 7581; -. DR Ensembl; ENST00000432900.7; ENSP00000402467.3; ENSG00000189180.16. [Q06730-2] DR Ensembl; ENST00000458705.6; ENSP00000387713.2; ENSG00000189180.16. [Q06730-1] DR Ensembl; ENST00000628825.2; ENSP00000485869.1; ENSG00000189180.16. [Q06730-3] DR GeneID; 7581; -. DR KEGG; hsa:7581; -. DR MANE-Select; ENST00000432900.7; ENSP00000402467.3; NM_006954.2; NP_008885.1. [Q06730-2] DR UCSC; uc001izg.4; human. [Q06730-1] DR AGR; HGNC:13096; -. DR CTD; 7581; -. DR GeneCards; ZNF33A; -. DR HGNC; HGNC:13096; ZNF33A. DR HPA; ENSG00000189180; Low tissue specificity. DR MIM; 194521; gene. DR neXtProt; NX_Q06730; -. DR OpenTargets; ENSG00000189180; -. DR PharmGKB; PA37671; -. DR VEuPathDB; HostDB:ENSG00000189180; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000162173; -. DR HOGENOM; CLU_002678_0_12_1; -. DR InParanoid; Q06730; -. DR OMA; CMNSHLI; -. DR OrthoDB; 9411774at2759; -. DR PhylomeDB; Q06730; -. DR TreeFam; TF337898; -. DR PathwayCommons; Q06730; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR Reactome; R-HSA-9843940; Regulation of endogenous retroelements by KRAB-ZFP proteins. DR SignaLink; Q06730; -. DR BioGRID-ORCS; 7581; 6 hits in 1167 CRISPR screens. DR ChiTaRS; ZNF33A; human. DR GeneWiki; ZNF33A; -. DR GenomeRNAi; 7581; -. DR Pharos; Q06730; Tbio. DR PRO; PR:Q06730; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q06730; protein. DR Bgee; ENSG00000189180; Expressed in cerebellar vermis and 194 other cell types or tissues. DR ExpressionAtlas; Q06730; baseline and differential. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR FunFam; 3.30.160.60:FF:000555; Zinc finger protein 1 homolog; 1. DR FunFam; 3.30.160.60:FF:000139; zinc finger protein 1 homolog; 1. DR FunFam; 3.30.160.60:FF:000782; Zinc finger protein 33A; 1. DR FunFam; 3.30.160.60:FF:001844; Zinc finger protein 33A; 1. DR FunFam; 3.30.160.60:FF:002343; Zinc finger protein 33A; 2. DR FunFam; 3.30.160.60:FF:000667; Zinc finger protein 33B; 1. DR FunFam; 3.30.160.60:FF:000699; Zinc finger protein 33B; 1. DR FunFam; 3.30.160.60:FF:001503; zinc finger protein 33B isoform X2; 1. DR FunFam; 3.30.160.60:FF:000016; zinc finger protein 37 homolog; 1. DR FunFam; 3.30.160.60:FF:000060; zinc finger protein 436; 1. DR FunFam; 3.30.160.60:FF:002254; Zinc finger protein 540; 2. DR FunFam; 3.30.160.60:FF:000149; Zinc finger protein 569; 1. DR FunFam; 3.30.160.60:FF:000069; Zinc finger protein 572; 2. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 16. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR050758; Znf_C2H2-type. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23234:SF8; C2H2-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR23234; ZNF44 PROTEIN; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 16. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 16. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 9. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 16. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Proteomics identification; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..810 FT /note="Zinc finger protein 33A" FT /id="PRO_0000047363" FT DOMAIN 12..83 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 328..350 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 356..378 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 384..406 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 412..434 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 440..462 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 468..490 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 496..518 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 524..546 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 552..574 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 580..602 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 608..630 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 636..658 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 664..686 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 692..714 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 720..742 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 748..770 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CROSSLNK 180 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:28112733" FT CROSSLNK 237 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 312 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 456 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 676 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 732 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..3 FT /note="MNK -> MANATRRGSG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055165" FT VAR_SEQ 83 FT /note="P -> PE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046420" FT VARIANT 549 FT /note="Q -> E (in dbSNP:rs2505232)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_052749" FT VARIANT 614 FT /note="G -> R (in dbSNP:rs12256916)" FT /id="VAR_052750" FT VARIANT 804 FT /note="D -> H (in dbSNP:rs10508862)" FT /id="VAR_052751" FT CONFLICT 129 FT /note="V -> A (in Ref. 3; BAG64490)" FT /evidence="ECO:0000305" FT CONFLICT 389 FT /note="C -> R (in Ref. 3; BAG64490)" FT /evidence="ECO:0000305" FT CONFLICT 721 FT /note="Q -> H (in Ref. 3; BAF85533)" FT /evidence="ECO:0000305" FT CONFLICT 745 FT /note="E -> K (in Ref. 3; BAF85533)" FT /evidence="ECO:0000305" FT CROSSLNK Q06730-2:72 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK Q06730-2:92 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" SQ SEQUENCE 810 AA; 94384 MW; 96AD969EF541B73E CRC64; MNKVEQKSQE SVSFKDVTVG FTQEEWQHLD PSQRALYRDV MLENYSNLVS VGYCVHKPEV IFRLQQGEEP WKQEEEFPSQ SFPVWTADHL KERSQENQSK HLWEVVFINN EMLTKEQGDV IGIPFNVDVS SFPSRKMFCQ CDSCGMSFNT VSELVISKIN YLGKKSDEFN ACGKLLLNIK HDETHTQEKN EVLKNRNTLS HHEETLQHEK IQTLEHNFEY SICQETLLEK AVFNTQKREN AEENNCDYNE FGRTLCDSSS LLFHQISPSR DNHYEFSDCE KFLCVKSTLS KPHGVSMKHY DCGESGNNFR RKLCLSHLQK GDKGEKHFEC NECGKAFWEK SHLTRHQRVH TGQKPFQCNE CEKAFWDKSN LTKHQRSHTG EKPFECNECG KAFSHKSALT LHQRTHTGEK PYQCNACGKT FCQKSDLTKH QRTHTGLKPY ECYECGKSFR VTSHLKVHQR THTGEKPFEC LECGKSFSEK SNLTQHQRIH IGDKSYECNA CGKTFYHKSL LTRHQIIHTG WKPYECYECG KTFCLKSDLT VHQRTHTGQK PFACPECGKF FSHKSTLSQH YRTHTGEKPY ECHECGKIFY NKSYLTKHNR THTGEKPYEC NECGKAFYQK SQLTQHQRIH IGEKPYKCNE CGKAFCHKSA LIVHQRTHTQ EKPYKCNECG KSFCVKSGLI FHERKHTGEK PYECNECGKF FRHKSSLTVH HRAHTGEKSC QCNECGKIFY RKSELAQHQR SHTGEKPYEC NTCRKTFSQK SNLIVHQRRH IGENLMNEMD IRNFQPQVSL HNASEYSHCG ESPDDILNVQ //