ZN281_MOUSE
ID ZN281_MOUSE Reviewed; 893 AA.
AC Q99LI5; Q3U063; Q4FK52;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein 281;
GN Name=Znf281; Synonyms=Zfp281;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
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 FUNCTION, AND DNA-BINDING.
RX PubMed=18757296; DOI=10.1634/stemcells.2008-0443;
RA Wang Z.X., Teh C.H., Chan C.M., Chu C., Rossbach M., Kunarso G.,
RA Allapitchay T.B., Wong K.Y., Stanton L.W.;
RT "The transcription factor Zfp281 controls embryonic stem cell pluripotency
RT by direct activation and repression of target genes.";
RL Stem Cells 26:2791-2799(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, AND INTERACTION WITH NANOG.
RX PubMed=21915945; DOI=10.1002/stem.736;
RA Fidalgo M., Shekar P.C., Ang Y.S., Fujiwara Y., Orkin S.H., Wang J.;
RT "Zfp281 functions as a transcriptional repressor for pluripotency of mouse
RT embryonic stem cells.";
RL Stem Cells 29:1705-1716(2011).
RN [8]
RP FUNCTION, INTERACTION WITH NANOG, AND INTERACTION WITH THE NURD COMPLEX.
RX PubMed=22988117; DOI=10.1073/pnas.1208533109;
RA Fidalgo M., Faiola F., Pereira C.F., Ding J., Saunders A., Gingold J.,
RA Schaniel C., Lemischka I.R., Silva J.C., Wang J.;
RT "Zfp281 mediates Nanog autorepression through recruitment of the NuRD
RT complex and inhibits somatic cell reprogramming.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16202-16207(2012).
CC -!- FUNCTION: Transcription repressor that plays a role in regulation of
CC embryonic stem cells (ESCs) differentiation. Required for ESCs
CC differentiation and acts by mediating autorepression of NANOG in ESCs:
CC binds to the NANOG promoter and promotes association of NANOG protein
CC to its own promoter and recruits the NuRD complex, which deacetylates
CC histones. Not required for establishement and maintenance of ESCs.
CC Represses the transcription of a number of genes including GAST, ODC1
CC and VIM. Binds to the G-rich box in the enhancer region of these genes.
CC {ECO:0000269|PubMed:18757296, ECO:0000269|PubMed:21915945,
CC ECO:0000269|PubMed:22988117}.
CC -!- SUBUNIT: Interacts with NANOG. Associates with the NuRD complex.
CC {ECO:0000269|PubMed:21915945, ECO:0000269|PubMed:22988117}.
CC -!- INTERACTION:
CC Q99LI5; Q80Z64: Nanog; NbExp=5; IntAct=EBI-2312719, EBI-2312517;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Embryos die between embryonic day 7.5 (E7.5) and
CC E8.5, due to dysregulation of pluripotency and lineage specific markers
CC in embryonic stem cells (ESCs). Embryos show abnormal embryonic body
CC differentiation. {ECO:0000269|PubMed:21915945}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK142218; BAE24981.1; -; mRNA.
DR EMBL; AK157189; BAE33992.1; -; mRNA.
DR EMBL; CT010200; CAJ18408.1; -; mRNA.
DR EMBL; AC126606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003243; AAH03243.1; -; mRNA.
DR EMBL; BC062153; AAH62153.1; -; mRNA.
DR CCDS; CCDS15327.1; -.
DR RefSeq; NP_001153723.1; NM_001160251.1.
DR RefSeq; NP_808311.1; NM_177643.4.
DR AlphaFoldDB; Q99LI5; -.
DR SMR; Q99LI5; -.
DR BioGRID; 230516; 40.
DR DIP; DIP-29927N; -.
DR IntAct; Q99LI5; 3.
DR MINT; Q99LI5; -.
DR STRING; 10090.ENSMUSP00000107677; -.
DR iPTMnet; Q99LI5; -.
DR PhosphoSitePlus; Q99LI5; -.
DR EPD; Q99LI5; -.
DR jPOST; Q99LI5; -.
DR MaxQB; Q99LI5; -.
DR PaxDb; Q99LI5; -.
DR PeptideAtlas; Q99LI5; -.
DR PRIDE; Q99LI5; -.
DR ProteomicsDB; 275071; -.
DR Antibodypedia; 20632; 205 antibodies from 32 providers.
DR DNASU; 226442; -.
DR Ensembl; ENSMUST00000047734; ENSMUSP00000039003; ENSMUSG00000041483.
DR Ensembl; ENSMUST00000112046; ENSMUSP00000107677; ENSMUSG00000041483.
DR GeneID; 226442; -.
DR KEGG; mmu:226442; -.
DR UCSC; uc007cuw.2; mouse.
DR CTD; 226442; -.
DR MGI; MGI:3029290; Zfp281.
DR VEuPathDB; HostDB:ENSMUSG00000041483; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161586; -.
DR HOGENOM; CLU_017625_0_0_1; -.
DR InParanoid; Q99LI5; -.
DR OMA; NNMGNLA; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q99LI5; -.
DR TreeFam; TF331779; -.
DR BioGRID-ORCS; 226442; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp281; mouse.
DR PRO; PR:Q99LI5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99LI5; protein.
DR Bgee; ENSMUSG00000041483; Expressed in 1st arch mandibular component and 263 other tissues.
DR Genevisible; Q99LI5; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:UniProtKB.
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:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Differentiation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..893
FT /note="Zinc finger protein 281"
FT /id="PRO_0000420492"
FT ZN_FING 258..280
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..308
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT MOD_RES 886
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 614
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 619
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 658
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 667
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 784
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 789
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 793
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CROSSLNK 838
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2X9"
FT CONFLICT 194
FT /note="V -> A (in Ref. 1; BAE33992)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="G -> S (in Ref. 1; BAE33992)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="Y -> C (in Ref. 2; CAJ18408)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> S (in Ref. 1; BAE33992)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="T -> S (in Ref. 2; CAJ18408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 96685 MW; 7F4EBA44C2CC2AF2 CRC64;
MKIGSGFLSG GGGPSSSGGS GSGGSSGSAS GGSGGGRRAE MEPTFPQSMV MFNHRLPPVT
SFTRPAGTAA PPPQCVLSSS TSAAPAAEPP PPPAPDMTFK KEPAASAAAF PSQRTSWGFL
QSLVSIKQEK PADPEEQPSH HHHHHHHYGG LFAGAEERSP GLGGGEGGSH GVIQDLSLLH
QHAQQQPAQH HRDVLLSSGS RTDEHGNQEP KQDANVKKAK RPKPESQGIK AKRKPSASSK
PLVGEGEGAV LSPSQKPHIC DHCSAAFRSS YHLRRHVLIH TGERPFQCSQ CSMGFIQKYL
LQRHEKIHSR EKPFGCDQCS MKFIQKYHME RHKRTHSGEK PYKCDTCQQY FSRTDRLLKH
RRTCGEAIAK GAASAEPGSS NHNSMGNLAV LSQGNTSSSR RKSKSKSIAI ENKEHKTGKT
NESQMSNNIN MQSYSVEMPT VSTSGSIIGT GIDELQKRVP KLIFKKGSRK NADKSYLNFV
SPLPDVVGQK SLSGKPGGSL GIVSNNSVET ISLLQSTSGK QGPISSNYDD AMQFSKKRRY
LPTASSNSAF SINVGHMVSQ QSVIQSAGVS VLDNEAPLSL IDSSALNAEI KSCHDKSGIP
DEVLQSILDQ YSGKSETQKE DPFNLTEPRV DLHTSGEHSE LVQEENLSPG TQTPSNDKTS
MLQEYSKYLQ QAFEKSTNAG FTLGHGFQFV SLSSPLHNHT LFPEKQIYTT SPLECGFGQS
VTSVLPSSLP KPPFGMLFGS QPGLYLSALD ATHQQLTPSQ ELDDLIDSQK NLETSSAFQS
SSQKLTSQKE QQKNLESSTS FQIPSQELAS QIDPQKDIEP RTTYQIENFA QAFGSQFKSG
SRVPMTFITN SNGEVDHRVR TSVSDFSGYT NMMSDVSEPC STRVKTPTSQ SYR
