CTCF_MOUSE
ID CTCF_MOUSE Reviewed; 736 AA.
AC Q61164;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcriptional repressor CTCF;
DE AltName: Full=11-zinc finger protein;
DE AltName: Full=CCCTC-binding factor;
DE AltName: Full=CTCFL paralog;
GN Name=Ctcf;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=BDF1;
RX PubMed=8649389; DOI=10.1128/mcb.16.6.2802;
RA Filippova G.N., Fagerlie S., Klenova E.M., Myers C., Dehner Y., Goodwin G.,
RA Neiman P.E., Collins S.J., Lobanenkov V.V.;
RT "An exceptionally conserved transcriptional repressor, CTCF, employs
RT different combinations of zinc fingers to bind diverged promoter sequences
RT of avian and mammalian c-myc oncogenes.";
RL Mol. Cell. Biol. 16:2802-2813(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Mammary gland, and Olfactory epithelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-201.
RC STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, and Placenta;
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 [4]
RP FUNCTION.
RX PubMed=11743158; DOI=10.1126/science.1065982;
RA Chao W., Huynh K.D., Spencer R.J., Davidow L.S., Lee J.T.;
RT "CTCF, a candidate trans-acting factor for X-inactivation choice.";
RL Science 295:345-347(2002).
RN [5]
RP FUNCTION.
RX PubMed=15669143; DOI=10.1016/j.devcel.2004.10.018;
RA Filippova G.N., Cheng M.K., Moore J.M., Truong J.-P., Hu Y.J., Nguyen D.K.,
RA Tsuchiya K.D., Disteche C.M.;
RT "Boundaries between chromosomal domains of X inactivation and escape bind
RT CTCF and lack CpG methylation during early development.";
RL Dev. Cell 8:31-42(2005).
RN [6]
RP FUNCTION.
RX PubMed=16951251; DOI=10.1101/gad.399506;
RA Splinter E., Heath H., Kooren J., Palstra R.-J., Klous P., Grosveld F.,
RA Galjart N., de Laat W.;
RT "CTCF mediates long-range chromatin looping and local histone modification
RT in the beta-globin locus.";
RL Genes Dev. 20:2349-2354(2006).
RN [7]
RP INTERACTION WITH CHD8.
RX PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
RA Ishihara K., Oshimura M., Nakao M.;
RT "CTCF-dependent chromatin insulator is linked to epigenetic remodeling.";
RL Mol. Cell 23:733-742(2006).
RN [8]
RP FUNCTION.
RX PubMed=16614224; DOI=10.1126/science.1123191;
RA Ling J.Q., Li T., Hu J.F., Vu T.H., Chen H.L., Qiu X.W., Cherry A.M.,
RA Hoffman A.R.;
RT "CTCF mediates interchromosomal colocalization between Igf2/H19 and
RT Wsb1/Nf1.";
RL Science 312:269-272(2006).
RN [9]
RP FUNCTION.
RX PubMed=17329968; DOI=10.4161/cc.6.4.3854;
RA Bergstroem R., Whitehead J., Kurukuti S., Ohlsson R.;
RT "CTCF regulates asynchronous replication of the imprinted H19/Igf2
RT domain.";
RL Cell Cycle 6:450-454(2007).
RN [10]
RP FUNCTION.
RX PubMed=17952071; DOI=10.1038/ng.2007.5;
RA Xu N., Donohoe M.E., Silva S.S., Lee J.T.;
RT "Evidence that homologous X-chromosome pairing requires transcription and
RT Ctcf protein.";
RL Nat. Genet. 39:1390-1396(2007).
RN [11]
RP FUNCTION.
RX PubMed=18614575; DOI=10.1242/dev.024539;
RA Wan L.-B., Pan H., Hannenhalli S., Cheng Y., Ma J., Fedoriw A.,
RA Lobanenkov V., Latham K.E., Schultz R.M., Bartolomei M.S.;
RT "Maternal depletion of CTCF reveals multiple functions during oocyte and
RT preimplantation embryo development.";
RL Development 135:2729-2738(2008).
RN [12]
RP SUMOYLATION AT LYS-74 AND LYS-698, AND MUTAGENESIS OF LYS-74 AND LYS-698.
RX PubMed=19029252; DOI=10.1128/mcb.00825-08;
RA MacPherson M.J., Beatty L.G., Zhou W., Du M., Sadowski P.D.;
RT "The CTCF insulator protein is posttranslationally modified by SUMO.";
RL Mol. Cell. Biol. 29:714-725(2009).
RN [13]
RP INTERACTION WITH LLPH.
RX PubMed=26961175; DOI=10.1038/srep22892;
RA Yu N.K., Kim H.F., Shim J., Kim S., Kim D.W., Kwak C., Sim S.E., Choi J.H.,
RA Ahn S., Yoo J., Choi S.L., Jang D.J., Lim C.S., Lee Y.S., Kang C.,
RA Choi S.Y., Kaang B.K.;
RT "A transducible nuclear/nucleolar protein, mLLP, regulates neuronal
RT morphogenesis and synaptic transmission.";
RL Sci. Rep. 6:22892-22892(2016).
CC -!- FUNCTION: Chromatin binding factor that binds to DNA sequence specific
CC sites. Involved in transcriptional regulation by binding to chromatin
CC insulators and preventing interaction between promoter and nearby
CC enhancers and silencers. Acts as transcriptional repressor binding to
CC promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK
CC and PIM1 promoters. Acts as a transcriptional activator of APP.
CC Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene
CC expression. Plays an essential role in oocyte and preimplantation
CC embryo development by activating or repressing transcription. Seems to
CC act as tumor suppressor. Plays a critical role in the epigenetic
CC regulation. Participates in the allele-specific gene expression at the
CC imprinted IGF2/H19 gene locus. On the maternal allele, binding within
CC the H19 imprinting control region (ICR) mediates maternally inherited
CC higher-order chromatin conformation to restrict enhancer access to
CC IGF2. Plays a critical role in gene silencing over considerable
CC distances in the genome. Preferentially interacts with unmethylated
CC DNA, preventing spreading of CpG methylation and maintaining
CC methylation-free zones. Inversely, binding to target sites is prevented
CC by CpG methylation. Plays an important role in chromatin remodeling.
CC Can dimerize when it is bound to different DNA sequences, mediating
CC long-range chromatin looping (By similarity). Mediates interchromosomal
CC association between IGF2/H19 and WSB1/NF1 and may direct distant DNA
CC segments to a common transcription factory. Causes local loss of
CC histone acetylation and gain of histone methylation in the beta-globin
CC locus, without affecting transcription. When bound to chromatin, it
CC provides an anchor point for nucleosomes positioning. Seems to be
CC essential for homologous X-chromosome pairing. May participate with
CC Tsix in establishing a regulatable epigenetic switch for X chromosome
CC inactivation. May play a role in preventing the propagation of stable
CC methylation at the escape genes from X-inactivation. Involved in sister
CC chromatid cohesion. Associates with both centromeres and chromosomal
CC arms during metaphase and required for cohesin localization to CTCF
CC sites. Regulates asynchronous replication of IGF2/H19. Plays a role in
CC the recruitment of CENPE to the pericentromeric/centromeric regions of
CC the chromosome during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:P49711, ECO:0000269|PubMed:11743158,
CC ECO:0000269|PubMed:15669143, ECO:0000269|PubMed:16614224,
CC ECO:0000269|PubMed:16951251, ECO:0000269|PubMed:17329968,
CC ECO:0000269|PubMed:17952071, ECO:0000269|PubMed:18614575}.
CC -!- SUBUNIT: Interacts with CHD8 (PubMed:16949368). Interacts with LLPH
CC (PubMed:26961175). Interacts with CENPE (By similarity).
CC {ECO:0000250|UniProtKB:P49711, ECO:0000269|PubMed:16949368,
CC ECO:0000269|PubMed:26961175}.
CC -!- INTERACTION:
CC Q61164; Q09XV5: Chd8; NbExp=3; IntAct=EBI-932785, EBI-1169080;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000305|PubMed:8649389}. Chromosome
CC {ECO:0000250|UniProtKB:P49711}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P49711}. Note=May translocate to the nucleolus
CC upon cell differentiation. Associates with both centromeres and
CC chromosomal arms during metaphase. Associates with the H19 ICR in
CC mitotic chromosomes. May be preferentially excluded from
CC heterochromatin during interphase. {ECO:0000250|UniProtKB:P49711}.
CC -!- PTM: Sumoylated on Lys-74 and Lys-698; sumoylation of CTCF contributes
CC to the repressive function of CTCF on the MYC P2 promoter.
CC {ECO:0000269|PubMed:19029252}.
CC -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U51037; AAC52928.1; -; mRNA.
DR EMBL; BC037456; AAH37456.1; -; mRNA.
DR EMBL; BC046398; AAH46398.1; -; mRNA.
DR EMBL; BC049131; AAH49131.1; -; mRNA.
DR EMBL; BC058240; AAH58240.1; -; mRNA.
DR EMBL; AK076192; BAC36245.1; -; mRNA.
DR CCDS; CCDS22606.1; -.
DR RefSeq; NP_851839.1; NM_181322.3.
DR RefSeq; XP_006530711.1; XM_006530648.2.
DR AlphaFoldDB; Q61164; -.
DR SMR; Q61164; -.
DR BioGRID; 198963; 47.
DR DIP; DIP-38020N; -.
DR IntAct; Q61164; 18.
DR MINT; Q61164; -.
DR STRING; 10090.ENSMUSP00000005841; -.
DR iPTMnet; Q61164; -.
DR PhosphoSitePlus; Q61164; -.
DR SwissPalm; Q61164; -.
DR EPD; Q61164; -.
DR jPOST; Q61164; -.
DR MaxQB; Q61164; -.
DR PaxDb; Q61164; -.
DR PeptideAtlas; Q61164; -.
DR PRIDE; Q61164; -.
DR ProteomicsDB; 277916; -.
DR Antibodypedia; 15816; 449 antibodies from 41 providers.
DR DNASU; 13018; -.
DR Ensembl; ENSMUST00000005841; ENSMUSP00000005841; ENSMUSG00000005698.
DR GeneID; 13018; -.
DR KEGG; mmu:13018; -.
DR UCSC; uc009ndm.2; mouse.
DR CTD; 10664; -.
DR MGI; MGI:109447; Ctcf.
DR VEuPathDB; HostDB:ENSMUSG00000005698; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156672; -.
DR HOGENOM; CLU_002678_77_1_1; -.
DR InParanoid; Q61164; -.
DR OMA; FLPSMDG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q61164; -.
DR TreeFam; TF106430; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 13018; 29 hits in 80 CRISPR screens.
DR ChiTaRS; Ctcf; mouse.
DR PRO; PR:Q61164; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61164; protein.
DR Bgee; ENSMUSG00000005698; Expressed in rostral migratory stream and 266 other tissues.
DR Genevisible; Q61164; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; ISO:MGI.
DR GO; GO:0001651; C:dense fibrillar component; ISO:MGI.
DR GO; GO:0001652; C:granular component; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0043035; F:chromatin insulator sequence binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0140588; P:chromatin looping; ISO:MGI.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; IDA:MGI.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; TAS:MGI.
DR GO; GO:0071514; P:genomic imprinting; ISO:MGI.
DR GO; GO:0010216; P:maintenance of DNA methylation; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IDA:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0035065; P:regulation of histone acetylation; IMP:UniProtKB.
DR GO; GO:0031060; P:regulation of histone methylation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Centromere; Chromatin regulator; Chromosome;
KW Chromosome partition; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..736
FT /note="Transcriptional repressor CTCF"
FT /id="PRO_0000047229"
FT ZN_FING 266..288
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..345
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..430
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..460
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..546
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 555..577
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 180..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..634
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49711"
FT MUTAGEN 74
FT /note="K->R: No sumoylation."
FT /evidence="ECO:0000269|PubMed:19029252"
FT MUTAGEN 698
FT /note="K->R: No sumoylation."
FT /evidence="ECO:0000269|PubMed:19029252"
FT CONFLICT 38
FT /note="C -> S (in Ref. 1; AAC52928)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="I -> K (in Ref. 2; AAH37456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 83745 MW; 7C49D4A7BDCFEFA1 CRC64;
MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM
VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV
PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
GELPPQEDSS WQKDPDYQPP AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV
NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG
RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS
VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG
TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY
ALIQHQKSHK NEKRFKCDQC DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR
KMRSKKEDSS DSEENAEPDL DDNEEEEEPA VEIEPEPEPQ PQPPPPPQPV APAPPPAKKR
RGRPPGRTNQ PKQNQPTAII QVEDQNTGAI ENIIVEVKKE PDAEPAEGEE EEAQAATTDA
PNGDLTPEMI LSMMDR
