TIF1B_RAT
ID TIF1B_RAT Reviewed; 835 AA.
AC O08629; B2RYN5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Transcription intermediary factor 1-beta {ECO:0000305};
DE Short=TIF1-beta;
DE AltName: Full=E3 SUMO-protein ligase TRIM28;
DE EC=2.3.2.27;
DE AltName: Full=KRAB-associated protein 1;
DE AltName: Full=Nuclear corepressor KAP-1;
DE AltName: Full=RING-type E3 ubiquitin transferase TIF1-beta {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 28;
GN Name=Trim28 {ECO:0000312|RGD:620289}; Synonyms=Kap1, Tif1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-281.
RA Emison E.S., Lewis B.C., Shim H., Li Q., Dang C.V., Lee L.A.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH ZNF382.
RX PubMed=11154279; DOI=10.1128/mcb.21.3.928-939.2001;
RA Gebelein B., Urrutia R.;
RT "Sequence-specific transcriptional repression by KS1, a multiple-zinc-
RT finger-Kruppel-associated box protein.";
RL Mol. Cell. Biol. 21:928-939(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-474; SER-502;
RP SER-684; SER-753 AND SER-758, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Nuclear corepressor for KRAB domain-containing zinc finger
CC proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a
CC subunit of the nucleosome remodeling and deacetylation (NuRD) complex,
CC and SETDB1 (which specifically methylates histone H3 at 'Lys-9'
CC (H3K9me)) to the promoter regions of KRAB target genes. Enhances
CC transcriptional repression by coordinating the increase in H3K9me, the
CC decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and
CC H3K14ac, respectively) and the disposition of HP1 proteins to silence
CC gene expression. Recruitment of SETDB1 induces heterochromatinization.
CC May play a role as a coactivator for CEBPB and NR3C1 in the
CC transcriptional activation of ORM1. Also a corepressor for ERBB4.
CC Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and
CC inhibiting E2F1 acetylation. May serve as a partial backup to prevent
CC E2F1-mediated apoptosis in the absence of RB1. Important regulator of
CC CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via
CC its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby
CC inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading
CC to its proteosomal degradation; the function is enhanced by MAGEC2 and
CC MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear
CC localization of KOX1, ZNF268 and ZNF300 transcription factors. In
CC association with isoform 2 of ZFP90, is required for the
CC transcriptional repressor activity of FOXP3 and the suppressive
CC function of regulatory T-cells (Treg). Probably forms a corepressor
CC complex required for activated KRAS-mediated promoter hypermethylation
CC and transcriptional silencing of tumor suppressor genes (TSGs) or other
CC tumor-related genes in colorectal cancer (CRC) cells. Required to
CC maintain a transcriptionally repressive state of genes in
CC undifferentiated embryonic stem cells (ESCs). In ESCs, in collaboration
CC with SETDB1, is also required for H3K9me3 and silencing of endogenous
CC and introduced retroviruses in a DNA-methylation independent-pathway.
CC Associates at promoter regions of tumor suppressor genes (TSGs) leading
CC to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a
CC role in recruiting ATRX to the 3'-exons of zinc finger genes with
CC atypical chromatin signatures to establish or maintain/protect H3K9me3
CC at these transcriptionally active regions.
CC {ECO:0000250|UniProtKB:Q13263, ECO:0000250|UniProtKB:Q62318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with ZNF382 (PubMed:11154279). Interacts with SETX.
CC Oligomer; the RBCC domain homotrimerizes and interacts with one
CC molecule of KRAB to form the KRAB-KAP1 corepressor complex. Binding to
CC a KRAB domain is an absolute requirement for silencing gene expression.
CC Interacts with CEBPB and NR3C1. Interacts with a number of KRAB-ZFP
CC proteins including ZNF10, ZFP53, ZFP68 and ZNF256. Interacts with
CC NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via the RING-type and PHD-
CC type zinc fingers). Component of a ternary complex that includes
CC TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5), a KRAB domain-containing
CC protein, and DNA. Interacts with CBX5 (via the PxVxL motif); the
CC interaction occurs in interphase nuclei and competes for binding POGZ.
CC Interacts with POGZ; the interaction competes for interaction with
CC CBX5. Interacts with SETDB1; the interaction is enhanced by KAP1
CC sumoylation, stimulates SETDB1 histone methyltransferase activity and
CC gene silencing. Interacts (via the PHD-type zinc finger) with UBE2I;
CC the interaction is required for sumoylation and repressor activity.
CC Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting
CC growth factor and DNA damage responses. Interacts directly with ERBB4;
CC the interaction represses ERBB4-mediated transcription activity.
CC Interacts with MDM2; the interaction contributes to p53/TP53
CC inactivation. Component of the TRIM28/KAP1-MDM2-p53/TP53; involved in
CC regulating p53/TP53 stabilization and activity. Interacts (via the
CC leucine zipper alpha helical coiled-coil) with E2F1 (central region);
CC the interaction inhibits E2F1 acetylation and transcriptional activity.
CC Interacts with PPP1CA; the interaction dephosphorylates TRIM28 at Ser-
CC 824 and forms a complex at the p21 promoter site. Interacts with
CC PPP1CB; the interaction is weak but is increased on dephosphorylation
CC at Ser-824. Interacts with SMARCAD1. Interacts with, and sumoylates
CC IRF7. Interacts with MAGEC2. Part of a complex composed of TRIM28,
CC HDAC1, HDAC2 and EHMT2. Interacts with AICDA. The large PER complex
CC involved in the histone methylation is composed of at least PER2, CBX3,
CC TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the
CC complex (By similarity). Interacts with NR4A3; the interactions
CC potentiates NR4A3 activity on NurRE promoter (By similarity). Interacts
CC (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain)
CC (By similarity). Probably part of a corepressor complex containing
CC ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with ATRX. Forms a complex
CC with ATRX, SETDB1 and ZNF274 (By similarity). Interacts with ZFP568;
CC the interaction mediates ZFP568 transcriptional repression activity (By
CC similarity). Interacts with RRP1B (By similarity). Interacts with CRY1
CC (By similarity). Interacts with ZNF263; recruited to the SIX3 promoter
CC along with other proteins involved in chromatin modification and
CC transcriptional corepression where it contributes to transcriptional
CC repression (By similarity). Interacts with CYREN (via XLF motif) (By
CC similarity). Interacts with TRIM17; this interaction prevents TRIM28
CC activity (By similarity). Interacts with ZNF746 (By similarity).
CC {ECO:0000250|UniProtKB:Q13263, ECO:0000250|UniProtKB:Q62318,
CC ECO:0000269|PubMed:11154279}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62318}.
CC Note=Associated with centromeric heterochromatin during cell
CC differentiation through CBX1. {ECO:0000250|UniProtKB:Q62318}.
CC -!- DOMAIN: The HP1 box is both necessary and sufficient for HP1 binding.
CC {ECO:0000250|UniProtKB:Q13263}.
CC -!- DOMAIN: The PHD-type zinc finger enhances CEBPB transcriptional
CC activity. The PHD-type zinc finger, the HP1 box and the bromo domain,
CC function together to assemble the machinery required for repression of
CC KRAB domain-containing proteins. Acts as an intramolecular SUMO E3
CC ligase for autosumoylation of bromodomain.
CC {ECO:0000250|UniProtKB:Q13263}.
CC -!- DOMAIN: The RING-finger-B Box-coiled-coil/tripartite motif (RBCC/TRIM
CC motif) is required for interaction with the KRAB domain of KRAB-zinc
CC finger proteins. Binds four zinc ions per molecule. The RING finger and
CC the N-terminal of the leucine zipper alpha helical coiled-coil region
CC of RBCC are required for oligomerization.
CC {ECO:0000250|UniProtKB:Q13263}.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain. {ECO:0000250|UniProtKB:Q13263}.
CC -!- PTM: ATM-induced phosphorylation on Ser-825 represses sumoylation
CC leading to the de-repression of expression of a subset of genes
CC involved in cell cycle control and apoptosis in response to genotoxic
CC stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms,
CC allows sumoylation and expression of TRIM28 target genes.
CC {ECO:0000250|UniProtKB:Q13263}.
CC -!- PTM: Sumoylation/desumoylation events regulate TRIM28-mediated
CC transcriptional repression. Sumoylation is required for interaction
CC with CHD3 and SETDB1 and the corepressor activity. Represses and is
CC repressed by Ser-824 phosphorylation. Enhances the TRIM28 corepressor
CC activity, inhibiting transcriptional activity of a number of genes
CC including GADD45A and CDKN1A/p21. Lys-555, Lys-780 and Lys-805 are the
CC major sites of sumoylation. In response to Dox-induced DNA damage,
CC enhanced phosphorylation on Ser-825 prevents sumoylation and allows de-
CC repression of CDKN1A/p21. {ECO:0000250|UniProtKB:Q13263}.
CC -!- PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
CC {ECO:0000250|UniProtKB:Q13263}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q62318}.
CC -!- PTM: ADP-ribosylated by SIRT6, promoting TRIM28/KAP1 interaction with
CC CBX5, thereby contributing to the packaging of LINE-1 retrotransposon
CC elements into transcriptionally repressive heterochromatin.
CC {ECO:0000250|UniProtKB:Q62318}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC166843; AAI66843.1; -; mRNA.
DR EMBL; U95041; AAB51518.1; -; mRNA.
DR RefSeq; NP_446368.1; NM_053916.1.
DR AlphaFoldDB; O08629; -.
DR BMRB; O08629; -.
DR SMR; O08629; -.
DR BioGRID; 250580; 5.
DR IntAct; O08629; 4.
DR STRING; 10116.ENSRNOP00000031061; -.
DR iPTMnet; O08629; -.
DR PhosphoSitePlus; O08629; -.
DR jPOST; O08629; -.
DR PaxDb; O08629; -.
DR PRIDE; O08629; -.
DR Ensembl; ENSRNOT00000029996; ENSRNOP00000031061; ENSRNOG00000027487.
DR GeneID; 116698; -.
DR KEGG; rno:116698; -.
DR UCSC; RGD:620289; rat.
DR CTD; 10155; -.
DR RGD; 620289; Trim28.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160527; -.
DR HOGENOM; CLU_005817_2_0_1; -.
DR InParanoid; O08629; -.
DR OMA; DCKDEVP; -.
DR OrthoDB; 756911at2759; -.
DR PhylomeDB; O08629; -.
DR TreeFam; TF106455; -.
DR Reactome; R-RNO-212436; Generic Transcription Pathway.
DR UniPathway; UPA00886; -.
DR PRO; PR:O08629; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000027487; Expressed in testis and 20 other tissues.
DR Genevisible; O08629; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019789; F:SUMO transferase activity; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; ISO:RGD.
DR GO; GO:0043045; P:DNA methylation involved in embryo development; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC-UCL.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:1901536; P:negative regulation of DNA demethylation; ISO:RGD.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0016925; P:protein sumoylation; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:2000653; P:regulation of genetic imprinting; ISO:RGD.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:RGD.
DR CDD; cd16765; RING-HC_TIF1beta; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037373; KAP1.
DR InterPro; IPR042713; TIF1beta_RING-HC.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR25462:SF274; PTHR25462:SF274; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 2.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Bromodomain; Chromatin regulator;
KW Citrullination; Coiled coil; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..835
FT /note="Transcription intermediary factor 1-beta"
FT /id="PRO_0000056394"
FT DOMAIN 698..802
FT /note="Bromo"
FT ZN_FING 67..123
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 150..197
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 206..247
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 626..673
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 14..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..378
FT /note="Leucine zipper alpha helical coiled-coil region"
FT /evidence="ECO:0000250"
FT REGION 249..378
FT /note="Interaction with MAGEC2"
FT /evidence="ECO:0000250"
FT REGION 368..372
FT /note="Involved in binding PPP1CA"
FT /evidence="ECO:0000250"
FT REGION 413..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..514
FT /note="HP1 box"
FT MOTIF 482..495
FT /note="PxVxL motif"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 268
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 306
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 342
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 379
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 471
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 473
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 756
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 771
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 775
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 780
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q62318"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT MOD_RES 825
FT /note="Phosphoserine; by ATM and ATR and dsDNA kinase"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 576
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 677
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 751
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 751
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 751
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 771
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 775
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 780
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 780
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CROSSLNK 805
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13263"
FT CONFLICT 220
FT /note="V -> A (in Ref. 2; AAB51518)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="K -> R (in Ref. 2; AAB51518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 88956 MW; 0E4245EA6CA45CA0 CRC64;
MAASAAAATA AASAATAASA ASGSPGSGEG SAGGEKRPAA SSAAAASASA SSPAGGGGEA
QELLEHCGVC RERLRPERDP RLLPCLHSAC SACLGPATPA AANNSGDGGS AGDGAMVDCP
VCKQQCYSKD IVENYFMRDS GSKASSDSQD ANQCCTSCED NAPATSYCVE CSEPLCETCV
EAHQRVKYTK DHTVRSTGPA KTRDGERTVY CNVHKHEPLV LFCESCDTLT CRDCQLNAHK
DHQYQFLEDA VRNQRKLLAS LVKRLGDKHA TLQKNTKEVR SSIRQVSDVQ KRVQVDVKMA
ILQIMKELNK RGRVLVNDAQ KVTEGQQERL ERQHWTMTKI QKHQEHILRF ASWALESDNN
TALLLSKKLI YFQLHRALKM IVDPVEPHGE MKFQWDLNAW TKSAEAFGKI VAERPGTNST
GPGPMAPPRA PGPLSKQGSG SSQPMEVQEG YGFGTDDPYS SAEPHVSGMK RSRSGEGEVS
GLMRKVPRVS LERLDLDLTS DSQPPVFKVF PGSTTEDYNL IVIERGAAAA AAGQAGTVPP
GAPGAPPLPG MAIVKEEETE AAIGAPPAAP EGPETKPVLM ALTEGPGAEG PRLASPSGST
SSGLEVVAPE VTSAPVSGPG ILDDSATICR VCQKPGDLVM CNQCEFCFHL DCHLPSLQDV
PGEEWSCSLC HVLPDLKEED GSLSLDGADS TGVVAKLSPA NQRKCERVLL ALFCHEPCRP
LHQLATDSTF SMEQPGGTLD LTLIRARLQE KLSPPYSSPQ EFAQDVGRMF KQFNKLTEDK
ADVQSIIGLQ RFFETRMNDA FGDTKFSAVL VEPPPLNLPS AGLSSQELSG PGDGP
