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Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-associated protein 1) (Nuclear corepressor KAP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)

 TIF1B_RAT               Reviewed;         835 AA.
O08629; B2RYN5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
20-JAN-2009, sequence version 2.
28-MAR-2018, entry version 148.
RecName: Full=Transcription intermediary factor 1-beta;
Short=TIF1-beta;
AltName: Full=E3 SUMO-protein ligase TRIM28;
EC=2.3.2.27;
AltName: Full=KRAB-associated protein 1;
AltName: Full=Nuclear corepressor KAP-1;
AltName: Full=RING-type E3 ubiquitin transferase TIF1-beta {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 28;
Name=Trim28; Synonyms=Kap1, Tif1b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 197-281.
Emison E.S., Lewis B.C., Shim H., Li Q., Dang C.V., Lee L.A.;
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH ZNF382.
PubMed=11154279; DOI=10.1128/MCB.21.3.928-939.2001;
Gebelein B., Urrutia R.;
"Sequence-specific transcriptional repression by KS1, a multiple-zinc-
finger-Kruppel-associated box protein.";
Mol. Cell. Biol. 21:928-939(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-474;
SER-502; SER-684; SER-753 AND SER-758, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Nuclear corepressor for KRAB domain-containing zinc
finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting
CHD3, a subunit of the nucleosome remodeling and deacetylation
(NuRD) complex, and SETDB1 (which specifically methylates histone
H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target
genes. Enhances transcriptional repression by coordinating the
increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14'
acetylation (H3K9ac and H3K14ac, respectively) and the disposition
of HP1 proteins to silence gene expression. Recruitment of SETDB1
induces heterochromatinization. May play a role as a coactivator
for CEBPB and NR3C1 in the transcriptional activation of ORM1.
Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating
E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May
serve as a partial backup to prevent E2F1-mediated apoptosis in
the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has
E3 SUMO-protein ligase activity toward itself via its PHD-type
zinc finger. Also specifically sumoylates IRF7, thereby inhibiting
its transactivation activity. Ubiquitinates p53/TP53 leading to
its proteosomal degradation; the function is enhanced by MAGEC2
and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear
localization of KOX1, ZNF268 and ZNF300 transcription factors. In
association with isoform 2 of ZFP90, is required for the
transcriptional repressor activity of FOXP3 and the suppressive
function of regulatory T-cells (Treg). Probably forms a
corepressor complex required for activated KRAS-mediated promoter
hypermethylation and transcriptional silencing of tumor suppressor
genes (TSGs) or other tumor-related genes in colorectal cancer
(CRC) cells. Also required to maintain a transcriptionally
repressive state of genes in undifferentiated embryonic stem cells
(ESCs). Associates at promoter regions of tumor suppressor genes
(TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274
complex may play a role in recruiting ATRX to the 3'-exons of zinc
finger genes with atypical chromatin signatures to establish or
maintain/protect H3K9me3 at these transcriptionally active
regions. Acts as a corepressor for ZFP568.
{ECO:0000250|UniProtKB:Q13263, ECO:0000250|UniProtKB:Q62318}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with ZNF382 (PubMed:11154279). Interacts with
SETX. Oligomer; the RBCC domain homotrimerizes and interacts with
one molecule of KRAB to form the KRAB-KAP1 corepressor complex.
Binding to a KRAB domain is an absolute requirement for silencing
gene expression. Interacts with CEBPB and NR3C1. Interacts with a
number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68 and
ZNF256. Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB
(via the RING-type and PHD-type zinc fingers). Component of a
ternary complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR
CBX5), a KRAB domain-containing protein, and DNA. Interacts with
CBX5 (via the PxVxL motif); the interaction occurs in interphase
nuclei and competes for binding POGZ. Interacts with POGZ; the
interaction competes for interaction with CBX5. Interacts with
SETDB1; the interaction is enhanced by KAP1 sumoylation,
stimulates SETB1 histone methyltransferase activity and gene
silencing. Interacts (via the PHD-type zinc finger) with UBE2I;
the interaction is required for sumoylation and repressor
activity. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved
in connecting growth factor and DNA damage responses. Interacts
directly with ERBB4; the interaction represses ERBB4-mediated
transcription activity. Interacts with MDM2; the interaction
contributes to p53/TP53 inactivation. Component of the
TRIM28/KAP1-MDM2-p53/TP53; involved in regulating p53/TP53
stabilization and activity. Interacts (via the leucine zipper
alpha helical coiled-coil) with E2F1 (central region); the
interaction inhibits E2F1 acetylation and transcriptional
activity. Interacts with PPP1CA; the interaction dephosphorylates
TRIM28 at Ser-824 and forms a complex at the p21 promoter site.
Interacts with PPP1CB; the interaction is weak but is increased on
dephosphorylation at Ser-824. Interacts with SMARCAD1. Interacts
with, and sumoylates IRF7. Interacts with MAGEC2. Part of a
complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with
AICDA. The large PER complex involved in the histone methylation
is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or
SUV39H2; CBX3 mediates the formation of the complex (By
similarity). Interacts with NR4A3; the interactions potentiates
NR4A3 activity on NurRE promoter (By similarity). Interacts
(unphosphorylated or phosphorylated form) with ZBTB1 (via BTB
domain) (By similarity). Probably part of a corepressor complex
containing ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with ATRX.
Forms a complex with ATRX, SETDB1 and ZNF274 (By similarity).
Interacts with ZFP568; the interaction mediates ZFP568
transcriptional repression activity (By similarity). Interacts
with RRP1B (By similarity). {ECO:0000250|UniProtKB:Q13263,
ECO:0000250|UniProtKB:Q62318, ECO:0000269|PubMed:11154279}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with
centromeric heterochromatin during cell differentiation through
CBX1. {ECO:0000250}.
-!- DOMAIN: The HP1 box is both necessary and sufficient for HP1
binding. {ECO:0000250}.
-!- DOMAIN: The PHD-type zinc finger enhances CEBPB transcriptional
activity. The PHD-type zinc finger, the HP1 box and the bromo
domain, function together to assemble the machinery required for
repression of KRAB domain-containing proteins. Acts as an
intramolecular SUMO E3 ligase for autosumoylation of bromodomain
(By similarity). {ECO:0000250}.
-!- DOMAIN: The RING-finger-B Box-coiled-coil/tripartite motif
(RBCC/TRIM motif) is required for interaction with the KRAB domain
of KRAB-zinc finger proteins. Binds four zinc ions per molecule.
The RING finger and the N-terminal of the leucine zipper alpha
helical coiled-coil region of RBCC are required for
oligomerization (By similarity). {ECO:0000250}.
-!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
required for interaction with chromoshadow domains. This motif
requires additional residues -7, -6, +4 and +5 of the central Val
which contact the chromoshadow domain (By similarity).
{ECO:0000250}.
-!- PTM: ATM-induced phosphorylation on Ser-825 represses sumoylation
leading to the de-repression of expression of a subset of genes
involved in cell cycle control and apoptosis in response to
genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA
and PP1CB forms, allows sumoylation and expression of TRIM28
target genes (By similarity). {ECO:0000250}.
-!- PTM: Sumoylation/desumoylation events regulate TRIM28-mediated
transcriptional repression. Sumoylation is required for
interaction with CHD3 and SETDB1 and the corepressor activity.
Represses and is repressed by Ser-824 phosphorylation. Enhances
the TRIM28 corepressor activity, inhibiting transcriptional
activity of a number of genes including GADD45A and CDKN1A/p21.
Lys-555, Lys-780 and Lys-805 are the major sites of sumoylation.
In response to Dox-induced DNA damage, enhanced phosphorylation on
Ser-825 prevents sumoylation and allows de-repression of
CDKN1A/p21 (By similarity). {ECO:0000250}.
-!- PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
{ECO:0000250}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; BC166843; AAI66843.1; -; mRNA.
EMBL; U95041; AAB51518.1; -; mRNA.
RefSeq; NP_446368.1; NM_053916.1.
UniGene; Rn.198494; -.
ProteinModelPortal; O08629; -.
SMR; O08629; -.
BioGrid; 250580; 3.
IntAct; O08629; 1.
STRING; 10116.ENSRNOP00000031061; -.
iPTMnet; O08629; -.
PhosphoSitePlus; O08629; -.
PaxDb; O08629; -.
PRIDE; O08629; -.
Ensembl; ENSRNOT00000029996; ENSRNOP00000031061; ENSRNOG00000027487.
GeneID; 116698; -.
KEGG; rno:116698; -.
UCSC; RGD:620289; rat.
CTD; 10155; -.
RGD; 620289; Trim28.
eggNOG; ENOG410ITES; Eukaryota.
eggNOG; ENOG41102KI; LUCA.
GeneTree; ENSGT00890000139374; -.
HOGENOM; HOG000137674; -.
HOVERGEN; HBG055353; -.
InParanoid; O08629; -.
KO; K08882; -.
OMA; NQRKCER; -.
OrthoDB; EOG091G01KK; -.
PhylomeDB; O08629; -.
TreeFam; TF106455; -.
UniPathway; UPA00886; -.
PRO; PR:O08629; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000027487; -.
Genevisible; O08629; RN.
GO; GO:0000785; C:chromatin; ISO:RGD.
GO; GO:0005719; C:nuclear euchromatin; ISO:RGD.
GO; GO:0005720; C:nuclear heterochromatin; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; ISO:RGD.
GO; GO:0005634; C:nucleus; ISS:HGNC.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0070087; F:chromo shadow domain binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0035851; F:Krueppel-associated box domain binding; ISS:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
GO; GO:0008270; F:zinc ion binding; ISO:RGD.
GO; GO:0060028; P:convergent extension involved in axis elongation; ISO:RGD.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0043045; P:DNA methylation involved in embryo development; ISO:RGD.
GO; GO:0006281; P:DNA repair; ISO:RGD.
GO; GO:0007566; P:embryo implantation; ISO:RGD.
GO; GO:0060669; P:embryonic placenta morphogenesis; ISO:RGD.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0045087; P:innate immune response; ISO:RGD.
GO; GO:1901536; P:negative regulation of DNA demethylation; ISO:RGD.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:1902187; P:negative regulation of viral release from host cell; ISO:RGD.
GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
GO; GO:0045739; P:positive regulation of DNA repair; ISO:RGD.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC.
GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
GO; GO:0051259; P:protein oligomerization; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
GO; GO:0016925; P:protein sumoylation; ISO:RGD.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:2000653; P:regulation of genetic imprinting; ISO:RGD.
CDD; cd00021; BBOX; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003649; Bbox_C.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR037373; KAP1.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR45156; PTHR45156; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF00643; zf-B_box; 2.
Pfam; PF14634; zf-RING_5; 1.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 2.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Bromodomain; Chromatin regulator; Citrullination;
Coiled coil; Complete proteome; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 835 Transcription intermediary factor 1-beta.
/FTId=PRO_0000056394.
DOMAIN 698 802 Bromo.
ZN_FING 67 123 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 150 197 B box-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
ZN_FING 206 247 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 626 673 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 248 378 Leucine zipper alpha helical coiled-coil
region. {ECO:0000250}.
REGION 249 378 Interaction with MAGEC2. {ECO:0000250}.
REGION 368 372 Involved in binding PPP1CA.
{ECO:0000250}.
REGION 477 514 HP1 box.
MOTIF 482 495 PxVxL motif.
COMPBIAS 2 60 Ala-rich.
COMPBIAS 55 58 Poly-Gly.
COMPBIAS 527 532 Poly-Ala.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 268 268 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 306 306 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 342 342 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 379 379 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 471 471 Citrulline. {ECO:0000250}.
MOD_RES 472 472 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 473 473 Citrulline. {ECO:0000250}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 756 756 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 758 758 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 771 771 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 775 775 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 780 780 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q62318}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 825 825 Phosphoserine; by ATM and ATR and dsDNA
kinase. {ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 36 36 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 201 201 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 256 256 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 274 274 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 306 306 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 321 321 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 368 368 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 379 379 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 379 379 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 409 409 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 436 436 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 470 470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 470 470 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 508 508 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 555 555 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 555 555 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 576 576 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 677 677 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 751 751 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 751 751 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 751 751 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 771 771 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 775 775 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 780 780 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 780 780 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 805 805 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CONFLICT 220 220 V -> A (in Ref. 2; AAB51518).
{ECO:0000305}.
CONFLICT 263 263 K -> R (in Ref. 2; AAB51518).
{ECO:0000305}.
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


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