ATRX_PANTR
ID ATRX_PANTR Reviewed; 2492 AA.
AC Q7YQM4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcriptional regulator ATRX;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase ATRX;
DE AltName: Full=X-linked helicase II;
DE AltName: Full=X-linked nuclear protein;
DE Short=XNP;
GN Name=ATRX;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12777533; DOI=10.1093/molbev/msg134;
RA Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT chimpanzees.";
RL Mol. Biol. Evol. 20:1281-1289(2003).
CC -!- FUNCTION: Involved in transcriptional regulation and chromatin
CC remodeling. Facilitates DNA replication in multiple cellular
CC environments and is required for efficient replication of a subset of
CC genomic loci. Binds to DNA tandem repeat sequences in both telomeres
CC and euchromatin and in vitro binds DNA quadruplex structures. May help
CC stabilizing G-rich regions into regular chromatin structures by
CC remodeling G4 DNA and incorporating H3.3-containing nucleosomes.
CC Catalytic component of the chromatin remodeling complex ATRX:DAXX which
CC has ATP-dependent DNA translocase activity and catalyzes the
CC replication-independent deposition of histone H3.3 in pericentric DNA
CC repeats outside S-phase and telomeres, and the in vitro remodeling of
CC H3.3-containing nucleosomes. Its heterochromatin targeting is proposed
CC to involve a combinatorial readout of histone H3 modifications
CC (specifically methylation states of H3K9 and H3K4) and association with
CC CBX5. Involved in maintaining telomere structural integrity in
CC embryonic stem cells which probably implies recruitment of CBX5 to
CC telomeres. May be involved in transcriptional regulation of telomeric
CC repeat-containing RNA (TERRA). Acts as negative regulator of chromatin
CC incorporation of transcriptionally repressive histone MACROH2A1,
CC particularily at telomeres. Participates in the allele-specific gene
CC expression at the imprinted IGF2/H19 gene locus. On the maternal
CC allele, required for the chromatin occupancy of SMC1 and CTCTF within
CC the H19 imprinting control region (ICR) and involved in esatblishment
CC of histone tails modifications in the ICR. May be involved in brain
CC development and facial morphogenesis. Binds to zinc-finger coding genes
CC with atypical chromatin signatures and regulates its H3K9me3 levels.
CC Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the
CC deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger
CC genes (By similarity). {ECO:0000250|UniProtKB:P46100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with DAXX to form the chromatin remodeling complex
CC ATRX:DAXX. Probably binds EZH2. Binds annexin V in a calcium and
CC phosphatidylcholine/phosphatidylserine-dependent manner. Interacts
CC directly with CBX5 via the PxVxL motif. Interacts with RAD50, MRE11 and
CC NBN; indicative for an association with the MRN complex. Interacts with
CC histone MACROH2A1. Interacts with histone H3 peptides methylated at
CC 'Lys-10' with preferences H3K9me3 > H3K9me2 > H3K9me1. Interacts with
CC histone H3 peptides unmethylated at 'Lys-5' (H3K4me0). Interacts with
CC MECP2, SMC1 and SMC3. Interacts with SETDB1, TRIM28 and ZNF274 (By
CC similarity). {ECO:0000250|UniProtKB:P46100}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Associated with
CC pericentromeric heterochromatin during interphase and mitosis, probably
CC by interacting with CBX5/HP1 alpha. Colocalizes with histone H3.3,
CC DAXX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with cohesin
CC (SMC1 and SMC3) and MECP2 at the maternal H19 ICR (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The ADD domain predominantly interacts with histone H3
CC trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3 mono- or
CC dimethylated at 'Lys-10') and simultanously to histone H3 unmethylated
CC at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is disrupted by the
CC presence of H3K4me3 suggesting a readout of the combined histone H3
CC methylation state (By similarity). {ECO:0000250}.
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.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AB102642; BAC81111.1; -; mRNA.
DR RefSeq; NP_001009018.1; NM_001009018.1.
DR AlphaFoldDB; Q7YQM4; -.
DR BMRB; Q7YQM4; -.
DR SMR; Q7YQM4; -.
DR STRING; 9598.ENSPTRP00000054614; -.
DR PaxDb; Q7YQM4; -.
DR Ensembl; ENSPTRT00000111037; ENSPTRP00000087577; ENSPTRG00000022047.
DR GeneID; 449625; -.
DR KEGG; ptr:449625; -.
DR CTD; 546; -.
DR VGNC; VGNC:53808; ATRX.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR InParanoid; Q7YQM4; -.
DR OrthoDB; 815681at2759; -.
DR Proteomes; UP000002277; Chromosome X.
DR Bgee; ENSPTRG00000022047; Expressed in thymus and 21 other tissues.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0070087; F:chromo shadow domain binding; IEA:Ensembl.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0000212; P:meiotic spindle organization; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; IEA:Ensembl.
DR GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISS:UniProtKB.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:UniProtKB.
DR GO; GO:1901582; P:positive regulation of telomeric RNA transcription from RNA pol II promoter; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0035128; P:post-embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chromatin regulator; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Metal-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2492
FT /note="Transcriptional regulator ATRX"
FT /id="PRO_0000074304"
FT DOMAIN 159..296
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT DOMAIN 1581..1768
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 2025..2205
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 170..206
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 217..272
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1326
FT /note="Interaction with DAXX"
FT /evidence="ECO:0000250"
FT REGION 1913..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2010..2280
FT /note="Interaction with MECP2"
FT /evidence="ECO:0000250"
FT REGION 2462..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 581..594
FT /note="PxVxL motif"
FT MOTIF 1719..1722
FT /note="DEGH box"
FT COMPBIAS 32..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1191
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1941..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2469..2483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1594..1601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 967
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 977
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1063
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1996
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 2220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 2474
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 2480
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1004
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1982
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1982
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1987
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
SQ SEQUENCE 2492 AA; 282570 MW; 56978AC7D37400DC CRC64;
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS
LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH
FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC
KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI
ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM
DAVNKEKNTK EHKVIDAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMDQNVPT
EEQRANKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS
SVDHQGDGSS GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK
TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK
QSETVDQNSD SDEMLAILKE VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK
RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR
IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERENFSS AEGTVDKDTT
IMELRDRLPK KQQASASTDG VDKFSGKEES FTSLEVRKVA ETKEKSKHLK TKTCKKVQDG
LSDTAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK KVIKMEQQYE SSSDGTEKLP
EREEICHFPK GIKQIKNGTT DGEKKSKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK
KSKNGAYGRE KKRCKLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL
SSKRNTKEIQ SGSSSSDAEE SSEDNKKKQQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD
DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV
NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE
DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS
NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL
KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS
TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI
IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS
RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN
SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM
SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS
LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF
SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV
YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS
EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA
EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN
SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY
QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM
