SUMO1_XENTR
ID SUMO1_XENTR Reviewed; 102 AA.
AC Q6DEP7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Small ubiquitin-related modifier 1;
DE Short=SUMO-1;
DE Flags: Precursor;
GN Name=sumo1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to
CC proteins as a monomer or a lysine-linked polymer (By similarity).
CC Covalent attachment via an isopeptide bond to its substrates requires
CC prior activation by the E1 complex sae1-sae2 and linkage to the E2
CC enzyme ube2i. This post-translational modification on lysine residues
CC of proteins plays a crucial role in a number of cellular processes such
CC as nuclear transport, DNA replication and repair, mitosis and signal
CC transduction. Polymeric sumo1 chains are also susceptible to
CC polyubiquitination which functions as a signal for proteasomal
CC degradation of modified proteins (By similarity).
CC {ECO:0000250|UniProtKB:O57686, ECO:0000250|UniProtKB:P63165}.
CC -!- SUBUNIT: Interacts with sae2, ube2i, ranbp2, pias1 and pias2 (By
CC similarity). Interacts with sox9 and sox10 (By similarity). Covalently
CC attached to a number of proteins (By similarity).
CC {ECO:0000250|UniProtKB:O57686, ECO:0000250|UniProtKB:P63165}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P63165}.
CC Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:P63165}. Cell membrane
CC {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}.
CC -!- PTM: Cleavage of precursor form by a sentrin-specific protease is
CC necessary for function. {ECO:0000250|UniProtKB:P63165}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; BC077048; AAH77048.1; -; mRNA.
DR RefSeq; NP_001005111.1; NM_001005111.1.
DR AlphaFoldDB; Q6DEP7; -.
DR SMR; Q6DEP7; -.
DR STRING; 8364.ENSXETP00000047766; -.
DR PaxDb; Q6DEP7; -.
DR DNASU; 448691; -.
DR GeneID; 448691; -.
DR KEGG; xtr:448691; -.
DR CTD; 7341; -.
DR Xenbase; XB-GENE-978491; sumo1.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_0_0_1; -.
DR InParanoid; Q6DEP7; -.
DR OMA; TIECHIE; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; Q6DEP7; -.
DR TreeFam; TF315116; -.
DR Reactome; R-XTR-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-XTR-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-XTR-3065679; SUMO is proteolytically processed.
DR Reactome; R-XTR-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-XTR-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-XTR-3232118; SUMOylation of transcription factors.
DR Reactome; R-XTR-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-XTR-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-XTR-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-XTR-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-XTR-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-XTR-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-XTR-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-XTR-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-XTR-4755510; SUMOylation of immune response proteins.
DR Reactome; R-XTR-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-XTR-877312; Regulation of IFNG signaling.
DR Reactome; R-XTR-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; ISS:AgBase.
DR CDD; cd16114; Ubl_SUMO1; 1.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR046332; SUMO1_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..98
FT /note="Small ubiquitin-related modifier 1"
FT /id="PRO_0000267622"
FT PROPEP 99..102
FT /evidence="ECO:0000250"
FT /id="PRO_0000267623"
FT DOMAIN 21..98
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 102 AA; 11630 MW; CA93B8E4509AC557 CRC64;
MSDQEAKPSS EDLGDKKEGG DYIKLKVIGQ DSSEIHFKVK MTTHLKKLKE SYCQRQGVPM
NSLRFLFEGQ RISDHQTPKE LGMEEEDVIE VYQEQTGGHS TI
