SUMO1_DANRE
ID SUMO1_DANRE Reviewed; 100 AA.
AC Q7SZR5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Small ubiquitin-related modifier 1;
DE Short=SUMO-1;
DE Flags: Precursor;
GN Name=sumo1; ORFNames=zgc:65934, zgc:85634;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) 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. Covalent attachment
CC via an isopeptide bond to its substrates requires prior activation by
CC the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post-
CC translational modification on lysine residues of proteins plays a
CC crucial role in a number of cellular processes such as nuclear
CC transport, DNA replication and repair, mitosis and signal transduction.
CC Polymeric sumo1 chains are also susceptible to polyubiquitination which
CC functions as a signal for proteasomal degradation of modified proteins.
CC {ECO:0000250|UniProtKB:P63165}.
CC -!- SUBUNIT: Interacts with sae2, ube2i, ranbp2, pias1 and pias2 (By
CC similarity). Covalently attached to a number of proteins (By
CC similarity). {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; BC056283; AAH56283.1; -; mRNA.
DR EMBL; BC067553; AAH67553.1; -; mRNA.
DR RefSeq; NP_998324.1; NM_213159.1.
DR AlphaFoldDB; Q7SZR5; -.
DR SMR; Q7SZR5; -.
DR STRING; 7955.ENSDARP00000064994; -.
DR PaxDb; Q7SZR5; -.
DR PeptideAtlas; Q7SZR5; -.
DR Ensembl; ENSDART00000064995; ENSDARP00000064994; ENSDARG00000044267.
DR GeneID; 406438; -.
DR KEGG; dre:406438; -.
DR CTD; 7341; -.
DR ZFIN; ZDB-GENE-040426-2186; sumo1.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00940000154319; -.
DR HOGENOM; CLU_148322_4_2_1; -.
DR InParanoid; Q7SZR5; -.
DR OMA; DQMVHIN; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; Q7SZR5; -.
DR TreeFam; TF315116; -.
DR Reactome; R-DRE-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-DRE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-DRE-3065679; SUMO is proteolytically processed.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-DRE-3232118; SUMOylation of transcription factors.
DR Reactome; R-DRE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DRE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DRE-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DRE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DRE-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-DRE-4755510; SUMOylation of immune response proteins.
DR Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DRE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DRE-877312; Regulation of IFNG signaling.
DR Reactome; R-DRE-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-DRE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q7SZR5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000044267; Expressed in testis and 29 other tissues.
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: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:0043009; P:chordate embryonic development; IGI:ZFIN.
DR GO; GO:0060216; P:definitive hemopoiesis; IGI:ZFIN.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
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..96
FT /note="Small ubiquitin-related modifier 1"
FT /id="PRO_0000267612"
FT PROPEP 97..100
FT /evidence="ECO:0000250"
FT /id="PRO_0000267613"
FT DOMAIN 19..96
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 100 AA; 11396 MW; 08CBD664F309019B CRC64;
MSDTETKPSS DGGEKKDGEY IKLKVIGQDN SEIHFKVKMT THLKKLKESY SQRQGVPVNS
LRFLFEGQRI TDNLTPKELG MEDEDVIEVY QEQTGGCRND
