ID SUMO2_DANRE Reviewed; 96 AA.
AC Q6DHL4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Small ubiquitin-related modifier 2 {ECO:0000305};
DE Short=SUMO-2 {ECO:0000305};
DE Flags: Precursor;
GN Name=sumo2 {ECO:0000305}; ORFNames=zgc:92241 {ECO:0000312|EMBL:AAH75956.1};
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].
RG NIH - Zebrafish Gene Collection (ZGC) 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 as a lysine-linked polymer. Covalent
CC attachment via an isopeptide bond to its substrates requires prior
CC activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme
CC ube2i, and can be promoted by an E3 ligase such as pias1-4. 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 sumo2 chains are also susceptible to polyubiquitination which
CC functions as a signal for proteasomal degradation of modified proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with sae2 and ube2i. Covalently attached to a number
CC of proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Polymeric chains can be formed through Lys-11 cross-linking.
CC {ECO:0000250}.
CC -!- PTM: Cleavage of precursor form by a sentrin-specific protease is
CC necessary for function. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; BC075956; AAH75956.1; -; mRNA.
DR RefSeq; NP_001003422.1; NM_001003422.2.
DR AlphaFoldDB; Q6DHL4; -.
DR SMR; Q6DHL4; -.
DR STRING; 7955.ENSDARP00000137571; -.
DR PaxDb; 7955-ENSDARP00000066628; -.
DR PeptideAtlas; Q6DHL4; -.
DR GeneID; 445027; -.
DR KEGG; dre:445027; -.
DR AGR; ZFIN:ZDB-GENE-040801-7; -.
DR CTD; 445027; -.
DR ZFIN; ZDB-GENE-040801-7; sumo2b.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_2_1_1; -.
DR InParanoid; Q6DHL4; -.
DR OMA; IKRSTPM; -.
DR OrthoDB; 5132985at2759; -.
DR PhylomeDB; Q6DHL4; -.
DR Reactome; R-DRE-196791; Vitamin D (calciferol) metabolism.
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-3232118; SUMOylation of transcription factors.
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-4755510; SUMOylation of immune response proteins.
DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DRE-5696395; Formation of Incision Complex in GG-NER.
DR PRO; PR:Q6DHL4; -.
DR Proteomes; UP000000437; Chromosome 3.
DR Bgee; ENSDARG00000102741; Expressed in pharyngeal gill and 31 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
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; cd16115; Ubl_SUMO2_3_4; 1.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10562; SMALL UBIQUITIN-RELATED MODIFIER; 1.
DR PANTHER; PTHR10562:SF74; SMALL UBIQUITIN-RELATED MODIFIER 2-RELATED; 1.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..93
FT /note="Small ubiquitin-related modifier 2"
FT /id="PRO_0000269469"
FT PROPEP 94..96
FT /evidence="ECO:0000250"
FT /id="PRO_0000269470"
FT DOMAIN 16..96
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 93
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 96 AA; 11029 MW; B797B5D4B322BEF0 CRC64;
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLTMRQIRF
RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGHRI
//
