SUMO2_CHICK
ID SUMO2_CHICK Reviewed; 95 AA.
AC Q5ZJM9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Small ubiquitin-related modifier 2;
DE Short=SUMO-2;
DE Flags: Precursor;
GN Name=SUMO2; ORFNames=RCJMB04_17a7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720405; CAG32064.1; -; mRNA.
DR RefSeq; NP_001074186.1; NM_001080717.2.
DR AlphaFoldDB; Q5ZJM9; -.
DR SMR; Q5ZJM9; -.
DR STRING; 9031.ENSGALP00000012928; -.
DR PaxDb; Q5ZJM9; -.
DR Ensembl; ENSGALT00000012943; ENSGALP00000012928; ENSGALG00000007971.
DR GeneID; 770125; -.
DR KEGG; gga:770125; -.
DR CTD; 6613; -.
DR VEuPathDB; HostDB:geneid_770125; -.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00950000182895; -.
DR HOGENOM; CLU_148322_2_1_1; -.
DR InParanoid; Q5ZJM9; -.
DR OMA; AYCDRVG; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; Q5ZJM9; -.
DR TreeFam; TF315116; -.
DR Reactome; R-GGA-3065679; SUMO is proteolytically processed.
DR Reactome; R-GGA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-GGA-3232118; SUMOylation of transcription factors.
DR Reactome; R-GGA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-GGA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-GGA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-GGA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-5696395; Formation of Incision Complex in GG-NER.
DR PRO; PR:Q5ZJM9; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000007971; Expressed in spermatid and 12 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
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:0016925; P:protein sumoylation; ISS:UniProtKB.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
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 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_0000269467"
FT PROPEP 94..95
FT /evidence="ECO:0000250"
FT /id="PRO_0000269468"
FT DOMAIN 16..95
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 95 AA; 10871 MW; F8F0426849BEF08B CRC64;
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLSMRQIRF
RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY
