ID   SUMO1_CHICK             Reviewed;         101 AA.
AC   Q8QGH2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Small ubiquitin-related modifier 1;
DE            Short=SUMO-1;
DE   Flags: Precursor;
GN   Name=SUMO1; ORFNames=RCJMB04_2j18;
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 [MRNA].
RC   TISSUE=Inner ear;
RA   Venkataramu C.R., Sokolowski B.H.A.;
RT   "Protein-protein interactions of Kvbeta.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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 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; AF461015; AAL85281.1; -; mRNA.
DR   EMBL; AJ719470; CAG31129.1; -; mRNA.
DR   RefSeq; NP_989466.1; NM_204135.2.
DR   AlphaFoldDB; Q8QGH2; -.
DR   SMR; Q8QGH2; -.
DR   STRING; 9031.ENSGALP00000013729; -.
DR   PaxDb; Q8QGH2; -.
DR   Ensembl; ENSGALT00000013744; ENSGALP00000013729; ENSGALG00000008435.
DR   GeneID; 373930; -.
DR   KEGG; gga:373930; -.
DR   CTD; 7341; -.
DR   VEuPathDB; HostDB:geneid_373930; -.
DR   eggNOG; KOG1769; Eukaryota.
DR   GeneTree; ENSGT00940000154319; -.
DR   HOGENOM; CLU_148322_0_0_1; -.
DR   InParanoid; Q8QGH2; -.
DR   OMA; TIECHIE; -.
DR   OrthoDB; 1583700at2759; -.
DR   PhylomeDB; Q8QGH2; -.
DR   Reactome; R-GGA-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; R-GGA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
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-3108232; SUMO E3 ligases SUMOylate target proteins.
DR   Reactome; R-GGA-3232118; SUMOylation of transcription factors.
DR   Reactome; R-GGA-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-GGA-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-GGA-4085377; SUMOylation of SUMOylation proteins.
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-4655427; SUMOylation of DNA methylation proteins.
DR   Reactome; R-GGA-4755510; SUMOylation of immune response proteins.
DR   Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-GGA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-GGA-877312; Regulation of IFNG signaling.
DR   Reactome; R-GGA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR   Reactome; R-GGA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   PRO; PR:Q8QGH2; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   Bgee; ENSGALG00000008435; Expressed in lung and 12 other tissues.
DR   ExpressionAtlas; Q8QGH2; baseline and differential.
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; ISS:UniProtKB.
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:UniProtKB.
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..97
FT                   /note="Small ubiquitin-related modifier 1"
FT                   /id="PRO_0000267614"
FT   PROPEP          98..101
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000267615"
FT   DOMAIN          20..97
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        97
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   101 AA;  11557 MW;  9415E7C69554FB33 CRC64;
     MSDQEAKPSA EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
     SLRFLFEGQR ITDNHTPKEL GMEEEDVIEV YQEQTGGHST V