ID   SUMO2_XENTR             Reviewed;          95 AA.
AC   Q28H04;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Small ubiquitin-related modifier 2;
DE            Short=SUMO-2;
DE   Flags: Precursor;
GN   Name=sumo2; ORFNames=TEgg046d06.1;
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=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2006) 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, including top2 (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; CR761130; CAJ81672.1; -; mRNA.
DR   RefSeq; NP_001016406.1; NM_001016406.2.
DR   AlphaFoldDB; Q28H04; -.
DR   SMR; Q28H04; -.
DR   STRING; 8364.ENSXETP00000027383; -.
DR   PaxDb; Q28H04; -.
DR   Ensembl; ENSXETT00000027383; ENSXETP00000027383; ENSXETG00000012516.
DR   GeneID; 549160; -.
DR   KEGG; xtr:549160; -.
DR   CTD; 6613; -.
DR   Xenbase; XB-GENE-969139; sumo2.
DR   eggNOG; KOG1769; Eukaryota.
DR   HOGENOM; CLU_148322_2_1_1; -.
DR   InParanoid; Q28H04; -.
DR   OMA; ENDHINP; -.
DR   OrthoDB; 1583700at2759; -.
DR   PhylomeDB; Q28H04; -.
DR   TreeFam; TF315116; -.
DR   Reactome; R-XTR-196791; Vitamin D (calciferol) metabolism.
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-3232118; SUMOylation of transcription factors.
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-4615885; SUMOylation of DNA replication proteins.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000012516; Expressed in gastrula and 18 other tissues.
DR   ExpressionAtlas; Q28H04; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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_0000269475"
FT   PROPEP          94..95
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000269476"
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;  10856 MW;  4BD09F6958BFF41C CRC64;
     MADDKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL NKLMKAYCER QGLSMRQIRF
     RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGSF