ID   SMO1B_XENLA             Reviewed;         102 AA.
AC   Q5EAX4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Small ubiquitin-related modifier 1-B;
DE            Short=SUMO-1-B;
DE   Flags: Precursor;
GN   Name=sumo1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) 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 (By similarity).
CC       Covalent attachment via an isopeptide bond to its substrates requires
CC       prior activation by the E1 complex sae1-sae2 and linkage to the E2
CC       enzyme ube2i. This post-translational modification on lysine residues
CC       of proteins plays a crucial role in a number of cellular processes such
CC       as nuclear transport, DNA replication and repair, mitosis and signal
CC       transduction. Polymeric sumo1 chains are also susceptible to
CC       polyubiquitination which functions as a signal for proteasomal
CC       degradation of modified proteins (By similarity).
CC       {ECO:0000250|UniProtKB:O57686, ECO:0000250|UniProtKB:P63165}.
CC   -!- SUBUNIT: Interacts with sae2, ube2i, ranbp2, pias1 and pias2 (By
CC       similarity). Interacts with sox9 and sox10 (By similarity). Covalently
CC       attached to a number of proteins (By similarity).
CC       {ECO:0000250|UniProtKB:O57686, 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; BC090210; AAH90210.1; -; mRNA.
DR   RefSeq; NP_001090274.1; NM_001096805.1.
DR   AlphaFoldDB; Q5EAX4; -.
DR   SMR; Q5EAX4; -.
DR   BioGRID; 607888; 1.
DR   MaxQB; Q5EAX4; -.
DR   DNASU; 779181; -.
DR   GeneID; 779181; -.
DR   KEGG; xla:779181; -.
DR   CTD; 779181; -.
DR   Xenbase; XB-GENE-978496; sumo1.S.
DR   OrthoDB; 1583700at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 779181; Expressed in gastrula and 19 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR   GO; GO:0016925; P:protein sumoylation; ISS:AgBase.
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..98
FT                   /note="Small ubiquitin-related modifier 1-B"
FT                   /id="PRO_0000267620"
FT   PROPEP          99..102
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000267621"
FT   DOMAIN          21..98
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        98
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   102 AA;  11630 MW;  CA93B8E4509AC557 CRC64;
     MSDQEAKPSS EDLGDKKEGG DYIKLKVIGQ DSSEIHFKVK MTTHLKKLKE SYCQRQGVPM
     NSLRFLFEGQ RISDHQTPKE LGMEEEDVIE VYQEQTGGHS TI