SUMO2_BOVIN
ID SUMO2_BOVIN Reviewed; 95 AA.
AC P61955; P55855; Q3ZCG1; Q5E979;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Small ubiquitin-related modifier 2 {ECO:0000305};
DE Short=SUMO-2 {ECO:0000305};
DE AltName: Full=Ubiquitin-like protein SMT3B {ECO:0000303|PubMed:9833880};
DE Short=Smt3B {ECO:0000303|PubMed:9833880};
DE Flags: Precursor;
GN Name=SUMO2 {ECO:0000305}; Synonyms=SMT3B {ECO:0000303|PubMed:9833880};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endometrium;
RX PubMed=9833880; DOI=10.1016/s0168-1702(98)00073-2;
RA Qi F., Ridpath J.F., Berry E.S.;
RT "Insertion of a bovine SMT3B gene in NS4B and duplication of NS3 in a
RT bovine viral diarrhea virus genome correlate with the cytopathogenicity of
RT the virus.";
RL Virus Res. 57:1-9(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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, RANBP2 or
CC CBX4. This post-translational modification on lysine residues of
CC proteins plays a crucial role in a number of cellular processes such as
CC nuclear transport, DNA replication and repair, mitosis and signal
CC transduction. Polymeric SUMO2 chains are also susceptible to
CC polyubiquitination which functions as a signal for proteasomal
CC degradation of modified proteins. Plays a role in the regulation of
CC sumoylation status of SETX (By similarity).
CC {ECO:0000250|UniProtKB:P61956}.
CC -!- SUBUNIT: Interacts with SAE2 and UBE2I. Interacts with ZNF451.
CC Identified in a complex with ZNF451 and UBE2I/UBC9, where one ZNF451
CC interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the
CC UBE2I/UBC9 active site and the other to another region of the same
CC UBE2I/UBC9 molecule. Covalently attached to a number of proteins.
CC Interacts with PELP1. Interacts with USP25; the interaction sumoylates
CC USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM
CC domains). Interacts with MTA1 (By similarity). Interacts with HINT1 (By
CC similarity). Interacts with GCNA (via SIM domains); this interaction
CC allows the GCNA recruitment to DPCs sites (By similarity).
CC {ECO:0000250|UniProtKB:P61956, ECO:0000250|UniProtKB:P61957}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
CC {ECO:0000250}.
CC -!- PTM: Polymeric chains can be formed through Lys-11 cross-linking.
CC Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-
CC 63'-linked polyubiquitination by RNF4 (By similarity). {ECO:0000250}.
CC -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
CC function. {ECO:0000250}.
CC -!- PTM: Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-
CC dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; U89439; AAB49682.1; -; mRNA.
DR EMBL; BT021041; AAX09058.1; -; mRNA.
DR EMBL; BC102379; AAI02380.1; -; mRNA.
DR RefSeq; NP_777194.1; NM_174769.2.
DR RefSeq; XP_015314492.1; XM_015459006.1.
DR AlphaFoldDB; P61955; -.
DR BMRB; P61955; -.
DR SMR; P61955; -.
DR PeptideAtlas; P61955; -.
DR PRIDE; P61955; -.
DR Ensembl; ENSBTAT00000042554; ENSBTAP00000040189; ENSBTAG00000030169.
DR GeneID; 286807; -.
DR KEGG; bta:286807; -.
DR CTD; 6613; -.
DR VEuPathDB; HostDB:ENSBTAG00000030169; -.
DR GeneTree; ENSGT00950000182895; -.
DR InParanoid; P61955; -.
DR OMA; AYCDRVG; -.
DR OrthoDB; 1583700at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030169; Expressed in oocyte and 104 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:0019789; F:SUMO transferase activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 Acetylation; 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_0000035945"
FT PROPEP 94..95
FT /evidence="ECO:0000250"
FT /id="PRO_0000035946"
FT DOMAIN 16..95
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOD_RES 11
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61956"
FT CROSSLNK 1
FT /note="Peptide (Met-Gly) (interchain with G-Cter in
FT ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61956"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61956"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61956"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61956"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P61956"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61956"
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
