SUMO1_RAT
ID SUMO1_RAT Reviewed; 101 AA.
AC Q5I0H3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Small ubiquitin-related modifier 1;
DE Short=SUMO-1;
DE Flags: Precursor;
GN Name=Sumo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP INTERACTION WITH PRKN.
RX PubMed=16955485; DOI=10.1002/jnr.21041;
RA Um J.W., Chung K.C.;
RT "Functional modulation of parkin through physical interaction with SUMO-
RT 1.";
RL J. Neurosci. Res. 84:1543-1554(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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, and can be
CC promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. 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 Involved for instance in targeting RANGAP1 to the nuclear pore complex
CC protein RANBP2. Covalently attached to the voltage-gated potassium
CC channel KCNB1; this modulates the gating characteristics of KCNB1.
CC Polymeric SUMO1 chains are also susceptible to polyubiquitination which
CC functions as a signal for proteasomal degradation of modified proteins.
CC May also regulate a network of genes involved in palate development.
CC Covalently attached to ZFHX3. {ECO:0000250|UniProtKB:P63165,
CC ECO:0000250|UniProtKB:P63166}.
CC -!- SUBUNIT: Covalently attached to KCNB1; UBE2I increases cross-linking
CC with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity).
CC Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (By similarity). Interacts
CC with PRKN (PubMed:16955485). Covalently attached to a number of
CC proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha,
CC MDM2, JUN, DNMT3B and TDG (By similarity). Also interacts with HIF1A,
CC HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (By similarity). Interacts
CC with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25
CC (By similarity). Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via
CC SIM domains) (By similarity). Interacts with BHLHE40/DEC1 (By
CC similarity). Interacts with RWDD3 (By similarity). Interacts with
CC UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3
CC (By similarity). Interacts with MTA1 (By similarity). Interacts with
CC SENP2 (By similarity). Interacts with HINT1 (By similarity).
CC {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166,
CC ECO:0000269|PubMed:16955485}.
CC -!- INTERACTION:
CC Q5I0H3; P42260: Grik2; NbExp=4; IntAct=EBI-7253100, EBI-7809795;
CC Q5I0H3; P38656: Ssb; NbExp=3; IntAct=EBI-7253100, EBI-15649175;
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 Note=Recruited by BCL11A into the nuclear body (By similarity). In the
CC presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the
CC nucleus some of which overlap or closely associate with PML body (By
CC similarity). {ECO:0000250|UniProtKB:P63165,
CC ECO:0000250|UniProtKB:P63166}.
CC -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
CC function. {ECO:0000250|UniProtKB:P63165}.
CC -!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4.
CC {ECO:0000250|UniProtKB:P63165}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; BC088322; AAH88322.1; -; mRNA.
DR RefSeq; NP_001009672.1; NM_001009672.1.
DR AlphaFoldDB; Q5I0H3; -.
DR SMR; Q5I0H3; -.
DR BioGRID; 256960; 13.
DR DIP; DIP-46501N; -.
DR IntAct; Q5I0H3; 7.
DR MINT; Q5I0H3; -.
DR STRING; 10116.ENSRNOP00000022048; -.
DR iPTMnet; Q5I0H3; -.
DR PhosphoSitePlus; Q5I0H3; -.
DR jPOST; Q5I0H3; -.
DR PaxDb; Q5I0H3; -.
DR PRIDE; Q5I0H3; -.
DR GeneID; 301442; -.
DR KEGG; rno:301442; -.
DR UCSC; RGD:1306919; rat.
DR CTD; 7341; -.
DR RGD; 1306919; Sumo1.
DR VEuPathDB; HostDB:ENSRNOG00000016133; -.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_0_0_1; -.
DR InParanoid; Q5I0H3; -.
DR OMA; TIECHIE; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; Q5I0H3; -.
DR TreeFam; TF315116; -.
DR Reactome; R-RNO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-RNO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-RNO-3065679; SUMO is proteolytically processed.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-RNO-3232118; SUMOylation of transcription factors.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-RNO-4755510; SUMOylation of immune response proteins.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-RNO-877312; Regulation of IFNG signaling.
DR Reactome; R-RNO-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:Q5I0H3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016133; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5I0H3; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0001650; C:fibrillar center; IDA:RGD.
DR GO; GO:0016604; C:nuclear body; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0001741; C:XY body; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0044388; F:small protein activating enzyme binding; ISO:RGD.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
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:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
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:0045759; P:negative regulation of action potential; ISS:UniProtKB.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030578; P:PML body organization; ISO:RGD.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0090204; P:protein localization to nuclear pore; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:1903169; P:regulation of calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; 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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CHAIN 2..97
FT /note="Small ubiquitin-related modifier 1"
FT /id="PRO_0000267610"
FT PROPEP 98..101
FT /evidence="ECO:0000250"
FT /id="PRO_0000267611"
FT DOMAIN 20..97
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 36
FT /note="Interaction with PIAS2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P63165"
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; 89BE97D2D054FB33 CRC64;
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V
