SUMO1_CERNI
ID SUMO1_CERNI Reviewed; 101 AA.
AC Q9MZD5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Small ubiquitin-related modifier 1;
DE Short=SUMO-1;
DE AltName: Full=Sentrin;
DE Flags: Precursor;
GN Name=SUMO1;
OS Cervus nippon (Sika deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=9863;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RX PubMed=15901557;
RA Sun L.G., Jiang Y., Yu Y.L.;
RT "Discovery of Cervus nippon Temminck-derived sentrin/SUMO.";
RL Yi Chuan 24:22-26(2002).
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 (By similarity). Covalently attached to a number of proteins
CC such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN,
CC DNMT3B and TDG (By similarity). Also interacts with HIF1A, HIPK2,
CC HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (By similarity). Interacts with
CC USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 (By
CC similarity). Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM
CC domains) (By similarity). Interacts with BHLHE40/DEC1 (By similarity).
CC Interacts with RWDD3 (By similarity). Interacts with UBE2I/UBC9 and
CC this interaction is enhanced in the presence of RWDD3 (By similarity).
CC Interacts with MTA1 (By similarity). Interacts with SENP2 (By
CC similarity). Interacts with HINT1 (By similarity).
CC {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
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, 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; AF242526; AAF97049.1; -; mRNA.
DR AlphaFoldDB; Q9MZD5; -.
DR SMR; Q9MZD5; -.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
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:0016925; P:protein sumoylation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acetylation; Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Ubl conjugation; 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_0000035937"
FT PROPEP 98..101
FT /evidence="ECO:0000250"
FT /id="PRO_0000035938"
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:0000250|UniProtKB:P63165"
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; 11566 MW; 89A1AAD2D054FB33 CRC64;
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YHEQTGGHST V
