SUMO3_MOUSE
ID SUMO3_MOUSE Reviewed; 110 AA.
AC Q9Z172; Q14C17; Q3TBL9; Q3UDI5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Small ubiquitin-related modifier 3 {ECO:0000305};
DE Short=SUMO-3 {ECO:0000305};
DE AltName: Full=SMT3 homolog 1 {ECO:0000312|MGI:MGI:1336201};
DE AltName: Full=Ubiquitin-like protein SMT3A {ECO:0000303|PubMed:9891849};
DE Short=Smt3A {ECO:0000303|PubMed:9891849};
DE Flags: Precursor;
GN Name=Sumo3 {ECO:0000312|MGI:MGI:1336201};
GN Synonyms=Smt3a {ECO:0000303|PubMed:9891849},
GN Smt3h1 {ECO:0000312|MGI:MGI:1336201};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9891849; DOI=10.1080/15216549800204722;
RA Chen A., Mannen H., Li S.S.-L.;
RT "Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and
RT gene/pseudogenes.";
RL Biochem. Mol. Biol. Int. 46:1161-1174(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Embryo, Kidney, Muellerian duct, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ARNTL/BMAL1.
RX PubMed=18644859; DOI=10.1128/mcb.00583-08;
RA Lee J., Lee Y., Lee M.J., Park E., Kang S.H., Chung C.H., Lee K.H., Kim K.;
RT "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian
RT activation of the CLOCK/BMAL1 complex.";
RL Mol. Cell. Biol. 28:6056-6065(2008).
CC -!- FUNCTION: Ubiquitin-like protein which can be covalently attached to
CC target lysines either as a monomer or as a lysine-linked polymer. Does
CC not seem to be involved in protein degradation and may function as an
CC antagonist of ubiquitin in the degradation process. Plays a role in a
CC number of cellular processes such as nuclear transport, DNA replication
CC and repair, mitosis and signal transduction. Covalent attachment to its
CC substrates requires prior activation by the E1 complex SAE1-SAE2 and
CC linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase
CC such as PIAS1-4, RANBP2 or CBX4. Plays a role in the regulation of
CC sumoylation status of SETX (By similarity).
CC {ECO:0000250|UniProtKB:P55854}.
CC -!- SUBUNIT: Interacts with SAE2 and UBE2I. Covalently attached to a number
CC of proteins. Interacts with USP25 (via ts SIM domain); the interaction
CC sumoylates USP25 and inhibits its ubiquitin hydrolyzing activity (By
CC similarity). Interacts with ARNTL/BMAL1. {ECO:0000250,
CC ECO:0000269|PubMed:18644859}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Nucleus, PML body {ECO:0000269|PubMed:18644859}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z172-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z172-2; Sequence=VSP_021948;
CC -!- PTM: Polymeric chains can be formed through Lys-11 cross-linking.
CC {ECO:0000250}.
CC -!- PTM: Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary
CC for function. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; AF063847; AAC99333.1; -; mRNA.
DR EMBL; AK012742; BAB28442.1; -; mRNA.
DR EMBL; AK013019; BAB28601.1; -; mRNA.
DR EMBL; AK148306; BAE28469.1; -; mRNA.
DR EMBL; AK150063; BAE29276.1; -; mRNA.
DR EMBL; AK150200; BAE29374.1; -; mRNA.
DR EMBL; AK160169; BAE35670.1; -; mRNA.
DR EMBL; AK162035; BAE36692.1; -; mRNA.
DR EMBL; AK167207; BAE39334.1; -; mRNA.
DR EMBL; AK168988; BAE40788.1; -; mRNA.
DR EMBL; AK171169; BAE42290.1; -; mRNA.
DR EMBL; AK170896; BAE42100.1; -; mRNA.
DR EMBL; BC115488; AAI15489.1; -; mRNA.
DR EMBL; BC115489; AAI15490.1; -; mRNA.
DR CCDS; CCDS23958.1; -. [Q9Z172-1]
DR CCDS; CCDS78843.1; -. [Q9Z172-2]
DR RefSeq; NP_001288600.1; NM_001301671.1. [Q9Z172-2]
DR RefSeq; NP_001288601.1; NM_001301672.1.
DR RefSeq; NP_001288602.1; NM_001301673.1.
DR RefSeq; NP_064313.1; NM_019929.4. [Q9Z172-1]
DR AlphaFoldDB; Q9Z172; -.
DR SMR; Q9Z172; -.
DR BioGRID; 203358; 22.
DR IntAct; Q9Z172; 16.
DR STRING; 10090.ENSMUSP00000020501; -.
DR iPTMnet; Q9Z172; -.
DR PhosphoSitePlus; Q9Z172; -.
DR EPD; Q9Z172; -.
DR jPOST; Q9Z172; -.
DR MaxQB; Q9Z172; -.
DR PaxDb; Q9Z172; -.
DR PeptideAtlas; Q9Z172; -.
DR PRIDE; Q9Z172; -.
DR ProteomicsDB; 254694; -. [Q9Z172-1]
DR ProteomicsDB; 254695; -. [Q9Z172-2]
DR DNASU; 20610; -.
DR Ensembl; ENSMUST00000020501; ENSMUSP00000020501; ENSMUSG00000020265. [Q9Z172-1]
DR Ensembl; ENSMUST00000099538; ENSMUSP00000097136; ENSMUSG00000020265. [Q9Z172-2]
DR GeneID; 20610; -.
DR KEGG; mmu:20610; -.
DR UCSC; uc007fvy.2; mouse. [Q9Z172-1]
DR UCSC; uc007fvz.2; mouse. [Q9Z172-2]
DR CTD; 6612; -.
DR MGI; MGI:1336201; Sumo3.
DR VEuPathDB; HostDB:ENSMUSG00000020265; -.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00950000182895; -.
DR HOGENOM; CLU_148322_2_1_1; -.
DR InParanoid; Q9Z172; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; Q9Z172; -.
DR TreeFam; TF315116; -.
DR Reactome; R-MMU-3065679; SUMO is proteolytically processed.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR BioGRID-ORCS; 20610; 2 hits in 69 CRISPR screens.
DR ChiTaRS; Sumo3; mouse.
DR PRO; PR:Q9Z172; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9Z172; protein.
DR Bgee; ENSMUSG00000020265; Expressed in embryonic brain and 78 other tissues.
DR ExpressionAtlas; Q9Z172; baseline and differential.
DR Genevisible; Q9Z172; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0106068; C:SUMO ligase complex; ISO:MGI.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0016925; P:protein sumoylation; IDA:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..92
FT /note="Small ubiquitin-related modifier 3"
FT /id="PRO_0000035959"
FT PROPEP 93..110
FT /evidence="ECO:0000250"
FT /id="PRO_0000035960"
FT DOMAIN 15..92
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 88..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55854"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55854"
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 SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P55854"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT VAR_SEQ 1..7
FT /note="MSEEKPK -> MTTVLAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021948"
SQ SEQUENCE 110 AA; 12430 MW; 2950B8B1A3F88DC8 CRC64;
MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR
FDGQPINETD TPAQLEMEDE DTIDVFQQQT GGSASRGSVP TPNRCPDLCY
