SUMO2_MOUSE
ID SUMO2_MOUSE Reviewed; 95 AA.
AC P61957; A2A9X2; P55855; Q542L8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Small ubiquitin-related modifier 2 {ECO:0000305};
DE Short=SUMO-2 {ECO:0000305};
DE AltName: Full=SMT3 homolog 2 {ECO:0000312|MGI:MGI:2158813};
DE AltName: Full=Ubiquitin-like protein SMT3B {ECO:0000303|PubMed:9891849};
DE Short=Smt3B {ECO:0000303|PubMed:9891849};
DE Flags: Precursor;
GN Name=Sumo2 {ECO:0000312|MGI:MGI:2158813};
GN Synonyms=Smt3b {ECO:0000312|MGI:MGI:2158813},
GN Smt3h2 {ECO:0000312|MGI:MGI:2158813};
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].
RC STRAIN=BALB/cJ; TISSUE=Brain;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Placenta, and Stomach;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP INTERACTION WITH HINT1.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
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. Interacts with HINT1 (PubMed:31088288).
CC Interacts with GCNA (via SIM domains); this interaction allows the GCNA
CC recruitment to DPCs sites (By similarity).
CC {ECO:0000250|UniProtKB:P61956, ECO:0000269|PubMed:31088288}.
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; L79948; AAL40136.1; -; mRNA.
DR EMBL; AK012619; BAB28360.1; -; mRNA.
DR EMBL; AK085238; BAC39397.1; -; mRNA.
DR EMBL; AK132213; BAE21037.1; -; mRNA.
DR EMBL; AK160404; BAE35772.1; -; mRNA.
DR EMBL; AK167308; BAE39412.1; -; mRNA.
DR EMBL; AL645470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017522; AAH17522.1; -; mRNA.
DR EMBL; BC083326; AAH83326.1; -; mRNA.
DR EMBL; BC095930; AAH95930.1; -; mRNA.
DR CCDS; CCDS36374.1; -.
DR RefSeq; NP_579932.1; NM_133354.2.
DR PDB; 5TVP; X-ray; 2.40 A; Q=10-88.
DR PDB; 5TVQ; X-ray; 2.35 A; B=10-93.
DR PDBsum; 5TVP; -.
DR PDBsum; 5TVQ; -.
DR AlphaFoldDB; P61957; -.
DR BMRB; P61957; -.
DR SMR; P61957; -.
DR BioGRID; 228466; 5.
DR STRING; 10090.ENSMUSP00000115044; -.
DR iPTMnet; P61957; -.
DR PhosphoSitePlus; P61957; -.
DR SwissPalm; P61957; -.
DR EPD; P61957; -.
DR jPOST; P61957; -.
DR MaxQB; P61957; -.
DR PaxDb; P61957; -.
DR PeptideAtlas; P61957; -.
DR PRIDE; P61957; -.
DR ProteomicsDB; 258772; -.
DR TopDownProteomics; P61957; -.
DR DNASU; 170930; -.
DR Ensembl; ENSMUST00000153892; ENSMUSP00000115044; ENSMUSG00000020738.
DR GeneID; 170930; -.
DR KEGG; mmu:170930; -.
DR UCSC; uc007mhw.1; mouse.
DR CTD; 6613; -.
DR MGI; MGI:2158813; Sumo2.
DR VEuPathDB; HostDB:ENSMUSG00000020738; -.
DR eggNOG; KOG1769; Eukaryota.
DR GeneTree; ENSGT00950000182895; -.
DR HOGENOM; CLU_148322_2_1_1; -.
DR InParanoid; P61957; -.
DR OMA; AYCDRVG; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; P61957; -.
DR TreeFam; TF315116; -.
DR Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
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-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR BioGRID-ORCS; 170930; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Sumo2; mouse.
DR PRO; PR:P61957; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P61957; protein.
DR Bgee; ENSMUSG00000020738; Expressed in embryonic post-anal tail and 75 other tissues.
DR ExpressionAtlas; P61957; baseline and differential.
DR Genevisible; P61957; MM.
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:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:MGI.
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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI: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 3D-structure; Acetylation; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..93
FT /note="Small ubiquitin-related modifier 2"
FT /id="PRO_0000035951"
FT PROPEP 94..95
FT /evidence="ECO:0000250"
FT /id="PRO_0000035952"
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:0007744|PubMed:23806337"
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"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5TVQ"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5TVQ"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:5TVQ"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5TVQ"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5TVQ"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:5TVQ"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:5TVQ"
SQ SEQUENCE 95 AA; 10871 MW; F8F0426849BEF08B CRC64;
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLSMRQIRF
RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY
