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   27-MAR-2024, entry version 169.
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}, Smt3h2
GN   {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyGen; P61957; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61957; -.
DR   PhosphoSitePlus; P61957; -.
DR   SwissPalm; P61957; -.
DR   EPD; P61957; -.
DR   jPOST; P61957; -.
DR   MaxQB; P61957; -.
DR   PaxDb; 10090-ENSMUSP00000115044; -.
DR   PeptideAtlas; P61957; -.
DR   ProteomicsDB; 258772; -.
DR   Pumba; P61957; -.
DR   TopDownProteomics; P61957; -.
DR   DNASU; 170930; -.
DR   Ensembl; ENSMUST00000153892.2; ENSMUSP00000115044.2; ENSMUSG00000020738.17.
DR   GeneID; 170930; -.
DR   KEGG; mmu:170930; -.
DR   UCSC; uc007mhw.1; mouse.
DR   AGR; MGI:2158813; -.
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; IKRSTPM; -.
DR   OrthoDB; 5132985at2759; -.
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 78 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 78 other cell types or tissues.
DR   ExpressionAtlas; P61957; baseline and differential.
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:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR   GO; GO:0031386; F:protein tag activity; 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:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0008104; P:protein localization; ISO:MGI.
DR   GO; GO:0016925; P:protein sumoylation; IDA:MGI.
DR   CDD; cd16115; Ubl_SUMO2_3_4; 1.
DR   InterPro; IPR022617; Rad60/SUMO-like_dom.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10562; SMALL UBIQUITIN-RELATED MODIFIER; 1.
DR   PANTHER; PTHR10562:SF74; SMALL UBIQUITIN-RELATED MODIFIER 2-RELATED; 1.
DR   Pfam; PF11976; Rad60-SLD; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   Genevisible; P61957; MM.
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
//