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Protein

Small ubiquitin-related modifier 2

Gene

Sumo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX (By similarity).By similarity

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. SUMO transferase activity Source: MGI
  3. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  2. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  3. protein sumoylation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_196649. SUMO is proteolytically processed.
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 2Curated
Short name:
SUMO-2Curated
Alternative name(s):
SMT3 homolog 2Imported
Ubiquitin-like protein SMT3B1 Publication
Short name:
Smt3B1 Publication
Gene namesi
Name:Sumo2Imported
Synonyms:Smt3bImported, Smt3h2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2158813. Sumo2.

Subcellular locationi

Nucleus By similarity. NucleusPML body By similarity

GO - Cellular componenti

  1. nucleus Source: MGI
  2. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Small ubiquitin-related modifier 2PRO_0000035951Add
BLAST
Propeptidei94 – 952By similarityPRO_0000035952

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei11 – 111N6-acetyllysine; alternate1 Publication
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki93 – 93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Post-translational modificationi

Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity).By similarity
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP61957.
PaxDbiP61957.
PRIDEiP61957.

PTM databases

PhosphoSiteiP61957.

Expressioni

Gene expression databases

BgeeiP61957.
CleanExiMM_SUMO2.
ExpressionAtlasiP61957. baseline.
GenevestigatoriP61957.

Interactioni

Subunit structurei

Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25 (By similarity). Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with MTA1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi228466. 17 interactions.
STRINGi10090.ENSMUSP00000115044.

Structurei

3D structure databases

ProteinModelPortaliP61957.
SMRiP61957. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9580Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP61957.
KOiK12160.
OMAiDAYCKKQ.
OrthoDBiEOG76X62R.
PhylomeDBiP61957.
TreeFamiTF315116.

Family and domain databases

InterProiIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61957-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER
60 70 80 90
QGLSMRQIRF RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY
Length:95
Mass (Da):10,871
Last modified:June 7, 2004 - v1
Checksum:iF8F0426849BEF08B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L79948 mRNA. Translation: AAL40136.1.
AK012619 mRNA. Translation: BAB28360.1.
AK085238 mRNA. Translation: BAC39397.1.
AK132213 mRNA. Translation: BAE21037.1.
AK160404 mRNA. Translation: BAE35772.1.
AK167308 mRNA. Translation: BAE39412.1.
AL645470 Genomic DNA. Translation: CAM23014.1.
BC017522 mRNA. Translation: AAH17522.1.
BC083326 mRNA. Translation: AAH83326.1.
BC095930 mRNA. Translation: AAH95930.1.
CCDSiCCDS36374.1.
RefSeqiNP_579932.1. NM_133354.2.
UniGeneiMm.29923.

Genome annotation databases

EnsembliENSMUST00000153892; ENSMUSP00000115044; ENSMUSG00000020738.
GeneIDi170930.
KEGGimmu:170930.
UCSCiuc007mhw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L79948 mRNA. Translation: AAL40136.1.
AK012619 mRNA. Translation: BAB28360.1.
AK085238 mRNA. Translation: BAC39397.1.
AK132213 mRNA. Translation: BAE21037.1.
AK160404 mRNA. Translation: BAE35772.1.
AK167308 mRNA. Translation: BAE39412.1.
AL645470 Genomic DNA. Translation: CAM23014.1.
BC017522 mRNA. Translation: AAH17522.1.
BC083326 mRNA. Translation: AAH83326.1.
BC095930 mRNA. Translation: AAH95930.1.
CCDSiCCDS36374.1.
RefSeqiNP_579932.1. NM_133354.2.
UniGeneiMm.29923.

3D structure databases

ProteinModelPortaliP61957.
SMRiP61957. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228466. 17 interactions.
STRINGi10090.ENSMUSP00000115044.

PTM databases

PhosphoSiteiP61957.

Proteomic databases

MaxQBiP61957.
PaxDbiP61957.
PRIDEiP61957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000153892; ENSMUSP00000115044; ENSMUSG00000020738.
GeneIDi170930.
KEGGimmu:170930.
UCSCiuc007mhw.1. mouse.

Organism-specific databases

CTDi6613.
MGIiMGI:2158813. Sumo2.

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP61957.
KOiK12160.
OMAiDAYCKKQ.
OrthoDBiEOG76X62R.
PhylomeDBiP61957.
TreeFamiTF315116.

Enzyme and pathway databases

ReactomeiREACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_196649. SUMO is proteolytically processed.
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

NextBioi370513.
PROiP61957.
SOURCEiSearch...

Gene expression databases

BgeeiP61957.
CleanExiMM_SUMO2.
ExpressionAtlasiP61957. baseline.
GenevestigatoriP61957.

Family and domain databases

InterProiIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes."
    Chen A., Mannen H., Li S.S.-L.
    Biochem. Mol. Biol. Int. 46:1161-1174(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo, Placenta and Stomach.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain, Eye and Mammary tumor.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSUMO2_MOUSE
AccessioniPrimary (citable) accession number: P61957
Secondary accession number(s): A2A9X2, P55855, Q542L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: March 4, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.