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Protein

Small ubiquitin-related modifier 1

Gene

Sumo1

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

Functioni

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or 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 E3 ligases 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. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to cadmium ion Source: UniProtKB
  • cellular response to heat Source: UniProtKB
  • negative regulation of action potential Source: UniProtKB
  • negative regulation of delayed rectifier potassium channel activity Source: UniProtKB
  • negative regulation of DNA binding Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • palate development Source: UniProtKB
  • PML body organization Source: MGI
  • positive regulation of calcium-transporting ATPase activity Source: BHF-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein complex assembly Source: MGI
  • protein localization to nuclear pore Source: MGI
  • protein stabilization Source: MGI
  • protein sumoylation Source: UniProtKB
  • regulation of calcium ion transmembrane transport Source: BHF-UCL
  • regulation of cardiac muscle cell contraction Source: BHF-UCL
  • regulation of protein stability Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Biological processi

Stress response, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-MMU-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-MMU-3065679. SUMO is proteolytically processed.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3232118. SUMOylation of transcription factors.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-877312. Regulation of IFNG signaling.
R-MMU-8866904. Negative regulation of activity of TFAP2 (AP-2) family transcription factors.

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 1
Short name:
SUMO-1
Alternative name(s):
SMT3 homolog 3
Ubiquitin-homology domain protein PIC1
Ubiquitin-like protein SMT3C
Short name:
Smt3C
Gene namesi
Name:Sumo1
Synonyms:Smt3c, Smt3h3, Ubl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1197010. Sumo1.

Subcellular locationi

  • Nucleus membrane
  • Nucleus speckle
  • Cytoplasm
  • NucleusPML body By similarity
  • Cell membrane By similarity
  • Nucleus By similarity

  • Note: Recruited by BCL11A into the nuclear body. In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity).By similarity1 Publication

GO - Cellular componenti

  • cytosol Source: Reactome
  • dendrite Source: Ensembl
  • fibrillar center Source: Ensembl
  • heterochromatin Source: Ensembl
  • nuclear body Source: UniProtKB
  • nuclear membrane Source: MGI
  • nuclear speck Source: UniProtKB-SubCell
  • nuclear stress granule Source: UniProtKB
  • nucleolus Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • plasma membrane Source: UniProtKB
  • PML body Source: UniProtKB
  • synapse Source: Ensembl
  • voltage-gated potassium channel complex Source: Ensembl
  • XY body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000359412 – 97Small ubiquitin-related modifier 1Add BLAST96
PropeptideiPRO_000003594298 – 101By similarity4

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineCombined sources1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei9PhosphoserineBy similarity1
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei32PhosphoserineBy similarity1
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Post-translational modificationi

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
Polymeric SUMO1 chains undergo polyubiquitination by RNF4.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP63166.
MaxQBiP63166.
PaxDbiP63166.
PeptideAtlasiP63166.
PRIDEiP63166.

PTM databases

iPTMnetiP63166.
PhosphoSitePlusiP63166.

Expressioni

Tissue specificityi

Ubiquitous.

Developmental stagei

Expressed at E13.5 strongly in the upper lip, primary palate and medial edge epithelia of the secondary palate. At E14.5 expression could be seen in the medial edge epithelial seam.1 Publication

Inductioni

By hypoxia.1 Publication

Gene expression databases

BgeeiENSMUSG00000026021.
CleanExiMM_SUMO1.
ExpressionAtlasiP63166. baseline and differential.
GenevisibleiP63166. MM.

Interactioni

Subunit structurei

Interacts with USP25 (via ts SIM domain) the interaction weakly sumoylates USP25. Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity). Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with BHLHE40/DEC1. Interacts with RWDD3. Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei36Interaction with PIAS2By similarity1

Binary interactionsi

WithEntry#Exp.IntActNotes
Ikzf1Q032672EBI-80152,EBI-908572
PTPN1P180312EBI-80152,EBI-968788From a different organism.
Srebf1Q9WTN32EBI-80152,EBI-5273743

GO - Molecular functioni

  • ion channel binding Source: MGI
  • transcription factor binding Source: AgBase
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi204420. 22 interactors.
DIPiDIP-29278N.
IntActiP63166. 9 interactors.
MINTiMINT-154756.
STRINGi10090.ENSMUSP00000088935.

Structurei

3D structure databases

ProteinModelPortaliP63166.
SMRiP63166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 97Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63166.
KOiK12160.
OMAiTDNHTPK.
OrthoDBiEOG091G10ZQ.
PhylomeDBiP63166.
TreeFamiTF315116.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiIPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
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.

P63166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES
60 70 80 90 100
YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST

V
Length:101
Mass (Da):11,557
Last modified:September 27, 2004 - v1
Checksum:i89BE97D2D054FB33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033353 mRNA. Translation: AAC39959.1.
AK002536 mRNA. Translation: BAB22172.1.
AK011074 mRNA. Translation: BAB27379.1.
AK089081 mRNA. Translation: BAC40739.1.
AK159366 mRNA. Translation: BAE35024.1.
BC082566 mRNA. Translation: AAH82566.1.
BC083158 mRNA. Translation: AAH83158.1.
CCDSiCCDS35586.1.
RefSeqiNP_033486.1. NM_009460.2.
UniGeneiMm.362118.

Genome annotation databases

EnsembliENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
GeneIDi22218.
KEGGimmu:22218.
UCSCiuc007bdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033353 mRNA. Translation: AAC39959.1.
AK002536 mRNA. Translation: BAB22172.1.
AK011074 mRNA. Translation: BAB27379.1.
AK089081 mRNA. Translation: BAC40739.1.
AK159366 mRNA. Translation: BAE35024.1.
BC082566 mRNA. Translation: AAH82566.1.
BC083158 mRNA. Translation: AAH83158.1.
CCDSiCCDS35586.1.
RefSeqiNP_033486.1. NM_009460.2.
UniGeneiMm.362118.

3D structure databases

ProteinModelPortaliP63166.
SMRiP63166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204420. 22 interactors.
DIPiDIP-29278N.
IntActiP63166. 9 interactors.
MINTiMINT-154756.
STRINGi10090.ENSMUSP00000088935.

PTM databases

iPTMnetiP63166.
PhosphoSitePlusiP63166.

Proteomic databases

EPDiP63166.
MaxQBiP63166.
PaxDbiP63166.
PeptideAtlasiP63166.
PRIDEiP63166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
GeneIDi22218.
KEGGimmu:22218.
UCSCiuc007bdx.1. mouse.

Organism-specific databases

CTDi7341.
MGIiMGI:1197010. Sumo1.

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP63166.
KOiK12160.
OMAiTDNHTPK.
OrthoDBiEOG091G10ZQ.
PhylomeDBiP63166.
TreeFamiTF315116.

Enzyme and pathway databases

ReactomeiR-MMU-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-MMU-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-MMU-3065679. SUMO is proteolytically processed.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3232118. SUMOylation of transcription factors.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-877312. Regulation of IFNG signaling.
R-MMU-8866904. Negative regulation of activity of TFAP2 (AP-2) family transcription factors.

Miscellaneous databases

PROiP63166.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026021.
CleanExiMM_SUMO1.
ExpressionAtlasiP63166. baseline and differential.
GenevisibleiP63166. MM.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiIPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
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...

Entry informationi

Entry nameiSUMO1_MOUSE
AccessioniPrimary (citable) accession number: P63166
Secondary accession number(s): P55856, Q3TX92, Q93068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: November 30, 2016
This is version 130 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

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 one 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.