Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Small ubiquitin-related modifier 1

Gene

Sumo1

Organism
Rattus norvegicus (Rat)
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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processUbl conjugation pathway

Enzyme and pathway databases

ReactomeiR-RNO-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-RNO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-RNO-3065679. SUMO is proteolytically processed.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3232118. SUMOylation of transcription factors.
R-RNO-4551638. SUMOylation of chromatin organization proteins.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-RNO-5693571. Nonhomologous End-Joining (NHEJ).
R-RNO-5693607. Processing of DNA double-strand break ends.
R-RNO-69473. G2/M DNA damage checkpoint.
R-RNO-877312. Regulation of IFNG signaling.
R-RNO-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
Gene namesi
Name:Sumo1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1306919. Sumo1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002676102 – 97Small ubiquitin-related modifier 1Add BLAST96
PropeptideiPRO_000026761198 – 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-linki23Glycyl 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-linki39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

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

PaxDbiQ5I0H3.
PRIDEiQ5I0H3.

PTM databases

iPTMnetiQ5I0H3.
PhosphoSitePlusiQ5I0H3.

Expressioni

Gene expression databases

BgeeiENSRNOG00000016133.
GenevisibleiQ5I0H3. RN.

Interactioni

Subunit structurei

Interacts with PRKN (PubMed:16955485). Interacts with SAE2, UBE2I, RANBP2, PIAS1 and PIAS2. Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN and DNMT3B. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, PIAS1, EXOSC9, TDG, RAD51 and RAD52. Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25. 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. Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei36Interaction with PIAS2By similarity1

GO - Molecular functioni

Protein-protein interaction databases

BioGridi256960. 12 interactors.
DIPiDIP-46501N.
IntActiQ5I0H3. 4 interactors.
MINTiMINT-4651872.
STRINGi10116.ENSRNOP00000022048.

Structurei

3D structure databases

ProteinModelPortaliQ5I0H3.
SMRiQ5I0H3.
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

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiQ5I0H3.
KOiK12160.
OMAiTDNHTPK.
OrthoDBiEOG091G10ZQ.
PhylomeDBiQ5I0H3.
TreeFamiTF315116.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiView protein in InterPro
IPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
PfamiView protein in Pfam
PF11976. Rad60-SLD. 1 hit.
SMARTiView protein in SMART
SM00213. UBQ. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiView protein in PROSITE
PS50053. UBIQUITIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5I0H3-1 [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:February 15, 2005 - v1
Checksum:i89BE97D2D054FB33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088322 mRNA. Translation: AAH88322.1.
RefSeqiNP_001009672.1. NM_001009672.1.
UniGeneiRn.1221.

Genome annotation databases

EnsembliENSRNOT00000022047; ENSRNOP00000022048; ENSRNOG00000016133.
GeneIDi301442.
KEGGirno:301442.
UCSCiRGD:1306919. rat.

Similar proteinsi

Entry informationi

Entry nameiSUMO1_RAT
AccessioniPrimary (citable) accession number: Q5I0H3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 15, 2005
Last modified: September 27, 2017
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families