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Q5I0H3 (SUMO1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Small ubiquitin-related modifier 1

Short name=SUMO-1
Gene names
Name:Sumo1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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 By similarity.

Subunit structure

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 By similarity. Interacts with PARK2. Ref.2

Subcellular location

Nucleus membrane By similarity. Nucleus speckle By similarity. Cytoplasm By similarity. Note: Recruited by BCL11A into the nuclear body By similarity.

Post-translational modification

Cleavage of precursor form by SENP1 or SENP2 is necessary for function By similarity.

Polymeric SUMO1 chains undergo polyubiquitination by RNF4 By similarity.

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9796Small ubiquitin-related modifier 1
PRO_0000267610
Propeptide98 – 1014 By similarity
PRO_0000267611

Regions

Domain20 – 9778Ubiquitin-like

Sites

Site361Interaction with PIAS2 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine By similarity
Modified residue91Phosphoserine By similarity
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Cross-link97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5I0H3 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 89BE97D2D054FB33

FASTA10111,557
        10         20         30         40         50         60 
MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN 

        70         80         90        100 
SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V 

« Hide

References

« Hide 'large scale' references
[1]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[2]"Functional modulation of parkin through physical interaction with SUMO-1."
Um J.W., Chung K.C.
J. Neurosci. Res. 84:1543-1554(2006) [PubMed: 16955485] [Abstract]
Cited for: INTERACTION WITH PARK2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC088322 mRNA. Translation: AAH88322.1.
IPIIPI00358028.
RefSeqNP_001009672.1. NM_001009672.1.
UniGeneRn.1221.

3D structure databases

HSSPHSSP built from PDB template 1A5R based on UniProtKB P63165.
ProteinModelPortalQ5I0H3.
SMRQ5I0H3. Positions 1-101.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46501N.
MINTMINT-4651872.
STRINGQ5I0H3.

Proteomic databases

PRIDEQ5I0H3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022047; ENSRNOP00000022048; ENSRNOG00000016133.
GeneID301442.
KEGGrno:301442.
UCSCNM_001009672. rat.

Organism-specific databases

CTD7341.
RGD1306919. Sumo1.

Phylogenomic databases

eggNOGmaNOG20287.
GeneTreeENSGT00390000018808.
HOVERGENHBG053025.
InParanoidQ5I0H3.
OrthoDBEOG42JNSX.
PhylomeDBQ5I0H3.

Gene expression databases

ArrayExpressQ5I0H3.
GenevestigatorQ5I0H3.
GermOnlineENSRNOG00000016133. Rattus norvegicus.

Family and domain databases

InterProIPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]
KOK12160.
PfamPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio648746.

Entry information

Entry nameSUMO1_RAT
AccessionPrimary (citable) accession number: Q5I0H3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 15, 2005
Last modified: November 16, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families