Q2EF74 · SUMO1_ICTTR

Function

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. 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 (By similarity).
May be involved in modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3

Miscellaneous

Massive conjugation to proteins occurs in brain, kidney and liver during hibernation torpor.

Features

Showing features for site.

1101102030405060708090100
TypeIDPosition(s)Description
Site36Interaction with PIAS2

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnuclear membrane
Cellular Componentnuclear speck
Cellular Componentnuclear stress granule
Cellular Componentplasma membrane
Cellular ComponentPML body
Molecular Functionpotassium channel regulator activity
Molecular Functionprotein tag activity
Molecular Functiontranscription factor binding
Molecular Functionubiquitin protein ligase binding
Biological Processcellular response to cadmium ion
Biological Processcellular response to heat
Biological Processnegative regulation of action potential
Biological Processnegative regulation of delayed rectifier potassium channel activity
Biological Processprotein sumoylation
Biological Processroof of mouth development

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Small ubiquitin-related modifier 1
  • Short names
    SUMO-1

Gene names

    • Name
      SUMO1

Organism names

Accessions

  • Primary accession
    Q2EF74

Proteomes

Subcellular Location

Nucleus membrane
Nucleus speckle
Cytoplasm
Nucleus, PML body
Cell membrane
Nucleus
Nucleus
Note: Recruited by BCL11A into the nuclear body (By similarity).
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).

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link, propeptide.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
Modified residue2Phosphoserine
ChainPRO_00002505172-97
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue9Phosphoserine
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residue32Phosphoserine
Cross-link37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link97Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
PropeptidePRO_000025051898-101

Post-translational modification

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

Keywords

Interaction

Subunit

Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity).
Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (By similarity).
Interacts with PRKN (By similarity).
Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG (By similarity).
Also interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (By similarity).
Interacts with USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 (By similarity).
Interacts with SIMC1, CASP8AP2, RNF111 and SOBP (via SIM domains) (By similarity).
Interacts with BHLHE40/DEC1 (By similarity).
Interacts with RWDD3 (By similarity).
Interacts with UBE2I/UBC9 and this interaction is enhanced in the presence of RWDD3 (By similarity).
Interacts with MTA1 (By similarity).
Interacts with SENP2 (By similarity).
Interacts with HINT1 (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain20-97Ubiquitin-like

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    101
  • Mass (Da)
    11,570
  • Last updated
    2006-03-21 v1
  • Checksum
    89AB77D2D054FB33
MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSNV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ385870
EMBL· GenBank· DDBJ
ABD39322.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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