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Protein

Small ubiquitin-related modifier 1

Gene

SUMO1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 1
Short name:
SUMO-1
Gene namesi
Name:SUMO1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

  • Nucleus membrane By similarity
  • Nucleus speckle By similarity
  • Cytoplasm By similarity
  • 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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 9796Small ubiquitin-related modifier 1PRO_0000035935Add
BLAST
Propeptidei98 – 1014By similarityPRO_0000035936

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei9 – 91PhosphoserineBy similarity
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki17 – 17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki25 – 25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki37 – 37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki97 – 97Glycyl 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

PaxDbiQ5E9D1.
PRIDEiQ5E9D1.

Interactioni

Subunit structurei

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 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei36 – 361Interaction with PIAS2By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi542597. 1 interaction.
STRINGi9913.ENSBTAP00000013000.

Structurei

3D structure databases

ProteinModelPortaliQ5E9D1.
SMRiQ5E9D1. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 9778Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ5E9D1.
KOiK12160.
OMAiTDNHTPK.
OrthoDBiEOG76X62R.
TreeFamiTF315116.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
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.

Q5E9D1-1 [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:March 15, 2005 - v1
Checksum:i89BE97D2D054FB33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020989 mRNA. Translation: AAX09006.1.
BC102884 mRNA. Translation: AAI02885.1.
RefSeqiNP_001030535.1. NM_001035458.1.
UniGeneiBt.7441.

Genome annotation databases

EnsembliENSBTAT00000013000; ENSBTAP00000013000; ENSBTAG00000009859.
GeneIDi614967.
KEGGibta:614967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020989 mRNA. Translation: AAX09006.1.
BC102884 mRNA. Translation: AAI02885.1.
RefSeqiNP_001030535.1. NM_001035458.1.
UniGeneiBt.7441.

3D structure databases

ProteinModelPortaliQ5E9D1.
SMRiQ5E9D1. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi542597. 1 interaction.
STRINGi9913.ENSBTAP00000013000.

Proteomic databases

PaxDbiQ5E9D1.
PRIDEiQ5E9D1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000013000; ENSBTAP00000013000; ENSBTAG00000009859.
GeneIDi614967.
KEGGibta:614967.

Organism-specific databases

CTDi7341.

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiQ5E9D1.
KOiK12160.
OMAiTDNHTPK.
OrthoDBiEOG76X62R.
TreeFamiTF315116.

Enzyme and pathway databases

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

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiSUMO1_BOVIN
AccessioniPrimary (citable) accession number: Q5E9D1
Secondary accession number(s): Q3ZC68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 100 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. 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.