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Protein

Small ubiquitin-related modifier 2

Gene

SUMO2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as 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 an E3 ligase 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. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-SSC-3065679. SUMO is proteolytically processed.
R-SSC-3108214. SUMOylation of DNA damage response and repair proteins.
R-SSC-3232118. SUMOylation of transcription factors.
R-SSC-4551638. SUMOylation of chromatin organization proteins.
R-SSC-4570464. SUMOylation of RNA binding proteins.
R-SSC-4615885. SUMOylation of DNA replication proteins.
R-SSC-5693607. Processing of DNA double-strand break ends.
R-SSC-5696395. Formation of Incision Complex in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 2
Short name:
SUMO-2
Alternative name(s):
MIF2 suppressor
SMT3 homolog 2
Sentrin-2
Ubiquitin-like protein SMT3A
Short name:
Smt3A
Gene namesi
Name:SUMO2
Synonyms:SMT3A, SMT3H2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 12

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Small ubiquitin-related modifier 2PRO_0000035953Add
BLAST
Propeptidei94 – 952By similarityPRO_0000035954

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei11 – 111N6-acetyllysine; alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki93 – 93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Post-translational modificationi

Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity).By similarity
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP61958.
PeptideAtlasiP61958.
PRIDEiP61958.

Expressioni

Gene expression databases

BgeeiENSSSCG00000017212.
GenevisibleiP61958. SS.

Interactioni

Subunit structurei

Interacts with SAE2 and UBE2I. Interacts with ZNF451. Identified in a complex with ZNF451 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with MTA1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000018235.

Structurei

3D structure databases

ProteinModelPortaliP61958.
SMRiP61958. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9580Ubiquitin-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.
HOVERGENiHBG053025.
InParanoidiP61958.
KOiK12160.
OMAiLMQAYCD.
OrthoDBiEOG091G10ZQ.
TreeFamiTF315116.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR027218. SUMO_chordates.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
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.

P61958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER
60 70 80 90
QGLSMRQIRF RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY
Length:95
Mass (Da):10,871
Last modified:June 7, 2004 - v1
Checksum:iF8F0426849BEF08B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77617 mRNA. Translation: AAL40163.1.
AM397626 mRNA. Translation: CAL37097.1.
RefSeqiNP_999149.1. NM_213984.1.
UniGeneiSsc.5454.

Genome annotation databases

EnsembliENSSSCT00000018737; ENSSSCP00000018235; ENSSSCG00000017212.
GeneIDi397044.
KEGGissc:397044.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77617 mRNA. Translation: AAL40163.1.
AM397626 mRNA. Translation: CAL37097.1.
RefSeqiNP_999149.1. NM_213984.1.
UniGeneiSsc.5454.

3D structure databases

ProteinModelPortaliP61958.
SMRiP61958. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000018235.

Proteomic databases

PaxDbiP61958.
PeptideAtlasiP61958.
PRIDEiP61958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000018737; ENSSSCP00000018235; ENSSSCG00000017212.
GeneIDi397044.
KEGGissc:397044.

Organism-specific databases

CTDi6613.

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOVERGENiHBG053025.
InParanoidiP61958.
KOiK12160.
OMAiLMQAYCD.
OrthoDBiEOG091G10ZQ.
TreeFamiTF315116.

Enzyme and pathway databases

ReactomeiR-SSC-3065679. SUMO is proteolytically processed.
R-SSC-3108214. SUMOylation of DNA damage response and repair proteins.
R-SSC-3232118. SUMOylation of transcription factors.
R-SSC-4551638. SUMOylation of chromatin organization proteins.
R-SSC-4570464. SUMOylation of RNA binding proteins.
R-SSC-4615885. SUMOylation of DNA replication proteins.
R-SSC-5693607. Processing of DNA double-strand break ends.
R-SSC-5696395. Formation of Incision Complex in GG-NER.

Gene expression databases

BgeeiENSSSCG00000017212.
GenevisibleiP61958. SS.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR027218. SUMO_chordates.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
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 nameiSUMO2_PIG
AccessioniPrimary (citable) accession number: P61958
Secondary accession number(s): A7WLH9, P55855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 7, 2016
This is version 92 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.