UniProt functional annotation for P61956



	UniProt functional annotation for P61956

UniProt code: P61956.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: 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, CBX4 or ZNF451 (PubMed:26524494). 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 (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:26524494, ECO:0000269|PubMed:9556629}.

Subunit: 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. Interacts with Epstein-barr virus BGLF4. {ECO:0000269|PubMed:12924945, ECO:0000269|PubMed:15479240, ECO:0000269|PubMed:16567619, ECO:0000269|PubMed:18538659, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:22398289, ECO:0000269|PubMed:23086935, ECO:0000269|PubMed:26524494, ECO:0000305}.

Subcellular location: Nucleus. Nucleus, PML body.

Tissue specificity: Broadly expressed. {ECO:0000269|PubMed:9556629}.

Ptm: 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. {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:23560854}.

Ptm: Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000269|PubMed:15487983}.

Ptm: Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4- dependent polyubiquitination by the UBE2V1-UBE2N heterodimer. {ECO:0000269|PubMed:18408734, ECO:0000269|PubMed:23560854}.

Similarity: Belongs to the ubiquitin family. SUMO subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		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, CBX4 or ZNF451 (PubMed:26524494). 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 (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744). {ECO:0000269\|PubMed:18408734, ECO:0000269\|PubMed:18538659, ECO:0000269\|PubMed:21965678, ECO:0000269\|PubMed:24105744, ECO:0000269\|PubMed:26524494, ECO:0000269\|PubMed:9556629}.


Subunit:		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. Interacts with Epstein-barr virus BGLF4. {ECO:0000269\|PubMed:12924945, ECO:0000269\|PubMed:15479240, ECO:0000269\|PubMed:16567619, ECO:0000269\|PubMed:18538659, ECO:0000269\|PubMed:21965678, ECO:0000269\|PubMed:22398289, ECO:0000269\|PubMed:23086935, ECO:0000269\|PubMed:26524494, ECO:0000305}.
Subcellular location:		Nucleus. Nucleus, PML body.
Tissue specificity:		Broadly expressed. {ECO:0000269\|PubMed:9556629}.
Ptm:		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. {ECO:0000269\|PubMed:18408734, ECO:0000269\|PubMed:23560854}.
Ptm:		Cleavage of precursor form by SENP1 or SENP2 is necessary for function. {ECO:0000269\|PubMed:15487983}.
Ptm:		Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4- dependent polyubiquitination by the UBE2V1-UBE2N heterodimer. {ECO:0000269\|PubMed:18408734, ECO:0000269\|PubMed:23560854}.
Similarity:		Belongs to the ubiquitin family. SUMO subfamily. {ECO:0000305}.