UniProt functional annotation for P63279



	UniProt functional annotation for P63279

UniProt code: P63279.

Organism: Homo sapiens (Human).

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

Function: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (PubMed:26620705). {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:26524494, ECO:0000269|PubMed:26620705, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:8668529}.

Pathway: Protein modification; protein sumoylation. {ECO:0000269|PubMed:26524494}.

Subunit: Forms a complex with SENP6 and UBE2I in response to UV irradiation (PubMed:17704809). Forms a tight complex with RANGAP1 and RANBP2 (PubMed:15378033, PubMed:15608651, PubMed:11853669, PubMed:15931224, PubMed:16732283). Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of the same UBE2I molecule (PubMed:12924945, PubMed:26524494). Interacts with SETX (PubMed:24105744). Interacts with HIPK1 and HIPK2 (By similarity). Interacts with PPM1J (By similarity). Interacts with RASD2 (By similarity). Interacts with TCF3 (By similarity). Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Interacts with SIAH1 (PubMed:9334332). Interacts with PARP (PubMed:9197546). Interacts with various transcription factors such as TFAP2A, TFAP2B, and TFAP2C (PubMed:12072434). Interacts with AR (PubMed:10383460). Interacts with ETS1 (PubMed:9333025). Interacts with SOX4 (PubMed:16631117). Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B (PubMed:17956732, PubMed:23469069). Interacts with FOXL2 (PubMed:19744555). Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain (PubMed:19638400). Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains (PubMed:20077568). Interacts with FHIT (PubMed:11085938). Interacts with PRKRA and p53/TP53 (By similarity). Interacts with UHRF2 (PubMed:23404503). Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3 (PubMed:23508108, PubMed:25918163). Interacts with MTA1 (PubMed:21965678). Interacts with ZNF451 (PubMed:26524494). Interacts with CPEB3 (By similarity). Interacts with SUMO1, SUMO2 and SUMO3 (PubMed:17466333). Interacts with IPO13 (PubMed:21139563). Interacts with DNMT1 (PubMed:19450230). Interacts with SUMO1P1/SUMO5 (PubMed:27211601). Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML-RARA oncoprotein (PubMed:15809060). Interacts with ZBED1/hDREF (PubMed:27068747). {ECO:0000250|UniProtKB:P63280, ECO:0000250|UniProtKB:P63281, ECO:0000269|PubMed:10383460, ECO:0000269|PubMed:11085938, ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:12072434, ECO:0000269|PubMed:12924945, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15608651, ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:16631117, ECO:0000269|PubMed:16732283, ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:17704809, ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:19450230, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:21139563, ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:23404503, ECO:0000269|PubMed:23469069, ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:25918163, ECO:0000269|PubMed:26524494, ECO:0000269|PubMed:27068747, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9197546, ECO:0000269|PubMed:9333025, ECO:0000269|PubMed:9334332, ECO:0000305}.

Subunit: (Microbial infection) Interacts with human herpesvirus 6 IE2. {ECO:0000269|PubMed:17005699}.

Subunit: (Microbial infection) Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation. {ECO:0000269|PubMed:20543865, ECO:0000269|PubMed:8824223}.

Subunit: (Microbial infection) Interacts with Epstein-barr virus protein LMP1. {ECO:0000269|PubMed:21795333}.

Subunit: (Microbial infection) Interacts with ebolavirus VP35; this interaction mediates the sumoylation of IRF7 and contributes to the viral inhibition of IFN-type I production. {ECO:0000269|PubMed:19557165}.

Subcellular location: Nucleus {ECO:0000269|PubMed:16631117, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:27068747}. Cytoplasm {ECO:0000269|PubMed:22214662}. Note=Mainly nuclear (By similarity). In spermatocytes, localizes in synaptonemal complexes (PubMed:8610150). Recruited by BCL11A into the nuclear body (By similarity). {ECO:0000250|UniProtKB:P63280, ECO:0000269|PubMed:8610150}.

Tissue specificity: Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. {ECO:0000269|PubMed:8610150}.

Ptm: Phosphorylation at Ser-71 significantly enhances SUMOylation activity. {ECO:0000269|PubMed:22509284}.

Similarity: Belongs to the ubiquitin-conjugating enzyme family. {ECO:0000255|PROSITE-ProRule:PRU00388}.

Sequence caution: Sequence=AAH51289.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAD92225.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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:		Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (PubMed:26620705). {ECO:0000269\|PubMed:11451954, ECO:0000269\|PubMed:15809060, ECO:0000269\|PubMed:17466333, ECO:0000269\|PubMed:19638400, ECO:0000269\|PubMed:19744555, ECO:0000269\|PubMed:20077568, ECO:0000269\|PubMed:26524494, ECO:0000269\|PubMed:26620705, ECO:0000269\|PubMed:27211601, ECO:0000269\|PubMed:8668529}.


Pathway:		Protein modification; protein sumoylation. {ECO:0000269\|PubMed:26524494}.
Subunit:		Forms a complex with SENP6 and UBE2I in response to UV irradiation (PubMed:17704809). Forms a tight complex with RANGAP1 and RANBP2 (PubMed:15378033, PubMed:15608651, PubMed:11853669, PubMed:15931224, PubMed:16732283). Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of the same UBE2I molecule (PubMed:12924945, PubMed:26524494). Interacts with SETX (PubMed:24105744). Interacts with HIPK1 and HIPK2 (By similarity). Interacts with PPM1J (By similarity). Interacts with RASD2 (By similarity). Interacts with TCF3 (By similarity). Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Interacts with SIAH1 (PubMed:9334332). Interacts with PARP (PubMed:9197546). Interacts with various transcription factors such as TFAP2A, TFAP2B, and TFAP2C (PubMed:12072434). Interacts with AR (PubMed:10383460). Interacts with ETS1 (PubMed:9333025). Interacts with SOX4 (PubMed:16631117). Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B (PubMed:17956732, PubMed:23469069). Interacts with FOXL2 (PubMed:19744555). Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain (PubMed:19638400). Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains (PubMed:20077568). Interacts with FHIT (PubMed:11085938). Interacts with PRKRA and p53/TP53 (By similarity). Interacts with UHRF2 (PubMed:23404503). Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3 (PubMed:23508108, PubMed:25918163). Interacts with MTA1 (PubMed:21965678). Interacts with ZNF451 (PubMed:26524494). Interacts with CPEB3 (By similarity). Interacts with SUMO1, SUMO2 and SUMO3 (PubMed:17466333). Interacts with IPO13 (PubMed:21139563). Interacts with DNMT1 (PubMed:19450230). Interacts with SUMO1P1/SUMO5 (PubMed:27211601). Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML-RARA oncoprotein (PubMed:15809060). Interacts with ZBED1/hDREF (PubMed:27068747). {ECO:0000250\|UniProtKB:P63280, ECO:0000250\|UniProtKB:P63281, ECO:0000269\|PubMed:10383460, ECO:0000269\|PubMed:11085938, ECO:0000269\|PubMed:11853669, ECO:0000269\|PubMed:12072434, ECO:0000269\|PubMed:12924945, ECO:0000269\|PubMed:15378033, ECO:0000269\|PubMed:15608651, ECO:0000269\|PubMed:15809060, ECO:0000269\|PubMed:15931224, ECO:0000269\|PubMed:16631117, ECO:0000269\|PubMed:16732283, ECO:0000269\|PubMed:17466333, ECO:0000269\|PubMed:17704809, ECO:0000269\|PubMed:17956732, ECO:0000269\|PubMed:19450230, ECO:0000269\|PubMed:19638400, ECO:0000269\|PubMed:19744555, ECO:0000269\|PubMed:20077568, ECO:0000269\|PubMed:21139563, ECO:0000269\|PubMed:21965678, ECO:0000269\|PubMed:23404503, ECO:0000269\|PubMed:23469069, ECO:0000269\|PubMed:23508108, ECO:0000269\|PubMed:24105744, ECO:0000269\|PubMed:25918163, ECO:0000269\|PubMed:26524494, ECO:0000269\|PubMed:27068747, ECO:0000269\|PubMed:27211601, ECO:0000269\|PubMed:9197546, ECO:0000269\|PubMed:9333025, ECO:0000269\|PubMed:9334332, ECO:0000305}.
Subunit:		(Microbial infection) Interacts with human herpesvirus 6 IE2. {ECO:0000269\|PubMed:17005699}.
Subunit:		(Microbial infection) Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation. {ECO:0000269\|PubMed:20543865, ECO:0000269\|PubMed:8824223}.
Subunit:		(Microbial infection) Interacts with Epstein-barr virus protein LMP1. {ECO:0000269\|PubMed:21795333}.
Subunit:		(Microbial infection) Interacts with ebolavirus VP35; this interaction mediates the sumoylation of IRF7 and contributes to the viral inhibition of IFN-type I production. {ECO:0000269\|PubMed:19557165}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:16631117, ECO:0000269\|PubMed:19744555, ECO:0000269\|PubMed:22214662, ECO:0000269\|PubMed:27068747}. Cytoplasm {ECO:0000269\|PubMed:22214662}. Note=Mainly nuclear (By similarity). In spermatocytes, localizes in synaptonemal complexes (PubMed:8610150). Recruited by BCL11A into the nuclear body (By similarity). {ECO:0000250\|UniProtKB:P63280, ECO:0000269\|PubMed:8610150}.
Tissue specificity:		Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus. {ECO:0000269\|PubMed:8610150}.
Ptm:		Phosphorylation at Ser-71 significantly enhances SUMOylation activity. {ECO:0000269\|PubMed:22509284}.
Similarity:		Belongs to the ubiquitin-conjugating enzyme family. {ECO:0000255\|PROSITE-ProRule:PRU00388}.
Sequence caution:		Sequence=AAH51289.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAD92225.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};