7MYH

Ubiquitin variant UbV.k.2 in complex with Ube2k

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000209	biological_process	protein polyubiquitination
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0010800	biological_process	positive regulation of peptidyl-threonine phosphorylation
A	0010994	biological_process	free ubiquitin chain polymerization
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032433	cellular_component	filopodium tip
A	0032434	biological_process	regulation of proteasomal ubiquitin-dependent protein catabolic process
A	0034450	molecular_function	ubiquitin-ubiquitin ligase activity
A	0035458	biological_process	cellular response to interferon-beta
A	0060337	biological_process	type I interferon-mediated signaling pathway
A	0060340	biological_process	positive regulation of type I interferon-mediated signaling pathway
A	0061631	molecular_function	ubiquitin conjugating enzyme activity
A	0070936	biological_process	protein K48-linked ubiquitination
A	1903265	biological_process	positive regulation of tumor necrosis factor-mediated signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL A 301

Chain	Residue
A	PHE68
A	ASN69
A	PRO70
A	LYS97
A	ASP98
A	TRP100
A	ARG107

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Functional Information from PROSITE/UniProt

site_id	PS00183
Number of Residues	17
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. WHPNIssvtGaICLdiL

Chain	Residue	Details
A	TRP80-LEU96

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site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
B	LYS27-ASP52

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	150
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	40
Details	Domain: {"description":"UBA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00212","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2010","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bilsland A.E.","Keith W.N."]}},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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