9GKM

Structure of HECT E3 TRIP12 forming K29/K48-branched Ubiquitin chains

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0061630	molecular_function	ubiquitin protein ligase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	LYS27-ASP52
C	LYS27-ASP52
B	LYS27-ASP52

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	107
Details	Domain: {"description":"HECT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	74
Details	Region: {"description":"K-box"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"G5E870","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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