4R62

Structure of Rad6~Ub

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000209	biological_process	protein polyubiquitination
A	0000722	biological_process	telomere maintenance via recombination
A	0000724	biological_process	double-strand break repair via homologous recombination
A	0000781	cellular_component	chromosome, telomeric region
A	0000785	cellular_component	chromatin
A	0003697	molecular_function	single-stranded DNA binding
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	0006281	biological_process	DNA repair
A	0006325	biological_process	chromatin organization
A	0006351	biological_process	DNA-templated transcription
A	0006353	biological_process	DNA-templated transcription termination
A	0006366	biological_process	transcription by RNA polymerase II
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006974	biological_process	DNA damage response
A	0009302	biological_process	sno(s)RNA transcription
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0017116	molecular_function	single-stranded DNA helicase activity
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
A	0031509	biological_process	subtelomeric heterochromatin formation
A	0031571	biological_process	mitotic G1 DNA damage checkpoint signaling
A	0033503	cellular_component	HULC complex
A	0034620	biological_process	cellular response to unfolded protein
A	0036503	biological_process	ERAD pathway
A	0042138	biological_process	meiotic DNA double-strand break formation
A	0042275	biological_process	error-free postreplication DNA repair
A	0042276	biological_process	error-prone translesion synthesis
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0061631	molecular_function	ubiquitin conjugating enzyme activity
A	0070628	molecular_function	proteasome binding
A	0070987	biological_process	error-free translesion synthesis
A	0071596	biological_process	ubiquitin-dependent protein catabolic process via the N-end rule pathway
A	0071629	biological_process	cytoplasm protein quality control by the ubiquitin-proteasome system
A	0090089	biological_process	regulation of dipeptide transport
A	0097505	cellular_component	Rad6-Rad18 complex
A	0120174	biological_process	stress-induced homeostatically regulated protein degradation pathway
A	1990303	cellular_component	UBR1-RAD6 ubiquitin ligase complex
A	1990304	cellular_component	MUB1-RAD6-UBR2 ubiquitin ligase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 201

Chain	Residue
A	HIS69
A	VAL70
A	ILE87

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LYS27-ASP52

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	146
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34789879","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by SGV1","evidences":[{"source":"PubMed","id":"16307922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Interacts with activating enzyme"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Essential for function"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylglycine","evidences":[{"source":"PubMed","id":"28525742","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 939

Chain	Residue	Details
A	LYS88	nucleophile

---