Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UDH

HHARI/ARIH1-UBCH7~Ubiquitin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0008270	molecular_function	zinc ion binding
A	0016567	biological_process	protein ubiquitination
A	0046872	molecular_function	metal ion binding
B	0004842	molecular_function	ubiquitin-protein transferase activity
B	0008270	molecular_function	zinc ion binding
B	0016567	biological_process	protein ubiquitination
B	0046872	molecular_function	metal ion binding
C	0000151	cellular_component	ubiquitin ligase complex
C	0000166	molecular_function	nucleotide binding
C	0000209	biological_process	protein polyubiquitination
C	0003713	molecular_function	transcription coactivator activity
C	0003723	molecular_function	RNA binding
C	0004842	molecular_function	ubiquitin-protein transferase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0008283	biological_process	cell population proliferation
C	0016567	biological_process	protein ubiquitination
C	0016740	molecular_function	transferase activity
C	0019787	molecular_function	ubiquitin-like protein transferase activity
C	0019899	molecular_function	enzyme binding
C	0031398	biological_process	positive regulation of protein ubiquitination
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032446	biological_process	protein modification by small protein conjugation
C	0036211	biological_process	protein modification process
C	0044770	biological_process	cell cycle phase transition
C	0045893	biological_process	positive regulation of DNA-templated transcription
C	0061631	molecular_function	ubiquitin conjugating enzyme activity
C	0070979	biological_process	protein K11-linked ubiquitination
C	0071383	biological_process	cellular response to steroid hormone stimulus
C	0071385	biological_process	cellular response to glucocorticoid stimulus
C	0097027	molecular_function	ubiquitin-protein transferase activator activity
C	1903955	biological_process	positive regulation of protein targeting to mitochondrion
D	0000151	cellular_component	ubiquitin ligase complex
D	0000166	molecular_function	nucleotide binding
D	0000209	biological_process	protein polyubiquitination
D	0003713	molecular_function	transcription coactivator activity
D	0003723	molecular_function	RNA binding
D	0004842	molecular_function	ubiquitin-protein transferase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006355	biological_process	regulation of DNA-templated transcription
D	0006511	biological_process	ubiquitin-dependent protein catabolic process
D	0008283	biological_process	cell population proliferation
D	0016567	biological_process	protein ubiquitination
D	0016740	molecular_function	transferase activity
D	0019787	molecular_function	ubiquitin-like protein transferase activity
D	0019899	molecular_function	enzyme binding
D	0031398	biological_process	positive regulation of protein ubiquitination
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0032446	biological_process	protein modification by small protein conjugation
D	0036211	biological_process	protein modification process
D	0044770	biological_process	cell cycle phase transition
D	0045893	biological_process	positive regulation of DNA-templated transcription
D	0061631	molecular_function	ubiquitin conjugating enzyme activity
D	0070979	biological_process	protein K11-linked ubiquitination
D	0071383	biological_process	cellular response to steroid hormone stimulus
D	0071385	biological_process	cellular response to glucocorticoid stimulus
D	0097027	molecular_function	ubiquitin-protein transferase activator activity
D	1903955	biological_process	positive regulation of protein targeting to mitochondrion

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 601

Chain	Residue
A	CYS344
A	CYS347
A	CYS362
A	CYS367

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 602

Chain	Residue
A	CYS372
A	CYS375
A	HIS382
A	CYS389

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 603

Chain	Residue
A	CYS281
A	CYS297
A	CYS299
A	CYS276

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN A 604

Chain	Residue
A	CYS304
A	CYS307
A	HIS312
A	CYS317

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN A 605

Chain	Residue
A	CYS186
A	CYS189
A	CYS208
A	CYS211

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN A 606

Chain	Residue
A	CYS203
A	HIS205
A	CYS231
A	ALA233
A	CYS236

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 601

Chain	Residue
B	CYS344
B	CYS347
B	CYS362
B	CYS367

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 602

Chain	Residue
B	CYS372
B	CYS375
B	HIS382
B	CYS389

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN B 603

Chain	Residue
B	CYS276
B	CYS281
B	CYS297
B	CYS299

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN B 604

Chain	Residue
B	CYS304
B	CYS307
B	HIS312
B	CYS317

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN B 605

Chain	Residue
B	CYS186
B	CYS189
B	CYS208
B	CYS211

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN B 606

Chain	Residue
B	CYS203
B	HIS205
B	CYS231
B	CYS236

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	LYS27-ASP52

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	100
Details	Zinc finger: {"description":"RING-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	122
Details	Zinc finger: {"description":"IBR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	62
Details	Zinc finger: {"description":"RING-type 2; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Region: {"description":"UBA-like","evidences":[{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21532592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15236971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24058416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WD2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2M9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24058416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2M9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z1K5","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	294
Details	Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
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

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 438

Chain	Residue	Details
B	MET175	nucleofuge

site_id	MCSA2
Number of Residues	1
Details	M-CSA 438

Chain	Residue	Details
D	LYS86	nucleofuge

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)