6IIK

USP14 catalytic domain with IU1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0016579	biological_process	protein deubiquitination
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
B	0004843	molecular_function	cysteine-type deubiquitinase activity
B	0016579	biological_process	protein deubiquitination
B	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue IU1 A 501

Chain	Residue
A	GLN197
A	GLN198
A	ASP199
A	LYS342
A	HIS426
A	SER431
A	SER433
A	TYR436
A	TYR476

---

site_id	AC2
Number of Residues	9
Details	binding site for residue IU1 B 501

Chain	Residue
B	GLN197
B	GLN198
B	ASP199
B	LYS342
B	HIS426
B	SER431
B	SER433
B	TYR436
B	TYR476

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Functional Information from PROSITE/UniProt

site_id	PS00972
Number of Residues	16
Details	USP_1 Ubiquitin specific protease (USP) domain signature 1. GLtnlGNtCYMNAtVQ

Chain	Residue	Details
A	GLY106-GLN121

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site_id	PS00973
Number of Residues	19
Details	USP_2 Ubiquitin specific protease (USP) domain signature 2. YdLqAVltHqGrssss.GHY

Chain	Residue	Details
A	TYR418-TYR436

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:16211010

Chain	Residue	Details
A	CYS114
B	CYS114

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093

Chain	Residue	Details
A	HIS435
B	HIS435

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	SER143
A	SER143

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9JMA1

Chain	Residue	Details
A	SER148
B	SER148

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR235
B	THR235

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER237
A	SER302
A	SER432
B	SER237
B	SER302
B	SER432

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS449
B	LYS449

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