UBP30_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBP30_HUMAN
• UniProt AC: Q70CQ3
• Protein Name: Ubiquitin carboxyl-terminal hydrolase 30
• Gene Name: USP30 {ECO:0000312|HGNC:HGNC:20065}
• Organism: Homo sapiens (Human).
• Sequence Length: 517
• Subcellular Localization: Mitochondrion outer membrane .
• Protein Description: Deubiquitinating enzyme tethered to the mitochondrial outer membrane that acts as a key inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes ubiquitin attached by parkin on target proteins, such as RHOT1/MIRO1 and TOMM20, thereby blocking parkin's ability to drive mitophagy. [PubMed: 18287522]
• Protein Sequence: MLSSRAEAAMTAADRAIQRFLRTGAAVRYKVMKNWGVIGGIAAALAAGIYVIWGPITERKKRRKGLVPGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDRQPRVTHLFDVHSLEQQSEITPKQITCRTRGSPHPTSNHWKSQHPFHGRLTSNMVCKHCEHQSPVRFDTFDSLSLSIPAATWGHPLTLDHCLHHFISSESVRDVVCDNCTKIEAKGTLNGEKVEHQRTTFVKQLKLGKLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEFLMMDIYKYHLLGHKPSQHNPKLNKNPGPTLELQDGPGAPTPVLNQPGAPKTQIFMNGACSPSLLPTLSAPMPFPLPVVPDYSSSTYLFRLMAVVVHHGDMHSGHFVTYRRSPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYERVLSRMQHQSQECKSEE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MLSSRAEAAMTA ---CCCHHHHHHHHH	32.83	115919617
15	Methylation	AAMTAADRAIQRFLR HHHHHHHHHHHHHHH	28.94	115919609
19	Methylation	AADRAIQRFLRTGAA HHHHHHHHHHHHCCH	26.84	115919613
76	Phosphorylation	GLVNLGNTCFMNSLL CHHHCCCCHHHHHHH	12.81	28258704
81	Phosphorylation	GNTCFMNSLLQGLSA CCCHHHHHHHHHHHH	20.76	28258704
191	Phosphorylation	THLFDVHSLEQQSEI EEEEECCCHHHCCCC	33.19	26471730
196	Phosphorylation	VHSLEQQSEITPKQI CCCHHHCCCCCCCEE	30.57	28555341
199	Phosphorylation	LEQQSEITPKQITCR HHHCCCCCCCEEEEE	22.00	21712546
201	Ubiquitination	QQSEITPKQITCRTR HCCCCCCCEEEEECC	45.76	-
207	Phosphorylation	PKQITCRTRGSPHPT CCEEEEECCCCCCCC	41.34	29449344
210	Phosphorylation	ITCRTRGSPHPTSNH EEEECCCCCCCCCCC	19.42	27251275
214	Phosphorylation	TRGSPHPTSNHWKSQ CCCCCCCCCCCCCCC	38.84	29449344
215	Phosphorylation	RGSPHPTSNHWKSQH CCCCCCCCCCCCCCC	31.02	29449344
235	Ubiquitination	LTSNMVCKHCEHQSP CCCCCHHCCCCCCCC	39.62	24896179
289	Ubiquitination	VVCDNCTKIEAKGTL HCCCCCCEEEEECCC	40.52	24896179
300	Ubiquitination	KGTLNGEKVEHQRTT ECCCCCCCCEEEEEH	55.08	-
310	Ubiquitination	HQRTTFVKQLKLGKL EEEEHHHHHHHCCCC	45.80	-
335	Phosphorylation	LSWSSHGTPLKRHEH CCCCCCCCCCCCCCC	21.74	-
338	Ubiquitination	SSHGTPLKRHEHVQF CCCCCCCCCCCCCCC	53.57	-
362	Ubiquitination	KYHLLGHKPSQHNPK HHHHHCCCCCCCCCC	44.56	-
364	Phosphorylation	HLLGHKPSQHNPKLN HHHCCCCCCCCCCCC	49.20	24275569
372	Ubiquitination	QHNPKLNKNPGPTLE CCCCCCCCCCCCCEE	74.98	-
388	Phosphorylation	QDGPGAPTPVLNQPG CCCCCCCCCCCCCCC	26.04	28555341
515	Phosphorylation	HQSQECKSEE----- HHHHHHHCCC-----	59.63	26471730

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
235	K	ubiquitylation	Ubiquitinated by parkin (PRKN) at Lys-235 and Lys-289, leading to its degradation.	24896179
289	K	ubiquitylation	Ubiquitinated by parkin (PRKN) at Lys-235 and Lys-289, leading to its degradation.	24896179

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of UBP30_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIM8A_HUMAN	TIMM8A	physical	19615732
QKI_HUMAN	QKI	physical	19615732
SF3A1_HUMAN	SF3A1	physical	19615732
CREST_HUMAN	SS18L1	physical	19615732
CLPB_HUMAN	CLPB	physical	19615732
MPND_HUMAN	MPND	physical	19615732
UBC_HUMAN	UBC	physical	25527291

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.