dbPTM

UCHL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UCHL3_HUMAN
UniProt AC	P15374
Protein Name	Ubiquitin carboxyl-terminal hydrolase isozyme L3
Gene Name	UCHL3
Organism	Homo sapiens (Human).
Sequence Length	230
Subcellular Localization	Cytoplasm.
Protein Description	Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders..
Protein Sequence	MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Phosphorylation	GMDPELLSMVPRPVC CCCHHHHCCCCCCCH	30.29	-
61	Ubiquitination	LLFPITEKYEVFRTE HHEECCCCEEECCCH	37.75	-
75	Phosphorylation	EEEEKIKSQGQDVTS HHHHHHHHCCCCHHH	42.91	17525332
81	Phosphorylation	KSQGQDVTSSVYFMK HHCCCCHHHHHHHHH	24.47	20068231
82	Phosphorylation	SQGQDVTSSVYFMKQ HCCCCHHHHHHHHHH	20.04	20068231
83	Phosphorylation	QGQDVTSSVYFMKQT CCCCHHHHHHHHHHH	16.09	28857561
85	Phosphorylation	QDVTSSVYFMKQTIS CCHHHHHHHHHHHHH	10.41	20068231
97	Phosphorylation	TISNACGTIGLIHAI HHHHHHHHHHHHHHH	16.26	-
110	Ubiquitination	AIANNKDKMHFESGS HHHCCCCCCCCCCCH	35.56	-
117	Phosphorylation	KMHFESGSTLKKFLE CCCCCCCHHHHHHHH	39.59	28857561
118	Phosphorylation	MHFESGSTLKKFLEE CCCCCCHHHHHHHHH	46.23	28857561
120	Ubiquitination	FESGSTLKKFLEESV CCCCHHHHHHHHHHH	41.38	-
121	Ubiquitination	ESGSTLKKFLEESVS CCCHHHHHHHHHHHC	59.29	21890473
126	Phosphorylation	LKKFLEESVSMSPEE HHHHHHHHHCCCHHH	15.32	23927012
128	Phosphorylation	KFLEESVSMSPEERA HHHHHHHCCCHHHHH	23.87	29255136
129	Sulfoxidation	FLEESVSMSPEERAR HHHHHHCCCHHHHHH	7.90	21406390
130	Phosphorylation	LEESVSMSPEERARY HHHHHCCCHHHHHHH	22.96	29255136
141	Phosphorylation	RARYLENYDAIRVTH HHHHHHCCCEEEEEE	9.44	28796482
147	Phosphorylation	NYDAIRVTHETSAHE CCCEEEEEECCCCCC	12.26	28450419
150	Phosphorylation	AIRVTHETSAHEGQT EEEEEECCCCCCCCC	24.49	28450419
151	Phosphorylation	IRVTHETSAHEGQTE EEEEECCCCCCCCCC	25.33	28450419
157	Phosphorylation	TSAHEGQTEAPSIDE CCCCCCCCCCCCCCC	45.00	29978859
157	O-linked_Glycosylation	TSAHEGQTEAPSIDE CCCCCCCCCCCCCCC	45.00	OGP
161	Phosphorylation	EGQTEAPSIDEKVDL CCCCCCCCCCCCCCE	50.12	25159151
165	Ubiquitination	EAPSIDEKVDLHFIA CCCCCCCCCCEEEEE	36.98	-
210	Ubiquitination	EDAIEVCKKFMERDP HHHHHHHHHHHHCCH	54.97	21890473
211	Ubiquitination	DAIEVCKKFMERDPD HHHHHHHHHHHCCHH	44.83	-
211	Acetylation	DAIEVCKKFMERDPD HHHHHHHHHHHCCHH	44.83	25953088

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
75	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UCHL3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of UCHL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLPB_HUMAN	CLPB	physical	19615732
SMAD1_HUMAN	SMAD1	physical	21453705
NSG2_HUMAN	HMP19	physical	21900206
POGK_HUMAN	POGK	physical	21900206
UBC_HUMAN	UBC	physical	20622874
UBE2S_HUMAN	UBE2S	physical	20622874
UBC_HUMAN	UBC	physical	22284438
UBC_HUMAN	UBC	physical	15531586
UCHL3_HUMAN	UCHL3	physical	15531586
UBC_HUMAN	UBC	physical	10518943
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZN593_HUMAN	ZNF593	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
XPO2_HUMAN	CSE1L	physical	22939629
XIAP_HUMAN	XIAP	physical	22939629
UNK_HUMAN	UNK	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
ZRAB2_HUMAN	ZRANB2	physical	22939629
VATF_HUMAN	ATP6V1F	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
VP33B_HUMAN	VPS33B	physical	22939629
LONF1_HUMAN	LONRF1	physical	23105109
TRI27_HUMAN	TRIM27	physical	23105109
CADH1_HUMAN	CDH1	physical	24798214
UBC_HUMAN	UBC	physical	9521656
PA2GA_HUMAN	PLA2G2A	physical	22118674
UBC_HUMAN	UBC	physical	9790970
NEDD8_HUMAN	NEDD8	physical	9790970
CLPB_HUMAN	CLPB	physical	26186194
ZMYM6_HUMAN	ZMYM6	physical	26186194
UBC_HUMAN	UBC	physical	25590432
THIM_HUMAN	ACAA2	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
GDIA_HUMAN	GDI1	physical	26344197
GPX4_HUMAN	GPX4	physical	26344197
HINT1_HUMAN	HINT1	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
MARE1_HUMAN	MAPRE1	physical	26344197
PEBP1_HUMAN	PEBP1	physical	26344197
6PGD_HUMAN	PGD	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
UBC_HUMAN	UBC	physical	27066941
RAD51_HUMAN	RAD51	physical	27941124
CLPB_HUMAN	CLPB	physical	28514442
ZMYM6_HUMAN	ZMYM6	physical	28514442
ZEB1_HUMAN	ZEB1	physical	29119051

Drug and Disease Associations

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

Regulatory Network of UCHL3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.	17525332 [Abstract]