UCHL1_HUMAN - dbPTM
UCHL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UCHL1_HUMAN
UniProt AC P09936
Protein Name Ubiquitin carboxyl-terminal hydrolase isozyme L1
Gene Name UCHL1
Organism Homo sapiens (Human).
Sequence Length 223
Subcellular Localization Cytoplasm . Endoplasmic reticulum membrane
Lipid-anchor . About 30% of total UCHL1 is associated with membranes in brain.
Protein Description Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity..
Protein Sequence MQLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA
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 Orthologous
Protein Cluster
1Acetylation-------MQLKPMEI
-------CCCCCCCC		10.71-
4Acetylation----MQLKPMEINPE
----CCCCCCCCCHH		25.987367441
4Ubiquitination----MQLKPMEINPE
----CCCCCCCCCHH		25.9821906983
15UbiquitinationINPEMLNKVLSRLGV
CCHHHHHHHHHHHCC		40.3621890473
18PhosphorylationEMLNKVLSRLGVAGQ
HHHHHHHHHHCCCCC		28.5729978859
38PhosphorylationVLGLEEESLGSVPAP
ECCCCHHHCCCCCHH		41.1125338102
64UbiquitinationAQHENFRKKQIEELK
HCCCCHHHHHHHHHC		44.91-
65UbiquitinationQHENFRKKQIEELKG
CCCCHHHHHHHHHCC		52.8617259170
65MalonylationQHENFRKKQIEELKG
CCCCHHHHHHHHHCC		52.8626320211
71UbiquitinationKKQIEELKGQEVSPK
HHHHHHHCCCCCCHH		62.92-
71MalonylationKKQIEELKGQEVSPK
HHHHHHHCCCCCCHH		62.9226320211
78UbiquitinationKGQEVSPKVYFMKQT
CCCCCCHHHEEEECC		41.9021890473
78AcetylationKGQEVSPKVYFMKQT
CCCCCCHHHEEEECC		41.9026210075
80NitrationQEVSPKVYFMKQTIG
CCCCHHHEEEECCCC		12.23-
83UbiquitinationSPKVYFMKQTIGNSC
CHHHEEEECCCCCCC		34.1021906983
89PhosphorylationMKQTIGNSCGTIGLI
EECCCCCCCHHHHHH		14.5420068231
105UbiquitinationAVANNQDKLGFEDGS
HHHCCCCCCCCCCHH		40.52-
112PhosphorylationKLGFEDGSVLKQFLS
CCCCCCHHHHHHHHH		36.2829514088
115UbiquitinationFEDGSVLKQFLSETE
CCCHHHHHHHHHHHH		36.5321906983
119PhosphorylationSVLKQFLSETEKMSP
HHHHHHHHHHHCCCH		43.70-
123UbiquitinationQFLSETEKMSPEDRA
HHHHHHHCCCHHHHH		52.69-
125PhosphorylationLSETEKMSPEDRAKC
HHHHHCCCHHHHHHH		35.88-
131MalonylationMSPEDRAKCFEKNEA
CCHHHHHHHHHHHHH		40.1126320211
132GlutathionylationSPEDRAKCFEKNEAI
CHHHHHHHHHHHHHH		5.3422555962
135UbiquitinationDRAKCFEKNEAIQAA
HHHHHHHHHHHHHHH		39.5721906983
152S-nitrosocysteineAVAQEGQCRVDDKVN
HHHHHCCCCCCCCEE		7.23-
152GlutathionylationAVAQEGQCRVDDKVN
HHHHHCCCCCCCCEE		7.2322555962
152S-nitrosylationAVAQEGQCRVDDKVN
HHHHHCCCCCCCCEE		7.2319483679
157UbiquitinationGQCRVDDKVNFHFIL
CCCCCCCCEEEEEEE		34.3221906983
179SulfoxidationLYELDGRMPFPVNHG
EEEECCCCCCCCCCC		4.9930846556
188PhosphorylationFPVNHGASSEDTLLK
CCCCCCCCCHHHHHH		38.5620068231
189PhosphorylationPVNHGASSEDTLLKD
CCCCCCCCHHHHHHH		38.6720068231
192PhosphorylationHGASSEDTLLKDAAK
CCCCCHHHHHHHHHH		29.9120068231
195AcetylationSSEDTLLKDAAKVCR
CCHHHHHHHHHHHHH		48.7319608861
195UbiquitinationSSEDTLLKDAAKVCR
CCHHHHHHHHHHHHH		48.7319608861
215PhosphorylationEQGEVRFSAVALCKA
HCCCEEEEEEHHHHC		15.9827732954
220FarnesylationRFSAVALCKAA----
EEEEEHHHHCC----		1.7119261853
220S-nitrosocysteineRFSAVALCKAA----
EEEEEHHHHCC----		1.71-
220S-nitrosylationRFSAVALCKAA----
EEEEEHHHHCC----		1.7119483679
220FarnesylationRFSAVALCKAA----
EEEEEHHHHCC----		1.7119261853
221UbiquitinationFSAVALCKAA-----
EEEEHHHHCC-----		48.47-
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
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:25403879
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UCHL1_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 UCHL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
12082530
RANB9_HUMANRANBP9physical
12082530
CSN5_HUMANCOPS5physical
12082530
P53_HUMANTP53physical
18666234
K1C17_HUMANKRT17physical
19615732
CCD14_HUMANCCDC14physical
19615732
CTNB1_HUMANCTNNB1physical
19536331
SMN_HUMANSMN1physical
20713032
UBC_HUMANUBCphysical
20622874
TBA1A_HUMANTUBA1Aphysical
18250096
HSP7C_HUMANHSPA8physical
18550537
HS90A_HUMANHSP90AA1physical
18550537
LAMP2_HUMANLAMP2physical
18635949
HSP7C_HUMANHSPA8physical
18635949
HS90A_HUMANHSP90AA1physical
18635949
UBC_HUMANUBCphysical
22284438
UBC_HUMANUBCphysical
20439756
WDR82_HUMANWDR82physical
22939629
DDB1_HUMANDDB1physical
23297343
CDK1_HUMANCDK1physical
23543736
CDK4_HUMANCDK4physical
23543736
CDK5_HUMANCDK5physical
23543736
CDK6_HUMANCDK6physical
23543736
APR_HUMANPMAIP1physical
23499448
NMRL1_HUMANNMRAL1physical
24763515
UBC_HUMANUBCphysical
9521656
TNR1A_HUMANTNFRSF1Aphysical
24980434
PA2GA_HUMANPLA2G2Aphysical
22118674
PRKN_HUMANPARK2physical
25403879
UBC_HUMANUBCphysical
27066941
AKT2_HUMANAKT2physical
28636190
P53_HUMANTP53physical
29126443
TE2IP_HUMANTERF2IPphysical
29126443
TERF2_HUMANTERF2physical
29126443
Drug and Disease Associations
Kegg Disease
H00057 Parkinson's disease (PD)
OMIM Disease
613643Parkinson disease 5 (PARK5)
615491Neurodegeneration with optic atrophy, childhood-onset (NDGOA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UCHL1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Prenylation
ReferencePubMed
"Membrane-associated farnesylated UCH-L1 promotes alpha-synucleinneurotoxicity and is a therapeutic target for Parkinson's disease.";
Liu Z., Meray R.K., Grammatopoulos T.N., Fredenburg R.A.,Cookson M.R., Liu Y., Logan T., Lansbury P.T. Jr.;
Proc. Natl. Acad. Sci. U.S.A. 106:4635-4640(2009).
Cited for: SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-220.

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