UBP18_HUMAN - dbPTM
UBP18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP18_HUMAN
UniProt AC Q9UMW8
Protein Name Ubl carboxyl-terminal hydrolase 18
Gene Name USP18
Organism Homo sapiens (Human).
Sequence Length 372
Subcellular Localization Isoform 1: Cytoplasm .
Isoform 2: Nucleus . Cytoplasm .
Protein Description Involved in the regulation of inflammatory response to interferon type 1. [PubMed: 27325888 Can efficiently cleave only ISG15 fusions including native ISG15 conjugates linked via isopeptide bonds. Necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms.; Isoform 2: Has enzymatic activity similar to isoform 1 and interferes with type I interferon signaling. Major deISGylation enzyme for nuclear proteins]
Protein Sequence MSKAFGLLRQICQSILAESSQSPADLEEKKEEDSNMKREQPRERPRAWDYPHGLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCNVPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHWQETAYLLVYMKMEC
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
3Ubiquitination-----MSKAFGLLRQ
-----CCHHHHHHHH
46.57-
87PhosphorylationTRILKRITVPRGADE
HHHHHHCCCCCCCCH
28.6129496963
125PhosphorylationVRPLELAYCLQKCNV
CHHHHHHHHHHHCCC
13.3022461510
130UbiquitinationLAYCLQKCNVPLFVQ
HHHHHHHCCCCEEEC
3.9121963094
133UbiquitinationCLQKCNVPLFVQHDA
HHHHCCCCEEECCCH
13.1922817900
169PhosphorylationERLQALYTIRVKDSL
HHHHHHHHEEECCCE
11.8024719451
173UbiquitinationALYTIRVKDSLICVD
HHHHEEECCCEEEEE
31.58-
175PhosphorylationYTIRVKDSLICVDCA
HHEEECCCEEEEECC
17.5730576142
186PhosphorylationVDCAMESSRNSSMLT
EECCCCCCCCCCCCC
23.3630576142
203PhosphorylationLSLFDVDSKPLKTLE
EHHHCCCCCCCCCHH
35.7024719451
204UbiquitinationSLFDVDSKPLKTLED
HHHCCCCCCCCCHHH
50.3221963094
207UbiquitinationDVDSKPLKTLEDALH
CCCCCCCCCHHHHHH
60.6422817900
251PhosphorylationKLTHLPQTLTIHLMR
HHHCCCCEEEEEEEE
24.7529038488
253PhosphorylationTHLPQTLTIHLMRFS
HCCCCEEEEEEEEEC
15.1129038488
260PhosphorylationTIHLMRFSIRNSQTR
EEEEEEECCCCCCCH
15.4129496963
268UbiquitinationIRNSQTRKICHSLYF
CCCCCCHHHHHHCCC
53.74-
288UbiquitinationFSQILPMKRESCDAE
HHHHCCCCHHHCCHH
51.58-

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 ligaseSKP2Q13309
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP18_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 UBP18_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYL6_HUMANMYL6physical
19615732
NDKA_HUMANNME1physical
19615732
KDM3B_HUMANKDM3Bphysical
19615732
INAR2_HUMANIFNAR2physical
16710296
PCNA_HUMANPCNAphysical
24768535
SKP2_HUMANSKP2physical
25307056
ISG15_HUMANISG15physical
25307056
HERC1_HUMANHERC1physical
26186194
TM14A_HUMANTMEM14Aphysical
21516116
IKKA_HUMANCHUKphysical
26240016
IKKB_HUMANIKBKBphysical
26240016
NEMO_HUMANIKBKGphysical
26240016
TAB1_HUMANTAB1physical
23825189
CAR11_HUMANCARD11physical
23825189
TAB2_HUMANTAB2physical
23825189
M3K7_HUMANMAP3K7physical
23825189
STING_HUMANTMEM173physical
27801882
M3K7_HUMANMAP3K7physical
28718215

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP18_HUMAN

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Related Literatures of Post-Translational Modification

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