SENP8_HUMAN - dbPTM
SENP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SENP8_HUMAN
UniProt AC Q96LD8
Protein Name Sentrin-specific protease 8
Gene Name SENP8
Organism Homo sapiens (Human).
Sequence Length 212
Subcellular Localization
Protein Description Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53..
Protein Sequence MDPVVLSYMDSLLRQSDVSLLDPPSWLNDHIIGFAFEYFANSQFHDCSDHVSFISPEVTQFIKCTSNPAEIAMFLEPLDLPNKRVVFLAINDNSNQAAGGTHWSLLVYLQDKNSFFHYDSHSRSNSVHAKQVAEKLEAFLGRKGDKLAFVEEKAPAQQNSYDCGMYVICNTEALCQNFFRQQTESLLQLLTPAYITKKRGEWKDLITTLAKK
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-------MDPVVLSY
-------CCHHHHHH
13.6722223895
7Phosphorylation-MDPVVLSYMDSLLR
-CCHHHHHHHHHHHH
13.5520068231
8PhosphorylationMDPVVLSYMDSLLRQ
CCHHHHHHHHHHHHH
10.7720068231
11PhosphorylationVVLSYMDSLLRQSDV
HHHHHHHHHHHHCCC
16.8720068231
146AcetylationFLGRKGDKLAFVEEK
HHCCCCCEEEEEEEC
50.8419820343

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

Oops, there are no upstream regulatory protein records of SENP8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SENP8_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 SENP8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKIP1_HUMANAKIP1physical
16998474
NEDD8_HUMANNEDD8physical
12759363
NEDD8_HUMANNEDD8physical
15775960
NEDD8_HUMANNEDD8physical
19328766
NEDD8_HUMANNEDD8physical
15567417
CUL1_HUMANCUL1physical
20190741
CUL4A_HUMANCUL4Aphysical
20190741
RS14_HUMANRPS14physical
23246961
CSN1_HUMANGPS1physical
23408908
SMUF1_HUMANSMURF1physical
24821572
CUL1_HUMANCUL1physical
23408908
PA2GA_HUMANPLA2G2Aphysical
22118674
CUL2_HUMANCUL2physical
12730221
TERF1_HUMANTERF1physical
27214791
HDGR3_HUMANHDGFRP3physical
28514442

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 SENP8_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.

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