JOS1_HUMAN - dbPTM
JOS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JOS1_HUMAN
UniProt AC Q15040
Protein Name Josephin-1
Gene Name JOSD1
Organism Homo sapiens (Human).
Sequence Length 202
Subcellular Localization Cell membrane . Cytoplasm . Ubiquitination increases localization the plasma membrane. In the cytosol, the unubiquitinated form may be associated with the cytoskeleton via ACTB-binding.
Protein Description Deubiquitinates monoubiquitinated probes (in vitro). When ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-ubiquitin chains (in vitro), hence may act as a deubiquitinating enzyme. May increase macropinocytosis and suppress clathrin- and caveolae-mediated endocytosis. May enhance membrane dynamics and cell motility independently of its catalytic activity..
Protein Sequence MSCVPWKGDKAKSESLELPQAAPPQIYHEKQRRELCALHALNNVFQDSNAFTRDTLQEIFQRLSPNTMVTPHKKSMLGNGNYDVNVIMAALQTKGYEAVWWDKRRDVGVIALTNVMGFIMNLPSSLCWGPLKLPLKRQHWICVREVGGAYYNLDSKLKMPEWIGGESELRKFLKHHLRGKNCELLLVVPEEVEAHQSWRTDV
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
2Phosphorylation------MSCVPWKGD
------CCCCCCCCC
24.6626074081
12UbiquitinationPWKGDKAKSESLELP
CCCCCHHCCCCCCCC
61.57-
13PhosphorylationWKGDKAKSESLELPQ
CCCCHHCCCCCCCCC
36.9623401153
15PhosphorylationGDKAKSESLELPQAA
CCHHCCCCCCCCCCC
33.9523927012
27PhosphorylationQAAPPQIYHEKQRRE
CCCCCCCCCHHHHHH
9.9323403867
30UbiquitinationPPQIYHEKQRRELCA
CCCCCCHHHHHHHHH
35.47-
70PhosphorylationLSPNTMVTPHKKSML
HCCCCEECCCCHHHC
14.6228674419
73UbiquitinationNTMVTPHKKSMLGNG
CCEECCCCHHHCCCC
47.98-
74UbiquitinationTMVTPHKKSMLGNGN
CEECCCCHHHCCCCC
37.7621906983
158UbiquitinationYNLDSKLKMPEWIGG
EECCCCCCCCHHHCC
57.0321906983
174UbiquitinationSELRKFLKHHLRGKN
HHHHHHHHHHHCCCC
31.92-
180UbiquitinationLKHHLRGKNCELLLV
HHHHHCCCCCEEEEE
52.5721906983

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 JOS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JOS1_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 JOS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIM8A_HUMANTIMM8Aphysical
19615732
UBC_HUMANUBCphysical
19382171
UBC_HUMANUBCphysical
23625928
TRIM1_HUMANMID2physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
K1C40_HUMANKRT40physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
UBC_HUMANUBCphysical
21118805
SOCS1_HUMANSOCS1physical
28355105

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 JOS1_HUMAN

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Related Literatures of Post-Translational Modification

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