DUS14_HUMAN - dbPTM
DUS14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS14_HUMAN
UniProt AC O95147
Protein Name Dual specificity protein phosphatase 14
Gene Name DUSP14
Organism Homo sapiens (Human).
Sequence Length 198
Subcellular Localization
Protein Description Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases..
Protein Sequence MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI
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
2O-linked_Glycosylation------MSSRGHSTL
------CCCCCCCCC
28.8330379171
3Phosphorylation-----MSSRGHSTLP
-----CCCCCCCCCC
40.7723532336
4Methylation----MSSRGHSTLPR
----CCCCCCCCCCC
39.27-
7Phosphorylation-MSSRGHSTLPRTLM
-CCCCCCCCCCCCCC
34.1719369195
8PhosphorylationMSSRGHSTLPRTLMA
CCCCCCCCCCCCCCC
34.8023532336
11MethylationRGHSTLPRTLMAPRM
CCCCCCCCCCCCCCC
43.54-
17MethylationPRTLMAPRMISEGDI
CCCCCCCCCCCCCCC
26.06-
96UbiquitinationYFDTVADKIHSVSRK
EEHHHHHHHHHHHHH
32.36-
99PhosphorylationTVADKIHSVSRKHGA
HHHHHHHHHHHHHCC
25.8427732954
101PhosphorylationADKIHSVSRKHGATL
HHHHHHHHHHHCCEE
38.3327732954
103UbiquitinationKIHSVSRKHGATLVH
HHHHHHHHHCCEEEH
38.59-
161PhosphorylationFWRQLIDYERQLFGK
HHHHHHHHHHHHHCC
13.15-
168UbiquitinationYERQLFGKSTVKMVQ
HHHHHHCCHHHEEEE
35.30-
169PhosphorylationERQLFGKSTVKMVQT
HHHHHCCHHHEEEEC
38.5218669648
172UbiquitinationLFGKSTVKMVQTPYG
HHCCHHHEEEECCCC
33.1821906983
176PhosphorylationSTVKMVQTPYGIVPD
HHHEEEECCCCCCCC
13.6818669648
178PhosphorylationVKMVQTPYGIVPDVY
HEEEECCCCCCCCHH
23.9120090780
185PhosphorylationYGIVPDVYEKESRHL
CCCCCCHHCHHHHCC
28.7620068231
187UbiquitinationIVPDVYEKESRHLMP
CCCCHHCHHHHCCCC
43.2121890473
195PhosphorylationESRHLMPYWGI----
HHHCCCCCCCC----
11.4227642862

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 ligaseTANKQ92844
PMID:26521044

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS14_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 DUS14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INO1_HUMANISYNA1physical
21988832
SPERT_HUMANSPERTphysical
25416956
TRAF2_HUMANTRAF2physical
26521044
AP3B1_HUMANAP3B1physical
27880917
NUDT5_HUMANNUDT5physical
27880917
P5CR1_HUMANPYCR1physical
27880917
P5CR2_HUMANPYCR2physical
27880917
ACOX1_HUMANACOX1physical
28514442
TFG_HUMANTFGphysical
28514442
F136A_HUMANFAM136Aphysical
28514442
ACAD8_HUMANACAD8physical
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 DUS14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND THR-8, AND MASSSPECTROMETRY.

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