DUS10_HUMAN - dbPTM
DUS10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS10_HUMAN
UniProt AC Q9Y6W6
Protein Name Dual specificity protein phosphatase 10
Gene Name DUSP10
Organism Homo sapiens (Human).
Sequence Length 482
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38..
Protein Sequence MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGVETVV
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
4Phosphorylation----MPPSPLDDRVV
----CCCCCCCCCEE
32.0216565220
15PhosphorylationDRVVVALSRPVRPQD
CCEEEEECCCCCHHH
25.4629514088
224PhosphorylationSCREGKDSFKRIFSK
HCCCCCHHHHHHHCC
35.83-
230PhosphorylationDSFKRIFSKEIIVYD
HHHHHHHCCEEEEEE
27.3224719451
236PhosphorylationFSKEIIVYDENTNEP
HCCEEEEEECCCCCC
13.7124719451
240PhosphorylationIIVYDENTNEPSRVM
EEEEECCCCCCCCCC
38.6224719451
313PhosphorylationLLPQPIPTTPDIENA
CCCCCCCCCCCCCCC
52.2428348404
314PhosphorylationLPQPIPTTPDIENAE
CCCCCCCCCCCCCCC
17.3828348404
380UbiquitinationLPATDSNKQNLRQYF
CCCCCCCHHHHHHHH
44.5129967540
415PhosphorylationCQAGVSRSATIVIAY
CCCCCCHHHHHHHHH
23.4320049867
417PhosphorylationAGVSRSATIVIAYLM
CCCCHHHHHHHHHHH
19.6120049867
422PhosphorylationSATIVIAYLMKHTRM
HHHHHHHHHHHHCCC
9.0120049867
427PhosphorylationIAYLMKHTRMTMTDA
HHHHHHHCCCCHHHH
19.3320049867
430PhosphorylationLMKHTRMTMTDAYKF
HHHHCCCCHHHHHHH
17.3920049867
432PhosphorylationKHTRMTMTDAYKFVK
HHCCCCHHHHHHHHC
14.3320049867
435PhosphorylationRMTMTDAYKFVKGKR
CCCHHHHHHHHCCCC
14.0420049867

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
224SPhosphorylationKinaseMTORP42345
PSP
230SPhosphorylationKinaseMTORP42345
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS10_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 DUS10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK14_HUMANMAPK14physical
10391943
MK08_HUMANMAPK8physical
10391943
MK09_HUMANMAPK9physical
11359773
MK10_HUMANMAPK10physical
11359773
SNX2_HUMANSNX2physical
21988832
FHL2_HUMANFHL2physical
21988832
FINC_HUMANFN1physical
21988832
RS11_HUMANRPS11physical
21988832
SLX1_HUMANSLX1Bphysical
21988832
CSKP_HUMANCASKphysical
27880917
MK09_HUMANMAPK9physical
27880917
OTUD4_HUMANOTUD4physical
27880917
ACTBL_HUMANACTBL2physical
28514442
ACTA_HUMANACTA2physical
28514442
EFHD1_HUMANEFHD1physical
28514442
ACTB_HUMANACTBphysical
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 DUS10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.

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