DUS16_HUMAN - dbPTM
DUS16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS16_HUMAN
UniProt AC Q9BY84
Protein Name Dual specificity protein phosphatase 16
Gene Name DUSP16
Organism Homo sapiens (Human).
Sequence Length 665
Subcellular Localization Cytoplasm. Nucleus. Cytoplasmic vesicle. After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.
Protein Description Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2..
Protein Sequence MAHEMIGTQIVTERLVALLESGTEKVLLIDSRPFVEYNTSHILEAININCSKLMKRRLQQDKVLITELIQHSAKHKVDIDCSQKVVVYDQSSQDVASLSSDCFLTVLLGKLEKSFNSVHLLAGGFAEFSRCFPGLCEGKSTLVPTCISQPCLPVANIGPTRILPNLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPDFIPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASNGCVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDYEKKIKNQTGASGPKSKLKLLHLEKPNEPVPAVSEGGQKSETPLSPPCADSATSEAAGQRPVHPASVPSVPSVQPSLLEDSPLVQALSGLHLSADRLEDSNKLKRSFSLDIKSVSYSASMAASLHGFSSSEDALEYYKPSTTLDGTNKLCQFSPVQELSEQTPETSPDKEEASIPKKLQTARPSDSQSKRLHSVRTSSSGTAQRSLLSPLHRSGSVEDNYHTSFLFGLSTSQQHLTKSAGLGLKGWHSDILAPQTSTPSLTSSWYFATESSHFYSASAIYGGSASYSAYSCSQLPTCGDQVYSVRRRQKPSDRADSRRSWHEESPFEKQFKRRSCQMEFGESIMSENRSREELGKVGSQSSFSGSMEIIEVS
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
8PhosphorylationMAHEMIGTQIVTERL
CCCCHHCCHHHHHHH
12.2824043423
12PhosphorylationMIGTQIVTERLVALL
HHCCHHHHHHHHHHH
19.6024043423
55AcetylationINCSKLMKRRLQQDK
CCHHHHHHHHHHHCH
44.8122547814
82PhosphorylationHKVDIDCSQKVVVYD
CCCCCCCCCCEEEEE
29.32-
145PhosphorylationGKSTLVPTCISQPCL
CCCCCCEEECCCCCC
18.2628348404
148PhosphorylationTLVPTCISQPCLPVA
CCCEEECCCCCCCCC
30.1624719451
218UbiquitinationVNDSFCEKILPWLDK
CCCHHHHHHHHHHHH
51.21-
225UbiquitinationKILPWLDKSVDFIEK
HHHHHHHHCHHHHHH
50.65-
232UbiquitinationKSVDFIEKAKASNGC
HCHHHHHHHHHCCCE
50.82-
399PhosphorylationDSNKLKRSFSLDIKS
CCCCHHHEEEEECCE
20.0129514088
401PhosphorylationNKLKRSFSLDIKSVS
CCHHHEEEEECCEEE
26.7825159151
446PhosphorylationTNKLCQFSPVQELSE
CCCCCCCCCHHHHHH
9.7830266825
452PhosphorylationFSPVQELSEQTPETS
CCCHHHHHHCCCCCC
27.2330266825
455PhosphorylationVQELSEQTPETSPDK
HHHHHHCCCCCCCCH
21.0230266825
458PhosphorylationLSEQTPETSPDKEEA
HHHCCCCCCCCHHHC
46.9230266825
459PhosphorylationSEQTPETSPDKEEAS
HHCCCCCCCCHHHCC
29.4630266825
466PhosphorylationSPDKEEASIPKKLQT
CCCHHHCCCCHHHHC
42.5827251275
473PhosphorylationSIPKKLQTARPSDSQ
CCCHHHHCCCCCCHH
34.7625072903
477PhosphorylationKLQTARPSDSQSKRL
HHHCCCCCCHHHCCC
44.3225072903
479PhosphorylationQTARPSDSQSKRLHS
HCCCCCCHHHCCCEE
40.4625072903
481PhosphorylationARPSDSQSKRLHSVR
CCCCCHHHCCCEEEE
24.5625072903
498PhosphorylationSSGTAQRSLLSPLHR
CCCHHHHHHCCCCCC
22.9123403867
501PhosphorylationTAQRSLLSPLHRSGS
HHHHHHCCCCCCCCC
30.6123898821
506PhosphorylationLLSPLHRSGSVEDNY
HCCCCCCCCCCCCCC
25.3624719451
508PhosphorylationSPLHRSGSVEDNYHT
CCCCCCCCCCCCCCH
24.4728857561
515PhosphorylationSVEDNYHTSFLFGLS
CCCCCCCHHHHCCCC
15.7128348404
516PhosphorylationVEDNYHTSFLFGLST
CCCCCCHHHHCCCCC
13.4628348404
604PhosphorylationVRRRQKPSDRADSRR
HHCCCCCCCCCHHHH
46.92-
609PhosphorylationKPSDRADSRRSWHEE
CCCCCCHHHHCCCCC
28.7123403867
612PhosphorylationDRADSRRSWHEESPF
CCCHHHHCCCCCCHH
31.5130266825
617PhosphorylationRRSWHEESPFEKQFK
HHCCCCCCHHHHHHH
31.7226330541
627PhosphorylationEKQFKRRSCQMEFGE
HHHHHHHHHHHHHHH
16.8530576142
635PhosphorylationCQMEFGESIMSENRS
HHHHHHHHHHCCCCC
24.7828348404
638PhosphorylationEFGESIMSENRSREE
HHHHHHHCCCCCHHH
30.0128348404
642PhosphorylationSIMSENRSREELGKV
HHHCCCCCHHHHHCC
56.4728348404
658PhosphorylationSQSSFSGSMEIIEVS
CCCCCCCCCEEEEEC
16.4327251275

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
446SPhosphorylationKinaseMK01P28482
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
55KAcetylation

22547814
446SPhosphorylation

12794087

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 DUS16_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK14_HUMANMAPK14physical
11359773
MK09_HUMANMAPK9physical
11359773
MK10_HUMANMAPK10physical
11359773
MK01_HUMANMAPK1physical
11489891
MK08_HUMANMAPK8physical
11489891
MK14_HUMANMAPK14physical
11489891
MK14_HUMANMAPK14physical
27880917
MK09_HUMANMAPK9physical
27880917
DUS16_HUMANDUSP16physical
27432908
MLF1_HUMANMLF1physical
27432908
TEBP_HUMANPTGES3physical
27432908
MK09_HUMANMAPK9physical
27432908
NXF2_HUMANNXF2physical
27432908
MK08_HUMANMAPK8physical
27432908
AIP_HUMANAIPphysical
27432908
KCD20_HUMANKCTD20physical
27432908
1433B_HUMANYWHABphysical
27432908
HSPB1_HUMANHSPB1physical
27432908
HIG1A_HUMANHIGD1Aphysical
27432908
MK14_HUMANMAPK14physical
27432908
ARF5_HUMANARF5physical
27432908
DNJB1_HUMANDNAJB1physical
27432908
PFD3_HUMANVBP1physical
27432908

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 DUS16_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASSSPECTROMETRY.
"Activation of ERK induces phosphorylation of MAPK phosphatase-7, aJNK specific phosphatase, at Ser-446.";
Masuda K., Shima H., Katagiri C., Kikuchi K.;
J. Biol. Chem. 278:32448-32456(2003).
Cited for: PHOSPHORYLATION AT SER-446.

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