DUS22_HUMAN - dbPTM
DUS22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS22_HUMAN
UniProt AC Q9NRW4
Protein Name Dual specificity protein phosphatase 22
Gene Name DUSP22
Organism Homo sapiens (Human).
Sequence Length 184
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) (By similarity)..
Protein Sequence MGNGMNKILPGLYIGNFKDARDAEQLSKNKVTHILSVHDSARPMLEGVKYLCIPAADSPSQNLTRHFKESIKFIHECRLRGESCLVHCLAGVSRSVTLVIAYIMTVTDFGWEDALHTVRAGRSCANPNVGFQRQLQEFEKHEVHQYRQWLKEEYGESPLQDAEEAKNILAAPGILKFWAFLRRL
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
2N-myristoyl glycine------MGNGMNKIL
------CCCCCHHCC
39.12-
2Myristoylation------MGNGMNKIL
------CCCCCHHCC
39.1220553486
18UbiquitinationGLYIGNFKDARDAEQ
CCEECCCCCHHHHHH
55.25-
18 (in isoform 2)Ubiquitination-55.25-
36PhosphorylationNKVTHILSVHDSARP
CCCEEEEECCCCCCH
19.4623312004
50PhosphorylationPMLEGVKYLCIPAAD
HHHCCCCEEEEECCC
12.3730108239
58PhosphorylationLCIPAADSPSQNLTR
EEEECCCCCCHHHHH
23.0223401153
60PhosphorylationIPAADSPSQNLTRHF
EECCCCCCHHHHHHH
35.3425159151
64PhosphorylationDSPSQNLTRHFKESI
CCCCHHHHHHHHHHH
29.6430576142
83PhosphorylationECRLRGESCLVHCLA
HHHHCCCHHHHHHHH
18.6422210691
93PhosphorylationVHCLAGVSRSVTLVI
HHHHHCCCHHHHHHH
20.2322210691
151UbiquitinationHQYRQWLKEEYGESP
HHHHHHHHHHHCCCC
45.61-
166UbiquitinationLQDAEEAKNILAAPG
CCCHHHHHHHHHHHH
48.04-
178 (in isoform 2)Phosphorylation-5.6324719451
188 (in isoform 2)Phosphorylation-28450419
189 (in isoform 2)Phosphorylation-28450419
197 (in isoform 2)Phosphorylation-28842319

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 DUS22_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS22_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 DUS22_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HXA1_HUMANHOXA1physical
21988832
DHB4_HUMANHSD17B4physical
27880917
RL27A_HUMANRPL27Aphysical
27880917
DUS22_HUMANDUSP22physical
27432908
ARF5_HUMANARF5physical
27432908
TAGL2_HUMANTAGLN2physical
27432908
DUS23_HUMANDUSP23physical
27432908
VTI1B_HUMANVTI1Bphysical
27432908
SVIP_HUMANSVIPphysical
27432908
PGRC1_HUMANPGRMC1physical
27432908
PGRC2_HUMANPGRMC2physical
27432908
RAB14_HUMANRAB14physical
27432908
DUS28_HUMANDUSP28physical
27432908
TMM11_HUMANTMEM11physical
27432908
HMOX2_HUMANHMOX2physical
27432908
NDKA_HUMANNME1physical
27432908
MFF_HUMANMFFphysical
27432908
RASK_HUMANKRASphysical
27432908
TMX1_HUMANTMX1physical
27432908
PRAF2_HUMANPRAF2physical
27432908
MSPD1_HUMANMOSPD1physical
27432908
SRPRA_HUMANSRPRphysical
27432908
RAB5C_HUMANRAB5Cphysical
27432908
PTH2_HUMANPTRH2physical
27432908
RAB5A_HUMANRAB5Aphysical
27432908
APT_HUMANAPRTphysical
27432908
RASH_HUMANHRASphysical
27432908
MCL1_HUMANMCL1physical
27432908
APOL2_HUMANAPOL2physical
27432908
ATX10_HUMANATXN10physical
27432908
GNAI3_HUMANGNAI3physical
27432908
SAM50_HUMANSAMM50physical
27432908
SNP23_HUMANSNAP23physical
27432908
SNG1_HUMANSYNGR1physical
27432908
GNAI1_HUMANGNAI1physical
27432908
ERGI1_HUMANERGIC1physical
27432908
GNAI2_HUMANGNAI2physical
27432908
MTCH1_HUMANMTCH1physical
27432908
DCAKD_HUMANDCAKDphysical
27432908
RAB10_HUMANRAB10physical
27432908
RAB9A_HUMANRAB9Aphysical
27432908
STX16_HUMANSTX16physical
27432908
TLDC1_HUMANTLDC1physical
27432908
WDR18_HUMANWDR18physical
27432908
NDK3_HUMANNME3physical
27432908
CYB5B_HUMANCYB5Bphysical
27432908
F177A_HUMANFAM177A1physical
27432908
TI17B_HUMANTIMM17Bphysical
27432908
TMCO1_HUMANTMCO1physical
27432908
PCYOX_HUMANPCYOX1physical
27432908
RAP1A_HUMANRAP1Aphysical
27432908
TMM70_HUMANTMEM70physical
27432908
CHP1_HUMANCHP1physical
27432908
TI17A_HUMANTIMM17Aphysical
27432908
MTCH2_HUMANMTCH2physical
27432908
QKI_HUMANQKIphysical
27432908
ARF1_HUMANARF1physical
27432908
MIC19_HUMANCHCHD3physical
27432908
ARF4_HUMANARF4physical
27432908
TMX3_HUMANTMX3physical
27432908
ARL1_HUMANARL1physical
27432908
SCAM3_HUMANSCAMP3physical
27432908
TOM40_HUMANTOMM40physical
27432908
PPM1A_HUMANPPM1Aphysical
27432908
CANT1_HUMANCANT1physical
27432908
TMUB1_HUMANTMUB1physical
27432908
GNA14_HUMANGNA14physical
28514442
NRN1_HUMANNRN1physical
28514442
CCYL1_HUMANCCNYL1physical
28514442
SYLM_HUMANLARS2physical
28514442
GNAQ_HUMANGNAQphysical
28514442
HPCL1_HUMANHPCAL1physical
28514442
ERIC5_HUMANERICH5physical
28514442
OCC1_HUMANC12orf75physical
28514442
RASH_HUMANHRASphysical
28514442
PTPRG_HUMANPTPRGphysical
28514442
POTEF_HUMANPOTEFphysical
28514442
KCD21_HUMANKCTD21physical
28514442
RAP1A_HUMANRAP1Aphysical
28514442
ARFP2_HUMANARFIP2physical
28514442
UBTD2_HUMANUBTD2physical
28514442
FBX7_HUMANFBXO7physical
28514442
I5P1_HUMANINPP5Aphysical
28514442
LTOR1_HUMANLAMTOR1physical
28514442
ULBP3_HUMANULBP3physical
28514442
ULBP2_HUMANULBP2physical
28514442
PHAG1_HUMANPAG1physical
28514442
IKIP_HUMANIKBIPphysical
28514442
IF4E2_HUMANEIF4E2physical
28514442
CTNA2_HUMANCTNNA2physical
28514442
SRP54_HUMANSRP54physical
28514442
GNA11_HUMANGNA11physical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
GBG5_HUMANGNG5physical
28514442
YES_HUMANYES1physical
28514442
VAMP3_HUMANVAMP3physical
28514442
GNA13_HUMANGNA13physical
28514442
KC1G3_HUMANCSNK1G3physical
28514442
SVIP_HUMANSVIPphysical
28514442
LTOR4_HUMANLAMTOR4physical
28514442
PALM_HUMANPALMphysical
28514442
CUED1_HUMANCUEDC1physical
28514442
GNAO_HUMANGNAO1physical
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 DUS22_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Myristoylation of the dual-specificity phosphatase c-JUN N-terminalkinase (JNK) stimulatory phosphatase 1 is necessary for its activationof JNK signaling and apoptosis.";
Schwertassek U., Buckley D.A., Xu C.F., Lindsay A.J., McCaffrey M.W.,Neubert T.A., Tonks N.K.;
FEBS J. 277:2463-2473(2010).
Cited for: MYRISTOYLATION AT GLY-2.

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