DUS12_HUMAN - dbPTM
DUS12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS12_HUMAN
UniProt AC Q9UNI6
Protein Name Dual specificity protein phosphatase 12
Gene Name DUSP12
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization Nucleus . Cytoplasm, cytosol . Primarily nuclear. Detected in a mesh-like pattern in the cytosol.
Protein Description Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues. Can dephosphorylate glucokinase (in vitro) (By similarity). Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and other in vitro substrates. [PubMed: 10446167]
Protein Sequence MLEAPGPSDGCELSNPSASRVSCAGQMLEVQPGLYFGGAAAVAEPDHLREAGITAVLTVDSEEPSFKAGPGVEDLWRLFVPALDKPETDLLSHLDRCVAFIGQARAEGRAVLVHCHAGVSRSVAIITAFLMKTDQLPFEKAYEKLQILKPEAKMNEGFEWQLKLYQAMGYEVDTSSAIYKQYRLQKVTEKYPELQNLPQELFAVDPTTVSQGLKDEVLYKCRKCRRSLFRSSSILDHREGSGPIAFAHKRMTPSSMLTTGRQAQCTSYFIEPVQWMESALLGVMDGQLLCPKCSAKLGSFNWYGEQCSCGRWITPAFQIHKNRVDEMKILPVLGSQTGKI
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
1Acetylation-------MLEAPGPS
-------CCCCCCCC		7.4322223895
8PhosphorylationMLEAPGPSDGCELSN
CCCCCCCCCCCCCCC		53.1827732954
14PhosphorylationPSDGCELSNPSASRV
CCCCCCCCCCCCCCC		25.1325627689
17PhosphorylationGCELSNPSASRVSCA
CCCCCCCCCCCCCCC		43.0327732954
19PhosphorylationELSNPSASRVSCAGQ
CCCCCCCCCCCCCCC		37.2427732954
54PhosphorylationHLREAGITAVLTVDS
HHHHCCCEEEEEECC		15.1428122231
58PhosphorylationAGITAVLTVDSEEPS
CCCEEEEEECCCCCC		18.7028122231
61PhosphorylationTAVLTVDSEEPSFKA
EEEEEECCCCCCCCC		39.2528122231
85UbiquitinationLFVPALDKPETDLLS
HHHHCCCCCCHHHHH		45.6724816145
119UbiquitinationLVHCHAGVSRSVAII
EEECCCCCCHHHHHH		4.4527667366
140UbiquitinationTDQLPFEKAYEKLQI
CCCCCHHHHHHHHHH		57.5629967540
144UbiquitinationPFEKAYEKLQILKPE
CHHHHHHHHHHCCCH		32.7729967540
149UbiquitinationYEKLQILKPEAKMNE
HHHHHHCCCHHHCCC		42.3029967540
149AcetylationYEKLQILKPEAKMNE
HHHHHHCCCHHHCCC		42.3025953088
231PhosphorylationCRRSLFRSSSILDHR
HHHHHHHCCCHHCCC		22.5420873877
232PhosphorylationRRSLFRSSSILDHRE
HHHHHHCCCHHCCCC		19.6923403867
233PhosphorylationRSLFRSSSILDHREG
HHHHHCCCHHCCCCC		28.5423403867
241PhosphorylationILDHREGSGPIAFAH
HHCCCCCCCCEEEEE		36.3223312004
249UbiquitinationGPIAFAHKRMTPSSM
CCEEEEECCCCCHHH		40.2027667366
249AcetylationGPIAFAHKRMTPSSM
CCEEEEECCCCCHHH		40.2025953088
252PhosphorylationAFAHKRMTPSSMLTT
EEEECCCCCHHHHCC		24.8525159151
254PhosphorylationAHKRMTPSSMLTTGR
EECCCCCHHHHCCCC		21.1520068231
255PhosphorylationHKRMTPSSMLTTGRQ
ECCCCCHHHHCCCCC		21.0020068231
258PhosphorylationMTPSSMLTTGRQAQC
CCCHHHHCCCCCCCC		20.6820068231
259PhosphorylationTPSSMLTTGRQAQCT
CCHHHHCCCCCCCCC		26.8020068231
266PhosphorylationTGRQAQCTSYFIEPV
CCCCCCCCCEEEEEH		17.8724043423
267PhosphorylationGRQAQCTSYFIEPVQ
CCCCCCCCEEEEEHH		26.1824043423
268PhosphorylationRQAQCTSYFIEPVQW
CCCCCCCEEEEEHHH		7.1624043423
278PhosphorylationEPVQWMESALLGVMD
EEHHHHHHHHHCCCC		14.2224043423
314PhosphorylationCSCGRWITPAFQIHK
CCCCCCCCCCHHHCC		11.12-
335PhosphorylationKILPVLGSQTGKI--
CEEHHCCCCCCCC--		22.0225159151
337PhosphorylationLPVLGSQTGKI----
EHHCCCCCCCC----		41.9823186163
339AcetylationVLGSQTGKI------
HCCCCCCCC------		48.9425953088
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 DUS12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS12_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 DUS12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBD6_HUMANMBD6physical
16169070
CE126_HUMANKIAA1377physical
16169070
PTN_HUMANPTNphysical
16169070
NR1H2_HUMANNR1H2physical
21900206
A4_HUMANAPPphysical
21832049
HSPB8_HUMANHSPB8physical
25416956
P2R3B_HUMANPPP2R3Bphysical
25416956
CU059_HUMANC21orf59physical
26344197
P2R3B_HUMANPPP2R3Bphysical
21516116
DUS12_HUMANDUSP12physical
27432908
DS13A_HUMANDUSP13physical
27432908
DS13B_HUMANDUSP13physical
27432908
PPM1A_HUMANPPM1Aphysical
27432908
DFFA_HUMANDFFAphysical
27432908
MBLC2_HUMANMBLAC2physical
27432908
PARK7_HUMANPARK7physical
27432908
RO60_HUMANTROVE2physical
27432908
HDDC2_HUMANHDDC2physical
27432908
CQ064_HUMANC17orf64physical
27432908
TMM11_HUMANTMEM11physical
27432908
ARF5_HUMANARF5physical
27432908
RASH_HUMANHRASphysical
27432908
T126A_HUMANTMEM126Aphysical
27432908
EIF2D_HUMANEIF2Dphysical
27432908
KAD6_HUMANAK6physical
27432908
LACRT_HUMANLACRTphysical
27432908
DCTN1_HUMANDCTN1physical
27432908
VPS4A_HUMANVPS4Aphysical
27432908
MMSA_HUMANALDH6A1physical
27432908
NCK1_HUMANNCK1physical
27432908
NDUAB_HUMANNDUFA11physical
27432908
PSD10_HUMANPSMD10physical
27432908
TBCB_HUMANTBCBphysical
27432908
DUS3_HUMANDUSP3physical
27432908
RAB28_HUMANRAB28physical
27432908
APT_HUMANAPRTphysical
27432908
MK01_HUMANMAPK1physical
27432908
PPAC_HUMANACP1physical
27432908
IF5A1_HUMANEIF5Aphysical
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 DUS12_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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