DUS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DUS3_HUMAN
• UniProt AC: P51452
• Protein Name: Dual specificity protein phosphatase 3
• Gene Name: DUSP3
• Organism: Homo sapiens (Human).
• Sequence Length: 185
• Subcellular Localization: Nucleus .
• Protein Description: Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2..
• Protein Sequence: MSGSFELSVQDLNDLLSDGSGCYSLPSQPCNEVTPRIYVGNASVAQDIPKLQKLGITHVLNAAEGRSFMHVNTNANFYKDSGITYLGIKANDTQEFNLSAYFERAADFIDQALAQKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSIVRQNREIGPNDGFLAQLCQLNDRLAKEGKLKP

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
2 (in isoform 2)	Phosphorylation	-	43.05	26552605
8	Phosphorylation	MSGSFELSVQDLNDL CCCCEEEEHHHHHHH	15.55	18491316
12	Ubiquitination	FELSVQDLNDLLSDG EEEEHHHHHHHHCCC	2.76	21890473
23	Phosphorylation	LSDGSGCYSLPSQPC HCCCCCCCCCCCCCC	19.44	22817900
38	Phosphorylation	NEVTPRIYVGNASVA CCCCCCEEECCHHHH	12.00	20068231
43	Phosphorylation	RIYVGNASVAQDIPK CEEECCHHHHCCCHH	23.22	25072903
50	Acetylation	SVAQDIPKLQKLGIT HHHCCCHHHHHCCCC	64.98	23236377
50	Ubiquitination	SVAQDIPKLQKLGIT HHHCCCHHHHHCCCC	64.98	23000965
53	Ubiquitination	QDIPKLQKLGITHVL CCCHHHHHCCCCEEE	60.15	23000965
53	Acetylation	QDIPKLQKLGITHVL CCCHHHHHCCCCEEE	60.15	25953088
57	Phosphorylation	KLQKLGITHVLNAAE HHHHCCCCEEEECCC	12.25	28857561
67	Phosphorylation	LNAAEGRSFMHVNTN EECCCCCCCEEEECC	37.47	29978859
75	Ubiquitination	FMHVNTNANFYKDSG CEEEECCCCEECCCC	12.89	21890473
81	Phosphorylation	NANFYKDSGITYLGI CCCEECCCCCEEEEE	28.13	21712546
85	Phosphorylation	YKDSGITYLGIKAND ECCCCCEEEEEECCC	10.87	27642862
93	Phosphorylation	LGIKANDTQEFNLSA EEEECCCCCEEEHHH	29.79	27251275
101	Phosphorylation	QEFNLSAYFERAADF CEEEHHHHHHHHHHH	11.55	-
116	Ubiquitination	IDQALAQKNGRVLVH HHHHHHHHCCEEEEE	56.62	23000965
128	Phosphorylation	LVHCREGYSRSPTLV EEECCCCCCCCHHHH	8.99	24719451
129	Phosphorylation	VHCREGYSRSPTLVI EECCCCCCCCHHHHH	36.82	24719451
131	Phosphorylation	CREGYSRSPTLVIAY CCCCCCCCHHHHHHH	19.12	24719451
133	Phosphorylation	EGYSRSPTLVIAYLM CCCCCCHHHHHHHHH	34.60	20068231
138	Phosphorylation	SPTLVIAYLMMRQKM CHHHHHHHHHHHCCC	5.52	20068231
149	Phosphorylation	RQKMDVKSALSIVRQ HCCCCHHHHHHHHHH	34.00	-
152	Phosphorylation	MDVKSALSIVRQNRE CCHHHHHHHHHHCCC	20.82	24719451
179	Ubiquitination	QLNDRLAKEGKLKP- HHHHHHHHCCCCCC-	72.15	24816145

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
38	Y	Phosphorylation	Kinase	SYK	P43405	PSP
38	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
138	Y	Phosphorylation	Kinase	SYK	P43405	PSP
138	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
138	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DUS3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DUS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGFR_HUMAN	EGFR	physical	1281549
MK03_HUMAN	MAPK3	physical	10224087
MK01_HUMAN	MAPK1	physical	10224087
A4_HUMAN	APP	physical	21832049
NDF1_HUMAN	NEUROD1	physical	21988832
DUS3_HUMAN	DUSP3	physical	27432908
CLC1B_HUMAN	CLEC1B	physical	27432908
5NTC_HUMAN	NT5C2	physical	27432908
DOC11_HUMAN	DOCK11	physical	27432908
HOOK3_HUMAN	HOOK3	physical	27432908
RPIA_HUMAN	RPIA	physical	27432908
CGT_HUMAN	UGT8	physical	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.