dbPTM

SPY4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPY4_HUMAN
UniProt AC	Q9C004
Protein Name	Protein sprouty homolog 4
Gene Name	SPRY4
Organism	Homo sapiens (Human).
Sequence Length	299
Subcellular Localization	Cytoplasm . Cell projection, ruffle membrane Peripheral membrane protein Cytoplasmic side .
Protein Description	Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras. Inhibits Ras-independent, but not Ras-dependent, activation of RAF1..
Protein Sequence	MEPPIPQSAPLTPNSVMVQPLLDSRMSHSRLQHPLTILPIDQVKTSHVENDYIDNPSLALTTGPKRTRGGAPELAPTPARCDQDVTHHWISFSGRPSSVSSSSSTSSDQRLLDHMAPPPVADQASPRAVRIQPKVVHCQPLDLKGPAVPPELDKHFLLCEACGKCKCKECASPRTLPSCWVCNQECLCSAQTLVNYGTCMCLVQGIFYHCTNEDDEGSCADHPCSCSRSNCCARWSFMGALSVVLPCLLCYLPATGCVKLAQRGYDRLRRPGCRCKHTNSVICKAASGDAKTSRPDKPF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEPPIPQS -------CCCCCCCC	18.41	22223895
8	Phosphorylation	MEPPIPQSAPLTPNS CCCCCCCCCCCCCCC	26.88	29255136
12	Phosphorylation	IPQSAPLTPNSVMVQ CCCCCCCCCCCEEHH	21.26	29255136
15	Phosphorylation	SAPLTPNSVMVQPLL CCCCCCCCEEHHHHC	16.88	29255136
24	Phosphorylation	MVQPLLDSRMSHSRL EHHHHCCCCCCCCCC	29.83	24719451
27	Phosphorylation	PLLDSRMSHSRLQHP HHCCCCCCCCCCCCC	19.73	24719451
29	Phosphorylation	LDSRMSHSRLQHPLT CCCCCCCCCCCCCEE	27.64	24043423
36	Phosphorylation	SRLQHPLTILPIDQV CCCCCCEEEEEHHHC	25.56	24043423
44	Ubiquitination	ILPIDQVKTSHVEND EEEHHHCCCCCCCCC	38.38	-
45	Phosphorylation	LPIDQVKTSHVENDY EEHHHCCCCCCCCCC	25.80	28152594
46	Phosphorylation	PIDQVKTSHVENDYI EHHHCCCCCCCCCCC	21.59	28152594
52	Phosphorylation	TSHVENDYIDNPSLA CCCCCCCCCCCCCCE	23.04	18707149
57	Phosphorylation	NDYIDNPSLALTTGP CCCCCCCCCEEECCC	32.31	28442448
75	Phosphorylation	RGGAPELAPTPARCD CCCCCCCCCCCCCCC	12.31	17389395
77	Phosphorylation	GAPELAPTPARCDQD CCCCCCCCCCCCCCC	24.79	29255136
97	Phosphorylation	ISFSGRPSSVSSSSS EEECCCCCCCCCCCC	41.85	29255136
98	Phosphorylation	SFSGRPSSVSSSSST EECCCCCCCCCCCCC	28.80	29255136
100	Phosphorylation	SGRPSSVSSSSSTSS CCCCCCCCCCCCCCC	26.84	29255136
101	Phosphorylation	GRPSSVSSSSSTSSD CCCCCCCCCCCCCCC	31.89	25850435
102	Phosphorylation	RPSSVSSSSSTSSDQ CCCCCCCCCCCCCCC	22.32	29255136
103	Phosphorylation	PSSVSSSSSTSSDQR CCCCCCCCCCCCCCH	39.31	29255136
104	Phosphorylation	SSVSSSSSTSSDQRL CCCCCCCCCCCCCHH	33.97	23312004
105	Phosphorylation	SVSSSSSTSSDQRLL CCCCCCCCCCCCHHH	33.91	23312004
106	Phosphorylation	VSSSSSTSSDQRLLD CCCCCCCCCCCHHHH	33.59	23312004
107	Phosphorylation	SSSSSTSSDQRLLDH CCCCCCCCCCHHHHH	37.54	29255136
125	Phosphorylation	PPVADQASPRAVRIQ CCCCCCCCCCEEEEC	14.86	29255136
148	Phosphorylation	LDLKGPAVPPELDKH CCCCCCCCCCHHHHC	10.27	27251275
276	Ubiquitination	RRPGCRCKHTNSVIC CCCCCCCCCCCCEEE	33.83	-
278	Phosphorylation	PGCRCKHTNSVICKA CCCCCCCCCCEEEEE	18.06	21406692
280	Phosphorylation	CRCKHTNSVICKAAS CCCCCCCCEEEEECC	17.64	28985074
284	Ubiquitination	HTNSVICKAASGDAK CCCCEEEEECCCCCC	35.54	-
303	Phosphorylation	DKPF----------- CCCC-----------		27251275

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 SPY4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPY4_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 SPY4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAF1_HUMAN	RAF1	physical	12717443
TESK1_HUMAN	TESK1	physical	12027893
TESK1_HUMAN	TESK1	physical	17974561
GRB2_HUMAN	GRB2	physical	16893902
PI42B_HUMAN	PIP4K2B	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615266	Hypogonadotropic hypogonadism 17 with or without anosmia (HH17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SPY4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-125, AND MASSSPECTROMETRY.	18669648 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.	17389395 [Abstract]