dbPTM

SPY2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPY2_HUMAN
UniProt AC	O43597
Protein Name	Protein sprouty homolog 2
Gene Name	SPRY2
Organism	Homo sapiens (Human).
Sequence Length	315
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, ruffle membrane . Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated ith EGF (epidermal growth factor).
Protein Description	May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis..
Protein Sequence	MEARAQSGNGSQPLLQTPRDGGRQRGEPDPRDALTQQVHVLSLDQIRAIRNTNEYTEGPTVVPRPGLKPAPRPSTQHKHERLHGLPEHRQPPRLQHSQVHSSARAPLSRSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPVADGIIRVQPKSELKPGELKPLSKEDLGLHAYRCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MEARAQSGNGSQPL -CCCCCCCCCCCCCC	32.99	29255136
11	Phosphorylation	RAQSGNGSQPLLQTP CCCCCCCCCCCEECC	32.40	29255136
17	Phosphorylation	GSQPLLQTPRDGGRQ CCCCCEECCCCCCCC	21.91	29255136
42	Phosphorylation	TQQVHVLSLDQIRAI HHHEEEEEHHHHHHH	28.89	22817900
52	Phosphorylation	QIRAIRNTNEYTEGP HHHHHCCCCCCCCCC	21.41	28152594
55	Phosphorylation	AIRNTNEYTEGPTVV HHCCCCCCCCCCEEC	16.50	21082442
56	Phosphorylation	IRNTNEYTEGPTVVP HCCCCCCCCCCEECC	28.43	28152594
60	Phosphorylation	NEYTEGPTVVPRPGL CCCCCCCEECCCCCC	45.02	28152594
75	Phosphorylation	KPAPRPSTQHKHERL CCCCCCCCCCHHHHH	37.06	20804972
78	Methylation	PRPSTQHKHERLHGL CCCCCCCHHHHHCCC	37.03	23644510
97	Phosphorylation	QPPRLQHSQVHSSAR CCCCCCCCHHCCCCC	22.42	27174698
101	Phosphorylation	LQHSQVHSSARAPLS CCCCHHCCCCCCCCC	27.17	27174698
102	Phosphorylation	QHSQVHSSARAPLSR CCCHHCCCCCCCCCC	13.59	27174698
108	Phosphorylation	SSARAPLSRSISTVS CCCCCCCCCCEEEEC	23.95	27174698
110	Phosphorylation	ARAPLSRSISTVSSG CCCCCCCCEEEECCC	19.95	27470641
112	Phosphorylation	APLSRSISTVSSGSR CCCCCCEEEECCCCC	24.81	16479008
113	Phosphorylation	PLSRSISTVSSGSRS CCCCCEEEECCCCCC	23.80	24425749
115	Phosphorylation	SRSISTVSSGSRSST CCCEEEECCCCCCCC	29.12	22817900
116	Phosphorylation	RSISTVSSGSRSSTR CCEEEECCCCCCCCC	36.13	22817900
118	Phosphorylation	ISTVSSGSRSSTRTS EEEECCCCCCCCCCC	30.82	22817900
120	Phosphorylation	TVSSGSRSSTRTSTS EECCCCCCCCCCCCC	37.45	23312004
121	Phosphorylation	VSSGSRSSTRTSTSS ECCCCCCCCCCCCCC	22.31	16479008
122	Phosphorylation	SSGSRSSTRTSTSSS CCCCCCCCCCCCCCC	38.93	23312004
124	Phosphorylation	GSRSSTRTSTSSSSS CCCCCCCCCCCCCHH	36.12	-
128	Phosphorylation	STRTSTSSSSSEQRL CCCCCCCCCHHHHHH	34.04	-
131	Phosphorylation	TSTSSSSSEQRLLGS CCCCCCHHHHHHHCC	39.43	-
138	Phosphorylation	SEQRLLGSSFSSGPV HHHHHHCCCCCCCCC	28.34	29255136
139	Phosphorylation	EQRLLGSSFSSGPVA HHHHHCCCCCCCCCC	27.61	29255136
141	Phosphorylation	RLLGSSFSSGPVADG HHHCCCCCCCCCCCC	36.01	29255136
142	Phosphorylation	LLGSSFSSGPVADGI HHCCCCCCCCCCCCE	45.14	29255136
156	Phosphorylation	IIRVQPKSELKPGEL EEEECCCCCCCCCCC	55.64	22817900
159	Ubiquitination	VQPKSELKPGELKPL ECCCCCCCCCCCCCC	47.10	29967540
164	Ubiquitination	ELKPGELKPLSKEDL CCCCCCCCCCCHHHC	39.34	29967540
167	Phosphorylation	PGELKPLSKEDLGLH CCCCCCCCHHHCCCE	42.39	25056879
168	Ubiquitination	GELKPLSKEDLGLHA CCCCCCCHHHCCCEE	64.03	29967540
176	Phosphorylation	EDLGLHAYRCEDCGK HHCCCEEEECCCCCC	12.68	22817900
190	Phosphorylation	KCKCKECTYPRPLPS CCCCCCCCCCCCCCC	37.34	22817900
191	Phosphorylation	CKCKECTYPRPLPSD CCCCCCCCCCCCCCC	14.65	22817900
197	Phosphorylation	TYPRPLPSDWICDKQ CCCCCCCCCCCCCCH	53.94	22817900
208	Phosphorylation	CDKQCLCSAQNVIDY CCCHHCCCCCCCCCC	21.68	22461510
215	Phosphorylation	SAQNVIDYGTCVCCV CCCCCCCCCHHEEEE	11.83	22461510
227	Phosphorylation	CCVKGLFYHCSNDDE EEEEHHHEECCCCCC	13.63	22817900
269	Phosphorylation	FLPCLWCYLPAKGCL HHHHHHHHCCCCHHH	12.25	22817900
283	Phosphorylation	LKLCQGCYDRVNRPG HHHHCCHHHHCCCCC	17.38	22817900
296	Phosphorylation	PGCRCKNSNTVCCKV CCCCCCCCCCEEEEC	21.26	-
298	Phosphorylation	CRCKNSNTVCCKVPT CCCCCCCCEEEECCC	18.10	-
305	Phosphorylation	TVCCKVPTVPPRNFE CEEEECCCCCCCCCC	48.94	22817900
313	Ubiquitination	VPPRNFEKPT----- CCCCCCCCCC-----	50.23	-

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
55	Y	Phosphorylation	Kinase	SRC	P12931	PSP
55	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
75	T	Phosphorylation	Kinase	DYR1A	Q13627	PhosphoELM
112	S	Phosphorylation	Kinase	MKNK1	Q9BUB5	GPS
112	S	Phosphorylation	Kinase	MKNK2	Q9HBH9	GPS
121	S	Phosphorylation	Kinase	MKNK1	Q9BUB5	GPS
121	S	Phosphorylation	Kinase	MKNK2	Q9HBH9	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:11983899
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH2	O43255	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:19864419

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPY2_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 SPY2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI51_HUMAN	TRIM51	physical	16189514
ATL4_HUMAN	ADAMTSL4	physical	16189514
KR412_HUMAN	KRTAP4-12	physical	16189514
RAF1_HUMAN	RAF1	physical	12717443
CBL_HUMAN	CBL	physical	11053437
CBL_HUMAN	CBL	physical	12234920
GRB2_HUMAN	GRB2	physical	10940627
CBL_HUMAN	CBL	physical	18273061
TESK1_HUMAN	TESK1	physical	17974561
PP2AA_HUMAN	PPP2CA	physical	17974561
CBL_HUMAN	CBL	physical	17974561
CBL_HUMAN	CBL	physical	12593796
CBL_HUMAN	CBL	physical	12593795
SIAH2_HUMAN	SIAH2	physical	16888801
CBL_HUMAN	CBL	physical	20124286
CBL_HUMAN	CBL	physical	20461437
NEDD4_HUMAN	NEDD4	physical	19864419
EGLN2_HUMAN	EGLN2	physical	22006925
SDHB_HUMAN	SDHB	physical	21900206
ZN266_HUMAN	ZNF266	physical	21900206
ZBT16_HUMAN	ZBTB16	physical	21900206
UBR1_HUMAN	UBR1	physical	21900206
FBN1_HUMAN	FBN1	physical	21900206
CATB_HUMAN	CTSB	physical	21900206
CRIP2_HUMAN	CRIP2	physical	21900206
DYN2_HUMAN	DNM2	physical	21900206
SEM5B_HUMAN	SEMA5B	physical	21900206
F219A_HUMAN	FAM219A	physical	21900206
NUBP1_HUMAN	NUBP1	physical	21900206
CYTB_HUMAN	CSTB	physical	21900206
DPYL1_HUMAN	CRMP1	physical	21900206
NR1H2_HUMAN	NR1H2	physical	21900206
RTF2_HUMAN	RTFDC1	physical	21900206
SH3K1_HUMAN	SH3KBP1	physical	15962011
CBL_HUMAN	CBL	physical	15962011
VPS25_HUMAN	VPS25	physical	21543492
VPS36_HUMAN	VPS36	physical	21543492
GRB2_HUMAN	GRB2	physical	17255109
CBL_HUMAN	CBL	physical	17255109
2AAA_HUMAN	PPP2R1A	physical	17255109
PP2AA_HUMAN	PPP2CA	physical	17255109
CBL_HUMAN	CBL	physical	12815057
SPY1_HUMAN	SPRY1	physical	15004239
SPY4_HUMAN	SPRY4	physical	15004239
CBL_HUMAN	CBL	physical	15004239
CBL_HUMAN	CBL	physical	16479008
GRB2_HUMAN	GRB2	physical	16893902
CBL_HUMAN	CBL	physical	16893902
CTNA3_HUMAN	CTNNA3	physical	23718855
PTN11_MOUSE	Ptpn11	physical	24216759
ITSN1_MOUSE	Itsn1	physical	24216759
KDM1A_HUMAN	KDM1A	physical	23455924
SPY2_HUMAN	SPRY2	physical	25416956
FRS3_HUMAN	FRS3	physical	25416956
UBP20_HUMAN	USP20	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
MABP1_HUMAN	MAPKBP1	physical	25416956
ZDH17_HUMAN	ZDHHC17	physical	25416956
PACN3_HUMAN	PACSIN3	physical	25416956
SH3K1_HUMAN	SH3KBP1	physical	25416956
UBS3A_HUMAN	UBASH3A	physical	25416956
FAIM1_HUMAN	FAIM	physical	25416956
RYDEN_HUMAN	C19orf66	physical	25416956
3BHS7_HUMAN	HSD3B7	physical	25416956
TXND5_HUMAN	TXNDC5	physical	25416956
KR412_HUMAN	KRTAP4-12	physical	25416956
KRA92_HUMAN	KRTAP9-2	physical	25416956
ATRIP_HUMAN	ATRIP	physical	25416956
ZN587_HUMAN	ZNF587	physical	25416956
UBS3B_HUMAN	UBASH3B	physical	25416956
KRA94_HUMAN	KRTAP9-4	physical	25416956
LONF1_HUMAN	LONRF1	physical	25416956
CTSR1_HUMAN	CATSPER1	physical	25416956
HEXI2_HUMAN	HEXIM2	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
LCE4A_HUMAN	LCE4A	physical	25416956
LCE1B_HUMAN	LCE1B	physical	25416956
LCE2D_HUMAN	LCE2D	physical	25416956
LCE3C_HUMAN	LCE3C	physical	25416956
LCE3E_HUMAN	LCE3E	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR101_HUMAN	KRTAP10-1	physical	25416956
KR10B_HUMAN	KRTAP10-11	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
KRA56_HUMAN	KRTAP5-6	physical	25416956
KR411_HUMAN	KRTAP4-11	physical	25416956
PLSI_HUMAN	PLS1	physical	26186194
ZDH17_HUMAN	ZDHHC17	physical	26186194
VANG1_HUMAN	VANGL1	physical	26186194
UB2D2_HUMAN	UBE2D2	physical	26186194
UB2E3_HUMAN	UBE2E3	physical	26186194
SNX3_HUMAN	SNX3	physical	26186194
VANG2_HUMAN	VANGL2	physical	26186194
CAB39_HUMAN	CAB39	physical	26186194
OTX1_HUMAN	OTX1	physical	21516116
UBS3A_HUMAN	UBASH3A	physical	21516116
3BHS7_HUMAN	HSD3B7	physical	21516116
TM14B_HUMAN	TMEM14B	physical	21516116
HIF1A_HUMAN	HIF1A	physical	27281823
UB2D2_HUMAN	UBE2D2	physical	28514442
PLSI_HUMAN	PLS1	physical	28514442
S10AD_HUMAN	S100A13	physical	28514442
SNX3_HUMAN	SNX3	physical	28514442
TES_HUMAN	TES	physical	28514442
ZDH17_HUMAN	ZDHHC17	physical	28514442
CGL_HUMAN	CTH	physical	28514442
BRAF_HUMAN	BRAF	physical	19690147
KPCD_HUMAN	PRKCD	physical	19458088
KPCD1_HUMAN	PRKD1	physical	19458088

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 SPY2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-142, ANDMASS SPECTROMETRY.	19690332 [Abstract]