dbPTM

CRKL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRKL_HUMAN
UniProt AC	P46109
Protein Name	Crk-like protein
Gene Name	CRKL
Organism	Homo sapiens (Human).
Sequence Length	303
Subcellular Localization
Protein Description	May mediate the transduction of intracellular signals..
Protein Sequence	MSSARFDSSDRSAWYMGPVSRQEAQTRLQGQRHGMFLVRDSSTCPGDYVLSVSENSRVSHYIINSLPNRRFKIGDQEFDHLPALLEFYKIHYLDTTTLIEPAPRYPSPPMGSVSAPNLPTAEDNLEYVRTLYDFPGNDAEDLPFKKGEILVIIEKPEEQWWSARNKDGRVGMIPVPYVEKLVRSSPHGKHGNRNSNSYGIPEPAHAYAQPQTTTPLPAVSGSPGAAITPLPSTQNGPVFAKAIQKRVPCAYDKTALALEVGDIVKVTRMNINGQWEGEVNGRKGLFPFTHVKIFDPQNPDENE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Methylation	ARFDSSDRSAWYMGP CCCCCCCCCCCCCCC	30.17	-
15	Phosphorylation	SSDRSAWYMGPVSRQ CCCCCCCCCCCCCHH	7.60	23917254
41	Phosphorylation	GMFLVRDSSTCPGDY CEEEEECCCCCCCCE	19.58	22167270
42	Phosphorylation	MFLVRDSSTCPGDYV EEEEECCCCCCCCEE	38.01	23401153
43	Phosphorylation	FLVRDSSTCPGDYVL EEEECCCCCCCCEEE	27.03	22167270
44	Glutathionylation	LVRDSSTCPGDYVLS EEECCCCCCCCEEEE	3.71	22555962
48	Phosphorylation	SSTCPGDYVLSVSEN CCCCCCCEEEEEECC	14.81	23663014
51	Phosphorylation	CPGDYVLSVSENSRV CCCCEEEEEECCCCE	17.35	23663014
53	Phosphorylation	GDYVLSVSENSRVSH CCEEEEEECCCCEEE	27.90	23403867
56	Phosphorylation	VLSVSENSRVSHYII EEEEECCCCEEEEEE	29.97	23403867
59	Phosphorylation	VSENSRVSHYIINSL EECCCCEEEEEECCC	14.95	28152594
61	Phosphorylation	ENSRVSHYIINSLPN CCCCEEEEEECCCCC	8.94	28152594
92	Phosphorylation	LEFYKIHYLDTTTLI HHHHEEEEEECCCCC	15.11	23090842
95	Phosphorylation	YKIHYLDTTTLIEPA HEEEEEECCCCCCCC	21.05	23090842
96	Phosphorylation	KIHYLDTTTLIEPAP EEEEEECCCCCCCCC	21.19	23090842
97	Phosphorylation	IHYLDTTTLIEPAPR EEEEECCCCCCCCCC	28.03	23090842
105	Phosphorylation	LIEPAPRYPSPPMGS CCCCCCCCCCCCCCC	13.65	30278072
107	Phosphorylation	EPAPRYPSPPMGSVS CCCCCCCCCCCCCCC	32.47	23401153
110	Sulfoxidation	PRYPSPPMGSVSAPN CCCCCCCCCCCCCCC	7.69	30846556
112	Phosphorylation	YPSPPMGSVSAPNLP CCCCCCCCCCCCCCC	13.47	30278072
114	Phosphorylation	SPPMGSVSAPNLPTA CCCCCCCCCCCCCCH	39.44	25159151
120	O-linked_Glycosylation	VSAPNLPTAEDNLEY CCCCCCCCHHHHHHH	45.93	OGP
120	Phosphorylation	VSAPNLPTAEDNLEY CCCCCCCCHHHHHHH	45.93	30108239
127	Phosphorylation	TAEDNLEYVRTLYDF CHHHHHHHEEEHHCC	9.82	22115753
130	Phosphorylation	DNLEYVRTLYDFPGN HHHHHEEEHHCCCCC	21.45	25106551
132	Phosphorylation	LEYVRTLYDFPGNDA HHHEEEHHCCCCCCH	18.22	20007894
145	Acetylation	DAEDLPFKKGEILVI CHHHCCCCCCEEEEE	58.91	25953088
145	Ubiquitination	DAEDLPFKKGEILVI CHHHCCCCCCEEEEE	58.91	32015554
172	Sulfoxidation	NKDGRVGMIPVPYVE CCCCCEEEEECHHHH	2.61	30846556
177	Phosphorylation	VGMIPVPYVEKLVRS EEEEECHHHHHHHHC	22.83	27362937
180	Acetylation	IPVPYVEKLVRSSPH EECHHHHHHHHCCCC	42.09	30587891
180	Ubiquitination	IPVPYVEKLVRSSPH EECHHHHHHHHCCCC	42.09	24816145
184	Phosphorylation	YVEKLVRSSPHGKHG HHHHHHHCCCCCCCC	40.52	23898821
185	Phosphorylation	VEKLVRSSPHGKHGN HHHHHHCCCCCCCCC	15.45	25849741
195	Phosphorylation	GKHGNRNSNSYGIPE CCCCCCCCCCCCCCC	24.74	21945579
197	Phosphorylation	HGNRNSNSYGIPEPA CCCCCCCCCCCCCCC	25.26	21945579
198	Phosphorylation	GNRNSNSYGIPEPAH CCCCCCCCCCCCCCC	24.27	21945579
207	Phosphorylation	IPEPAHAYAQPQTTT CCCCCCCCCCCCCCC	8.90	15268851
212	Phosphorylation	HAYAQPQTTTPLPAV CCCCCCCCCCCCCCC	39.04	21945579
213	Phosphorylation	AYAQPQTTTPLPAVS CCCCCCCCCCCCCCC	22.59	21945579
214	O-linked_Glycosylation	YAQPQTTTPLPAVSG CCCCCCCCCCCCCCC	26.64	OGP
214	Phosphorylation	YAQPQTTTPLPAVSG CCCCCCCCCCCCCCC	26.64	21945579
220	Phosphorylation	TTPLPAVSGSPGAAI CCCCCCCCCCCCCEE	35.34	21945579
222	Phosphorylation	PLPAVSGSPGAAITP CCCCCCCCCCCEECC	16.80	21945579
228	O-linked_Glycosylation	GSPGAAITPLPSTQN CCCCCEECCCCCCCC	17.66	OGP
228	Phosphorylation	GSPGAAITPLPSTQN CCCCCEECCCCCCCC	17.66	21945579
232	Phosphorylation	AAITPLPSTQNGPVF CEECCCCCCCCCCHH	50.75	21945579
233	Phosphorylation	AITPLPSTQNGPVFA EECCCCCCCCCCHHH	24.90	21945579
251	Phosphorylation	QKRVPCAYDKTALAL HHHCCCCCCCCEEEE	25.37	27273156
253	Ubiquitination	RVPCAYDKTALALEV HCCCCCCCCEEEEEC	24.03	29967540
253	Acetylation	RVPCAYDKTALALEV HCCCCCCCCEEEEEC	24.03	23749302
254	Phosphorylation	VPCAYDKTALALEVG CCCCCCCCEEEEECC	24.81	28152594
283	Ubiquitination	EGEVNGRKGLFPFTH EEEECCCCCEEECEE	62.45	29967540
292	Ubiquitination	LFPFTHVKIFDPQNP EEECEEEEECCCCCC	30.01	22817900

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
207	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
207	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
207	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:12671687

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAXI_HUMAN	PXN	physical	7493940
ABL1_HUMAN	ABL1	physical	8978305
CBL_HUMAN	CBL	physical	10907644
M4K1_HUMAN	MAP4K1	physical	9788432
RPGF1_HUMAN	RAPGEF1	physical	9820532
CASL_HUMAN	NEDD9	physical	9820532
ABL1_HUMAN	ABL1	physical	9820532
FCGR1_HUMAN	FCGR1A	physical	9820532
RPGF1_HUMAN	RAPGEF1	physical	11167825
RPGF1_HUMAN	RAPGEF1	physical	9374471
TYK2_HUMAN	TYK2	physical	9374471
PAXI_HUMAN	PXN	physical	11463817
STA5A_HUMAN	STAT5A	physical	9837784
KSYK_HUMAN	SYK	physical	11313252
WASP_HUMAN	WAS	physical	11313252
CASL_HUMAN	NEDD9	physical	9498705
BCAR1_HUMAN	BCAR1	physical	9498705
BLNK_HUMAN	BLNK	physical	11489945
IRS4_HUMAN	IRS4	physical	9614078
P85B_HUMAN	PIK3R2	physical	9092574
KIT_HUMAN	KIT	physical	9092574
CBL_HUMAN	CBL	physical	9092574
CBL_HUMAN	CBL	physical	10204582
CBL_HUMAN	CBL	physical	9162067
CASL_HUMAN	NEDD9	physical	9162067
CBL_HUMAN	CBL	physical	9461587
P85A_HUMAN	PIK3R1	physical	9461587
SHC1_HUMAN	SHC1	physical	9344843
PTN11_HUMAN	PTPN11	physical	9344843
CBL_HUMAN	CBL	physical	9344843
RPGF1_HUMAN	RAPGEF1	physical	9344843
EPOR_HUMAN	EPOR	physical	9344843
M4K1_HUMAN	MAP4K1	physical	9891069
RPGF1_HUMAN	RAPGEF1	physical	11466412
EPOR_HUMAN	EPOR	physical	11443118
SHIP1_HUMAN	INPP5D	physical	11443118
GAB2_HUMAN	GAB2	physical	11334882
M4K1_HUMAN	MAP4K1	physical	11279207
DOCK2_HUMAN	DOCK2	physical	12393632
GAB1_HUMAN	GAB1	physical	10753869
RPGF1_HUMAN	RAPGEF1	physical	10753869
CBLB_HUMAN	CBLB	physical	10022120
MSL1_HUMAN	MSL1	physical	18654987
PKHA1_HUMAN	PLEKHA1	physical	18654987
MEGF6_HUMAN	MEGF6	physical	18654987
LTBP4_HUMAN	LTBP4	physical	18654987
GRN_HUMAN	GRN	physical	18654987
PLS1_HUMAN	PLSCR1	physical	18654987
LAMA5_HUMAN	LAMA5	physical	18654987
NOTC2_HUMAN	NOTCH2	physical	18654987
RPGF1_HUMAN	RAPGEF1	physical	10907644
P85A_HUMAN	PIK3R1	physical	11418612
CBL_HUMAN	CBL	physical	7545163
CBL_HUMAN	CBL	physical	9311917
RPGF1_HUMAN	RAPGEF1	physical	9311917
CBL_HUMAN	CBL	physical	9129019
EPOR_HUMAN	EPOR	physical	9129019
RPGF1_HUMAN	RAPGEF1	physical	9129019
ABL1_HUMAN	ABL1	physical	19823681
CBL_HUMAN	CBL	physical	10608804
RPGF1_HUMAN	RAPGEF1	physical	10608804
CBL_HUMAN	CBL	physical	10657627
CBL_HUMAN	CBL	physical	11263968
CBL_HUMAN	CBL	physical	8524328
ABL1_HUMAN	ABL1	physical	8524328
STA5A_HUMAN	STAT5A	physical	9657743
CBL_HUMAN	CBL	physical	9195915
CBL_HUMAN	CBL	physical	11399323
CBL_HUMAN	CBL	physical	11157475
ABL1_HUMAN	ABL1	physical	9710592
CBL_HUMAN	CBL	physical	15358160
ABL1_HUMAN	ABL1	physical	14604282
CBL_HUMAN	CBL	physical	14604282
CBL_HUMAN	CBL	physical	8662998
DOK1_HUMAN	DOK1	physical	9822717
CBL_HUMAN	CBL	physical	11553620
P85B_HUMAN	PIK3R2	physical	11553620
DOK1_HUMAN	DOK1	physical	11553620
WAC_HUMAN	WAC	physical	21988832
PHC2_HUMAN	PHC2	physical	21988832
RL31_HUMAN	RPL31	physical	21988832
TYY1_HUMAN	YY1	physical	21988832
LIPB2_HUMAN	PPFIBP2	physical	21988832
KHDR1_HUMAN	KHDRBS1	physical	21988832
TNS2_HUMAN	TENC1	physical	21988832
GARE1_HUMAN	GAREM	physical	21988832
SHAN3_HUMAN	SHANK3	physical	21988832
CBL_HUMAN	CBL	physical	24886428
RPGF1_HUMAN	RAPGEF1	physical	16443220
HIP1R_HUMAN	HIP1R	physical	26344197
HNRH2_HUMAN	HNRNPH2	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
AREL1_HUMAN	AREL1	physical	25814554
SOCS1_HUMAN	SOCS1	physical	25814554
TM168_HUMAN	TMEM168	physical	25814554
APOB_HUMAN	APOB	physical	26496610
DDX6_HUMAN	DDX6	physical	26496610
DOCK1_HUMAN	DOCK1	physical	26496610
RPGF1_HUMAN	RAPGEF1	physical	26496610
SOS1_HUMAN	SOS1	physical	26496610
MPZL1_HUMAN	MPZL1	physical	26496610
MARF1_HUMAN	KIAA0430	physical	26496610
TELO2_HUMAN	TELO2	physical	26496610
TRAP1_HUMAN	TRAP1	physical	26496610
PNRC1_HUMAN	PNRC1	physical	26496610
EDC4_HUMAN	EDC4	physical	26496610
IMPCT_HUMAN	IMPACT	physical	26496610
DCP1A_HUMAN	DCP1A	physical	26496610
UBL5_HUMAN	UBL5	physical	26496610
ELMO2_HUMAN	ELMO2	physical	26496610
PEAK1_HUMAN	PEAK1	physical	26496610
DOCK5_HUMAN	DOCK5	physical	26496610
EDC3_HUMAN	EDC3	physical	26496610
PRR3_HUMAN	PRR3	physical	26496610
GORAB_HUMAN	GORAB	physical	26496610
PRAG1_HUMAN	SGK223	physical	26496610
DCP2_HUMAN	DCP2	physical	26496610
CO054_HUMAN	C15orf54	physical	26496610
PGFRA_HUMAN	PDGFRA	physical	25241761

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 CRKL_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 TYR-127, AND MASSSPECTROMETRY.	19690332 [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-132; TYR-207 ANDTYR-251, AND MASS SPECTROMETRY.	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-132 AND TYR-198, ANDMASS SPECTROMETRY.	17389395 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207 AND TYR-251, ANDMASS SPECTROMETRY.	15592455 [Abstract]