CRKL_MOUSE - dbPTM
CRKL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRKL_MOUSE
UniProt AC P47941
Protein Name Crk-like protein
Gene Name Crkl
Organism Mus musculus (Mouse).
Sequence Length 303
Subcellular Localization
Protein Description May mediate the transduction of intracellular signals..
Protein Sequence MSSARFDSSDRSAWYMGPVTRQEAQTRLQGQRHGMFLVRDSSTCPGDYVLSVSENSRVSHYIINSLPNRRFKIGDQEFDHLPALLEFYKIHYLDTTTLIEPAPRYPSPPVGSVSAPNLPTAEENLEYVRTLYDFPGNDAEDLPFKKGELLVIIEKPEEQWWSARNKDGRVGMIPVPYVEKLVRSSPHGKHGNRNSNSYGIPEPAHAYAQPQTTTPLPTVASTPGAAINPLPSTQNGPVFAKAIQKRVPCAYDKTALALEVGDIVKVTRMNINGQWEGEVNGRKGLFPFTHVKIFDPQNPDDNE
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
41PhosphorylationGMFLVRDSSTCPGDY
CEEEEECCCCCCCCE		19.5825619855
42PhosphorylationMFLVRDSSTCPGDYV
EEEEECCCCCCCCEE		38.0125619855
43PhosphorylationFLVRDSSTCPGDYVL
EEEECCCCCCCCEEE		27.0325619855
48PhosphorylationSSTCPGDYVLSVSEN
CCCCCCCEEEEEECC		14.8125619855
51PhosphorylationCPGDYVLSVSENSRV
CCCCEEEEEECCCCE		17.3525619855
53PhosphorylationGDYVLSVSENSRVSH
CCEEEEEECCCCEEE		27.9025619855
56PhosphorylationVLSVSENSRVSHYII
EEEEECCCCEEEEEE		29.9725619855
92PhosphorylationLEFYKIHYLDTTTLI
HHHHEEEEEECCCCC		15.1122817900
95PhosphorylationYKIHYLDTTTLIEPA
HEEEEEECCCCCCCC		21.0523984901
96PhosphorylationKIHYLDTTTLIEPAP
EEEEEECCCCCCCCC		21.1923984901
97PhosphorylationIHYLDTTTLIEPAPR
EEEEECCCCCCCCCC		28.0323984901
105PhosphorylationLIEPAPRYPSPPVGS
CCCCCCCCCCCCCCC		13.6524925903
107PhosphorylationEPAPRYPSPPVGSVS
CCCCCCCCCCCCCCC		32.6625521595
112PhosphorylationYPSPPVGSVSAPNLP
CCCCCCCCCCCCCCC		17.0925521595
114PhosphorylationSPPVGSVSAPNLPTA
CCCCCCCCCCCCCCH		39.4426239621
120PhosphorylationVSAPNLPTAEENLEY
CCCCCCCCHHHHHHH		50.2824925903
127PhosphorylationTAEENLEYVRTLYDF
CHHHHHHHHEEHHCC		9.8224925903
130PhosphorylationENLEYVRTLYDFPGN
HHHHHHEEHHCCCCC		21.4522499769
132PhosphorylationLEYVRTLYDFPGNDA
HHHHEEHHCCCCCCH		18.2228725479
177PhosphorylationVGMIPVPYVEKLVRS
EEEEECHHHHHHHHC		22.8329514104
180UbiquitinationIPVPYVEKLVRSSPH
EECHHHHHHHHCCCC		42.09-
184PhosphorylationYVEKLVRSSPHGKHG
HHHHHHHCCCCCCCC		40.5222324799
185PhosphorylationVEKLVRSSPHGKHGN
HHHHHHCCCCCCCCC		15.4530352176
195PhosphorylationGKHGNRNSNSYGIPE
CCCCCCCCCCCCCCC		24.7425168779
197PhosphorylationHGNRNSNSYGIPEPA
CCCCCCCCCCCCCCC		25.2625619855
198PhosphorylationGNRNSNSYGIPEPAH
CCCCCCCCCCCCCCH		24.2725619855
207PhosphorylationIPEPAHAYAQPQTTT
CCCCCHHCCCCCCCC		8.9022169110
212PhosphorylationHAYAQPQTTTPLPTV
HHCCCCCCCCCCCCC		39.0425619855
213PhosphorylationAYAQPQTTTPLPTVA
HCCCCCCCCCCCCCC		22.5925619855
214PhosphorylationYAQPQTTTPLPTVAS
CCCCCCCCCCCCCCC		26.6425619855
218PhosphorylationQTTTPLPTVASTPGA
CCCCCCCCCCCCCCC		36.0725619855
221PhosphorylationTPLPTVASTPGAAIN
CCCCCCCCCCCCCCC		30.6925619855
222PhosphorylationPLPTVASTPGAAINP
CCCCCCCCCCCCCCC		18.9225619855
232PhosphorylationAAINPLPSTQNGPVF
CCCCCCCCCCCCCHH		50.7525619855
233PhosphorylationAINPLPSTQNGPVFA
CCCCCCCCCCCCHHH		24.9025619855
249GlutathionylationAIQKRVPCAYDKTAL
HHHHHCCCCCCCCEE		5.1224333276
251PhosphorylationQKRVPCAYDKTALAL
HHHCCCCCCCCEEEE		25.3722499769
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
-KUbiquitinationE3 ubiquitin ligaseCblP22682
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRKL_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBLB_MOUSECblbphysical
12697763
ZAP70_MOUSEZap70physical
12697763
ABL1_MOUSEAbl1physical
8978305
SOS1_MOUSESos1physical
8978305
PAXI_MOUSEPxnphysical
8978305
CBL_MOUSECblphysical
8978305
BCAR1_MOUSEBcar1physical
8978305
PRDX1_MOUSEPrdx1physical
20697350
CH60_MOUSEHspd1physical
20697350
SPN90_MOUSENckipsdphysical
20697350
CBL_MOUSECblphysical
10391678
DAB1_MOUSEDab1physical
15062102
CBL_MOUSECblphysical
9067577
CBL_MOUSECblphysical
11069064
SHIP1_MOUSEInpp5dphysical
11031258
CBL_MOUSECblphysical
11031258
P85A_MOUSEPik3r1physical
11031258
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRKL_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132 AND TYR-207, ANDMASS SPECTROMETRY.
"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-251, AND MASSSPECTROMETRY.

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