NCK1_MOUSE - dbPTM
NCK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCK1_MOUSE
UniProt AC Q99M51
Protein Name Cytoplasmic protein NCK1
Gene Name Nck1
Organism Mus musculus (Mouse).
Sequence Length 377
Subcellular Localization Cytoplasm. Endoplasmic reticulum. Nucleus. Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hy
Protein Description Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA (By similarity)..
Protein Sequence MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDTASPADDSFVDPGERLYDLNMPAFVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQIGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTIMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS
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
2Acetylation------MAEEVVVVA
------CCCEEEEEE		22.96-
35PhosphorylationRLWLLDDSKSWWRVR
CEEEECCCCCHHHHC		28.4026745281
53PhosphorylationNKTGFVPSNYVERKN
CCCCCCCHHHHHHCC		35.1829514104
55PhosphorylationTGFVPSNYVERKNSA
CCCCCHHHHHHCCCH		14.1829514104
61PhosphorylationNYVERKNSARKASIV
HHHHHCCCHHHHHHH		32.2723375375
66PhosphorylationKNSARKASIVKNLKD
CCCHHHHHHHHHHHH		30.8323375375
74PhosphorylationIVKNLKDTLGIGKVK
HHHHHHHHHCCCCCC		25.8722817900
85PhosphorylationGKVKRKPSVPDTASP
CCCCCCCCCCCCCCC		49.6827087446
89PhosphorylationRKPSVPDTASPADDS
CCCCCCCCCCCCCCC		23.9827742792
91PhosphorylationPSVPDTASPADDSFV
CCCCCCCCCCCCCCC		23.7826824392
96PhosphorylationTASPADDSFVDPGER
CCCCCCCCCCCCCCC		27.9326824392
105PhosphorylationVDPGERLYDLNMPAF
CCCCCCEECCCCCEE		25.3025521595
147PhosphorylationSDGWWRGSYNGQIGW
CCCEEECCCCCEEEE		13.5725619855
148PhosphorylationDGWWRGSYNGQIGWF
CCEEECCCCCEEEEE		26.5725619855
157PhosphorylationGQIGWFPSNYVTEEG
CEEEEECHHHCCCCC		31.1725619855
159PhosphorylationIGWFPSNYVTEEGDS
EEEECHHHCCCCCCC		17.0625619855
161PhosphorylationWFPSNYVTEEGDSPL
EECHHHCCCCCCCCC		20.2625619855
166PhosphorylationYVTEEGDSPLGDHVG
HCCCCCCCCCHHHHC		32.6424925903
174PhosphorylationPLGDHVGSLSEKLAA
CCHHHHCCHHHHHHH		27.8625619855
176PhosphorylationGDHVGSLSEKLAAVV
HHHHCCHHHHHHHHH		34.0925619855
246PhosphorylationVGLVPKNYVTIMQNN
EEECCCCEEEEEECC		12.7029514104
248PhosphorylationLVPKNYVTIMQNNPL
ECCCCEEEEEECCCC		10.6025367039
262PhosphorylationLTSGLEPSPPQCDYI
CCCCCCCCCCCCCCC		39.5825293948
268PhosphorylationPSPPQCDYIRPSLTG
CCCCCCCCCCHHHCC		13.3725367039
272PhosphorylationQCDYIRPSLTGKFAG
CCCCCCHHHCCCCCC		28.8125293948
274PhosphorylationDYIRPSLTGKFAGNP
CCCCHHHCCCCCCCC		42.5425293948
312PhosphorylationFLIRDSESSPNDFSV
EEEECCCCCCCCEEE		55.8630635358
313PhosphorylationLIRDSESSPNDFSVS
EEECCCCCCCCEEEE		24.5429899451
318PhosphorylationESSPNDFSVSLKAQG
CCCCCCEEEEEEECC		17.4130635358
337PhosphorylationFKVQLKETVYCIGQR
EEEEEEEEEEEEECC		18.3925367039
339PhosphorylationVQLKETVYCIGQRKF
EEEEEEEEEEECCCC		5.9325367039
347PhosphorylationCIGQRKFSTMEELVE
EEECCCCCCHHHHHH		29.8528833060
348PhosphorylationIGQRKFSTMEELVEH
EECCCCCCHHHHHHH		31.5628833060
371PhosphorylationSEQGEKLYLVKHLS-
CCCCCEEEEEEECC-		22.1029514104
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 NCK1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCK1_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 NCK1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBL_MOUSECblphysical
7517397
ACK1_MOUSETnk2physical
16777958
DOK1_MOUSEDok1physical
20697350
ABL1_MOUSEAbl1physical
10967110
CBL_MOUSECblphysical
8635998
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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-105, AND MASSSPECTROMETRY.

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