dbPTM

NCK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NCK1_HUMAN
UniProt AC	P16333
Protein Name	Cytoplasmic protein NCK1
Gene Name	NCK1
Organism	Homo sapiens (Human).
Sequence Length	377
Subcellular Localization	Cytoplasm. Endoplasmic reticulum. Nucleus. Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires the interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation
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. May play a role in cell adhesion and migration through interaction with ephrin receptors..
Protein Sequence	MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEEVVVVA ------CCCEEEEEE	22.96	22223895
12 (in isoform 2)	Phosphorylation	-	35.97	23909892
13	Phosphorylation	VVVAKFDYVAQQEQE EEEEECCEECCCCEE	10.79	-
21 (in isoform 2)	Phosphorylation	-	9.13	25159151
25 (in isoform 2)	Phosphorylation	-	65.46	25159151
27 (in isoform 2)	Phosphorylation	-	59.01	29507054
48	Phosphorylation	VRNSMNKTGFVPSNY HCCCCCCCCCCCHHH	30.74	23882029
53	Phosphorylation	NKTGFVPSNYVERKN CCCCCCCHHHHHHCC	35.18	23882029
55	Phosphorylation	TGFVPSNYVERKNSA CCCCCHHHHHHCCCH	14.18	26074081
61	Phosphorylation	NYVERKNSARKASIV HHHHHCCCHHHHHHH	32.27	26074081
66	Phosphorylation	KNSARKASIVKNLKD CCCHHHHHHHHHHHH	30.83	29514088
69	Ubiquitination	ARKASIVKNLKDTLG HHHHHHHHHHHHHHC	55.69	-
74	Phosphorylation	IVKNLKDTLGIGKVK HHHHHHHHHCCCCCC	25.87	18212344
79	Acetylation	KDTLGIGKVKRKPSV HHHHCCCCCCCCCCC	42.54	25953088
79	Ubiquitination	KDTLGIGKVKRKPSV HHHHCCCCCCCCCCC	42.54	-
85	Phosphorylation	GKVKRKPSVPDSASP CCCCCCCCCCCCCCC	49.68	29255136
89	Phosphorylation	RKPSVPDSASPADDS CCCCCCCCCCCCCCC	25.28	29255136
91	Phosphorylation	PSVPDSASPADDSFV CCCCCCCCCCCCCCC	25.27	29255136
96	Phosphorylation	SASPADDSFVDPGER CCCCCCCCCCCCCCC	27.93	21945579
105	Phosphorylation	VDPGERLYDLNMPAY CCCCCCCCCCCCCEE	25.30	25159151
109	Sulfoxidation	ERLYDLNMPAYVKFN CCCCCCCCCEEEEEE	2.33	31801345
112	Phosphorylation	YDLNMPAYVKFNYMA CCCCCCEEEEEEECC	9.78	21945579
117	Phosphorylation	PAYVKFNYMAEREDE CEEEEEEECCCCCCH	10.80	26074081
126	Phosphorylation	AEREDELSLIKGTKV CCCCCHHHCCCCCEE	26.46	26074081
129	Ubiquitination	EDELSLIKGTKVIVM CCHHHCCCCCEEEEE	66.86	-
131	Phosphorylation	ELSLIKGTKVIVMEK HHHCCCCCEEEEEEE	19.69	26074081
147	Phosphorylation	SDGWWRGSYNGQVGW CCCEEECCCCCCEEE	13.57	23663014
148	Phosphorylation	DGWWRGSYNGQVGWF CCEEECCCCCCEEEE	26.57	26074081
157	Phosphorylation	GQVGWFPSNYVTEEG CCEEEECHHHCCCCC	31.17	28450419
159	Phosphorylation	VGWFPSNYVTEEGDS EEEECHHHCCCCCCC	17.06	28450419
161	Phosphorylation	WFPSNYVTEEGDSPL EECHHHCCCCCCCCC	20.26	28787133
166	Phosphorylation	YVTEEGDSPLGDHVG HCCCCCCCCCHHHHC	32.64	25159151
174	Phosphorylation	PLGDHVGSLSEKLAA CCHHHHCCHHHHHHH	27.86	28787133
176	Phosphorylation	GDHVGSLSEKLAAVV HHHHCCHHHHHHHHH	34.09	28450419
178	Ubiquitination	HVGSLSEKLAAVVNN HHCCHHHHHHHHHHC	39.80	-
202	Phosphorylation	VQALYPFSSSNDEEL EEECCCCCCCCCCCC	28.49	27251275
203	Phosphorylation	QALYPFSSSNDEELN EECCCCCCCCCCCCC	33.27	27251275
204	Phosphorylation	ALYPFSSSNDEELNF ECCCCCCCCCCCCCC	47.29	27251275
231	Ubiquitination	ENDPEWWKCRKINGM CCCHHHHHEEEECCE	25.82	-
246	Phosphorylation	VGLVPKNYVTVMQNN EEECCCCEEEEEECC	12.01	20068231
248	Phosphorylation	LVPKNYVTVMQNNPL ECCCCEEEEEECCCC	10.41	27251275
256	Phosphorylation	VMQNNPLTSGLEPSP EEECCCCCCCCCCCC	23.23	20068231
257	Phosphorylation	MQNNPLTSGLEPSPP EECCCCCCCCCCCCC	49.41	29978859
262	Phosphorylation	LTSGLEPSPPQCDYI CCCCCCCCCCCCCCC	39.58	23403867
268	Phosphorylation	PSPPQCDYIRPSLTG CCCCCCCCCCHHHCC	13.37	20068231
272	Phosphorylation	QCDYIRPSLTGKFAG CCCCCCHHHCCCCCC	28.81	23403867
274	Phosphorylation	DYIRPSLTGKFAGNP CCCCHHHCCCCCCCC	42.54	29978859
286	Ubiquitination	GNPWYYGKVTRHQAE CCCCCCCEEEHHHHH	25.06	-
310	Phosphorylation	GDFLIRDSESSPNDF CCEEEECCCCCCCCE	29.54	27251275
312	Phosphorylation	FLIRDSESSPNDFSV EEEECCCCCCCCEEE	55.86	20068231
313	Phosphorylation	LIRDSESSPNDFSVS EEECCCCCCCCEEEE	24.54	25159151
318	Phosphorylation	ESSPNDFSVSLKAQG CCCCCCEEEEEEECC	17.41	28857561
322	Ubiquitination	NDFSVSLKAQGKNKH CCEEEEEEECCCCCC	31.02	-
339	Phosphorylation	VQLKETVYCIGQRKF EEEEEEEEEEECCCC	5.93	25839225
345	Ubiquitination	VYCIGQRKFSTMEEL EEEEECCCCCCHHHH	35.46	-
347	Phosphorylation	CIGQRKFSTMEELVE EEECCCCCCHHHHHH	29.85	28450419
348	Phosphorylation	IGQRKFSTMEELVEH EECCCCCCHHHHHHH	31.56	28450419
357	Ubiquitination	EELVEHYKKAPIFTS HHHHHHHHHCCEEEC	44.35	-
358	Ubiquitination	ELVEHYKKAPIFTSE HHHHHHHHCCEEECC	52.83	-
364	Phosphorylation	KKAPIFTSEQGEKLY HHCCEEECCCCCEEE	19.71	29496907
369	Ubiquitination	FTSEQGEKLYLVKHL EECCCCCEEEEEEEC	49.62	-

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
105	Y	Phosphorylation	Kinase	ABL1	P00519	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NCK1_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 NCK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPHB1_HUMAN	EPHB1	physical	9430661
MINK1_HUMAN	MINK1	physical	15469942
RHG32_HUMAN	ARHGAP32	physical	12819203
MTA1_MOUSE	Mta1	physical	11483358
MTA3_MOUSE	Mta3	physical	11483358
SOS1_HUMAN	SOS1	physical	10206341
DYN1_HUMAN	DNM1	physical	10206341
SOCS1_HUMAN	SOCS1	physical	10022833
PKN2_HUMAN	PKN2	physical	8910519
WASL_HUMAN	WASL	physical	11340081
RRAS_HUMAN	RRAS	physical	10671570
EGFR_HUMAN	EGFR	physical	9362449
KHDR1_HUMAN	KHDRBS1	physical	9362449
M4K4_HUMAN	MAP4K4	physical	9135144
LCP2_HUMAN	LCP2	physical	10229072
SOS1_HUMAN	SOS1	physical	7862111
CASL_HUMAN	NEDD9	physical	8879209
FAK1_HUMAN	PTK2	physical	8879209
DCC_HUMAN	DCC	physical	12149262
EGFR_HUMAN	EGFR	physical	1333047
PGFRB_HUMAN	PDGFRB	physical	1333047
TBK1_HUMAN	TBK1	physical	7706279
SOS1_HUMAN	SOS1	physical	8810325
PAK1_HUMAN	PAK1	physical	11157752
SOCS7_HUMAN	SOCS7	physical	9344857
TNFL6_HUMAN	FASLG	physical	11741599
M4K1_HUMAN	MAP4K1	physical	9891069
CD3E_HUMAN	CD3E	physical	12110186
FAK1_HUMAN	PTK2	physical	11950595
PKN2_HUMAN	PKN2	physical	10026169
PAK1_HUMAN	PAK1	physical	10026169
SOS1_HUMAN	SOS1	physical	10026169
EGFR_HUMAN	EGFR	physical	10026169
PGFRB_HUMAN	PDGFRB	physical	10026169
ABL1_HUMAN	ABL1	physical	11494134
CBL_HUMAN	CBL	physical	11494134
GAB2_HUMAN	GAB2	physical	10391903
WASP_HUMAN	WAS	physical	12135674
KHDR1_HUMAN	KHDRBS1	physical	9010224
PROF1_HUMAN	PFN1	physical	9694849
PAK1_HUMAN	PAK1	physical	8824201
M4K1_HUMAN	MAP4K1	physical	11279207
SPN90_HUMAN	NCKIPSD	physical	11278500
RASA1_HUMAN	RASA1	physical	21664272
RL40_HUMAN	UBA52	physical	21900206
KHDR1_HUMAN	KHDRBS1	physical	22745667
CBL_HUMAN	CBL	physical	9851874
PAK1_HUMAN	PAK1	physical	9851874
P85A_HUMAN	PIK3R1	physical	11418612
SHIP1_HUMAN	INPP5D	physical	22267732
LCP2_HUMAN	LCP2	physical	22267732
UBS3B_HUMAN	UBASH3B	physical	22267732
GRB2_HUMAN	GRB2	physical	22267732
CBL_HUMAN	CBL	physical	10829062
CBL_HUMAN	CBL	physical	10967110
ABL1_HUMAN	ABL1	physical	10967110
TBA1A_HUMAN	TUBA1A	physical	17868192
ERBB3_HUMAN	ERBB3	physical	16273093
DOK1_HUMAN	DOK1	physical	11551902
DOK1_MOUSE	Dok1	physical	10202139
PHC2_HUMAN	PHC2	physical	21988832
SHAN3_HUMAN	SHANK3	physical	21988832
CBL_HUMAN	CBL	physical	24287595
OLIG1_HUMAN	OLIG1	physical	25814554
P55G_HUMAN	PIK3R3	physical	25814554
SH21A_HUMAN	SH2D1A	physical	25814554
IF2B_HUMAN	EIF2S2	physical	11959995
APBB2_HUMAN	APBB2	physical	26496610
WIPF1_HUMAN	WIPF1	physical	26496610
TRRAP_HUMAN	TRRAP	physical	26496610
UXT_HUMAN	UXT	physical	26496610
RAD54_HUMAN	RAD54L	physical	26496610
WASL_HUMAN	WASL	physical	26496610
PAPS1_HUMAN	PAPSS1	physical	26496610
EPN4_HUMAN	CLINT1	physical	26496610
TRI14_HUMAN	TRIM14	physical	26496610
ACK1_HUMAN	TNK2	physical	26496610
UBR4_HUMAN	UBR4	physical	26496610
RNC_HUMAN	DROSHA	physical	26496610
RTEL1_HUMAN	RTEL1	physical	26496610
HEAT3_HUMAN	HEATR3	physical	26496610
WIPF2_HUMAN	WIPF2	physical	26496610
GHR_HUMAN	GHR	physical	25241761
ABL2_HUMAN	ABL2	physical	25241761
BLNK_HUMAN	BLNK	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 NCK1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
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-85; SER-96 AND TYR-105,AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-85; SER-91 AND SER-96,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-96 AND TYR-105,AND MASS SPECTROMETRY.	17287340 [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-105, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASSSPECTROMETRY.	18088087 [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-105, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND MASSSPECTROMETRY.	15951569 [Abstract]