dbPTM

YBOX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YBOX1_HUMAN
UniProt AC	P67809
Protein Name	Nuclease-sensitive element-binding protein 1
Gene Name	YBX1
Organism	Homo sapiens (Human).
Sequence Length	324
Subcellular Localization	Cytoplasm. Nucleus. Cytoplasmic granule . Secreted. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between nucleus and cytoplasm. Predominantly cytoplasmic in proliferating cells. Cytotoxic stress and DNA damage enhanc
Protein Description	Mediates pre-mRNA alternative splicing regulation. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Regulates the transcription of numerous genes. Its transcriptional activity on the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA (in vitro). May play a role in DNA repair. Component of the CRD-mediated complex that promotes MYC mRNA stability. Binds preferentially to the 5'-[CU]CUGCG-3' motif in vitro.; The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation..
Protein Sequence	MSSEAETQQPPAAPPAAPALSAADTKPGTTGSGAGSGGPGGLTSAAPAGGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVQGSKYAADRNHYRRYPRRRGPPRNYQQNYQNSESGEKNEGSESAPEGQAQQRRPYRRRRFPPYYMRRPYGRRPQYSNPPVQGEVMEGADNQGAGEQGRPVRQNMYRGYRPRFRRGPPRQRQPREDGNEEDKENQGDETQGQQPPQRRYRRNFNYRRRRPENPKPQDGKETKAADPPAENSSAPEAEQGGAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSEAETQQ ------CCCHHHHCC	36.56	25159151
2	Acetylation	------MSSEAETQQ ------CCCHHHHCC	36.56	18491316
3	Phosphorylation	-----MSSEAETQQP -----CCCHHHHCCC	39.26	25159151
7	Phosphorylation	-MSSEAETQQPPAAP -CCCHHHHCCCCCCC	39.28	25159151
21	Phosphorylation	PPAAPALSAADTKPG CCCCCCCCCCCCCCC	24.42	25159151
25	Phosphorylation	PALSAADTKPGTTGS CCCCCCCCCCCCCCC	34.12	23663014
26	Ubiquitination	ALSAADTKPGTTGSG CCCCCCCCCCCCCCC	41.83	23000965
26	Sumoylation	ALSAADTKPGTTGSG CCCCCCCCCCCCCCC	41.83	28112733
29	Phosphorylation	AADTKPGTTGSGAGS CCCCCCCCCCCCCCC	36.19	23663014
30	Phosphorylation	ADTKPGTTGSGAGSG CCCCCCCCCCCCCCC	34.95	23663014
32	O-linked_Glycosylation	TKPGTTGSGAGSGGP CCCCCCCCCCCCCCC	24.31	31373491
32	Phosphorylation	TKPGTTGSGAGSGGP CCCCCCCCCCCCCCC	24.31	25159151
36	Phosphorylation	TTGSGAGSGGPGGLT CCCCCCCCCCCCCCC	39.79	25159151
43	Phosphorylation	SGGPGGLTSAAPAGG CCCCCCCCCCCCCCC	21.42	23663014
44	Phosphorylation	GGPGGLTSAAPAGGD CCCCCCCCCCCCCCC	27.72	23663014
52	Ubiquitination	AAPAGGDKKVIATKV CCCCCCCCCEEEEEE	52.82	33845483
53	Ubiquitination	APAGGDKKVIATKVL CCCCCCCCEEEEEEC	43.55	22817900
58	Ubiquitination	DKKVIATKVLGTVKW CCCEEEEEECEEEEE	26.83	23000965
58	Acetylation	DKKVIATKVLGTVKW CCCEEEEEECEEEEE	26.83	26051181
64	Acetylation	TKVLGTVKWFNVRNG EEECEEEEEEECCCC	46.00	88983
64	Ubiquitination	TKVLGTVKWFNVRNG EEECEEEEEEECCCC	46.00	23000965
72	Phosphorylation	WFNVRNGYGFINRND EEECCCCEEEECCCC	16.65	28152594
80	Phosphorylation	GFINRNDTKEDVFVH EEECCCCCCCCEEEE	39.62	27050516
81	Malonylation	FINRNDTKEDVFVHQ EECCCCCCCCEEEEH	55.57	32601280
81	Acetylation	FINRNDTKEDVFVHQ EECCCCCCCCEEEEH	55.57	19608861
81	Ubiquitination	FINRNDTKEDVFVHQ EECCCCCCCCEEEEH	55.57	23000965
89	Phosphorylation	EDVFVHQTAIKKNNP CCEEEEHHHHHCCCH	18.57	25159151
92	Methylation	FVHQTAIKKNNPRKY EEEHHHHHCCCHHHH	47.16	-
92	Ubiquitination	FVHQTAIKKNNPRKY EEEHHHHHCCCHHHH	47.16	23000965
93	Ubiquitination	VHQTAIKKNNPRKYL EEHHHHHCCCHHHHH	56.71	23000965
98	Ubiquitination	IKKNNPRKYLRSVGD HHCCCHHHHHEECCC	50.31	23000965
99	Phosphorylation	KKNNPRKYLRSVGDG HCCCHHHHHEECCCC	14.50	28450419
101	Methylation	NNPRKYLRSVGDGET CCHHHHHEECCCCCE	26.63	-
102	Phosphorylation	NPRKYLRSVGDGETV CHHHHHEECCCCCEE	28.05	19664994
108	Phosphorylation	RSVGDGETVEFDVVE EECCCCCEEEEEEEE	30.75	30266825
118	Ubiquitination	FDVVEGEKGAEAANV EEEEECCCCCCCCCC	74.42	21906983
126	Phosphorylation	GAEAANVTGPGGVPV CCCCCCCCCCCCCCC	37.15	28555341
126	O-linked_Glycosylation	GAEAANVTGPGGVPV CCCCCCCCCCCCCCC	37.15	31373491
136	Phosphorylation	GGVPVQGSKYAADRN CCCCCCCCCCCCCCC	12.85	21712546
137	Neddylation	GVPVQGSKYAADRNH CCCCCCCCCCCCCCC	45.81	32015554
137	Ubiquitination	GVPVQGSKYAADRNH CCCCCCCCCCCCCCC	45.81	23000965
137	Acetylation	GVPVQGSKYAADRNH CCCCCCCCCCCCCCC	45.81	23236377
138	Phosphorylation	VPVQGSKYAADRNHY CCCCCCCCCCCCCCH	14.55	28152594
142	Methylation	GSKYAADRNHYRRYP CCCCCCCCCCHHCCC	27.39	80701193
145	Phosphorylation	YAADRNHYRRYPRRR CCCCCCCHHCCCHHH	10.59	28152594
158	Phosphorylation	RRGPPRNYQQNYQNS HHCCCCCHHHHHCCC	16.86	22167270
162	Phosphorylation	PRNYQQNYQNSESGE CCCHHHHHCCCCCCC	12.53	22167270
165	Phosphorylation	YQQNYQNSESGEKNE HHHHHCCCCCCCCCC	20.02	19664994
167	Phosphorylation	QNYQNSESGEKNEGS HHHCCCCCCCCCCCC	52.66	19664994
170	Ubiquitination	QNSESGEKNEGSESA CCCCCCCCCCCCCCC	64.92	21906983
170	Acetylation	QNSESGEKNEGSESA CCCCCCCCCCCCCCC	64.92	23236377
174	Phosphorylation	SGEKNEGSESAPEGQ CCCCCCCCCCCCCCH	23.38	19664994
176	Phosphorylation	EKNEGSESAPEGQAQ CCCCCCCCCCCCHHH	51.31	19664994
185	Methylation	PEGQAQQRRPYRRRR CCCHHHHCCCCHHHC	29.48	26494307
186	Methylation	EGQAQQRRPYRRRRF CCHHHHCCCCHHHCC	28.41	115920189
188	Phosphorylation	QAQQRRPYRRRRFPP HHHHCCCCHHHCCCC	18.23	26074081
189	Methylation	AQQRRPYRRRRFPPY HHHCCCCHHHCCCCC	28.45	18966581
190	Methylation	QQRRPYRRRRFPPYY HHCCCCHHHCCCCCC	28.43	115920193
196	Phosphorylation	RRRRFPPYYMRRPYG HHHCCCCCCCCCCCC	15.33	21945579
197	Phosphorylation	RRRFPPYYMRRPYGR HHCCCCCCCCCCCCC	7.01	21945579
198	Sulfoxidation	RRFPPYYMRRPYGRR HCCCCCCCCCCCCCC	2.12	28183972
199	Methylation	RFPPYYMRRPYGRRP CCCCCCCCCCCCCCC	21.94	18600999
199	Dimethylation	RFPPYYMRRPYGRRP CCCCCCCCCCCCCCC	21.94	-
200	Methylation	FPPYYMRRPYGRRPQ CCCCCCCCCCCCCCC	16.56	54560695
204	Methylation	YMRRPYGRRPQYSNP CCCCCCCCCCCCCCC	41.06	97804761
205	Methylation	MRRPYGRRPQYSNPP CCCCCCCCCCCCCCC	20.50	115920197
208	Phosphorylation	PYGRRPQYSNPPVQG CCCCCCCCCCCCCCC	17.07	21945579
209	Phosphorylation	YGRRPQYSNPPVQGE CCCCCCCCCCCCCCC	37.30	21945579
209	O-linked_Glycosylation	YGRRPQYSNPPVQGE CCCCCCCCCCCCCCC	37.30	31373491
218	Sulfoxidation	PPVQGEVMEGADNQG CCCCCCEECCCCCCC	3.24	30846556
231	Methylation	QGAGEQGRPVRQNMY CCCCCCCCCCHHHHH	26.66	115920201
234	Methylation	GEQGRPVRQNMYRGY CCCCCCCHHHHHCCC	25.49	115920205
238	Phosphorylation	RPVRQNMYRGYRPRF CCCHHHHHCCCCCCC	14.40	21945579
239	Methylation	PVRQNMYRGYRPRFR CCHHHHHCCCCCCCC	25.54	54560687
242	Methylation	QNMYRGYRPRFRRGP HHHHCCCCCCCCCCC	20.81	82797819
244	Methylation	MYRGYRPRFRRGPPR HHCCCCCCCCCCCCC	28.80	115920209
264	Acetylation	EDGNEEDKENQGDET CCCCHHHHHCCCCCC	62.94	26051181
264	Ubiquitination	EDGNEEDKENQGDET CCCCHHHHHCCCCCC	62.94	27667366
271	O-linked_Glycosylation	KENQGDETQGQQPPQ HHCCCCCCCCCCCCC	42.62	31373491
271	Phosphorylation	KENQGDETQGQQPPQ HHCCCCCCCCCCCCC	42.62	21712546
279	Methylation	QGQQPPQRRYRRNFN CCCCCCCHHHHHHCC	43.29	26494301
280	Methylation	GQQPPQRRYRRNFNY CCCCCCHHHHHHCCC	24.86	115920213
281	Phosphorylation	QQPPQRRYRRNFNYR CCCCCHHHHHHCCCC	19.00	-
287	Phosphorylation	RYRRNFNYRRRRPEN HHHHHCCCCCCCCCC	11.02	26356563
296	Ubiquitination	RRRPENPKPQDGKET CCCCCCCCCCCCCCC	67.88	27667366
296	Acetylation	RRRPENPKPQDGKET CCCCCCCCCCCCCCC	67.88	26210075
301	Acetylation	NPKPQDGKETKAADP CCCCCCCCCCCCCCC	71.19	19483673
301	Ubiquitination	NPKPQDGKETKAADP CCCCCCCCCCCCCCC	71.19	19483673
303	O-linked_Glycosylation	KPQDGKETKAADPPA CCCCCCCCCCCCCCC	29.48	31373491
303	Phosphorylation	KPQDGKETKAADPPA CCCCCCCCCCCCCCC	29.48	28111955
304	Acetylation	PQDGKETKAADPPAE CCCCCCCCCCCCCCC	42.54	19483673
304	Ubiquitination	PQDGKETKAADPPAE CCCCCCCCCCCCCCC	42.54	19483673
313	O-linked_Glycosylation	ADPPAENSSAPEAEQ CCCCCCCCCCCHHHH	21.27	31373491
313	Phosphorylation	ADPPAENSSAPEAEQ CCCCCCCCCCCHHHH	21.27	22167270
314	Phosphorylation	DPPAENSSAPEAEQG CCCCCCCCCCHHHHC	60.47	22167270

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
80	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
102	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
102	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
102	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
102	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
176	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RBBP6	Q7Z6E9	PMID:18851979
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO33	Q7Z6M2	PMID:16797541

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YBOX1_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 YBOX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRSF9_HUMAN	SRSF9	physical	12604611
ANKR2_HUMAN	ANKRD2	physical	15136035
P53_HUMAN	TP53	physical	15136035
CTCF_HUMAN	CTCF	physical	10906122
FUS_HUMAN	FUS	physical	12168660
IREB2_HUMAN	IREB2	physical	12192037
PCNA_HUMAN	PCNA	physical	9927044
P53_HUMAN	TP53	physical	11175333
RBBP6_HUMAN	RBBP6	physical	18851979
P53_HUMAN	TP53	physical	21344396
KS6A1_HUMAN	RPS6KA1	physical	19036157
EWS_HUMAN	EWSR1	physical	20972445
FBX33_HUMAN	FBXO33	physical	16797541
CUL1_HUMAN	CUL1	physical	16797541
HNRPD_HUMAN	HNRNPD	physical	12674497
LSM3_HUMAN	LSM3	physical	22365833
SMU1_HUMAN	SMU1	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
ACTA_HUMAN	ACTA2	physical	22619371
ROA2_HUMAN	HNRNPA2B1	physical	22863883
ROAA_HUMAN	HNRNPAB	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
MTAP2_HUMAN	MAP2	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
TBA4A_HUMAN	TUBA4A	physical	22863883
TBB5_HUMAN	TUBB	physical	22863883
AKT1_HUMAN	AKT1	physical	16354698
C1QBP_HUMAN	C1QBP	physical	26344197
COX5A_HUMAN	COX5A	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197
NDUA9_HUMAN	NDUFA9	physical	26344197
SK2L2_HUMAN	SKIV2L2	physical	26344197
HACE1_HUMAN	HACE1	physical	26343856
VP37B_HUMAN	VPS37B	physical	26343856
VAPB_HUMAN	VAPB	physical	26343856
EXOS9_HUMAN	EXOSC9	physical	26343856
AP2A2_HUMAN	AP2A2	physical	26343856
CAPR1_HUMAN	CAPRIN1	physical	26343856
MCM5_HUMAN	MCM5	physical	26343856
CDC20_HUMAN	CDC20	physical	26343856
SRP72_HUMAN	SRP72	physical	26343856
SMC2_HUMAN	SMC2	physical	26343856
VIGLN_HUMAN	HDLBP	physical	26343856
UBP10_HUMAN	USP10	physical	26343856
G3BP1_HUMAN	G3BP1	physical	26343856
PA2G4_HUMAN	PA2G4	physical	26343856
SRPK2_HUMAN	SRPK2	physical	26343856
BUB3_HUMAN	BUB3	physical	26343856

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 YBOX1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Y-box protein-1 is actively secreted through a non-classical pathwayand acts as an extracellular mitogen."; Frye B.C., Halfter S., Djudjaj S., Muehlenberg P., Weber S.,Raffetseder U., En-Nia A., Knott H., Baron J.M., Dooley S.,Bernhagen J., Mertens P.R.; EMBO Rep. 10:783-789(2009). Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-301 AND LYS-304,AND ACETYLATION AT LYS-301 AND LYS-304.	19483673 [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-165; SER-167; SER-174AND SER-176, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162; SER-165; SER-167;SER-174; SER-176; SER-313 AND SER-314, AND MASS SPECTROMETRY.	19413330 [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-165; SER-174 ANDSER-176, 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-314, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167 ANDSER-174, AND MASS SPECTROMETRY.	17487921 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-176 ANDSER-314, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Akt phosphorylates the Y-box binding protein 1 at Ser102 located inthe cold shock domain and affects the anchorage-independent growth ofbreast cancer cells."; Sutherland B.W., Kucab J., Wu J., Lee C., Cheang M.C.U., Yorida E.,Turbin D., Dedhar S., Nelson C., Pollak M., Leighton Grimes H.,Miller K., Badve S., Huntsman D., Blake-Gilks C., Chen M.,Pallen C.J., Dunn S.E.; Oncogene 24:4281-4292(2005). Cited for: PHOSPHORYLATION AT SER-102, INTERACTION WITH AKT1, SUBCELLULARLOCATION, AND MUTAGENESIS OF SER-102.	15806160 [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-162, AND MASSSPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-137, AND MASSSPECTROMETRY.	18781797 [Abstract]