YBOX1_MOUSE - dbPTM
YBOX1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YBOX1_MOUSE
UniProt AC P62960
Protein Name Nuclease-sensitive element-binding protein 1
Gene Name Ybx1
Organism Mus musculus (Mouse).
Sequence Length 322
Subcellular Localization Cytoplasm. Nucleus. Cytoplasmic granule . Secreted. Shuttles between nucleus and cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between nucleus and cytoplasm. Predominantly cytoplasmic in proliferating cells
Protein Description Mediates pre-mRNA alternative splicing regulation. Component of the CRD-mediated complex that promotes MYC mRNA stability. 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. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as HLA class II genes. Regulates the transcription of numerous 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. 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 preferentially to 5'-[CU]CUGCG-3' motif in vitro (By similarity).; The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation..
Protein Sequence MSSEAETQQPPAAPAAALSAADTKPGSTGSGAGSGGPGGLTSAAPAGGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVQGSKYAADRNHYRRYPRRRGPPRNYQQNYQNSESGEKNEGSESAPEGQAQQRRPYRRRRFPPYYMRRPYARRPQYSNPPVQGEVMEGADNQGAGEQGRPVRQNMYRGYRPRFRRGPPRQRQPREDGNEEDKENQGDETQGQQPPQRRYRRNFNYRRRRPENPKPQDGKETKAADPPAENSSAPEAEQGGAE
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------MSSEAETQQ
------CCCHHHHCC		36.56-
2Phosphorylation------MSSEAETQQ
------CCCHHHHCC		36.5626824392
3Phosphorylation-----MSSEAETQQP
-----CCCHHHHCCC		39.2625619855
7Phosphorylation-MSSEAETQQPPAAP
-CCCHHHHCCCCCHH		39.2825619855
19PhosphorylationAAPAAALSAADTKPG
CHHHHHHHHHHCCCC		19.3825619855
23PhosphorylationAALSAADTKPGSTGS
HHHHHHHCCCCCCCC		34.1225619855
24UbiquitinationALSAADTKPGSTGSG
HHHHHHCCCCCCCCC		48.18-
27PhosphorylationAADTKPGSTGSGAGS
HHHCCCCCCCCCCCC		37.8225619855
28PhosphorylationADTKPGSTGSGAGSG
HHCCCCCCCCCCCCC		41.0825619855
30PhosphorylationTKPGSTGSGAGSGGP
CCCCCCCCCCCCCCC		26.0920469934
34PhosphorylationSTGSGAGSGGPGGLT
CCCCCCCCCCCCCCC		39.7925619855
41PhosphorylationSGGPGGLTSAAPAGG
CCCCCCCCCCCCCCC		21.4225619855
42PhosphorylationGGPGGLTSAAPAGGD
CCCCCCCCCCCCCCC		27.7225619855
56UbiquitinationDKKVIATKVLGTVKW
CCCEEEEEECEEEEE		26.83-
56AcetylationDKKVIATKVLGTVKW
CCCEEEEEECEEEEE		26.8322826441
62UbiquitinationTKVLGTVKWFNVRNG
EEECEEEEEEECCCC		46.0022790023
70PhosphorylationWFNVRNGYGFINRND
EEECCCCEEEECCCC		16.6529514104
78PhosphorylationGFINRNDTKEDVFVH
EEECCCCCCCCEEEE		39.6226370283
79UbiquitinationFINRNDTKEDVFVHQ
EECCCCCCCCEEEEH		55.57-
90UbiquitinationFVHQTAIKKNNPRKY
EEEHHHHHCCCHHHH		47.1622790023
91UbiquitinationVHQTAIKKNNPRKYL
EEHHHHHCCCHHHHH		56.7122790023
97PhosphorylationKKNNPRKYLRSVGDG
HCCCHHHHHEECCCC		14.5023984901
100PhosphorylationNPRKYLRSVGDGETV
CHHHHHEECCCCCEE		28.0526824392
106PhosphorylationRSVGDGETVEFDVVE
EECCCCCEEEEEEEE		30.7528833060
134PhosphorylationGGVPVQGSKYAADRN
CCCCCCCCCCCCCCC		12.8529176673
135UbiquitinationGVPVQGSKYAADRNH
CCCCCCCCCCCCCCC		45.8122790023
135AcetylationGVPVQGSKYAADRNH
CCCCCCCCCCCCCCC		45.8123806337
143PhosphorylationYAADRNHYRRYPRRR
CCCCCCCHHCCCHHH		10.5925367039
156PhosphorylationRRGPPRNYQQNYQNS
HHCCCCCHHHHHCCC		16.8627149854
160PhosphorylationPRNYQQNYQNSESGE
CCCHHHHHCCCCCCC		12.5325521595
163PhosphorylationYQQNYQNSESGEKNE
HHHHHCCCCCCCCCC		20.0227087446
165PhosphorylationQNYQNSESGEKNEGS
HHHCCCCCCCCCCCC		52.6627087446
168UbiquitinationQNSESGEKNEGSESA
CCCCCCCCCCCCCCC		64.9222790023
172PhosphorylationSGEKNEGSESAPEGQ
CCCCCCCCCCCCCCH		23.3827087446
174PhosphorylationEKNEGSESAPEGQAQ
CCCCCCCCCCCCHHH		51.3127087446
186PhosphorylationQAQQRRPYRRRRFPP
HHHHCCCCHHHCCCC		18.2329514104
187MethylationAQQRRPYRRRRFPPY
HHHCCCCHHHCCCCH		28.4518966577
194PhosphorylationRRRRFPPYYMRRPYA
HHHCCCCHHHCCCCC		15.3329514104
195PhosphorylationRRRFPPYYMRRPYAR
HHCCCCHHHCCCCCC		7.0129514104
197MethylationRFPPYYMRRPYARRP
CCCCHHHCCCCCCCC		21.9418601005
206PhosphorylationPYARRPQYSNPPVQG
CCCCCCCCCCCCCCC		17.0725619855
207PhosphorylationYARRPQYSNPPVQGE
CCCCCCCCCCCCCCC		37.3027087446
237MethylationPVRQNMYRGYRPRFR
CCHHHHHCCCCCCCC		25.5454560689
262UbiquitinationEDGNEEDKENQGDET
CCCCHHHHHCCCCCC		62.94-
269PhosphorylationKENQGDETQGQQPPQ
HHCCCCCCCCCCCCC		42.6226525534
285PhosphorylationRYRRNFNYRRRRPEN
HHHHHCCCCCCCCCC		11.0225367039
294UbiquitinationRRRPENPKPQDGKET
CCCCCCCCCCCCCCC		67.88-
299UbiquitinationNPKPQDGKETKAADP
CCCCCCCCCCCCCCC		71.19-
299AcetylationNPKPQDGKETKAADP
CCCCCCCCCCCCCCC		71.19-
302AcetylationPQDGKETKAADPPAE
CCCCCCCCCCCCCCC		42.54-
302UbiquitinationPQDGKETKAADPPAE
CCCCCCCCCCCCCCC		42.54-
311PhosphorylationADPPAENSSAPEAEQ
CCCCCCCCCCCHHHH		21.2717203969
312PhosphorylationDPPAENSSAPEAEQG
CCCCCCCCCCHHHHC		60.4727087446
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
100SPhosphorylationKinaseAKT1P31750
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFbxo33Q8VE08
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YBOX1_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 YBOX1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F120A_HUMANFAM120Aphysical
20360068
RT35_HUMANMRPS35physical
20360068
RL1D1_HUMANRSL1D1physical
20360068
RM47_HUMANMRPL47physical
20360068
MATR3_HUMANMATR3physical
20360068
SYYM_HUMANYARS2physical
20360068
RM43_HUMANMRPL43physical
20360068
RT34_HUMANMRPS34physical
20360068
RALY_HUMANRALYphysical
20360068
HNRPQ_HUMANSYNCRIPphysical
20360068
DHX30_HUMANDHX30physical
20360068
RM24_HUMANMRPL24physical
20360068
RT07_HUMANMRPS7physical
20360068
DDX28_HUMANDDX28physical
20360068
NOP58_HUMANNOP58physical
20360068
CLPX_HUMANCLPXphysical
20360068
POP1_HUMANPOP1physical
20360068
NOP56_HUMANNOP56physical
20360068
LA_HUMANSSBphysical
20360068
HNRL2_HUMANHNRNPUL2physical
20360068
RM16_HUMANMRPL16physical
20360068
PTCD3_HUMANPTCD3physical
20360068
FBRL_HUMANFBLphysical
20360068
ROAA_HUMANHNRNPABphysical
20360068
MOV10_HUMANMOV10physical
20360068
RT26_HUMANMRPS26physical
20360068
IF2B3_HUMANIGF2BP3physical
20360068
NOP2_HUMANNOP2physical
20360068
ZFR_HUMANZFRphysical
20360068
ZN326_HUMANZNF326physical
20360068
TRUB2_HUMANTRUB2physical
20360068
IF2B1_HUMANIGF2BP1physical
20360068
RM12_HUMANMRPL12physical
20360068
HNRPR_HUMANHNRNPRphysical
20360068
HNRPU_HUMANHNRNPUphysical
20360068
HNRPF_HUMANHNRNPFphysical
20360068
DDX21_HUMANDDX21physical
20360068
PABP1_HUMANPABPC1physical
20360068
LARP7_HUMANLARP7physical
20360068
RT18B_HUMANMRPS18Bphysical
20360068
RT22_HUMANMRPS22physical
20360068
RBMX_HUMANRBMXphysical
20360068
TRA2B_HUMANTRA2Bphysical
20360068
ROA0_HUMANHNRNPA0physical
20360068
HNRDL_HUMANHNRNPDLphysical
20360068
DHX9_HUMANDHX9physical
20360068
RRP12_HUMANRRP12physical
20360068
LARP1_HUMANLARP1physical
20360068
ILF3_HUMANILF3physical
20360068
RM18_HUMANMRPL18physical
20360068
DDX5_HUMANDDX5physical
20360068
PABP4_HUMANPABPC4physical
20360068
HNRPK_HUMANHNRNPKphysical
20360068
DKC1_HUMANDKC1physical
20360068
ROA3_HUMANHNRNPA3physical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YBOX1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASSSPECTROMETRY.
"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-172 AND SER-174, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-172, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-312, ANDMASS SPECTROMETRY.

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