ZFR_MOUSE - dbPTM
ZFR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZFR_MOUSE
UniProt AC O88532
Protein Name Zinc finger RNA-binding protein
Gene Name Zfr
Organism Mus musculus (Mouse).
Sequence Length 1074
Subcellular Localization Nucleus. Cytoplasm. Cytoplasmic granule. Chromosome. Associated with chromosome foci in meiotic cells. Localizes in somatodendritic compartment of primary hippocampal neurons (By similarity). Colocalizes with STAU2 in several cytosolic RNA granules (
Protein Description Involved in postimplantation and gastrulation stages of development. Binds to DNA and RNA. Involved in the nucleocytoplasmic shuttling of STAU2 (By similarity)..
Protein Sequence MIPICPVVSFTYVPSRLGEDAKMATGNYFGFTHSGAAAAAAAAQYSQQPASGVAYSHPTTVASYTVHQAPVAAHTVTAAYAPAAATVAVARPAPVAVAAAATAAAYGGYPTAHTATDYGYTQRQQEAPPPPPPATTQNYQDSYSYVRSTAPAVAYDSKQYYQQPTATAAAVAAAAQPQPSVAETYYQTAPKAGYSQGATQYTQAQQARQVTAIKPATPSPATTTFSIYPVSSTVQPVAAAATVVPSYTQSATYSTTAVTYSGTSYSGYEAAVYSAASSYYQQQQQQQKQAAAAAAAAAATAAWTGTTFTKKTPFQNKQLKPKQPPKPPQIHYCDVCKISCAGPQTYKEHLEGQKHKKKEAALKASQNTSSSNNSTRGTQNQLRCELCDVSCTGADAYAAHIRGAKHQKVVKLHTKLGKPIPSTEPNVVSQATSSTAASASKPTASPSSIGASNCTLNTSSIATSSVKGLSTTGNSSLNSTSNTKVSAIPTNMAAKKTSTPKINFVGGNKLQSTGNKTEDLKGIDCVKNTPAASAVQIPEVKQDAGSEPVTPASLAALQSDVQPVGHDYVEEVRNDEGKVIRFHCKLCECSFNDPNAKEMHLKGRRHRLQYKKKVNPDLQVEVKPSIRARKIQEEKMRKQMQKEEYWRRREEEERWRMEIRRYEEDMYWRRMEEEQHHWDDRRRMPDGGYPHGPPGPLGLLGVRPGMPPQPQGPAPLRRPDSSDDRYVMTKHATIYPTEEELQAVQKIVSITERALKLVSDSLSEHEKSKNKEGDDKKEGGKDRALKGVLRVGVLAKGLLLRGDRNVNLVLLCSEKPSKSLLSRIAENLPKQLAVISPEKYDIKCAVSEAAIILNSCVEPKMQVTITLTSPIIREENMREGDVTSGMVKDPPDVLDRQKCLDALAALRHAKWFQARANGLQSCVIIIRILRDLCQRVPTWSDFPSWAMELLVEKAISSASSPQSPGDALRRVFECISSGIILKGSPGLLDPCEKDPFDTLATMTDQQREDITSSAQFALRLLAFRQIHKVLGMDPLPQMNQRFNIHNNRKRRRDSDGVDGFEAEGKKDKKDYDNF
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
15PhosphorylationVSFTYVPSRLGEDAK
EEEEEECCCCCCCCC		30.05-
135O-linked_GlycosylationPPPPPPATTQNYQDS
CCCCCCCCCCCCHHC		34.3928528544
136O-linked_GlycosylationPPPPPATTQNYQDSY
CCCCCCCCCCCHHCC		19.5428528544
195O-linked_GlycosylationTAPKAGYSQGATQYT
CCCCCCCCCCCCHHH		22.6328528544
202O-linked_GlycosylationSQGATQYTQAQQARQ
CCCCCHHHHHHHHHH		13.9628528544
300O-linked_GlycosylationAAAAAAATAAWTGTT
HHHHHHHHHHHHCCC		16.5128528544
300PhosphorylationAAAAAAATAAWTGTT
HHHHHHHHHHHHCCC		16.5129109428
374PhosphorylationNTSSSNNSTRGTQNQ
CCCCCCCCCCCCCCH		24.5925338131
414PhosphorylationQKVVKLHTKLGKPIP
HHEEHHHHCCCCCCC		38.10-
422PhosphorylationKLGKPIPSTEPNVVS
CCCCCCCCCCCCHHC		46.23-
438PhosphorylationATSSTAASASKPTAS
CCCCCCCCCCCCCCC		30.52-
440PhosphorylationSSTAASASKPTASPS
CCCCCCCCCCCCCHH		36.35-
443PhosphorylationAASASKPTASPSSIG
CCCCCCCCCCHHHCC		43.4326643407
445PhosphorylationSASKPTASPSSIGAS
CCCCCCCCHHHCCCC		28.0026643407
445UbiquitinationSASKPTASPSSIGAS
CCCCCCCCHHHCCCC		28.0027667366
447PhosphorylationSKPTASPSSIGASNC
CCCCCCHHHCCCCCC		31.9026643407
448PhosphorylationKPTASPSSIGASNCT
CCCCCHHHCCCCCCE		28.5526643407
453UbiquitinationPSSIGASNCTLNTSS
HHHCCCCCCEECCCC		23.4327667366
455PhosphorylationSIGASNCTLNTSSIA
HCCCCCCEECCCCCE		27.5624453211
465UbiquitinationTSSIATSSVKGLSTT
CCCCEECCCCCCCCC		24.4027667366
476PhosphorylationLSTTGNSSLNSTSNT
CCCCCCCCCCCCCCC		35.2529514104
479PhosphorylationTGNSSLNSTSNTKVS
CCCCCCCCCCCCEEC		38.2129514104
490PhosphorylationTKVSAIPTNMAAKKT
CEECCCCCCCCCCCC		31.3622802335
505UbiquitinationSTPKINFVGGNKLQS
CCCCEEEECCCCCCC		9.2027667366
509AcetylationINFVGGNKLQSTGNK
EEEECCCCCCCCCCC		51.7023806337
509UbiquitinationINFVGGNKLQSTGNK
EEEECCCCCCCCCCC		51.7027667366
516AcetylationKLQSTGNKTEDLKGI
CCCCCCCCCCCCCCC		55.4223806337
517UbiquitinationLQSTGNKTEDLKGID
CCCCCCCCCCCCCCC		38.4427667366
550PhosphorylationDAGSEPVTPASLAAL
CCCCCCCCHHHHHHH		24.6930352176
630AcetylationKPSIRARKIQEEKMR
CHHHHHHHHHHHHHH		47.9919856623
761PhosphorylationALKLVSDSLSEHEKS
HHHHHHHHHHHHHHH		26.7021454597
817PhosphorylationLLCSEKPSKSLLSRI
EEECCCCCHHHHHHH		46.0429895711
819PhosphorylationCSEKPSKSLLSRIAE
ECCCCCHHHHHHHHH		38.5924719451
822PhosphorylationKPSKSLLSRIAENLP
CCCHHHHHHHHHHCC		27.2524719451
883PhosphorylationNMREGDVTSGMVKDP
HCCCCCCCCCCCCCC		25.05-
1001UbiquitinationDPFDTLATMTDQQRE
CCCCCHHCCCHHHHH		24.5827667366
1009UbiquitinationMTDQQREDITSSAQF
CCHHHHHHHHHHHHH		52.2127667366
1021UbiquitinationAQFALRLLAFRQIHK
HHHHHHHHHHHHHHH		3.2427667366
1054PhosphorylationNRKRRRDSDGVDGFE
CCCCCCCCCCCCCCH		34.1627087446
1061UbiquitinationSDGVDGFEAEGKKDK
CCCCCCCHHCCCCCC		51.8727667366
1065UbiquitinationDGFEAEGKKDKKDYD
CCCHHCCCCCCCCCC		49.6727667366
1073UbiquitinationKDKKDYDNF------
CCCCCCCCC------		37.9927667366
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 ZFR_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZFR_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 ZFR_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZFR_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZFR_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-1054, AND MASSSPECTROMETRY.

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