RAVR2_HUMAN - dbPTM
RAVR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAVR2_HUMAN
UniProt AC Q9HCJ3
Protein Name Ribonucleoprotein PTB-binding 2
Gene Name RAVER2
Organism Homo sapiens (Human).
Sequence Length 691
Subcellular Localization Nucleus. Cytoplasm. May shuttle between the nucleus and the cytoplasm..
Protein Description May bind single-stranded nucleic acids..
Protein Sequence MAAAAGDGGGEGGAGLGSAAGLGPGPGLRGQGPSAEAHEGAPDPMPAALHPEEVAARLQRMQRELSNRRKILVKNLPQDSNCQEVHDLLKDYDLKYCYVDRNKRTAFVTLLNGEQAQNAIQMFHQYSFRGKDLIVQLQPTDALLCITNVPISFTSEEFEELVRAYGNIERCFLVYSEVTGHSKGYGFVEYMKKDFAAKARLELLGRQLGASALFAQWMDVNLLASELIHSKCLCIDKLPSDYRDSEELLQIFSSVHKPVFCQLAQDEGSYVGGFAVVEYSTAEQAEEVQQAADGMTIKGSKVQVSFCAPGAPGRSTLAALIAAQRVMHSNQKGLLPEPNPVQIMKSLNNPAMLQVLLQPQLCGRAVKPAVLGTPHSLPHLMNPSISPAFLHLNKAHQSSVMGNTSNLFLQNLSHIPLAQQQLMKFENIHTNNKPGLLGEPPAVVLQTALGIGSVLPLKKELGHHHGEAHKTSSLIPTQTTITAGMGMLPFFPNQHIAGQAGPGHSNTQEKQPATVGMAEGNFSGSQPYLQSFPNLAAGSLLVGHHKQQQSQPKGTEISSGAASKNQTSLLGEPPKEIRLSKNPYLNLASVLPSVCLSSPASKTTLHKTGIASSILDAISQGSESQHALEKCIAYSPPFGDYAQVSSLRNEKRGSSYLISAPEGGSVECVDQHSQGTGAYYMETYLKKKRVY
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------MAAAAGDGG
------CCCCCCCCC		13.0522814378
18PhosphorylationEGGAGLGSAAGLGPG
CCCCCCCCCCCCCCC		21.7120068231
74UbiquitinationNRRKILVKNLPQDSN
HCHHHHHHCCCCCCC		49.6929967540
90UbiquitinationQEVHDLLKDYDLKYC
HHHHHHHHHCCCCEE		62.6329967540
95UbiquitinationLLKDYDLKYCYVDRN
HHHHCCCCEEEEECC		30.3129967540
185PhosphorylationVTGHSKGYGFVEYMK
CCCCCCCCCHHHHHH		15.8926552605
190PhosphorylationKGYGFVEYMKKDFAA
CCCCHHHHHHHHHHH		14.6626552605
240PhosphorylationLCIDKLPSDYRDSEE
EEEECCCCCCCCHHH		58.6820068231
242PhosphorylationIDKLPSDYRDSEELL
EECCCCCCCCHHHHH		22.2120068231
245PhosphorylationLPSDYRDSEELLQIF
CCCCCCCHHHHHHHH		24.7920068231
253PhosphorylationEELLQIFSSVHKPVF
HHHHHHHHCCCCCEE		32.8320068231
254PhosphorylationELLQIFSSVHKPVFC
HHHHHHHCCCCCEEE		19.9320068231
305PhosphorylationKGSKVQVSFCAPGAP
CCCEEEEEEECCCCC		9.4929449344
329PhosphorylationAAQRVMHSNQKGLLP
HHHHHHHCCCCCCCC		23.9026552605
346PhosphorylationNPVQIMKSLNNPAML
CHHHHHHCCCCHHHH		20.9626552605
373PhosphorylationVKPAVLGTPHSLPHL
CCHHHCCCCCCCHHH		17.4225159151
376PhosphorylationAVLGTPHSLPHLMNP
HHCCCCCCCHHHCCC		44.81-
384PhosphorylationLPHLMNPSISPAFLH
CHHHCCCCCCHHHHH		30.60-
386PhosphorylationHLMNPSISPAFLHLN
HHCCCCCCHHHHHHH		17.9525159151
551UbiquitinationHHKQQQSQPKGTEIS
CCCCCCCCCCCCCCC		39.1129967540
555PhosphorylationQQSQPKGTEISSGAA
CCCCCCCCCCCCCCC		35.95-
558PhosphorylationQPKGTEISSGAASKN
CCCCCCCCCCCCCCC		19.2529759185
559PhosphorylationPKGTEISSGAASKNQ
CCCCCCCCCCCCCCC		37.8129759185
562UbiquitinationTEISSGAASKNQTSL
CCCCCCCCCCCCCCC		25.2729967540
564AcetylationISSGAASKNQTSLLG
CCCCCCCCCCCCCCC		48.6326051181
567PhosphorylationGAASKNQTSLLGEPP
CCCCCCCCCCCCCCC		30.6420860994
568PhosphorylationAASKNQTSLLGEPPK
CCCCCCCCCCCCCCC		16.3129759185
580PhosphorylationPPKEIRLSKNPYLNL
CCCCCCCCCCCCCCH		22.1227251275
581UbiquitinationPKEIRLSKNPYLNLA
CCCCCCCCCCCCCHH		67.54-
584PhosphorylationIRLSKNPYLNLASVL
CCCCCCCCCCHHHHC		20.0224719451
585PhosphorylationRLSKNPYLNLASVLP
CCCCCCCCCHHHHCC		4.4618669648
588PhosphorylationKNPYLNLASVLPSVC
CCCCCCHHHHCCHHH		9.1218669648
589PhosphorylationNPYLNLASVLPSVCL
CCCCCHHHHCCHHHH		27.6120873877
593PhosphorylationNLASVLPSVCLSSPA
CHHHHCCHHHHCCCC		22.6920873877
594UbiquitinationLASVLPSVCLSSPAS
HHHHCCHHHHCCCCC		3.4329967540
597PhosphorylationVLPSVCLSSPASKTT
HCCHHHHCCCCCCCC		29.2020873877
598PhosphorylationLPSVCLSSPASKTTL
CCHHHHCCCCCCCCH		16.1318669648
601PhosphorylationVCLSSPASKTTLHKT
HHHCCCCCCCCHHHC		33.6418669648
606PhosphorylationPASKTTLHKTGIASS
CCCCCCHHHCCHHHH		24.4417525332
611PhosphorylationTLHKTGIASSILDAI
CHHHCCHHHHHHHHH		9.8927251275
612PhosphorylationLHKTGIASSILDAIS
HHHCCHHHHHHHHHH		18.9127732954
613PhosphorylationHKTGIASSILDAISQ
HHCCHHHHHHHHHHC		20.3922115753
619PhosphorylationSSILDAISQGSESQH
HHHHHHHHCCCHHHH		30.1517525332
622PhosphorylationLDAISQGSESQHALE
HHHHHCCCHHHHHHH		26.8328450419
624PhosphorylationAISQGSESQHALEKC
HHHCCCHHHHHHHHH		29.0328450419
634PhosphorylationALEKCIAYSPPFGDY
HHHHHHHHCCCCCCH		11.2026074081
635PhosphorylationLEKCIAYSPPFGDYA
HHHHHHHCCCCCCHH		19.6426657352
641PhosphorylationYSPPFGDYAQVSSLR
HCCCCCCHHHHHHHC		10.1826074081
645PhosphorylationFGDYAQVSSLRNEKR
CCCHHHHHHHCCCCC		16.1524719451
646PhosphorylationGDYAQVSSLRNEKRG
CCHHHHHHHCCCCCC		32.2724719451
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 RAVR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAVR2_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 RAVR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RAVR2_HUMAN !!
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 RAVR2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.

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