RAVR1_HUMAN - dbPTM
RAVR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAVR1_HUMAN
UniProt AC Q8IY67
Protein Name Ribonucleoprotein PTB-binding 1
Gene Name RAVER1
Organism Homo sapiens (Human).
Sequence Length 606
Subcellular Localization Nucleus. Cytoplasm. Nuclear, in perinucleolar structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts. Associated with myotubes during muscle differentiation (By similarity)..
Protein Description Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity)..
Protein Sequence MAADVSVTHRPPLSPKSGAEVEAGDAAERRAPEEELPPLDPEEIRKRLEHTERQFRNRRKILIRGLPGDVTNQEVHDLLSDYELKYCFVDKYKGTAFVTLLNGEQAEAAINAFHQSRLRERELSVQLQPTDALLCVANLPPSLTQQQFEELVRPFGSLERCFLVYSERTGQSKGYGFAEYMKKDSAARAKSDLLGKPLGPRTLYVHWTDAGQLTPALLHSRCLCVDRLPPGFNDVDALCRALSAVHSPTFCQLACGQDGQLKGFAVLEYETAEMAEEAQQQADGLSLGGSHLRVSFCAPGPPGRSMLAALIAAQATALNRGKGLLPEPNILQLLNNLGPSASLQLLLNPLLHGSAGGKQGLLGAPPAMPLLNGPALSTALLQLALQTQGQKKPGILGDSPLGALQPGAQPANPLLGELPAGGGLPPELPPRRGKPPPLLPSVLGPAGGDREALGLGPPAAQLTPPPAPVGLRGSGLRGPLSHFYSGSPTSYFTSGLQAGLKQSHLSKAIGSSPLGSGEGLLGLSPGPNGHSHLLKVRAGGGDMQGWEAPAPQRPLTRPALPSVSRPHWAARNAALPTCCPRPSPAQKAAMWASTPRASAATTRTPT
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------MAADVSVTH
------CCCCCEECC
16.6320068231
6Phosphorylation--MAADVSVTHRPPL
--CCCCCEECCCCCC
23.1125159151
8PhosphorylationMAADVSVTHRPPLSP
CCCCCEECCCCCCCC
12.5021955146
14PhosphorylationVTHRPPLSPKSGAEV
ECCCCCCCCCCCCEE
35.7429255136
16 (in isoform 3)Ubiquitination-59.1421890473
17PhosphorylationRPPLSPKSGAEVEAG
CCCCCCCCCCEEECC
46.7729255136
17 (in isoform 2)Phosphorylation-46.7718669648
23PhosphorylationKSGAEVEAGDAAERR
CCCCEEECCCHHHHC
26.7517081983
25PhosphorylationGAEVEAGDAAERRAP
CCEEECCCHHHHCCC
50.0517081983
30MethylationAGDAAERRAPEEELP
CCCHHHHCCCHHHCC
46.10115490363
31PhosphorylationGDAAERRAPEEELPP
CCHHHHCCCHHHCCC
23.2918691976
33SumoylationAAERRAPEEELPPLD
HHHHCCCHHHCCCCC
64.22-
34PhosphorylationAERRAPEEELPPLDP
HHHCCCHHHCCCCCH
64.8718669648
47MethylationDPEEIRKRLEHTERQ
CHHHHHHHHHHHHHH
35.14-
80PhosphorylationQEVHDLLSDYELKYC
HHHHHHHHCCEEEEE
45.50-
82PhosphorylationVHDLLSDYELKYCFV
HHHHHHCCEEEEEEE
21.56-
86PhosphorylationLSDYELKYCFVDKYK
HHCCEEEEEEEECCC
12.0728152594
912-HydroxyisobutyrylationLKYCFVDKYKGTAFV
EEEEEEECCCCEEEE
43.49-
91AcetylationLKYCFVDKYKGTAFV
EEEEEEECCCCEEEE
43.4926822725
92PhosphorylationKYCFVDKYKGTAFVT
EEEEEECCCCEEEEE
15.36-
97PhosphorylationDKYKGTAFVTLLNGE
ECCCCEEEEEEECHH
4.30-
99PhosphorylationYKGTAFVTLLNGEQA
CCCEEEEEEECHHHH
21.05-
102UbiquitinationTAFVTLLNGEQAEAA
EEEEEEECHHHHHHH
55.88-
103PhosphorylationAFVTLLNGEQAEAAI
EEEEEECHHHHHHHH
28.50-
108UbiquitinationLNGEQAEAAINAFHQ
ECHHHHHHHHHHHHH
19.36-
109PhosphorylationNGEQAEAAINAFHQS
CHHHHHHHHHHHHHH
6.25-
157PhosphorylationELVRPFGSLERCFLV
HHHHHCCCCCEEEEE
27.6926091039
175PhosphorylationRTGQSKGYGFAEYMK
CCCCCCCCCHHHHHH
16.8918083107
185PhosphorylationAEYMKKDSAARAKSD
HHHHHHCHHHHHHHH
32.4828634120
190SumoylationKDSAARAKSDLLGKP
HCHHHHHHHHHCCCC
38.66-
190UbiquitinationKDSAARAKSDLLGKP
HCHHHHHHHHHCCCC
38.66-
191PhosphorylationDSAARAKSDLLGKPL
CHHHHHHHHHCCCCC
32.2920873877
196UbiquitinationAKSDLLGKPLGPRTL
HHHHHCCCCCCCCEE
36.72-
196 (in isoform 1)Ubiquitination-36.7221890473
207SumoylationPRTLYVHWTDAGQLT
CCEEEEEECCHHHCC
5.97-
207UbiquitinationPRTLYVHWTDAGQLT
CCEEEEEECCHHHCC
5.97-
213UbiquitinationHWTDAGQLTPALLHS
EECCHHHCCHHHHHC
6.40-
213 (in isoform 2)Ubiquitination-6.4021890473
214PhosphorylationWTDAGQLTPALLHSR
ECCHHHCCHHHHHCC
9.91-
231PhosphorylationCVDRLPPGFNDVDAL
ECCCCCCCCCHHHHH
31.86-
243PhosphorylationDALCRALSAVHSPTF
HHHHHHHHHHCCCCE
27.5327067055
297GlutathionylationSHLRVSFCAPGPPGR
CEEEEEEECCCCCCH
3.3022555962
399PhosphorylationKPGILGDSPLGALQP
CCCCCCCCCCCCCCC
21.8929496963
416PhosphorylationQPANPLLGELPAGGG
CCCCCCCCCCCCCCC
41.92-
441PhosphorylationKPPPLLPSVLGPAGG
CCCCCCHHHCCCCCC
29.9124732914
451UbiquitinationGPAGGDREALGLGPP
CCCCCCHHHCCCCCC
53.65-
458PhosphorylationEALGLGPPAAQLTPP
HHCCCCCCHHHCCCC
38.1320068231
463PhosphorylationGPPAAQLTPPPAPVG
CCCHHHCCCCCCCCC
22.9729255136
463 (in isoform 2)Phosphorylation-22.9718669648
472MethylationPPAPVGLRGSGLRGP
CCCCCCCCCCCCCCC
31.1654558519
474PhosphorylationAPVGLRGSGLRGPLS
CCCCCCCCCCCCCCH
28.3729496963
474 (in isoform 2)Phosphorylation-28.3720068231
477MethylationGLRGSGLRGPLSHFY
CCCCCCCCCCCHHHC
48.4881452779
480PhosphorylationGSGLRGPLSHFYSGS
CCCCCCCCHHHCCCC
7.4719664995
483 (in isoform 2)Phosphorylation-4.7030266825
485PhosphorylationGPLSHFYSGSPTSYF
CCCHHHCCCCCCHHH
31.6720068231
487PhosphorylationLSHFYSGSPTSYFTS
CHHHCCCCCCHHHHH
21.0422496350
488 (in isoform 2)Phosphorylation-28.9630266825
489PhosphorylationHFYSGSPTSYFTSGL
HHCCCCCCHHHHHHH
37.4425627689
491PhosphorylationYSGSPTSYFTSGLQA
CCCCCCHHHHHHHHH
17.2220068231
493 (in isoform 2)Phosphorylation-17.4130266825
501MethylationSGLQAGLKQSHLSKA
HHHHHHHCHHHHHHH
49.16115985349
502 (in isoform 2)Phosphorylation-40.9228111955
505PhosphorylationAGLKQSHLSKAIGSS
HHHCHHHHHHHHCCC
7.3220068231
507AcetylationLKQSHLSKAIGSSPL
HCHHHHHHHHCCCCC
50.8430591765
509 (in isoform 2)Phosphorylation-6.7225884760
510PhosphorylationSHLSKAIGSSPLGSG
HHHHHHHCCCCCCCC
27.2520068231
511PhosphorylationHLSKAIGSSPLGSGE
HHHHHHCCCCCCCCC
23.7525159151
512PhosphorylationLSKAIGSSPLGSGEG
HHHHHCCCCCCCCCC
20.9425159151
514 (in isoform 2)Phosphorylation-10.3528442448
516PhosphorylationIGSSPLGSGEGLLGL
HCCCCCCCCCCCCCC
41.1625159151
524PhosphorylationGEGLLGLSPGPNGHS
CCCCCCCCCCCCCCC
26.4729255136
531PhosphorylationSPGPNGHSHLLKVRA
CCCCCCCCEEEEEEE
19.7529255136
544 (in isoform 2)Phosphorylation-59.60-
553 (in isoform 2)Phosphorylation-27.4328985074
554 (in isoform 2)Phosphorylation-32.6025262027
556 (in isoform 2)Phosphorylation-36.9725627689
562PhosphorylationLTRPALPSVSRPHWA
CCCCCCCCCCCCCHH
33.31-
563 (in isoform 2)Phosphorylation-5.4822199227
567 (in isoform 2)Phosphorylation-26.2019664994
570 (in isoform 2)Phosphorylation-10.4830266825
571 (in isoform 2)Phosphorylation-26.1025159151
574 (in isoform 2)Ubiquitination-20.0221890473
577PhosphorylationARNAALPTCCPRPSP
HHCCCCCCCCCCCCH
27.8228555341
580PhosphorylationAALPTCCPRPSPAQK
CCCCCCCCCCCHHHH
54.0520068231
581MethylationALPTCCPRPSPAQKA
CCCCCCCCCCHHHHH
30.34115490355
581 (in isoform 2)Phosphorylation-30.3427251275
583PhosphorylationPTCCPRPSPAQKAAM
CCCCCCCCHHHHHHH
33.8621712546
583 (in isoform 2)Phosphorylation-33.8629116813
584PhosphorylationTCCPRPSPAQKAAMW
CCCCCCCHHHHHHHH
41.2019664994
584 (in isoform 2)Phosphorylation-41.2027251275
585 (in isoform 2)Phosphorylation-28.0429116813
587MethylationPRPSPAQKAAMWAST
CCCCHHHHHHHHHCC
39.97115976315
588 (in isoform 2)Phosphorylation-7.1721552520
590 (in isoform 2)Phosphorylation-3.5229116813
594PhosphorylationKAAMWASTPRASAAT
HHHHHHCCCCCCCCC
14.73-
596MethylationAMWASTPRASAATTR
HHHHCCCCCCCCCCC
41.06115490351
601PhosphorylationTPRASAATTRTPT--
CCCCCCCCCCCCC--
19.2729396449
602PhosphorylationPRASAATTRTPT---
CCCCCCCCCCCC---
28.0229396449
604PhosphorylationASAATTRTPT-----
CCCCCCCCCC-----
29.2329396449
634Phosphorylation-----------------------------------
-----------------------------------
20166139
638Phosphorylation---------------------------------------
---------------------------------------
19651622
648Phosphorylation-------------------------------------------------
-------------------------------------------------
20068231
658Phosphorylation-----------------------------------------------------------
-----------------------------------------------------------
20068231
660Phosphorylation-------------------------------------------------------------
-------------------------------------------------------------
20068231
674Methylation---------------------------------------------------------------------------
---------------------------------------------------------------------------
-
684Phosphorylation-------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------
20068231
685Phosphorylation--------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------
20068231
689Phosphorylation------------------------------------------------------------------------------------------
------------------------------------------------------------------------------------------
20068231
697Phosphorylation--------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------
20068231
704Phosphorylation---------------------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------------------
20068231
724Phosphorylation-----------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------
20068231
728Phosphorylation---------------------------------------------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------------------------------------------
20068231

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
700SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAVR1_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 RAVR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR4_HUMANPFASphysical
26344197
GORS2_HUMANGORASP2physical
27173435
UBAP2_HUMANUBAP2physical
27173435

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 RAVR1_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-14 AND THR-463, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-14, AND MASSSPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-14 AND THR-463, AND MASS SPECTROMETRY.
"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-17; THR-463; SER-474;SER-512 AND SER-524, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567(ISOFORM 2), AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-463; SER-512 ANDSER-524, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; SER-617;SER-707 AND SER-711 (ISOFORM 2), AND MASS SPECTROMETRY.
"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-14, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, AND MASSSPECTROMETRY.

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