RALY_HUMAN - dbPTM
RALY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RALY_HUMAN
UniProt AC Q9UKM9
Protein Name RNA-binding protein Raly
Gene Name RALY
Organism Homo sapiens (Human).
Sequence Length 306
Subcellular Localization Nucleus .
Protein Description RNA-binding protein that acts as a transcriptional cofactor for cholesterol biosynthetic genes in the liver. Binds the lipid-responsive non-coding RNA LeXis and is required for LeXis-mediated effect on cholesterogenesis (By similarity). May be a heterogeneous nuclear ribonucleoprotein (hnRNP). [PubMed: 9376072]
Protein Sequence MSLKLQASNVTNKNDPKSINSRVFIGNLNTALVKKSDVETIFSKYGRVAGCSVHKGYAFVQYSNERHARAAVLGENGRVLAGQTLDINMAGEPKPDRPKGLKRAASAIYSGYIFDYDYYRDDFYDRLFDYRGRLSPVPVPRAVPVKRPRVTVPLVRRVKTNVPVKLFARSTAVTTSSAKIKLKSSELQAIKTELTQIKSNIDALLSRLEQIAAEQKANPDGKKKGDGGGAGGGGGGGGSGGGGSGGGGGGGSSRPPAPQENTTSEAGLPQGEARTRDDGDEEGLLTHSEEELEHSQDTDADDGALQ
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------MSLKLQASN
------CCCEEECCC		33.9222814378
2Phosphorylation------MSLKLQASN
------CCCEEECCC		33.9223401153
4Methylation----MSLKLQASNVT
----CCCEEECCCCC		31.1144500987
4Sumoylation----MSLKLQASNVT
----CCCEEECCCCC		31.11-
4Ubiquitination----MSLKLQASNVT
----CCCEEECCCCC		31.1121890473
4Sumoylation----MSLKLQASNVT
----CCCEEECCCCC		31.1128112733
4Acetylation----MSLKLQASNVT
----CCCEEECCCCC		31.1125953088
4 (in isoform 1)Ubiquitination-31.1121890473
4 (in isoform 2)Ubiquitination-31.1121890473
8PhosphorylationMSLKLQASNVTNKND
CCCEEECCCCCCCCC		20.9029978859
11PhosphorylationKLQASNVTNKNDPKS
EEECCCCCCCCCCCH		44.7329978859
13UbiquitinationQASNVTNKNDPKSIN
ECCCCCCCCCCCHHC		54.0521906983
13AcetylationQASNVTNKNDPKSIN
ECCCCCCCCCCCHHC		54.0526051181
13 (in isoform 1)Ubiquitination-54.0521890473
13 (in isoform 2)Ubiquitination-54.0521890473
17UbiquitinationVTNKNDPKSINSRVF
CCCCCCCCHHCCEEE		67.82-
18PhosphorylationTNKNDPKSINSRVFI
CCCCCCCHHCCEEEE		32.1824144214
21PhosphorylationNDPKSINSRVFIGNL
CCCCHHCCEEEEEEC		28.3128509920
30PhosphorylationVFIGNLNTALVKKSD
EEEEECCEEEEEHHH		25.24-
34UbiquitinationNLNTALVKKSDVETI
ECCEEEEEHHHHHHH		47.6221890473
34 (in isoform 2)Ubiquitination-47.6221890473
34AcetylationNLNTALVKKSDVETI
ECCEEEEEHHHHHHH		47.6225953088
34 (in isoform 1)Ubiquitination-47.6221890473
35UbiquitinationLNTALVKKSDVETIF
CCEEEEEHHHHHHHH		44.39-
36PhosphorylationNTALVKKSDVETIFS
CEEEEEHHHHHHHHH		40.9722199227
40PhosphorylationVKKSDVETIFSKYGR
EEHHHHHHHHHHHCC		27.4621406692
43PhosphorylationSDVETIFSKYGRVAG
HHHHHHHHHHCCCCC		22.5522199227
44AcetylationDVETIFSKYGRVAGC
HHHHHHHHHCCCCCC		40.7625825284
44UbiquitinationDVETIFSKYGRVAGC
HHHHHHHHHCCCCCC		40.7621890473
44 (in isoform 1)Ubiquitination-40.7621890473
44 (in isoform 2)Ubiquitination-40.7621890473
55AcetylationVAGCSVHKGYAFVQY
CCCCEEECCEEEEEE		52.0025825284
55UbiquitinationVAGCSVHKGYAFVQY
CCCCEEECCEEEEEE		52.0021906983
55 (in isoform 1)Ubiquitination-52.0021890473
55 (in isoform 2)Ubiquitination-52.0021890473
57PhosphorylationGCSVHKGYAFVQYSN
CCEEECCEEEEEECC		11.1520090780
62PhosphorylationKGYAFVQYSNERHAR
CCEEEEEECCHHHEE		14.2529396449
63PhosphorylationGYAFVQYSNERHARA
CEEEEEECCHHHEEE		18.3425159151
84PhosphorylationGRVLAGQTLDINMAG
CCEECCCEEEEECCC		26.0222817901
94UbiquitinationINMAGEPKPDRPKGL
EECCCCCCCCCCHHH		56.07-
94AcetylationINMAGEPKPDRPKGL
EECCCCCCCCCCHHH		56.0726051181
94SumoylationINMAGEPKPDRPKGL
EECCCCCCCCCCHHH		56.0728112733
99UbiquitinationEPKPDRPKGLKRAAS
CCCCCCCHHHHHHHH		77.19-
99SumoylationEPKPDRPKGLKRAAS
CCCCCCCHHHHHHHH		77.1928112733
106PhosphorylationKGLKRAASAIYSGYI
HHHHHHHHHHHHCCC		17.7620044836
106 (in isoform 2)Phosphorylation-17.7630266825
109PhosphorylationKRAASAIYSGYIFDY
HHHHHHHHHCCCCCC		8.8528450419
109 (in isoform 2)Phosphorylation-8.8528176443
110PhosphorylationRAASAIYSGYIFDYD
HHHHHHHHCCCCCCC		21.0028450419
112PhosphorylationASAIYSGYIFDYDYY
HHHHHHCCCCCCCCC		7.7728450419
116PhosphorylationYSGYIFDYDYYRDDF
HHCCCCCCCCCCCCH		8.6227080861
118PhosphorylationGYIFDYDYYRDDFYD
CCCCCCCCCCCCHHH		8.31-
119 (in isoform 2)Phosphorylation-12.5025849741
124PhosphorylationDYYRDDFYDRLFDYR
CCCCCCHHHHHHCCC		13.72-
126MethylationYRDDFYDRLFDYRGR
CCCCHHHHHHCCCCC		26.35115490213
130PhosphorylationFYDRLFDYRGRLSPV
HHHHHHCCCCCCCCC		13.9724532841
131MethylationYDRLFDYRGRLSPVP
HHHHHCCCCCCCCCC		26.1254558491
135PhosphorylationFDYRGRLSPVPVPRA
HCCCCCCCCCCCCCC		23.6129255136
141MethylationLSPVPVPRAVPVKRP
CCCCCCCCCCCCCCC		48.7554558483
146MethylationVPRAVPVKRPRVTVP
CCCCCCCCCCCEECE		51.09116253935
146UbiquitinationVPRAVPVKRPRVTVP
CCCCCCCCCCCEECE		51.09-
146AcetylationVPRAVPVKRPRVTVP
CCCCCCCCCCCEECE		51.0925953088
149AcetylationAVPVKRPRVTVPLVR
CCCCCCCCEECEEEE		40.5519608861
149UbiquitinationAVPVKRPRVTVPLVR
CCCCCCCCEECEEEE		40.5519608861
149 (in isoform 2)Ubiquitination-40.5521890473
151PhosphorylationPVKRPRVTVPLVRRV
CCCCCCEECEEEEEC		20.0630266825
159SumoylationVPLVRRVKTNVPVKL
CEEEEECCCCCCEEE		32.35-
159UbiquitinationVPLVRRVKTNVPVKL
CEEEEECCCCCCEEE		32.35-
159SumoylationVPLVRRVKTNVPVKL
CEEEEECCCCCCEEE		32.3528112733
159AcetylationVPLVRRVKTNVPVKL
CEEEEECCCCCCEEE		32.3525953088
160PhosphorylationPLVRRVKTNVPVKLF
EEEEECCCCCCEEEE		38.2923312004
165AcetylationVKTNVPVKLFARSTA
CCCCCCEEEEEECCC		31.6419608861
165SumoylationVKTNVPVKLFARSTA
CCCCCCEEEEEECCC		31.64-
165UbiquitinationVKTNVPVKLFARSTA
CCCCCCEEEEEECCC		31.6421890473
165SumoylationVKTNVPVKLFARSTA
CCCCCCEEEEEECCC		31.6428112733
165 (in isoform 1)Ubiquitination-31.6421890473
170PhosphorylationPVKLFARSTAVTTSS
CEEEEEECCCCCCCC		19.7928985074
171PhosphorylationVKLFARSTAVTTSSA
EEEEEECCCCCCCCC		21.4225599653
174PhosphorylationFARSTAVTTSSAKIK
EEECCCCCCCCCEEE		20.6329396449
175PhosphorylationARSTAVTTSSAKIKL
EECCCCCCCCCEEEE		17.6829396449
175 (in isoform 2)Ubiquitination-17.6821890473
176PhosphorylationRSTAVTTSSAKIKLK
ECCCCCCCCCEEEEC		20.9525159151
177PhosphorylationSTAVTTSSAKIKLKS
CCCCCCCCCEEEECH		31.3325159151
179UbiquitinationAVTTSSAKIKLKSSE
CCCCCCCEEEECHHH		42.18-
179AcetylationAVTTSSAKIKLKSSE
CCCCCCCEEEECHHH		42.1825953088
179SumoylationAVTTSSAKIKLKSSE
CCCCCCCEEEECHHH		42.1828112733
181AcetylationTTSSAKIKLKSSELQ
CCCCCEEEECHHHHH		49.5128642531
181UbiquitinationTTSSAKIKLKSSELQ
CCCCCEEEECHHHHH		49.51-
183AcetylationSSAKIKLKSSELQAI
CCCEEEECHHHHHHH		47.1128642539
183UbiquitinationSSAKIKLKSSELQAI
CCCEEEECHHHHHHH		47.11-
183MalonylationSSAKIKLKSSELQAI
CCCEEEECHHHHHHH		47.1126320211
184PhosphorylationSAKIKLKSSELQAIK
CCEEEECHHHHHHHH		39.2125159151
185PhosphorylationAKIKLKSSELQAIKT
CEEEECHHHHHHHHH		40.5127251275
191UbiquitinationSSELQAIKTELTQIK
HHHHHHHHHHHHHHH		38.6721890473
191SumoylationSSELQAIKTELTQIK
HHHHHHHHHHHHHHH		38.6728112733
191AcetylationSSELQAIKTELTQIK
HHHHHHHHHHHHHHH		38.6726051181
191 (in isoform 1)Ubiquitination-38.6721890473
195PhosphorylationQAIKTELTQIKSNID
HHHHHHHHHHHHHHH		23.2430108239
198UbiquitinationKTELTQIKSNIDALL
HHHHHHHHHHHHHHH		27.86-
199PhosphorylationTELTQIKSNIDALLS
HHHHHHHHHHHHHHH		40.4230108239
200 (in isoform 2)Ubiquitination-31.0221890473
206PhosphorylationSNIDALLSRLEQIAA
HHHHHHHHHHHHHHH		35.3530108239
216UbiquitinationEQIAAEQKANPDGKK
HHHHHHHHCCCCCCC		41.452190698
216MalonylationEQIAAEQKANPDGKK
HHHHHHHHCCCCCCC		41.4526320211
216AcetylationEQIAAEQKANPDGKK
HHHHHHHHCCCCCCC		41.4525953088
216 (in isoform 1)Ubiquitination-41.4521890473
239PhosphorylationGGGGGGGSGGGGSGG
CCCCCCCCCCCCCCC		37.2222496350
244PhosphorylationGGSGGGGSGGGGGGG
CCCCCCCCCCCCCCC		37.2220873877
244O-linked_GlycosylationGGSGGGGSGGGGGGG
CCCCCCCCCCCCCCC		37.22OGP
252PhosphorylationGGGGGGGSSRPPAPQ
CCCCCCCCCCCCCCC		26.8428985074
252O-linked_GlycosylationGGGGGGGSSRPPAPQ
CCCCCCCCCCCCCCC		26.84OGP
253PhosphorylationGGGGGGSSRPPAPQE
CCCCCCCCCCCCCCC		52.6720873877
262PhosphorylationPPAPQENTTSEAGLP
CCCCCCCCCCCCCCC		30.8320873877
263PhosphorylationPAPQENTTSEAGLPQ
CCCCCCCCCCCCCCC		35.8320873877
264PhosphorylationAPQENTTSEAGLPQG
CCCCCCCCCCCCCCC		24.3420873877
275PhosphorylationLPQGEARTRDDGDEE
CCCCCCCCCCCCCCC		45.5623401153
286PhosphorylationGDEEGLLTHSEEELE
CCCCCCCCCCHHHHH		28.5322167270
288PhosphorylationEEGLLTHSEEELEHS
CCCCCCCCHHHHHHC		41.2822167270
295PhosphorylationSEEELEHSQDTDADD
CHHHHHHCCCCCCCC		22.0022167270
298PhosphorylationELEHSQDTDADDGAL
HHHHCCCCCCCCCCC		26.0022167270
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
135SPhosphorylationKinaseCDK2P24941
PSP
160TPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RALY_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 RALY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNR40_HUMANSNRNP40physical
22939629
RBM39_HUMANRBM39physical
22939629
RNPS1_HUMANRNPS1physical
22939629
ROA0_HUMANHNRNPA0physical
22939629
RS20_HUMANRPS20physical
22939629
HNRPC_HUMANHNRNPCphysical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
HNRPD_HUMANHNRNPDphysical
22365833
HNRH1_HUMANHNRNPH1physical
22365833
QKI_HUMANQKIphysical
22365833
KHDR1_HUMANKHDRBS1physical
22365833
CELF1_HUMANCELF1physical
22365833
HNRL2_HUMANHNRNPUL2physical
26344197
PRP8_HUMANPRPF8physical
26344197
RBP2_HUMANRANBP2physical
26344197
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 RALY_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-106; THR-286; SER-288;SER-295 AND THR-298, AND MASS SPECTROMETRY.
"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 SER-288, AND MASSSPECTROMETRY.
"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-135; THR-286; SER-288;SER-295 AND THR-298, 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-135, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.
"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-288; SER-295 ANDTHR-298, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.
"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-135; THR-286 ANDSER-288, 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-135; THR-286; SER-288;SER-295 AND THR-298, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND SER-295, ANDMASS SPECTROMETRY.

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