ROAA_HUMAN - dbPTM
ROAA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROAA_HUMAN
UniProt AC Q99729
Protein Name Heterogeneous nuclear ribonucleoprotein A/B
Gene Name HNRNPAB
Organism Homo sapiens (Human).
Sequence Length 332
Subcellular Localization Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description Binds single-stranded RNA. Has a high affinity for G-rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site..
Protein Sequence MSEAGEEQPMETTGATENGHEAVPEASRGRGWTGAAAGAGGATAAPPSGNQNGAEGDQINASKNEEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFKDAASVEKVLDQKEHRLDGRVIDPKKAMAMKKDPVKKIFVGGLNPESPTEEKIREYFGEFGEIEAIELPMDPKLNKRRGFVFITFKEEEPVKKVLEKKFHTVSGSKCEIKVAQPKEVYQQQQYGSGGRGNRNRGNRGSGGGGGGGGQSQSWNQGYGNYWNQGYGYQQGYGPGYGGYDYSPYGYYGYGPGYDYSQGSTNYGKSQRRGGHQNNYKPY
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
2Phosphorylation------MSEAGEEQP
------CCCCCCCCC		35.83-
2 (in isoform 2)Phosphorylation-35.8319664995
2 (in isoform 3)Phosphorylation-35.8319664995
2 (in isoform 4)Phosphorylation-35.8319664995
28 (in isoform 2)Phosphorylation-45.9719664995
28 (in isoform 3)Phosphorylation-45.9719664995
28 (in isoform 4)Phosphorylation-45.9719664995
43PhosphorylationAAGAGGATAAPPSGN
CCCCCCCCCCCCCCC		26.9926657352
48PhosphorylationGATAAPPSGNQNGAE
CCCCCCCCCCCCCCC		49.6826657352
70AcetylationKNEEDAGKMFVGGLS
CCHHHHHHHCCCEEC		30.7725953088
77PhosphorylationKMFVGGLSWDTSKKD
HHCCCEECCCCCHHH		26.6123403867
80PhosphorylationVGGLSWDTSKKDLKD
CCEECCCCCHHHHHH		35.8723403867
81PhosphorylationGGLSWDTSKKDLKDY
CEECCCCCHHHHHHH		34.9221955146
82AcetylationGLSWDTSKKDLKDYF
EECCCCCHHHHHHHH		53.0125953088
82MalonylationGLSWDTSKKDLKDYF
EECCCCCHHHHHHHH		53.0126320211
82UbiquitinationGLSWDTSKKDLKDYF
EECCCCCHHHHHHHH		53.01-
82 (in isoform 1)Ubiquitination-53.0121890473
83NeddylationLSWDTSKKDLKDYFT
ECCCCCHHHHHHHHH		68.9732015554
83UbiquitinationLSWDTSKKDLKDYFT
ECCCCCHHHHHHHHH		68.9723000965
83 (in isoform 2)Malonylation-68.9726320211
83 (in isoform 2)Ubiquitination-68.9721890473
83 (in isoform 3)Ubiquitination-68.9721890473
83 (in isoform 4)Ubiquitination-68.9721890473
84UbiquitinationSWDTSKKDLKDYFTK
CCCCCHHHHHHHHHH		63.7923000965
84 (in isoform 2)Ubiquitination-63.79-
86AcetylationDTSKKDLKDYFTKFG
CCCHHHHHHHHHHHH		61.5925825284
86UbiquitinationDTSKKDLKDYFTKFG
CCCHHHHHHHHHHHH		61.5921890473
86 (in isoform 1)Ubiquitination-61.5921890473
87UbiquitinationTSKKDLKDYFTKFGE
CCHHHHHHHHHHHHC		51.5923000965
87 (in isoform 2)Ubiquitination-51.5921890473
87 (in isoform 3)Ubiquitination-51.5921890473
87 (in isoform 4)Ubiquitination-51.5921890473
88PhosphorylationSKKDLKDYFTKFGEV
CHHHHHHHHHHHHCE		16.1528152594
90PhosphorylationKDLKDYFTKFGEVVD
HHHHHHHHHHHCEEE		21.1628152594
91AcetylationDLKDYFTKFGEVVDC
HHHHHHHHHHCEEEE		41.2825825284
91UbiquitinationDLKDYFTKFGEVVDC
HHHHHHHHHHCEEEE		41.2821890473
91 (in isoform 1)Ubiquitination-41.2821890473
92NeddylationLKDYFTKFGEVVDCT
HHHHHHHHHCEEEEE		10.2932015554
92UbiquitinationLKDYFTKFGEVVDCT
HHHHHHHHHCEEEEE		10.2923000965
92 (in isoform 2)Ubiquitination-10.2921890473
92 (in isoform 3)Ubiquitination-10.2921890473
92 (in isoform 4)Ubiquitination-10.2921890473
98S-nitrosylationKFGEVVDCTIKMDPN
HHHCEEEEEEEECCC		2.612212679
99PhosphorylationFGEVVDCTIKMDPNT
HHCEEEEEEEECCCC		21.1119664994
100PhosphorylationGEVVDCTIKMDPNTG
HCEEEEEEEECCCCC		4.3519664994
101AcetylationEVVDCTIKMDPNTGR
CEEEEEEEECCCCCC		21.0625953088
101UbiquitinationEVVDCTIKMDPNTGR
CEEEEEEEECCCCCC		21.0621890473
101 (in isoform 1)Ubiquitination-21.0621890473
102NeddylationVVDCTIKMDPNTGRS
EEEEEEEECCCCCCC		10.2832015554
102UbiquitinationVVDCTIKMDPNTGRS
EEEEEEEECCCCCCC		10.2833845483
102 (in isoform 2)Malonylation-10.2826320211
102 (in isoform 2)Ubiquitination-10.2821890473
102 (in isoform 3)Ubiquitination-10.2821890473
102 (in isoform 4)Ubiquitination-10.2821890473
118AcetylationGFGFILFKDAASVEK
CEEEEEECCHHHHHH		42.9126051181
118UbiquitinationGFGFILFKDAASVEK
CEEEEEECCHHHHHH		42.9121890473
118 (in isoform 1)Ubiquitination-42.9121890473
119UbiquitinationFGFILFKDAASVEKV
EEEEEECCHHHHHHH		39.7821890473
119 (in isoform 2)Ubiquitination-39.7821890473
119 (in isoform 3)Ubiquitination-39.7821890473
119 (in isoform 4)Ubiquitination-39.7821890473
122PhosphorylationILFKDAASVEKVLDQ
EEECCHHHHHHHHHC		32.3124719451
125AcetylationKDAASVEKVLDQKEH
CCHHHHHHHHHCCHH		46.0426051181
125UbiquitinationKDAASVEKVLDQKEH
CCHHHHHHHHHCCHH		46.0421890473
125 (in isoform 1)Ubiquitination-46.0421890473
126UbiquitinationDAASVEKVLDQKEHR
CHHHHHHHHHCCHHH		4.5123000965
126 (in isoform 2)Ubiquitination-4.5121890473
126 (in isoform 3)Ubiquitination-4.5121890473
126 (in isoform 4)Ubiquitination-4.5121890473
130SuccinylationVEKVLDQKEHRLDGR
HHHHHHCCHHHCCCE		55.9723954790
130SumoylationVEKVLDQKEHRLDGR
HHHHHHCCHHHCCCE		55.9728112733
130UbiquitinationVEKVLDQKEHRLDGR
HHHHHHCCHHHCCCE		55.97-
130 (in isoform 1)Ubiquitination-55.9721890473
131UbiquitinationEKVLDQKEHRLDGRV
HHHHHCCHHHCCCEE		28.7123000965
131 (in isoform 2)Ubiquitination-28.7121890473
131 (in isoform 3)Ubiquitination-28.7121890473
131 (in isoform 4)Ubiquitination-28.7121890473
144UbiquitinationRVIDPKKAMAMKKDP
EECCHHHHHHCCCCC		9.3323503661
149UbiquitinationKKAMAMKKDPVKKIF
HHHHHCCCCCCCEEE		54.9323000965
150UbiquitinationKAMAMKKDPVKKIFV
HHHHCCCCCCCEEEE		47.9423000965
150 (in isoform 2)Ubiquitination-47.94-
154UbiquitinationMKKDPVKKIFVGGLN
CCCCCCCEEEECCCC		41.4323000965
155UbiquitinationKKDPVKKIFVGGLNP
CCCCCCEEEECCCCC		2.5423000965
155 (in isoform 2)Malonylation-2.5426320211
155 (in isoform 2)Ubiquitination-2.5421890473
155 (in isoform 3)Ubiquitination-2.5421890473
169UbiquitinationPESPTEEKIREYFGE
CCCCCHHHHHHHHHC		40.6123000965
169 (in isoform 2)Ubiquitination-40.6121890473
169 (in isoform 3)Ubiquitination-40.6121890473
187SulfoxidationIEAIELPMDPKLNKR
EEEEECCCCCCCCCC		25.0430846556
190UbiquitinationIELPMDPKLNKRRGF
EECCCCCCCCCCCCE		61.5029967540
203AcetylationGFVFITFKEEEPVKK
CEEEEEECCCCHHHH		56.4126051181
203SumoylationGFVFITFKEEEPVKK
CEEEEEECCCCHHHH		56.4128112733
209AcetylationFKEEEPVKKVLEKKF
ECCCCHHHHHHHHHE		48.1326051181
209UbiquitinationFKEEEPVKKVLEKKF
ECCCCHHHHHHHHHE		48.1333845483
215AcetylationVKKVLEKKFHTVSGS
HHHHHHHHEEECCCC		32.7625825284
215UbiquitinationVKKVLEKKFHTVSGS
HHHHHHHHEEECCCC		32.7629967540
223AcetylationFHTVSGSKCEIKVAQ
EEECCCCCCEEEECC		39.1425953088
223UbiquitinationFHTVSGSKCEIKVAQ
EEECCCCCCEEEECC		39.1423000965
223 (in isoform 3)Ubiquitination-39.14-
227AcetylationSGSKCEIKVAQPKEV
CCCCCEEEECCCHHH		14.8226051181
227UbiquitinationSGSKCEIKVAQPKEV
CCCCCEEEECCCHHH		14.8223000965
232AcetylationEIKVAQPKEVYQQQQ
EEEECCCHHHHHHCC		47.9726051181
232SuccinylationEIKVAQPKEVYQQQQ
EEEECCCHHHHHHCC		47.9723954790
232UbiquitinationEIKVAQPKEVYQQQQ
EEEECCCHHHHHHCC		47.9723000965
232 (in isoform 1)Ubiquitination-47.9721890473
232 (in isoform 2)Ubiquitination-47.9721890473
232 (in isoform 3)Ubiquitination-47.9721890473
233 (in isoform 4)Ubiquitination-53.8121890473
235PhosphorylationVAQPKEVYQQQQYGS
ECCCHHHHHHCCCCC		11.1617287340
235 (in isoform 3)Phosphorylation-11.1617287340
236 (in isoform 4)Phosphorylation-39.5217287340
240PhosphorylationEVYQQQQYGSGGRGN
HHHHHCCCCCCCCCC		14.6627273156
242PhosphorylationYQQQQYGSGGRGNRN
HHHCCCCCCCCCCCC		32.8925159151
245DimethylationQQYGSGGRGNRNRGN
CCCCCCCCCCCCCCC		42.62-
245MethylationQQYGSGGRGNRNRGN
CCCCCCCCCCCCCCC		42.6212018057
248DimethylationGSGGRGNRNRGNRGS
CCCCCCCCCCCCCCC		36.73-
248MethylationGSGGRGNRNRGNRGS
CCCCCCCCCCCCCCC		36.7312018073
250MethylationGGRGNRNRGNRGSGG
CCCCCCCCCCCCCCC		40.2916187677
250 (in isoform 3)Methylation-40.2924129315
251 (in isoform 4)Methylation-31.5624129315
253MethylationGNRNRGNRGSGGGGG
CCCCCCCCCCCCCCC		43.4012020127
253 (in isoform 3)Methylation-43.4024129315
254 (in isoform 4)Methylation-34.3424129315
255PhosphorylationRNRGNRGSGGGGGGG
CCCCCCCCCCCCCCC		30.9023663014
255 (in isoform 3)Phosphorylation-30.9025159151
256 (in isoform 4)Phosphorylation-41.4025159151
266 (in isoform 3)Phosphorylation-44.5728176443
267 (in isoform 3)Phosphorylation-32.9928176443
267 (in isoform 4)Phosphorylation-32.9928176443
268 (in isoform 4)Phosphorylation-8.1028176443
269 (in isoform 3)Phosphorylation-30.5528176443
270 (in isoform 4)Phosphorylation-39.9828176443
271AcetylationQSQSWNQGYGNYWNQ
CCCCCCCCCCCCCCC		29.1519608861
271UbiquitinationQSQSWNQGYGNYWNQ
CCCCCCCCCCCCCCC		29.1523000965
271 (in isoform 3)Acetylation-29.1519608861
271 (in isoform 3)Ubiquitination-29.15-
272 (in isoform 3)Phosphorylation-7.7626434776
272 (in isoform 4)Acetylation-7.7619608861
273 (in isoform 4)Phosphorylation-27.8126434776
275MethylationWNQGYGNYWNQGYGY
CCCCCCCCCCCCCCC		11.0215782174
283AcetylationWNQGYGYQQGYGPGY
CCCCCCCCCCCCCCC		26.3419608861
300PhosphorylationYDYSPYGYYGYGPGY
CCCCCCCCCCCCCCC		6.46-
309PhosphorylationGYGPGYDYSQGSTNY
CCCCCCCCCCCCCCC		8.3926074081
310PhosphorylationYGPGYDYSQGSTNYG
CCCCCCCCCCCCCCC		25.7626074081
313PhosphorylationGYDYSQGSTNYGKSQ
CCCCCCCCCCCCCCC		13.0726074081
314PhosphorylationYDYSQGSTNYGKSQR
CCCCCCCCCCCCCCC		39.0126074081
316PhosphorylationYSQGSTNYGKSQRRG
CCCCCCCCCCCCCCC		26.4726074081
318AcetylationQGSTNYGKSQRRGGH
CCCCCCCCCCCCCCC		32.8126051181
318UbiquitinationQGSTNYGKSQRRGGH
CCCCCCCCCCCCCCC		32.8123000965
319PhosphorylationGSTNYGKSQRRGGHQ
CCCCCCCCCCCCCCC		25.2626074081
321MethylationTNYGKSQRRGGHQNN
CCCCCCCCCCCCCCC		46.4354548183
322Asymmetric dimethylarginineNYGKSQRRGGHQNNY
CCCCCCCCCCCCCCC		48.05-
322MethylationNYGKSQRRGGHQNNY
CCCCCCCCCCCCCCC		48.0512017981
329PhosphorylationRGGHQNNYKPY----
CCCCCCCCCCC----		22.3828152594
330AcetylationGGHQNNYKPY-----
CCCCCCCCCC-----		39.7123749302
330MethylationGGHQNNYKPY-----
CCCCCCCCCC-----		39.7122641123
332PhosphorylationHQNNYKPY-------
CCCCCCCC-------		27.3428152594
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 ROAA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
322RMethylation

15782174
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 ROAA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P63_HUMANTP63physical
12692135
HXC13_HUMANHOXC13physical
20211142
HXD4_HUMANHOXD4physical
20211142
RFOX2_HUMANRBFOX2physical
20211142
DEDD2_HUMANDEDD2physical
20211142
RT18B_HUMANMRPS18Bphysical
22939629
RT07_HUMANMRPS7physical
22939629
RT25_HUMANMRPS25physical
22939629
SNP23_HUMANSNAP23physical
22939629
VAS1_HUMANATP6AP1physical
22939629
PTBP1_HUMANPTBP1physical
22365833
PTBP2_HUMANPTBP2physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
HMGA1_HUMANHMGA1physical
18850631
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 ROAA_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-318 AND LYS-330, AND MASSSPECTROMETRY.
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322, AND MASS SPECTROMETRY.
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, 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-242, AND MASSSPECTROMETRY.
"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-242, 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 SER-242, AND MASSSPECTROMETRY.

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