RBMS2_HUMAN - dbPTM
RBMS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBMS2_HUMAN
UniProt AC Q15434
Protein Name RNA-binding motif, single-stranded-interacting protein 2
Gene Name RBMS2
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MLLSVTSRPGISTFGYNRNNKKPYVSLAQQMAPPSPSNSTPNSSSGSNGNDQLSKTNLYIRGLQPGTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPSAAQKAVTALKASGVQAQMAKQQEQDPTNLYISNLPLSMDEQELEGMLKPFGQVISTRILRDTSGTSRGVGFARMESTEKCEAIITHFNGKYIKTPPGVPAPSDPLLCKFADGGPKKRQNQGKFVQNGRAWPRNADMGVMALTYDPTTALQNGFYPAPYNITPNRMLAQSALSPYLSSPVSSYQRVTQTSPLQVPNPSWMHHHSYLMQPSGSVLTPGMDHPISLQPASMMGPLTQQLGHLSLSSTGTYMPTAAAMQGAYISQYTPVPSSSVSVEESSGQQNQVAVDAPSEHGVYSFQFNK
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
1Acetylation-------MLLSVTSR
-------CCCCCCCC		8.4022814378
4Phosphorylation----MLLSVTSRPGI
----CCCCCCCCCCC		21.2729523821
6Phosphorylation--MLLSVTSRPGIST
--CCCCCCCCCCCCC		18.6828857561
7Phosphorylation-MLLSVTSRPGISTF
-CCCCCCCCCCCCCC		34.0328857561
12PhosphorylationVTSRPGISTFGYNRN
CCCCCCCCCCCCCCC		24.4929523821
13PhosphorylationTSRPGISTFGYNRNN
CCCCCCCCCCCCCCC		21.1129523821
24PhosphorylationNRNNKKPYVSLAQQM
CCCCCCCCEEHHHHC		16.1430576142
26PhosphorylationNNKKPYVSLAQQMAP
CCCCCCEEHHHHCCC		16.4929514088
35PhosphorylationAQQMAPPSPSNSTPN
HHHCCCCCCCCCCCC		39.6425159151
37PhosphorylationQMAPPSPSNSTPNSS
HCCCCCCCCCCCCCC		47.9923403867
39PhosphorylationAPPSPSNSTPNSSSG
CCCCCCCCCCCCCCC		49.9726657352
40PhosphorylationPPSPSNSTPNSSSGS
CCCCCCCCCCCCCCC		30.6430576142
43PhosphorylationPSNSTPNSSSGSNGN
CCCCCCCCCCCCCCC		27.3830576142
44PhosphorylationSNSTPNSSSGSNGND
CCCCCCCCCCCCCCC		45.4130576142
45PhosphorylationNSTPNSSSGSNGNDQ
CCCCCCCCCCCCCCC		46.1729514088
47PhosphorylationTPNSSSGSNGNDQLS
CCCCCCCCCCCCCCH		43.4429514088
54PhosphorylationSNGNDQLSKTNLYIR
CCCCCCCHHCCEEEC		31.6230576142
56PhosphorylationGNDQLSKTNLYIRGL
CCCCCHHCCEEECCC		27.38-
59PhosphorylationQLSKTNLYIRGLQPG
CCHHCCEEECCCCCC		7.2219690332
67PhosphorylationIRGLQPGTTDQDLVK
ECCCCCCCCHHHHHH		33.6022817900
68PhosphorylationRGLQPGTTDQDLVKL
CCCCCCCCHHHHHHH		37.2622817900
74UbiquitinationTTDQDLVKLCQPYGK
CCHHHHHHHHHCCCC		51.3333845483
79PhosphorylationLVKLCQPYGKIVSTK
HHHHHHCCCCEEEEH		12.7429496907
81UbiquitinationKLCQPYGKIVSTKAI
HHHHCCCCEEEEHHH		33.8129967540
84PhosphorylationQPYGKIVSTKAILDK
HCCCCEEEEHHHHHC		27.8823403867
85PhosphorylationPYGKIVSTKAILDKT
CCCCEEEEHHHHHCC		17.3823403867
91MalonylationSTKAILDKTTNKCKG
EEHHHHHCCCCCCCC		54.5326320211
91UbiquitinationSTKAILDKTTNKCKG
EEHHHHHCCCCCCCC		54.5333845483
92PhosphorylationTKAILDKTTNKCKGY
EHHHHHCCCCCCCCC		34.96-
93PhosphorylationKAILDKTTNKCKGYG
HHHHHCCCCCCCCCC		38.12-
95UbiquitinationILDKTTNKCKGYGFV
HHHCCCCCCCCCCCC		34.92-
99PhosphorylationTTNKCKGYGFVDFDS
CCCCCCCCCCCCCCC		7.9023663014
106PhosphorylationYGFVDFDSPSAAQKA
CCCCCCCCHHHHHHH		22.2822167270
108PhosphorylationFVDFDSPSAAQKAVT
CCCCCCHHHHHHHHH		39.9430266825
112UbiquitinationDSPSAAQKAVTALKA
CCHHHHHHHHHHHHH		39.8529967540
118UbiquitinationQKAVTALKASGVQAQ
HHHHHHHHHHHHHHH		37.7329967540
184PhosphorylationVGFARMESTEKCEAI
CCEEECCCHHHCCEE		32.3030624053
199PhosphorylationITHFNGKYIKTPPGV
EEEECCCEECCCCCC		14.7329396449
201UbiquitinationHFNGKYIKTPPGVPA
EECCCEECCCCCCCC		52.4629967540
202PhosphorylationFNGKYIKTPPGVPAP
ECCCEECCCCCCCCC		25.7621815630
210PhosphorylationPPGVPAPSDPLLCKF
CCCCCCCCCCEEEEE		54.7022210691
215S-nitrosylationAPSDPLLCKFADGGP
CCCCCEEEEECCCCC		4.4822126794
216SumoylationPSDPLLCKFADGGPK
CCCCEEEEECCCCCC		43.48-
216UbiquitinationPSDPLLCKFADGGPK
CCCCEEEEECCCCCC		43.4829967540
266PhosphorylationNGFYPAPYNITPNRM
CCCCCCCCCCCCCCH		22.6920068231
269PhosphorylationYPAPYNITPNRMLAQ
CCCCCCCCCCCHHHH		15.7522199227
277PhosphorylationPNRMLAQSALSPYLS
CCCHHHHHHCHHHHC		26.1030576142
280PhosphorylationMLAQSALSPYLSSPV
HHHHHHCHHHHCCCC		15.9425159151
282PhosphorylationAQSALSPYLSSPVSS
HHHHCHHHHCCCCHH		18.8122199227
284PhosphorylationSALSPYLSSPVSSYQ
HHCHHHHCCCCHHCC		27.1029496963
285PhosphorylationALSPYLSSPVSSYQR
HCHHHHCCCCHHCCC		27.0725159151
285O-linked_GlycosylationALSPYLSSPVSSYQR
HCHHHHCCCCHHCCC		27.0730059200
288PhosphorylationPYLSSPVSSYQRVTQ
HHHCCCCHHCCCCCC		27.0622199227
288O-linked_GlycosylationPYLSSPVSSYQRVTQ
HHHCCCCHHCCCCCC		27.0630059200
289PhosphorylationYLSSPVSSYQRVTQT
HHCCCCHHCCCCCCC		26.0622199227
290PhosphorylationLSSPVSSYQRVTQTS
HCCCCHHCCCCCCCC		7.8829759185
401PhosphorylationAPSEHGVYSFQFNK-
CCCCCCEEEEEECC-		14.36-
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 RBMS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBMS2_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 RBMS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRA2B_HUMANTRA2Bphysical
22939629
TSR1_HUMANTSR1physical
22939629
RM16_HUMANMRPL16physical
22939629
SRSF3_HUMANSRSF3physical
22939629
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 RBMS2_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-67; THR-68 AND SER-106,AND MASS SPECTROMETRY.
"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-106, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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-106; THR-269; SER-280AND SER-285, 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-106, AND MASSSPECTROMETRY.

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