RBM41_HUMAN - dbPTM
RBM41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM41_HUMAN
UniProt AC Q96IZ5
Protein Name RNA-binding protein 41
Gene Name RBM41
Organism Homo sapiens (Human).
Sequence Length 413
Subcellular Localization
Protein Description May bind RNA..
Protein Sequence MKRVNSCVKSDEHVLEELETEGERQLKSLLQHQLDTSVSIEECMSKKESFAPGTMYKPFGKEAAGTMTLSQFQTLHEKDQETASLRELGLNETEILIWKSHVSGEKKTKLRATPEAIQNRLQDIEERISERQRILCLPQRFAKSKQLTRREMEIEKSLFQGADRHSFLKALYYQDEPQKKNKGDPMNNLESFYQEMIMKKRLEEFQLMRGEPFASHSLVSATSVGDSGTAESPSLLQDKGKQAAQGKGPSLHVANVIDFSPEQCWTGPKKLTQPIEFVPEDEIQRNRLSEEEIRKIPMFSSYNPGEPNKVLYLKNLSPRVTERDLVSLFARFQEKKGPPIQFRMMTGRMRGQAFITFPNKEIAWQALHLVNGYKLHGKILVIEFGKNKKQRSNLQATSLISCATGSTTEISGS
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
6Phosphorylation--MKRVNSCVKSDEH
--CCCCHHHCCCCHH		19.8926074081
10PhosphorylationRVNSCVKSDEHVLEE
CCHHHCCCCHHHHHH		28.0326074081
47UbiquitinationIEECMSKKESFAPGT
HHHHHCCCCCCCCCC		51.8129967540
49PhosphorylationECMSKKESFAPGTMY
HHHCCCCCCCCCCCC		35.2728555341
57UbiquitinationFAPGTMYKPFGKEAA
CCCCCCCCCCCCCCC		24.0529967540
100PhosphorylationTEILIWKSHVSGEKK
CEEEEEECCCCCCCC		17.7126657352
100O-linked_GlycosylationTEILIWKSHVSGEKK
CEEEEEECCCCCCCC		17.7130379171
103PhosphorylationLIWKSHVSGEKKTKL
EEEECCCCCCCCHHH		35.4926657352
103O-linked_GlycosylationLIWKSHVSGEKKTKL
EEEECCCCCCCCHHH		35.4930379171
113PhosphorylationKKTKLRATPEAIQNR
CCHHHCCCHHHHHHH		18.4128674419
166PhosphorylationFQGADRHSFLKALYY
HCCCCHHHHHHHHHC		32.9224719451
172PhosphorylationHSFLKALYYQDEPQK
HHHHHHHHCCCCCCC		12.1629496907
173PhosphorylationSFLKALYYQDEPQKK
HHHHHHHCCCCCCCC		15.4429496907
181 (in isoform 3)Phosphorylation-61.6530631047
188 (in isoform 3)Phosphorylation-38.6430631047
200UbiquitinationYQEMIMKKRLEEFQL
HHHHHHHHHHHHHHH		44.8529967540
232PhosphorylationGDSGTAESPSLLQDK
CCCCCCCCHHHHHCH		19.8218669648
239UbiquitinationSPSLLQDKGKQAAQG
CHHHHHCHHHHHHCC		55.8629967540
260PhosphorylationVANVIDFSPEQCWTG
EEEEEECCHHHHCCC		24.6325159151
266 (in isoform 3)Phosphorylation-51.7624043423
267 (in isoform 3)Phosphorylation-13.9224043423
268 (in isoform 3)Phosphorylation-24.1918669648
270UbiquitinationQCWTGPKKLTQPIEF
HHCCCCCCCCCCCEE		60.9629967540
270 (in isoform 3)Phosphorylation-60.9624043423
270SumoylationQCWTGPKKLTQPIEF
HHCCCCCCCCCCCEE		60.96-
270SumoylationQCWTGPKKLTQPIEF
HHCCCCCCCCCCCEE		60.96-
275 (in isoform 3)Phosphorylation-4.6324043423
278 (in isoform 3)Phosphorylation-3.0918669648
280 (in isoform 3)Phosphorylation-64.0724043423
283 (in isoform 3)Phosphorylation-7.8324043423
284 (in isoform 3)Phosphorylation-34.2524043423
285 (in isoform 3)Phosphorylation-35.5824043423
288 (in isoform 3)Phosphorylation-9.6124043423
295UbiquitinationLSEEEIRKIPMFSSY
CCHHHHHCCCCCCCC		57.7429967540
295 (in isoform 3)Phosphorylation-57.7424043423
297 (in isoform 3)Phosphorylation-22.3224043423
302PhosphorylationKIPMFSSYNPGEPNK
CCCCCCCCCCCCCCC		24.9522817900
386AcetylationILVIEFGKNKKQRSN
EEEEECCCCHHHCCC		71.5526051181
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 RBM41_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM41_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 RBM41_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RALYL_HUMANRALYLphysical
16189514
TRI54_HUMANTRIM54physical
25416956
RINT1_HUMANRINT1physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
RALYL_HUMANRALYLphysical
25416956
MIPO1_HUMANMIPOL1physical
25416956
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 RBM41_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-232, AND MASSSPECTROMETRY.

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