HNRPM_RAT - dbPTM
HNRPM_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPM_RAT
UniProt AC Q62826
Protein Name Heterogeneous nuclear ribonucleoprotein M
Gene Name Hnrnpm
Organism Rattus norvegicus (Rat).
Sequence Length 690
Subcellular Localization Nucleus matrix .
Protein Description Pre-mRNA binding protein, binds avidly to poly(G) and poly(U) RNA homopolymers. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines..
Protein Sequence MAAGVEAAAEVAATEPKMEEESGAPCVPSGNGAPVPKGEERPTQNEKRKEKNIKRGGNRFEPYANPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQSIEAVQAISMFNGQLLFDRPMHVKMDERALPKGDFFPPERPQQLPHGLGGIGMGLGPGGQPIDANHLNKGIGMGNLGPAGMGMEGIGFGINKIGGMEGPFGGGMENMGRFGSGMNMGRINEILSNALKRGEIIAKQGGSGAGGSVPGIERMGPGIDRISGAGMERMGAGLGHGMDRVGSEIERMGLVMDRMGSVERMGSGIERMGPLGLDHMASSIERMGQTMERIGSGVERMGAGMGFGLERMAAPIDRVGQTIERMGSGVERMGPAIERMGLSMDRMVPTGMGAGLERMGPVMDRMATGLERMGANNLERMGLERMGANSLERMGLERMGANSLERMGPAMGPALGAGIERMGLAMGGAGGASFDRTIEMERGNFGGSFAGSFGGAGGHAPGVARKACQIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVKFESPEVAERACRMMNGMKLSGREIDVRIDRNA
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------MAAGVEAAA
------CCCHHHHHH
16.96-
29PhosphorylationSGAPCVPSGNGAPVP
CCCCCCCCCCCCCCC
25.21-
85PhosphorylationPFDVKWQSLKDLVKE
CCCCCHHHHHHHHHH
35.9523984901
133AcetylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC
30.34-
137PhosphorylationVLNKHSLSGRPLKVK
HHHHCCCCCCCCCCC
35.4523984901
144SuccinylationSGRPLKVKEDPDGEH
CCCCCCCCCCCCHHH
55.6126843850
164PhosphorylationQKAGRLGSTVFVANL
HHHCCCCCEEEEECC
26.4523984901
165PhosphorylationKAGRLGSTVFVANLD
HHCCCCCEEEEECCC
19.0323984901
199SuccinylationRADILEDKDGKSRGI
EEEEEECCCCCCCCC
60.0326843850
199AcetylationRADILEDKDGKSRGI
EEEEEECCCCCCCCC
60.0322902405
237AcetylationFDRPMHVKMDERALP
ECCCEECCCCCCCCC
26.42-
238AcetylationDRPMHVKMDERALPK
CCCEECCCCCCCCCC
6.69-
325PhosphorylationENMGRFGSGMNMGRI
CCCCCCCCCCCHHHH
31.9623984901
337PhosphorylationGRINEILSNALKRGE
HHHHHHHHHHHHHCC
26.2223984901
357PhosphorylationGGSGAGGSVPGIERM
CCCCCCCCCCCHHHC
24.99-
372PhosphorylationGPGIDRISGAGMERM
CCCCCCCCCCCHHHH
24.3923984901
387UbiquitinationGAGLGHGMDRVGSEI
CCCCCCCHHHCCHHH
2.17-
392PhosphorylationHGMDRVGSEIERMGL
CCHHHCCHHHHHHCH
32.3229779826
396PhosphorylationRVGSEIERMGLVMDR
HCCHHHHHHCHHHHC
30.08-
406PhosphorylationLVMDRMGSVERMGSG
HHHHCCCCHHCCCCC
16.0921630457
412PhosphorylationGSVERMGSGIERMGP
CCHHCCCCCHHHCCC
27.53-
427PhosphorylationLGLDHMASSIERMGQ
CCHHHHHHHHHHHHH
25.0323984901
428PhosphorylationGLDHMASSIERMGQT
CHHHHHHHHHHHHHH
20.9427097102
431PhosphorylationHMASSIERMGQTMER
HHHHHHHHHHHHHHH
32.63-
441PhosphorylationQTMERIGSGVERMGA
HHHHHHHCCHHHCCC
36.9829779826
445PhosphorylationRIGSGVERMGAGMGF
HHHCCHHHCCCCCCC
26.82-
456MethylationGMGFGLERMAAPIDR
CCCCCHHHCCCCHHH
25.69-
467PhosphorylationPIDRVGQTIERMGSG
CHHHHHHHHHHHCCC
20.9023984901
473PhosphorylationQTIERMGSGVERMGP
HHHHHHCCCHHHHHH
30.2628432305
480PhosphorylationSGVERMGPAIERMGL
CCHHHHHHHHHHCCC
22.26-
488PhosphorylationAIERMGLSMDRMVPT
HHHHCCCCCCCCCCC
16.9528432305
495MethylationSMDRMVPTGMGAGLE
CCCCCCCCCCCCCHH
28.52-
527PhosphorylationANNLERMGLERMGAN
HHHHHHHCHHHCCCH
30.52-
535PhosphorylationLERMGANSLERMGLE
HHHCCCHHHHHHCHH
30.9521738781
548PhosphorylationLERMGANSLERMGPA
HHHCCCCHHHHHCCH
30.9521738781
574PhosphorylationMGLAMGGAGGASFDR
HCCCCCCCCCCCCCC
13.91-
578PhosphorylationMGGAGGASFDRTIEM
CCCCCCCCCCCEEEE
30.8427097102
587PhosphorylationDRTIEMERGNFGGSF
CCEEEECCCCCCCCC
44.00-
593PhosphorylationERGNFGGSFAGSFGG
CCCCCCCCCCCCCCC
16.5927097102
597PhosphorylationFGGSFAGSFGGAGGH
CCCCCCCCCCCCCCC
19.7927097102
625PhosphorylationRNLPFDFTWKMLKDK
HCCCCCCHHHHHHHH
26.4823984901
632AcetylationTWKMLKDKFNECGHV
HHHHHHHHHHCCCCE
48.80-
658AcetylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH
40.7925786129
661PhosphorylationCGVVKFESPEVAERA
CEEEEECCHHHHHHH
29.5027097102
697AcetylationA--------------
C--------------
-
700Phosphorylation-----------------
-----------------
-

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 HNRPM_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRPM_RAT !!

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 HNRPM_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEAM5_HUMANCEACAM5physical
11406629

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPM_RAT

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Related Literatures of Post-Translational Modification

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