HNRPM_MOUSE - dbPTM
HNRPM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPM_MOUSE
UniProt AC Q9D0E1
Protein Name Heterogeneous nuclear ribonucleoprotein M
Gene Name Hnrnpm
Organism Mus musculus (Mouse).
Sequence Length 729
Subcellular Localization Nucleus.
Protein Description Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. 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 (By similarity)..
Protein Sequence MAAGVEAAAEVAATEPKMEEESGAPCVPSGNGAPGPKGEERPTQNEKRKEKNIKRGGNRFEPYSNPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKVMATTGGMGMGPGGPGMINIPPSILNNPNIPNEIIHALQAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGIVTFEQSIEAVQAISMFNGQLLFDRPMHVKMDERALPKGDFFPPERPQQLPHGLGGIGMGLGPGGQPIDANHLSKGIGMGNLGPAGMGMEGIGFGINKIGGMEGPFGGGMENMGRFGSGMNMGRINEILSNALKRGEIIAKQGGGGAGGSVPGIERMGPGIDRISGAGMERMGAGLGHGMDRVGSEIERMGLVMDRMGSVERMGSSIERMGPLGLDHMASSIERMGQTMERIGSGVERMGAGMGFGLERMAAPIDRVGQTIERMGSGVERMGPAIERMGLSMDRMVPTGMGASLERMGPVMDRMATGLERMGANNLERMGLERMGANSLERMGLERMGANSLERMGPAMGPALGAGIERMGLAMGGAGGASFDRAIEMERGNFGGSFAGSFGGAGGHAPGVARKACQIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVKFESPEVAERACRMMNGMKLSGREIDVRIDRNA
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-
22PhosphorylationEPKMEEESGAPCVPS
CCCCCHHCCCCCCCC		43.4627717184
26GlutathionylationEEESGAPCVPSGNGA
CHHCCCCCCCCCCCC		7.5324333276
29PhosphorylationSGAPCVPSGNGAPGP
CCCCCCCCCCCCCCC		25.2127717184
63PhosphorylationGGNRFEPYSNPTKRY
CCCCCCCCCCCCHHH		17.5522817900
64PhosphorylationGNRFEPYSNPTKRYR
CCCCCCCCCCCHHHH		47.2325338131
67PhosphorylationFEPYSNPTKRYRAFI
CCCCCCCCHHHHEEC		32.1929176673
68UbiquitinationEPYSNPTKRYRAFIT
CCCCCCCHHHHEECC		49.00-
75PhosphorylationKRYRAFITNIPFDVK
HHHHEECCCCCCCCC		22.2023984901
82AcetylationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.1622826441
82UbiquitinationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.16-
85PhosphorylationPFDVKWQSLKDLVKE
CCCCCHHHHHHHHHH		35.9521659605
87UbiquitinationDVKWQSLKDLVKEKV
CCCHHHHHHHHHHHC		55.02-
113S-nitrosylationAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.2320925432
113S-nitrosocysteineAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.23-
113GlutathionylationAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.2324333276
133MalonylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.3426320211
133AcetylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.3423806337
133UbiquitinationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.34-
135PhosphorylationAEVLNKHSLSGRPLK
HHHHHHCCCCCCCCC		26.3229176673
137PhosphorylationVLNKHSLSGRPLKVK
HHHHCCCCCCCCCCC		35.4529176673
164 (in isoform 2)Phosphorylation-21.5329514104
203PhosphorylationLQAGRLGSTVFVANL
HHCCCCCCEEEEEEC		26.4525338131
238AcetylationRADILEDKDGKSRGI
EEEEEECCCCCCCCE		60.0323954790
276AcetylationFDRPMHVKMDERALP
ECCCEECCCCCCCCC		26.42-
364PhosphorylationENMGRFGSGMNMGRI
CCCCCCCCCCCHHHH		31.9622817900
376PhosphorylationGRINEILSNALKRGE
HHHHHHHHHHHHHCC		26.2222817900
380UbiquitinationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.82-
380AcetylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.8222826441
380MalonylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.8226320211
387UbiquitinationKRGEIIAKQGGGGAG
HHCCEEEECCCCCCC		38.78-
396PhosphorylationGGGGAGGSVPGIERM
CCCCCCCCCCCHHHC		24.9923527152
411PhosphorylationGPGIDRISGAGMERM
CCCCCCCCCCCHHHH		24.3926824392
431PhosphorylationHGMDRVGSEIERMGL
CCHHHCCHHHHHHCH		32.3223527152
445PhosphorylationLVMDRMGSVERMGSS
HHHHCCCCHHHHCCC		16.0924453211
451PhosphorylationGSVERMGSSIERMGP
CCHHHHCCCHHHHCC		20.8524453211
452PhosphorylationSVERMGSSIERMGPL
CHHHHCCCHHHHCCC		23.8024068923
466PhosphorylationLGLDHMASSIERMGQ
CCHHHHHHHHHHHHH		25.0328507225
467PhosphorylationGLDHMASSIERMGQT
CHHHHHHHHHHHHHH		20.9426643407
480PhosphorylationQTMERIGSGVERMGA
HHHHHHHCCHHHCCC		36.9823684622
495MethylationGMGFGLERMAAPIDR
CCCCCHHHCCCCHHH		25.6924391387
506PhosphorylationPIDRVGQTIERMGSG
CHHHHHHHHHHHCCC		20.9029514104
512PhosphorylationQTIERMGSGVERMGP
HHHHHHCCCHHHHHH		30.2622817900
527PhosphorylationAIERMGLSMDRMVPT
HHHHCCCCCCCCCCC		16.9527149854
534PhosphorylationSMDRMVPTGMGASLE
CCCCCCCCCCCHHHH		28.5228833060
539PhosphorylationVPTGMGASLERMGPV
CCCCCCHHHHHHHHH		25.6514729942
552PhosphorylationPVMDRMATGLERMGA
HHHHHHHHHHHHHCH		32.7227600695
574PhosphorylationLERMGANSLERMGLE
HHHCCCHHHHHHCHH		30.9523527152
587PhosphorylationLERMGANSLERMGPA
HHHCCCCHHHHHCCH		30.9523527152
617PhosphorylationMGGAGGASFDRAIEM
CCCCCCCCHHHHHHC		30.8425521595
632PhosphorylationERGNFGGSFAGSFGG
CCCCCCCCCCCCCCC		16.5927899381
636PhosphorylationFGGSFAGSFGGAGGH
CCCCCCCCCCCCCCC		19.7926824392
650MalonylationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.7226320211
650UbiquitinationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.72-
657MethylationKACQIFVRNLPFDFT
HHHHHHHHCCCCCCH		28.3718963569
657DimethylationKACQIFVRNLPFDFT
HHHHHHHHCCCCCCH		28.37-
664PhosphorylationRNLPFDFTWKMLKDK
HCCCCCCHHHHHHHH		26.4827600695
671AcetylationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.8023806337
680PhosphorylationNECGHVLYADIKMEN
HHCCCEEEEEEEEEC		10.9229514104
691MalonylationKMENGKSKGCGVVKF
EEECCCCCCCEEEEE		62.8026320211
691AcetylationKMENGKSKGCGVVKF
EEECCCCCCCEEEEE		62.8022826441
697MalonylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.7926320211
697AcetylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.7923806337
700PhosphorylationCGVVKFESPEVAERA
CEEEEECCHHHHHHH		29.5026824392
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRPM_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HNRPM_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPM_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND MASSSPECTROMETRY.

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