HNRPM_HUMAN - dbPTM
HNRPM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPM_HUMAN
UniProt AC P52272
Protein Name Heterogeneous nuclear ribonucleoprotein M
Gene Name HNRNPM
Organism Homo sapiens (Human).
Sequence Length 730
Subcellular Localization Nucleus, nucleolus .
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..
Protein Sequence MAAGVEAAAEVAATEIKMEEESGAPGVPSGNGAPGPKGEGERPAQNEKRKEKNIKRGGNRFEPYANPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKVMATTGGMGMGPGGPGMITIPPSILNNPNIPNEIIHALQAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQSIEAVQAISMFNGQLLFDRPMHVKMDERALPKGDFFPPERPQQLPHGLGGIGMGLGPGGQPIDANHLNKGIGMGNIGPAGMGMEGIGFGINKMGGMEGPFGGGMENMGRFGSGMNMGRINEILSNALKRGEIIAKQGGGGGGGSVPGIERMGPGIDRLGGAGMERMGAGLGHGMDRVGSEIERMGLVMDRMGSVERMGSGIERMGPLGLDHMASSIERMGQTMERIGSGVERMGAGMGFGLERMAAPIDRVGQTIERMGSGVERMGPAIERMGLSMERMVPAGMGAGLERMGPVMDRMATGLERMGANNLERMGLERMGANSLERMGLERMGANSLERMGPAMGPALGAGIERMGLAMGGGGGASFDRAIEMERGNFGGSFAGSFGGAGGHAPGVARKACQIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVKFESPEVAERACRMMNGMKLSGREIDVRIDRNA
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		16.9622223895
14PhosphorylationAAAEVAATEIKMEEE
HHHHHHHHCCCHHHH		28.6221406692
17SumoylationEVAATEIKMEEESGA
HHHHHCCCHHHHHCC		33.74-
17SumoylationEVAATEIKMEEESGA
HHHHHCCCHHHHHCC		33.7428112733
22PhosphorylationEIKMEEESGAPGVPS
CCCHHHHHCCCCCCC		43.4619664995
29PhosphorylationSGAPGVPSGNGAPGP
HCCCCCCCCCCCCCC		42.3525159151
37AcetylationGNGAPGPKGEGERPA
CCCCCCCCCCCCCCC		75.4226051181
37SumoylationGNGAPGPKGEGERPA
CCCCCCCCCCCCCCC		75.4228112733
37UbiquitinationGNGAPGPKGEGERPA
CCCCCCCCCCCCCCC		75.4221906983
37 (in isoform 1)Ubiquitination-75.4221890473
37 (in isoform 2)Ubiquitination-75.4221890473
48AcetylationERPAQNEKRKEKNIK
CCCCCHHHHHHHCCC		76.0723749302
48UbiquitinationERPAQNEKRKEKNIK
CCCCCHHHHHHHCCC		76.0721906983
48 (in isoform 1)Ubiquitination-76.0721890473
48 (in isoform 2)Ubiquitination-76.0721890473
52MethylationQNEKRKEKNIKRGGN
CHHHHHHHCCCCCCC		67.99116252415
55SumoylationKRKEKNIKRGGNRFE
HHHHHCCCCCCCCCC		55.15-
56MethylationRKEKNIKRGGNRFEP
HHHHCCCCCCCCCCC		55.22115479331
64NitrationGGNRFEPYANPTKRY
CCCCCCCCCCCCCCC		16.29-
64PhosphorylationGGNRFEPYANPTKRY
CCCCCCCCCCCCCCC		16.2921945579
68PhosphorylationFEPYANPTKRYRAFI
CCCCCCCCCCCEEEC		28.1421945579
692-HydroxyisobutyrylationEPYANPTKRYRAFIT
CCCCCCCCCCEEECC		49.00-
69AcetylationEPYANPTKRYRAFIT
CCCCCCCCCCEEECC		49.0025953088
69SumoylationEPYANPTKRYRAFIT
CCCCCCCCCCEEECC		49.0028112733
69UbiquitinationEPYANPTKRYRAFIT
CCCCCCCCCCEEECC		49.0021890473
69 (in isoform 1)Ubiquitination-49.0021890473
69 (in isoform 2)Ubiquitination-49.0021890473
71PhosphorylationYANPTKRYRAFITNI
CCCCCCCCEEECCCC		14.0928152594
76PhosphorylationKRYRAFITNIPFDVK
CCCEEECCCCCCCCC		22.2028152594
83SumoylationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.16-
832-HydroxyisobutyrylationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.16-
83AcetylationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.1625825284
83SumoylationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.1628112733
83UbiquitinationTNIPFDVKWQSLKDL
CCCCCCCCHHHHHHH		41.1621890473
83 (in isoform 1)Ubiquitination-41.1621890473
83 (in isoform 2)Ubiquitination-41.1621890473
86PhosphorylationPFDVKWQSLKDLVKE
CCCCCHHHHHHHHHH		35.9527696853
88SumoylationDVKWQSLKDLVKEKV
CCCHHHHHHHHHHHC		55.02-
882-HydroxyisobutyrylationDVKWQSLKDLVKEKV
CCCHHHHHHHHHHHC		55.02-
88AcetylationDVKWQSLKDLVKEKV
CCCHHHHHHHHHHHC		55.0226051181
88SumoylationDVKWQSLKDLVKEKV
CCCHHHHHHHHHHHC		55.0228112733
88UbiquitinationDVKWQSLKDLVKEKV
CCCHHHHHHHHHHHC		55.0221890473
88 (in isoform 1)Ubiquitination-55.0221890473
88 (in isoform 2)Ubiquitination-55.0221890473
92UbiquitinationQSLKDLVKEKVGEVT
HHHHHHHHHHCCEEE		60.14-
94UbiquitinationLKDLVKEKVGEVTYV
HHHHHHHHCCEEEEE		50.23-
99PhosphorylationKEKVGEVTYVELLMD
HHHCCEEEEEEEEEC		19.97-
100PhosphorylationEKVGEVTYVELLMDA
HHCCEEEEEEEEECC		9.3329759185
105SulfoxidationVTYVELLMDAEGKSR
EEEEEEEECCCCCCC		7.7821406390
110SumoylationLLMDAEGKSRGCAVV
EEECCCCCCCCEEEE		28.60-
110AcetylationLLMDAEGKSRGCAVV
EEECCCCCCCCEEEE		28.6026051181
110SumoylationLLMDAEGKSRGCAVV
EEECCCCCCCCEEEE		28.60-
110UbiquitinationLLMDAEGKSRGCAVV
EEECCCCCCCCEEEE		28.6021906983
110 (in isoform 1)Ubiquitination-28.6021890473
110 (in isoform 2)Ubiquitination-28.6021890473
114S-nitrosocysteineAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.23-
114GlutathionylationAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.2322555962
114S-nitrosylationAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.2319483679
114S-palmitoylationAEGKSRGCAVVEFKM
CCCCCCCEEEEEEEC		2.2326865113
120SumoylationGCAVVEFKMEESMKK
CEEEEEEECHHHHHH		31.71-
120AcetylationGCAVVEFKMEESMKK
CEEEEEEECHHHHHH		31.7126051181
120SumoylationGCAVVEFKMEESMKK
CEEEEEEECHHHHHH		31.71-
120UbiquitinationGCAVVEFKMEESMKK
CEEEEEEECHHHHHH		31.71-
124PhosphorylationVEFKMEESMKKAAEV
EEEECHHHHHHHHHH		23.6927067055
126SumoylationFKMEESMKKAAEVLN
EECHHHHHHHHHHHH		48.84-
1262-HydroxyisobutyrylationFKMEESMKKAAEVLN
EECHHHHHHHHHHHH		48.84-
126AcetylationFKMEESMKKAAEVLN
EECHHHHHHHHHHHH		48.8425953088
126SumoylationFKMEESMKKAAEVLN
EECHHHHHHHHHHHH		48.84-
126UbiquitinationFKMEESMKKAAEVLN
EECHHHHHHHHHHHH		48.8421906983
126 (in isoform 1)Ubiquitination-48.8421890473
126 (in isoform 2)Ubiquitination-48.8421890473
127SumoylationKMEESMKKAAEVLNK
ECHHHHHHHHHHHHH		44.16-
127SumoylationKMEESMKKAAEVLNK
ECHHHHHHHHHHHHH		44.1628112733
127UbiquitinationKMEESMKKAAEVLNK
ECHHHHHHHHHHHHH		44.16-
134SumoylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.34-
134AcetylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.3425825284
134MalonylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.3426320211
134SumoylationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.3428112733
134UbiquitinationKAAEVLNKHSLSGRP
HHHHHHHHCCCCCCC		30.34-
134 (in isoform 1)Ubiquitination-30.3421890473
134 (in isoform 2)Ubiquitination-30.3421890473
136PhosphorylationAEVLNKHSLSGRPLK
HHHHHHCCCCCCCCC		26.3230108239
138PhosphorylationVLNKHSLSGRPLKVK
HHHHCCCCCCCCCCC		35.4530108239
143AcetylationSLSGRPLKVKEDPDG
CCCCCCCCCCCCCCC		54.6825953088
143SumoylationSLSGRPLKVKEDPDG
CCCCCCCCCCCCCCC		54.6828112733
143UbiquitinationSLSGRPLKVKEDPDG
CCCCCCCCCCCCCCC		54.68-
145SumoylationSGRPLKVKEDPDGEH
CCCCCCCCCCCCCHH		55.61-
145AcetylationSGRPLKVKEDPDGEH
CCCCCCCCCCCCCHH		55.6126051181
145SumoylationSGRPLKVKEDPDGEH
CCCCCCCCCCCCCHH		55.6128112733
145UbiquitinationSGRPLKVKEDPDGEH
CCCCCCCCCCCCCHH		55.6121906983
145 (in isoform 1)Ubiquitination-55.6121890473
145 (in isoform 2)Ubiquitination-55.6121890473
159UbiquitinationHARRAMQKVMATTGG
HHHHHHHHHHHHHCC		22.38-
159 (in isoform 2)Ubiquitination-22.3821890473
175 (in isoform 2)Ubiquitination-24.3321890473
182 (in isoform 2)Ubiquitination-34.0621890473
200 (in isoform 2)Ubiquitination-16.6321890473
203 (in isoform 2)Ubiquitination-21.6521890473
204PhosphorylationLQAGRLGSTVFVANL
HHCCCCCCEEEEEEC		26.4530108239
205PhosphorylationQAGRLGSTVFVANLD
HCCCCCCEEEEEECC		19.0330108239
213PhosphorylationVFVANLDYKVGWKKL
EEEEECCCCCCHHHH		15.6722817900
214AcetylationFVANLDYKVGWKKLK
EEEECCCCCCHHHHH		33.6624431195
214UbiquitinationFVANLDYKVGWKKLK
EEEECCCCCCHHHHH		33.6621906983
214 (in isoform 1)Ubiquitination-33.6621890473
218UbiquitinationLDYKVGWKKLKEVFS
CCCCCCHHHHHHHHH		42.15-
221SumoylationKVGWKKLKEVFSMAG
CCCHHHHHHHHHHCC		61.79-
221AcetylationKVGWKKLKEVFSMAG
CCCHHHHHHHHHHCC		61.7926051181
221SumoylationKVGWKKLKEVFSMAG
CCCHHHHHHHHHHCC		61.7928112733
221UbiquitinationKVGWKKLKEVFSMAG
CCCHHHHHHHHHHCC		61.7921906983
221 (in isoform 1)Ubiquitination-61.7921890473
225PhosphorylationKKLKEVFSMAGVVVR
HHHHHHHHHCCEEEE		16.9523403867
226SulfoxidationKLKEVFSMAGVVVRA
HHHHHHHHCCEEEEE		2.2728183972
238AcetylationVRADILEDKDGKSRG
EEEEEEECCCCCCCC		51.4019608861
239SumoylationRADILEDKDGKSRGI
EEEEEECCCCCCCCC		60.03-
239AcetylationRADILEDKDGKSRGI
EEEEEECCCCCCCCC		60.0323954790
239MalonylationRADILEDKDGKSRGI
EEEEEECCCCCCCCC		60.0326320211
239SumoylationRADILEDKDGKSRGI
EEEEEECCCCCCCCC		60.03-
239UbiquitinationRADILEDKDGKSRGI
EEEEEECCCCCCCCC		60.03-
239 (in isoform 1)Ubiquitination-60.0321890473
242AcetylationILEDKDGKSRGIGTV
EEECCCCCCCCCCEE		47.3025953088
242SumoylationILEDKDGKSRGIGTV
EEECCCCCCCCCCEE		47.30-
242UbiquitinationILEDKDGKSRGIGTV
EEECCCCCCCCCCEE		47.3021906983
242 (in isoform 1)Ubiquitination-47.3021890473
248PhosphorylationGKSRGIGTVTFEQSI
CCCCCCCEEEHHHHH		17.9121406692
250PhosphorylationSRGIGTVTFEQSIEA
CCCCCEEEHHHHHHH		22.6921406692
254PhosphorylationGTVTFEQSIEAVQAI
CEEEHHHHHHHHHHH		18.3920068231
262PhosphorylationIEAVQAISMFNGQLL
HHHHHHHHHHCCEEE		21.9721406692
277SumoylationFDRPMHVKMDERALP
ECCCEECCCCCCCCC		26.42-
277AcetylationFDRPMHVKMDERALP
ECCCEECCCCCCCCC		26.4219608861
277SumoylationFDRPMHVKMDERALP
ECCCEECCCCCCCCC		26.4228112733
277UbiquitinationFDRPMHVKMDERALP
ECCCEECCCCCCCCC		26.4219608861
285SumoylationMDERALPKGDFFPPE
CCCCCCCCCCCCCCC		72.4728112733
285UbiquitinationMDERALPKGDFFPPE
CCCCCCCCCCCCCCC		72.47-
306 (in isoform 2)Ubiquitination-3.6521890473
322SumoylationIDANHLNKGIGMGNI
CCHHHCCCCCCCCCC		59.26-
322UbiquitinationIDANHLNKGIGMGNI
CCHHHCCCCCCCCCC		59.26-
326SulfoxidationHLNKGIGMGNIGPAG
HCCCCCCCCCCCCCC		3.3428183972
342 (in isoform 2)Ubiquitination-19.8321890473
345SumoylationGIGFGINKMGGMEGP
CCCCCCCCCCCCCCC		36.6828112733
345UbiquitinationGIGFGINKMGGMEGP
CCCCCCCCCCCCCCC		36.6821906983
345 (in isoform 1)Ubiquitination-36.6821890473
349SulfoxidationGINKMGGMEGPFGGG
CCCCCCCCCCCCCCC		4.4528183972
349 (in isoform 2)Ubiquitination-4.4521890473
357SulfoxidationEGPFGGGMENMGRFG
CCCCCCCCCCCCCCC		3.6828465586
360SulfoxidationFGGGMENMGRFGSGM
CCCCCCCCCCCCCCC		2.3128465586
365PhosphorylationENMGRFGSGMNMGRI
CCCCCCCCCCCHHHH		31.9623401153
371MethylationGSGMNMGRINEILSN
CCCCCHHHHHHHHHH		20.14115385849
377PhosphorylationGRINEILSNALKRGE
HHHHHHHHHHHHHCC		26.2221406692
381SumoylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.82-
3812-HydroxyisobutyrylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.82-
381AcetylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.8225953088
381SuccinylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.8223954790
381SumoylationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.8228112733
381UbiquitinationEILSNALKRGEIIAK
HHHHHHHHHCCEEEE		56.8221890473
381 (in isoform 1)Ubiquitination-56.8221890473
388SumoylationKRGEIIAKQGGGGGG
HHCCEEEECCCCCCC		38.78-
388AcetylationKRGEIIAKQGGGGGG
HHCCEEEECCCCCCC		38.7825953088
388MalonylationKRGEIIAKQGGGGGG
HHCCEEEECCCCCCC		38.7826320211
388SumoylationKRGEIIAKQGGGGGG
HHCCEEEECCCCCCC		38.7828112733
388UbiquitinationKRGEIIAKQGGGGGG
HHCCEEEECCCCCCC		38.7821890473
388 (in isoform 1)Ubiquitination-38.7821890473
397PhosphorylationGGGGGGGSVPGIERM
CCCCCCCCCCCHHHC		28.5429255136
404SulfoxidationSVPGIERMGPGIDRL
CCCCHHHCCCCCCCC		5.0128183972
410MethylationRMGPGIDRLGGAGME
HCCCCCCCCCCCCHH		33.06115479315
419SulfoxidationGGAGMERMGAGLGHG
CCCCHHHHCCCCCCC		2.4830846556
427SulfoxidationGAGLGHGMDRVGSEI
CCCCCCCHHHCCHHH		2.1730846556
429MethylationGLGHGMDRVGSEIER
CCCCCHHHCCHHHHH		26.29115479291
432PhosphorylationHGMDRVGSEIERMGL
CCHHHCCHHHHHHCH		32.3222617229
443MethylationRMGLVMDRMGSVERM
HHCHHHHCCCCHHCC		17.17115479307
446PhosphorylationLVMDRMGSVERMGSG
HHHHCCCCHHCCCCC		16.0926846344
452PhosphorylationGSVERMGSGIERMGP
CCHHCCCCCHHHCCC		27.5323401153
457SulfoxidationMGSGIERMGPLGLDH
CCCCHHHCCCCCHHH		4.1521406390
467PhosphorylationLGLDHMASSIERMGQ
CCHHHHHHHHHHHHH		25.0323401153
468PhosphorylationGLDHMASSIERMGQT
CHHHHHHHHHHHHHH		20.9422617229
474 (in isoform 2)Phosphorylation-28.4717081983
475PhosphorylationSIERMGQTMERIGSG
HHHHHHHHHHHHHCC		18.4423090842
481PhosphorylationQTMERIGSGVERMGA
HHHHHHHCCHHHCCC		36.9823401153
485MethylationRIGSGVERMGAGMGF
HHHCCHHHCCCCCCC		26.82115479283
486SulfoxidationIGSGVERMGAGMGFG
HHCCHHHCCCCCCCC		2.4628465586
490SulfoxidationVERMGAGMGFGLERM
HHHCCCCCCCCHHHC		3.8928465586
496MethylationGMGFGLERMAAPIDR
CCCCCHHHCCCCHHH		25.6924129315
503MethylationRMAAPIDRVGQTIER
HCCCCHHHHHHHHHH		34.8782954875
507PhosphorylationPIDRVGQTIERMGSG
CHHHHHHHHHHHCCC		20.9023312004
513PhosphorylationQTIERMGSGVERMGP
HHHHHHCCCHHHHHH		30.2623401153
518SulfoxidationMGSGVERMGPAIERM
HCCCHHHHHHHHHHC		4.8228183972
528PhosphorylationAIERMGLSMERMVPA
HHHHCCCCHHHHCCC		16.9323927012
532SulfoxidationMGLSMERMVPAGMGA
CCCCHHHHCCCCCCC		2.4221406390
537SulfoxidationERMVPAGMGAGLERM
HHHCCCCCCCCHHHH		3.4528183972
543MethylationGMGAGLERMGPVMDR
CCCCCHHHHHHHHHH		40.16115385857
544SulfoxidationMGAGLERMGPVMDRM
CCCCHHHHHHHHHHH		5.3428183972
550MethylationRMGPVMDRMATGLER
HHHHHHHHHHHHHHH		9.87115479323
553PhosphorylationPVMDRMATGLERMGA
HHHHHHHHHHHHHCH		32.7224173317
558SulfoxidationMATGLERMGANNLER
HHHHHHHHCHHHHHH		4.3128183972
565MethylationMGANNLERMGLERMG
HCHHHHHHHCHHHCC		27.86115479299
571SulfoxidationERMGLERMGANSLER
HHHCHHHCCCHHHHH		4.3128183972
575PhosphorylationLERMGANSLERMGLE
HHHCCCHHHHHHCHH		30.9529255136
584SulfoxidationERMGLERMGANSLER
HHHCHHHCCCCHHHH		4.3128183972
588PhosphorylationLERMGANSLERMGPA
HHHCCCCHHHHHCCH		30.9529255136
592SulfoxidationGANSLERMGPAMGPA
CCCHHHHHCCHHHHH		5.7221406390
596SulfoxidationLERMGPAMGPALGAG
HHHHCCHHHHHHHHC		8.1128183972
607SulfoxidationLGAGIERMGLAMGGG
HHHCHHHCCCCCCCC		3.1521406390
611SulfoxidationIERMGLAMGGGGGAS
HHHCCCCCCCCCCCC		6.5328183972
612 (in isoform 2)Ubiquitination-26.4521890473
618PhosphorylationMGGGGGASFDRAIEM
CCCCCCCCHHHHHHC		30.8429255136
621DimethylationGGGASFDRAIEMERG
CCCCCHHHHHHCCCC		35.14-
621MethylationGGGASFDRAIEMERG
CCCCCHHHHHHCCCC		35.14115390435
627MethylationDRAIEMERGNFGGSF
HHHHHCCCCCCCCCC		44.00115479275
628 (in isoform 2)Ubiquitination-22.1021890473
633PhosphorylationERGNFGGSFAGSFGG
CCCCCCCCCCCCCCC		16.5923927012
637PhosphorylationFGGSFAGSFGGAGGH
CCCCCCCCCCCCCCC		19.7925159151
646 (in isoform 2)Ubiquitination-31.9221890473
651SumoylationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.72-
651MalonylationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.7226320211
651MethylationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.7223748837
651SumoylationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.7228112733
651UbiquitinationHAPGVARKACQIFVR
CCCHHHHHHHHHHHH		43.7221890473
651 (in isoform 1)Ubiquitination-43.7221890473
651 (in isoform 2)Ubiquitination-43.7221890473
653GlutathionylationPGVARKACQIFVRNL
CHHHHHHHHHHHHCC		3.4122555962
653 (in isoform 2)Ubiquitination-3.4121890473
659AcetylationACQIFVRNLPFDFTW
HHHHHHHCCCCCCHH		46.9219608861
659UbiquitinationACQIFVRNLPFDFTW
HHHHHHHCCCCCCHH		46.9219608861
659 (in isoform 2)Ubiquitination-46.9221890473
662 (in isoform 2)Phosphorylation-15.8117081983
665PhosphorylationRNLPFDFTWKMLKDK
HCCCCCCHHHHHHHH		26.4828464451
667SumoylationLPFDFTWKMLKDKFN
CCCCCHHHHHHHHHH		31.15-
667AcetylationLPFDFTWKMLKDKFN
CCCCCHHHHHHHHHH		31.1526051181
667SumoylationLPFDFTWKMLKDKFN
CCCCCHHHHHHHHHH		31.1528112733
667UbiquitinationLPFDFTWKMLKDKFN
CCCCCHHHHHHHHHH		31.1521890473
667 (in isoform 1)Ubiquitination-31.1521890473
670AcetylationDFTWKMLKDKFNECG
CCHHHHHHHHHHHCC		56.2125953088
670UbiquitinationDFTWKMLKDKFNECG
CCHHHHHHHHHHHCC		56.21-
672SumoylationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.80-
6722-HydroxyisobutyrylationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.80-
672AcetylationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.8025825284
672MalonylationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.8026320211
672SumoylationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.80-
672UbiquitinationTWKMLKDKFNECGHV
HHHHHHHHHHHCCCE		48.80-
676S-nitrosocysteineLKDKFNECGHVLYAD
HHHHHHHCCCEEEEE		4.85-
676GlutathionylationLKDKFNECGHVLYAD
HHHHHHHCCCEEEEE		4.8522555962
676S-nitrosylationLKDKFNECGHVLYAD
HHHHHHHCCCEEEEE		4.8522178444
677 (in isoform 2)Ubiquitination-14.0421890473
681PhosphorylationNECGHVLYADIKMEN
HHCCCEEEEEEEEEC		10.9225159151
685SumoylationHVLYADIKMENGKSK
CEEEEEEEEECCCCC		40.48-
685AcetylationHVLYADIKMENGKSK
CEEEEEEEEECCCCC		40.4823749302
685SumoylationHVLYADIKMENGKSK
CEEEEEEEEECCCCC		40.4828112733
685UbiquitinationHVLYADIKMENGKSK
CEEEEEEEEECCCCC		40.4821906983
685 (in isoform 1)Ubiquitination-40.4821890473
690UbiquitinationDIKMENGKSKGCGVV
EEEEECCCCCCCEEE		61.6521906983
690 (in isoform 1)Ubiquitination-61.6521890473
692SumoylationKMENGKSKGCGVVKF
EEECCCCCCCEEEEE		62.8028112733
692UbiquitinationKMENGKSKGCGVVKF
EEECCCCCCCEEEEE		62.8021906983
692 (in isoform 1)Ubiquitination-62.8021890473
694S-nitrosocysteineENGKSKGCGVVKFES
ECCCCCCCEEEEECC		4.26-
694GlutathionylationENGKSKGCGVVKFES
ECCCCCCCEEEEECC		4.2622555962
694S-nitrosylationENGKSKGCGVVKFES
ECCCCCCCEEEEECC		4.2619483679
698SumoylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.79-
698AcetylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.7919608861
698MalonylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.7926320211
698SumoylationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.7919608861
698UbiquitinationSKGCGVVKFESPEVA
CCCCEEEEECCHHHH		40.7921890473
698 (in isoform 1)Ubiquitination-40.7921890473
701PhosphorylationCGVVKFESPEVAERA
CEEEEECCHHHHHHH		29.5029255136
716SumoylationCRMMNGMKLSGREID
HHHHCCCCCCCCEEE		40.68-
716AcetylationCRMMNGMKLSGREID
HHHHCCCCCCCCEEE		40.6825953088
716SumoylationCRMMNGMKLSGREID
HHHHCCCCCCCCEEE		40.6828112733
716UbiquitinationCRMMNGMKLSGREID
HHHHCCCCCCCCEEE		40.6821890473
716 (in isoform 1)Ubiquitination-40.6821890473
718PhosphorylationMMNGMKLSGREIDVR
HHCCCCCCCCEEEEE		30.2228450419
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
432SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRPM_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 HNRPM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRC2A_HUMANPRRC2Aphysical
14667819
RBM4B_HUMANRBM4Bphysical
16189514
LMO3_HUMANLMO3physical
16189514
ECM29_HUMANKIAA0368physical
20682791
ROA1_HUMANHNRNPA1physical
22939629
TCRG1_HUMANTCERG1physical
22939629
RBM8A_HUMANRBM8Aphysical
22939629
U2AF2_HUMANU2AF2physical
22939629
PRP6_HUMANPRPF6physical
22939629
U5S1_HUMANEFTUD2physical
22939629
NH2L1_HUMANNHP2L1physical
22939629
SMD1_HUMANSNRPD1physical
22939629
SF3B3_HUMANSF3B3physical
22939629
SF3A1_HUMANSF3A1physical
22939629
RU2A_HUMANSNRPA1physical
22939629
SF3B1_HUMANSF3B1physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SMD3_HUMANSNRPD3physical
22939629
SRSF1_HUMANSRSF1physical
22939629
THOC4_HUMANALYREFphysical
22939629
HNRPR_HUMANHNRNPRphysical
22939629
PRP8_HUMANPRPF8physical
22939629
RNPS1_HUMANRNPS1physical
22939629
SRSF5_HUMANSRSF5physical
22939629
SRSF3_HUMANSRSF3physical
22939629
SRRM2_HUMANSRRM2physical
22939629
HNRPQ_HUMANSYNCRIPphysical
22939629
SFPQ_HUMANSFPQphysical
22939629
NONO_HUMANNONOphysical
22939629
RBM25_HUMANRBM25physical
22939629
ROA0_HUMANHNRNPA0physical
22939629
RL10A_HUMANRPL10Aphysical
22939629
RS6_HUMANRPS6physical
22939629
RL7_HUMANRPL7physical
22939629
RALY_HUMANRALYphysical
22939629
RS24_HUMANRPS24physical
22939629
RS8_HUMANRPS8physical
22939629
RL11_HUMANRPL11physical
22939629
RL23A_HUMANRPL23Aphysical
22939629
RS23_HUMANRPS23physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RL12_HUMANRPL12physical
22939629
RL31_HUMANRPL31physical
22939629
RS13_HUMANRPS13physical
22939629
RL6_HUMANRPL6physical
22939629
RL14_HUMANRPL14physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS16_HUMANRPS16physical
22939629
RLA0_HUMANRPLP0physical
22939629
RL18_HUMANRPL18physical
22939629
RL5_HUMANRPL5physical
22939629
RS11_HUMANRPS11physical
22939629
TOP1_HUMANTOP1physical
22939629
RS7_HUMANRPS7physical
22939629
RS2_HUMANRPS2physical
22939629
RS14_HUMANRPS14physical
22939629
PRP19_HUMANPRPF19physical
22939629
RL10_HUMANRPL10physical
22939629
RL19_HUMANRPL19physical
22939629
RL23_HUMANRPL23physical
22939629
RL18A_HUMANRPL18Aphysical
22939629
RL30_HUMANRPL30physical
22939629
RL22_HUMANRPL22physical
22939629
PUF60_HUMANPUF60physical
22939629
RS26_HUMANRPS26physical
22939629
SRRT_HUMANSRRTphysical
22939629
RS4X_HUMANRPS4Xphysical
22939629
PR40A_HUMANPRPF40Aphysical
22939629
RSSA_HUMANRPSAphysical
22939629
RS21_HUMANRPS21physical
22939629
PRPF3_HUMANPRPF3physical
22939629
RS5_HUMANRPS5physical
22939629
RS28_HUMANRPS28physical
22939629
RS25_HUMANRPS25physical
22939629
RBM14_HUMANRBM14physical
22939629
SND1_HUMANSND1physical
22939629
RBP2_HUMANRANBP2physical
22939629
RM37_HUMANMRPL37physical
22939629
K1C16_HUMANKRT16physical
22939629
STOM_HUMANSTOMphysical
22939629
MBD3_HUMANMBD3physical
22939629
QCR9_HUMANUQCR10physical
22939629
SCMC1_HUMANSLC25A24physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
RRBP1_HUMANRRBP1physical
22939629
VTNC_HUMANVTNphysical
22939629
RCC1_HUMANRCC1physical
22939629
RRS1_HUMANRRS1physical
22939629
ZN326_HUMANZNF326physical
22939629
PCDA2_HUMANPCDHA2physical
22939629
LMNA_HUMANLMNAphysical
22939629
SMC3_HUMANSMC3physical
22939629
SON_HUMANSONphysical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
RAB31_HUMANRAB31physical
22939629
RTN4_HUMANRTN4physical
22939629
SMCA5_HUMANSMARCA5physical
22939629
LMNB1_HUMANLMNB1physical
22939629
RM55_HUMANMRPL55physical
22939629
MYH10_HUMANMYH10physical
22939629
RAP1A_HUMANRAP1Aphysical
22939629
SSRA_HUMANSSR1physical
22939629
TR150_HUMANTHRAP3physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
SEPT2_HUMANSEPT2physical
22939629
RT28_HUMANMRPS28physical
22939629
TOIP1_HUMANTOR1AIP1physical
22939629
SAM50_HUMANSAMM50physical
22939629
TOM70_HUMANTOMM70Aphysical
22939629
RCC2_HUMANRCC2physical
22939629
PYRD_HUMANDHODHphysical
22939629
RM23_HUMANMRPL23physical
22939629
RT09_HUMANMRPS9physical
22939629
TIM9_HUMANTIMM9physical
22939629
MTA2_HUMANMTA2physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
ZN207_HUMANZNF207physical
22365833
RBM4_HUMANRBM4physical
22365833
MEP50_HUMANWDR77physical
22365833
RBTN2_HUMANLMO2physical
21988832
STAT3_HUMANSTAT3physical
21988832
MRE11_HUMANMRE11Aphysical
22863883
AKAP9_HUMANAKAP9physical
25416956
TEKT4_HUMANTEKT4physical
25416956
PLRG1_HUMANPLRG1physical
20467437
CDC5L_HUMANCDC5Lphysical
20467437
LRC59_HUMANLRRC59physical
26344197
QCR2_HUMANUQCRC2physical
26344197
U2AF1_HUMANU2AF1physical
20467437
U2AF2_HUMANU2AF2physical
20467437
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPM_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-588, AND MASS SPECTROMETRY.
"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-277 AND LYS-698, AND MASSSPECTROMETRY.
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 SER-618; SER-637 ANDSER-701, AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-588, AND MASS SPECTROMETRY.
"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-432; SER-468; SER-528;SER-588; SER-618; SER-633; SER-637 AND SER-701, 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-588; SER-618 ANDSER-701, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-588 ANDSER-701, AND MASS SPECTROMETRY.
"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-701, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-618 ANDSER-701, AND MASS SPECTROMETRY.

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