MCES_HUMAN - dbPTM
MCES_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCES_HUMAN
UniProt AC O43148
Protein Name mRNA cap guanine-N7 methyltransferase
Gene Name RNMT
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Nucleus .
Protein Description Catalytic subunit of the mRNA-capping methyltransferase RNMT:RAM/FAM103A1 complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. [PubMed: 9790902]
Protein Sequence MANSAKAEEYEKMSLEQAKASVNSETESSFNINENTTASGTGLSEKTSVCRQVDIARKRKEFEDDLVKESSSCGKDTPSKKRKLDPEIVPEEKDCGDAEGNSKKRKRETEDVPKDKSSTGDGTQNKRKIALEDVPEKQKNLEEGHSSTVAAHYNELQEVGLEKRSQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMQALEPYPANESSKLVSEKVDDYEHAAKYMKNSQVRLPLGTLSKSEWEATSIYLVFAFEKQQ
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
6Acetylation--MANSAKAEEYEKM
--CCCCHHHHHHHHC
57.0323749302
10PhosphorylationNSAKAEEYEKMSLEQ
CCHHHHHHHHCCHHH
16.62-
14PhosphorylationAEEYEKMSLEQAKAS
HHHHHHCCHHHHHHH
39.5627134283
21PhosphorylationSLEQAKASVNSETES
CHHHHHHHCCCCCCC
22.5628450419
24PhosphorylationQAKASVNSETESSFN
HHHHHCCCCCCCCEE
43.6828450419
26PhosphorylationKASVNSETESSFNIN
HHHCCCCCCCCEECC
40.7728450419
28PhosphorylationSVNSETESSFNINEN
HCCCCCCCCEECCCC
47.8827251275
29PhosphorylationVNSETESSFNINENT
CCCCCCCCEECCCCC
18.9728450419
39PhosphorylationINENTTASGTGLSEK
CCCCCCCCCCCCCCC
34.4927251275
44PhosphorylationTASGTGLSEKTSVCR
CCCCCCCCCCCCHHH
38.09-
70PhosphorylationEDDLVKESSSCGKDT
HHHHHHHHHCCCCCC
23.1026552605
71PhosphorylationDDLVKESSSCGKDTP
HHHHHHHHCCCCCCC
30.6426552605
72PhosphorylationDLVKESSSCGKDTPS
HHHHHHHCCCCCCCC
35.8525849741
75AcetylationKESSSCGKDTPSKKR
HHHHCCCCCCCCCCC
63.8626051181
77PhosphorylationSSSCGKDTPSKKRKL
HHCCCCCCCCCCCCC
32.7123401153
79PhosphorylationSCGKDTPSKKRKLDP
CCCCCCCCCCCCCCC
53.5628985074
93AcetylationPEIVPEEKDCGDAEG
CCCCCCCCCCCCCCC
57.5725953088
118PhosphorylationDVPKDKSSTGDGTQN
CCCCCCCCCCCCCCC
41.99-
126AcetylationTGDGTQNKRKIALED
CCCCCCCCEEEEHHH
45.2920167786
128AcetylationDGTQNKRKIALEDVP
CCCCCCEEEEHHHCC
33.6620167786
128UbiquitinationDGTQNKRKIALEDVP
CCCCCCEEEEHHHCC
33.66-
137AcetylationALEDVPEKQKNLEEG
EHHHCCHHHHCHHCC
61.5820167786
137MalonylationALEDVPEKQKNLEEG
EHHHCCHHHHCHHCC
61.5826320211
137UbiquitinationALEDVPEKQKNLEEG
EHHHCCHHHHCHHCC
61.58-
139UbiquitinationEDVPEKQKNLEEGHS
HHCCHHHHCHHCCCH
74.66-
148PhosphorylationLEEGHSSTVAAHYNE
HHCCCHHHHHHHHHH
19.7228555341
153PhosphorylationSSTVAAHYNELQEVG
HHHHHHHHHHHHHHC
12.9528796482
163 (in isoform 1)Ubiquitination-63.4921906983
163 (in isoform 2)Ubiquitination-63.4921906983
163UbiquitinationLQEVGLEKRSQSRIF
HHHHCCCCCCCCCEE
63.4921906983
165PhosphorylationEVGLEKRSQSRIFYL
HHCCCCCCCCCEEEE
43.5023898821
167PhosphorylationGLEKRSQSRIFYLRN
CCCCCCCCCEEEEEC
28.7023898821
171PhosphorylationRSQSRIFYLRNFNNW
CCCCCEEEEECCCHH
11.4623898821
180MethylationRNFNNWMKSVLIGEF
ECCCHHHHHHHHHHH
29.09115976819
181PhosphorylationNFNNWMKSVLIGEFL
CCCHHHHHHHHHHHH
13.1720068231
190UbiquitinationLIGEFLEKVRQKKKR
HHHHHHHHHHHHHCC
44.88-
190 (in isoform 2)Ubiquitination-44.88-
208UbiquitinationVLDLGCGKGGDLLKW
EEECCCCCCHHHHHC
64.89-
208AcetylationVLDLGCGKGGDLLKW
EEECCCCCCHHHHHC
64.8926051181
208 (in isoform 2)Ubiquitination-64.89-
214UbiquitinationGKGGDLLKWKKGRIN
CCCHHHHHCCCCCCC
65.35-
222 (in isoform 2)Ubiquitination-39.67-
222UbiquitinationWKKGRINKLVCTDIA
CCCCCCCEEEECHHH
39.67-
222AcetylationWKKGRINKLVCTDIA
CCCCCCCEEEECHHH
39.6725953088
226PhosphorylationRINKLVCTDIADVSV
CCCEEEECHHHHCCH
23.9820068231
232PhosphorylationCTDIADVSVKQCQQR
ECHHHHCCHHHHHHH
24.9320068231
234 (in isoform 2)Ubiquitination-37.54-
234UbiquitinationDIADVSVKQCQQRYE
HHHHCCHHHHHHHHH
37.54-
309PhosphorylationRNACERLSPGGYFIG
HHHHHHCCCCCEEEE
27.9325262027
313PhosphorylationERLSPGGYFIGTTPN
HHCCCCCEEEECCCC
9.6525262027
317PhosphorylationPGGYFIGTTPNSFEL
CCCEEEECCCCHHHH
33.9725262027
318PhosphorylationGGYFIGTTPNSFELI
CCEEEECCCCHHHHH
18.4325262027
321PhosphorylationFIGTTPNSFELIRRL
EEECCCCHHHHHHHH
22.6925262027
331PhosphorylationLIRRLEASETESFGN
HHHHHHHHHCCCCCC
35.36-
333PhosphorylationRRLEASETESFGNEI
HHHHHHHCCCCCCEE
34.14-
341PhosphorylationESFGNEIYTVKFQKK
CCCCCEEEEEEEEEC
10.17-
385PhosphorylationLNEMAKKYNMKLVYK
HHHHHHHHCCEEEEH
21.56-
393UbiquitinationNMKLVYKKTFLEFYE
CCEEEEHHHHHHHHH
27.16-
421PhosphorylationRMQALEPYPANESSK
HHHHCCCCCCCCCCC
12.9525332170
426PhosphorylationEPYPANESSKLVSEK
CCCCCCCCCCCHHHH
32.3625332170
427PhosphorylationPYPANESSKLVSEKV
CCCCCCCCCCHHHHC
24.6725332170
428 (in isoform 2)Ubiquitination-63.2921906983
428 (in isoform 1)Ubiquitination-63.2921906983
428UbiquitinationYPANESSKLVSEKVD
CCCCCCCCCHHHHCC
63.292190698
433AcetylationSSKLVSEKVDDYEHA
CCCCHHHHCCCHHHH
43.3823749302
433UbiquitinationSSKLVSEKVDDYEHA
CCCCHHHHCCCHHHH
43.38-
433 (in isoform 2)Ubiquitination-43.38-
442AcetylationDDYEHAAKYMKNSQV
CCHHHHHHHHHHCCE
46.8125953088
442UbiquitinationDDYEHAAKYMKNSQV
CCHHHHHHHHHHCCE
46.81-
445 (in isoform 2)Ubiquitination-50.81-
445UbiquitinationEHAAKYMKNSQVRLP
HHHHHHHHHCCEEEC
50.81-
447PhosphorylationAAKYMKNSQVRLPLG
HHHHHHHCCEEECCC
25.2421406692
455 (in isoform 2)Phosphorylation-35.2329888752
455PhosphorylationQVRLPLGTLSKSEWE
CEEECCCCCCHHHHH
35.2321406692
457PhosphorylationRLPLGTLSKSEWEAT
EECCCCCCHHHHHEE
33.6921406692
457 (in isoform 2)Phosphorylation-33.6929888752
459 (in isoform 2)Phosphorylation-44.5629888752
464 (in isoform 2)Phosphorylation-12.2529888752
467 (in isoform 2)Phosphorylation-9.1529978859
469 (in isoform 2)Phosphorylation-1.5029978859
477 (in isoform 2)Phosphorylation-20068231
478 (in isoform 2)Phosphorylation-29978859
489 (in isoform 2)Phosphorylation-20068231
490 (in isoform 2)Phosphorylation-20068231

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
77TPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCES_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 MCES_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF23_HUMANKIF23physical
26344197
NF2IP_HUMANNFATC2IPphysical
26344197
RAM_HUMANFAM103A1physical
28514442
IMA7_HUMANKPNA6physical
28514442
IMA5_HUMANKPNA1physical
28514442
IMA6_HUMANKPNA5physical
28514442

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 MCES_HUMAN

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Related Literatures of Post-Translational Modification

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