CMTR2_HUMAN - dbPTM
CMTR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CMTR2_HUMAN
UniProt AC Q8IYT2
Protein Name Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2
Gene Name CMTR2
Organism Homo sapiens (Human).
Sequence Length 770
Subcellular Localization Nucleus . Cytoplasm .
Protein Description S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs..
Protein Sequence MSKCRKTPVQQLASPASFSPDILADIFELFAKNFSYGKPLNNEWQLPDPSEIFTCDHTELNAFLDLKNSLNEVKNLLSDKKLDEWHEHTAFTNKAGKIISHVRKSVNAELCTQAWCKFHEILCSFPLIPQEAFQNGKLNSLHLCEAPGAFIASLNHYLKSHRFPCHWSWVANTLNPYHEANDDLMMIMDDRLIANTLHWWYFGPDNTGDIMTLKFLTGLQNFISSMATVHLVTADGSFDCQGNPGEQEALVSSLHYCEVVTALTTLGNGGSFVLKMFTMFEHCSINLMYLLNCCFDQVHVFKPATSKAGNSEVYVVCLHYKGREAIHPLLSKMTLNFGTEMKRKALFPHHVIPDSFLKRHEECCVFFHKYQLETISENIRLFECMGKAEQEKLNNLRDCAIQYFMQKFQLKHLSRNNWLVKKSSIGCSTNTKWFGQRNKYFKTYNERKMLEALSWKDKVAKGYFNSWAEEHGVYHPGQSSILEGTASNLECHLWHILEGKKLPKVKCSPFCNGEILKTLNEAIEKSLGGAFNLDSKFRPKQQYSCSCHVFSEELIFSELCSLTECLQDEQVVVPSNQIKCLLVGFSTLRNIKMHIPLEVRLLESAELTTFSCSLLHDGDPTYQRLFLDCLLHSLRELHTGDVMILPVLSCFTRFMAGLIFVLHSCFRFITFVCPTSSDPLRTCAVLLCVGYQDLPNPVFRYLQSVNELLSTLLNSDSPQQVLQFVPMEVLLKGALLDFLWDLNAAIAKRHLHFIIQREREEIINSLQLQN
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
14PhosphorylationTPVQQLASPASFSPD
CCHHHHCCCCCCCHH
25159151
17PhosphorylationQQLASPASFSPDILA
HHHCCCCCCCHHHHH
25627689
74AcetylationKNSLNEVKNLLSDKK
HHHHHHHHHHHCCCC
25953088
74UbiquitinationKNSLNEVKNLLSDKK
HHHHHHHHHHHCCCC
29967540
74MalonylationKNSLNEVKNLLSDKK
HHHHHHHHHHHCCCC
26320211
81UbiquitinationKNLLSDKKLDEWHEH
HHHHCCCCHHHHHHH
29967540
94UbiquitinationEHTAFTNKAGKIISH
HHHHHCCCHHHHHHH
29967540
97UbiquitinationAFTNKAGKIISHVRK
HHCCCHHHHHHHHHH
29967540
100PhosphorylationNKAGKIISHVRKSVN
CCHHHHHHHHHHHCC
-
311PhosphorylationATSKAGNSEVYVVCL
CCCCCCCCEEEEEEE
30631047
332UbiquitinationAIHPLLSKMTLNFGT
HHHHHHHHCCCCCCH
29967540
334PhosphorylationHPLLSKMTLNFGTEM
HHHHHHCCCCCCHHH
-
342UbiquitinationLNFGTEMKRKALFPH
CCCCHHHHHHHHCCC
-
342AcetylationLNFGTEMKRKALFPH
CCCCHHHHHHHHCCC
25953088
344UbiquitinationFGTEMKRKALFPHHV
CCHHHHHHHHCCCCC
29967540
355PhosphorylationPHHVIPDSFLKRHEE
CCCCCCHHHHHHHHH
24719451
358UbiquitinationVIPDSFLKRHEECCV
CCCHHHHHHHHHHHE
-
370PhosphorylationCCVFFHKYQLETISE
HHEEEEEHHHHHHHH
29083192
374PhosphorylationFHKYQLETISENIRL
EEEHHHHHHHHHHHH
29083192
376PhosphorylationKYQLETISENIRLFE
EHHHHHHHHHHHHHH
29083192
387UbiquitinationRLFECMGKAEQEKLN
HHHHHCCHHHHHHHH
22817900
392UbiquitinationMGKAEQEKLNNLRDC
CCHHHHHHHHHHHHH
21906983
422UbiquitinationRNNWLVKKSSIGCST
CCCEEEEHHHCCCCC
29967540
423PhosphorylationNNWLVKKSSIGCSTN
CCEEEEHHHCCCCCC
26657352
424PhosphorylationNWLVKKSSIGCSTNT
CEEEEHHHCCCCCCC
24719451
432UbiquitinationIGCSTNTKWFGQRNK
CCCCCCCCCCCCCCC
-
439UbiquitinationKWFGQRNKYFKTYNE
CCCCCCCCCCCHHCH
23000965
442UbiquitinationGQRNKYFKTYNERKM
CCCCCCCCHHCHHHH
23000965
442MethylationGQRNKYFKTYNERKM
CCCCCCCCHHCHHHH
-
448UbiquitinationFKTYNERKMLEALSW
CCHHCHHHHHHHHCH
23000965
456AcetylationMLEALSWKDKVAKGY
HHHHHCHHHHHHHHH
19826891
456UbiquitinationMLEALSWKDKVAKGY
HHHHHCHHHHHHHHH
29967540
506UbiquitinationGKKLPKVKCSPFCNG
CCCCCCCCCCCCCCH
-
525UbiquitinationTLNEAIEKSLGGAFN
HHHHHHHHHHCCCCC
21906983
536UbiquitinationGAFNLDSKFRPKQQY
CCCCCCCCCCCCCCE
29967540
608PhosphorylationLLESAELTTFSCSLL
ECCCCCCEEEEEHHC
24719451
609PhosphorylationLESAELTTFSCSLLH
CCCCCCEEEEEHHCC
24719451
675PhosphorylationFITFVCPTSSDPLRT
HHHHCCCCCCCHHHH
-

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 CMTR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CMTR2_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 CMTR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PARVA_HUMANPARVAphysical
26344197

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 CMTR2_HUMAN

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Related Literatures of Post-Translational Modification

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