MCE1_HUMAN - dbPTM
MCE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCE1_HUMAN
UniProt AC O60942
Protein Name mRNA-capping enzyme
Gene Name RNGTT
Organism Homo sapiens (Human).
Sequence Length 597
Subcellular Localization Nucleus.
Protein Description Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus..
Protein Sequence MAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPLLPDWCFEDDEDEDEDEDGKKESEPGSSASFGKRRKERLKLGAIFLEGVTVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEGNFAKEVSHEMDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT
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
28UbiquitinationAGRFLPLKTMLGPRY
CCCCCCCCHHCCCCC		29.9221890473
28SumoylationAGRFLPLKTMLGPRY
CCCCCCCCHHCCCCC		29.92-
28SumoylationAGRFLPLKTMLGPRY
CCCCCCCCHHCCCCC		29.92-
28 (in isoform 1)Ubiquitination-29.9221890473
28 (in isoform 2)Ubiquitination-29.9221890473
28 (in isoform 3)Ubiquitination-29.9221890473
28 (in isoform 4)Ubiquitination-29.9221890473
34MethylationLKTMLGPRYDSQVAE
CCHHCCCCCCHHHHH		46.20115491443
81UbiquitinationYDRNDIEKEGIKYIK
CCCCHHHHHCEEEEE		62.67-
85UbiquitinationDIEKEGIKYIKLQCK
HHHHHCEEEEEEEEC		52.35-
88UbiquitinationKEGIKYIKLQCKGHG
HHCEEEEEEEECCCC		29.43-
92UbiquitinationKYIKLQCKGHGECPT
EEEEEEECCCCCCCC		40.77-
171 (in isoform 3)Ubiquitination-46.2521890473
171UbiquitinationIYKGDYLKELFRRYG
CCCCHHHHHHHHHHC		46.2521890473
171 (in isoform 1)Ubiquitination-46.2521890473
171 (in isoform 2)Ubiquitination-46.2521890473
171 (in isoform 4)Ubiquitination-46.2521890473
210PhosphorylationDEDGKKESEPGSSAS
CCCCCCCCCCCCCCC		58.9520068231
214PhosphorylationKKESEPGSSASFGKR
CCCCCCCCCCCHHHH		33.1820068231
215PhosphorylationKESEPGSSASFGKRR
CCCCCCCCCCHHHHH		33.5720068231
217PhosphorylationSEPGSSASFGKRRKE
CCCCCCCCHHHHHHH		36.1624173317
220UbiquitinationGSSASFGKRRKERLK
CCCCCHHHHHHHHHH		47.20-
249UbiquitinationTQVTTQPKLGEVQQK
EEEECCCCHHHHHHH		60.34-
256UbiquitinationKLGEVQQKCHQFCGW
CHHHHHHHHHHHHCC		19.32-
278UbiquitinationAQPVSMDKQNIKLLD
CCCCCCCCCCEEEEE		36.28-
282UbiquitinationSMDKQNIKLLDLKPY
CCCCCCEEEEECCCE		51.01-
287SumoylationNIKLLDLKPYKVSWK
CEEEEECCCEEEEEE		46.07-
287UbiquitinationNIKLLDLKPYKVSWK
CEEEEECCCEEEEEE		46.07-
287AcetylationNIKLLDLKPYKVSWK
CEEEEECCCEEEEEE		46.0725953088
290UbiquitinationLLDLKPYKVSWKADG
EEECCCEEEEEEECC		38.02-
294UbiquitinationKPYKVSWKADGTRYM
CCEEEEEEECCCEEE		29.15-
298PhosphorylationVSWKADGTRYMMLID
EEEEECCCEEEEEEE		21.1230387612
300PhosphorylationWKADGTRYMMLIDGT
EEECCCEEEEEEECC		6.16-
307PhosphorylationYMMLIDGTNEVFMID
EEEEEECCCEEEEEC		25.1830387612
359PhosphorylationNGQAVPRYLIYDIIK
CCCCCCCEEEEEHHH		7.4422817900
362PhosphorylationAVPRYLIYDIIKFNS
CCCCEEEEEHHHCCC		9.8622817900
390PhosphorylationCIEREIISPRHEKMK
HEEEEECCCCHHHCC		22.8824719451
395AcetylationIISPRHEKMKTGLID
ECCCCHHHCCCCCCC		39.3019608861
397UbiquitinationSPRHEKMKTGLIDKT
CCCHHHCCCCCCCCC		50.9719608861
397AcetylationSPRHEKMKTGLIDKT
CCCHHHCCCCCCCCC		50.9719608861
403AcetylationMKTGLIDKTQEPFSV
CCCCCCCCCCCCCCC		45.1525953088
403 (in isoform 4)Ubiquitination-45.1521890473
403 (in isoform 3)Ubiquitination-45.1521890473
403 (in isoform 2)Ubiquitination-45.1521890473
403UbiquitinationMKTGLIDKTQEPFSV
CCCCCCCCCCCCCCC		45.152190698
403 (in isoform 1)Ubiquitination-45.1521890473
413UbiquitinationEPFSVRNKPFFDICT
CCCCCCCCCCHHHHH		32.41-
423SumoylationFDICTSRKLLEGNFA
HHHHHCHHHHCCCCH		58.13-
423UbiquitinationFDICTSRKLLEGNFA
HHHHHCHHHHCCCCH		58.13-
423SumoylationFDICTSRKLLEGNFA
HHHHHCHHHHCCCCH		58.13-
431UbiquitinationLLEGNFAKEVSHEMD
HHCCCCHHHHCCCCC		55.28-
447UbiquitinationLIFQPTGKYKPGRCD
EEECCCCCCCCCCCC		53.21-
502AcetylationERPFAQIKVTKELKQ
CCCCEEEEECHHHHH		31.607407375
508UbiquitinationIKVTKELKQYDNKII
EEECHHHHHHCCCEE		48.15-
523PhosphorylationECKFENNSWVFMRQR
EEEEECCCEEEEEEC		35.88-
557SulfoxidationSNPVTKEMLFEFIDR
CCCCCHHHHHHHHHH		5.7521406390
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 MCE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCE1_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 MCE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCES_HUMANRNMTphysical
9705270
RPB1_HUMANPOLR2Aphysical
27880917
RPB2_HUMANPOLR2Bphysical
27880917
RPB3_HUMANPOLR2Cphysical
27880917
RPB4_HUMANPOLR2Dphysical
27880917
RPAB1_HUMANPOLR2Ephysical
27880917
RPB7_HUMANPOLR2Gphysical
27880917
PP4C_HUMANPPP4Cphysical
27880917
PP4R2_HUMANPPP4R2physical
27880917
P4R3A_HUMANSMEK1physical
27880917
P4R3B_HUMANSMEK2physical
27880917
SPT5H_HUMANSUPT5Hphysical
27880917
RPB9_HUMANPOLR2Iphysical
28514442
MCE1_HUMANRNGTTphysical
27432908
SPT5H_HUMANSUPT5Hphysical
27432908
P4R3A_HUMANSMEK1physical
27432908
PP4R2_HUMANPPP4R2physical
27432908
LACRT_HUMANLACRTphysical
27432908
SG2A1_HUMANSCGB2A1physical
27432908
PROL1_HUMANPROL1physical
27432908
SPT4H_HUMANSUPT4H1physical
27432908
SNX18_HUMANSNX18physical
27432908
RPB4_HUMANPOLR2Dphysical
27432908
SNX9_HUMANSNX9physical
27432908
RPB3_HUMANPOLR2Cphysical
27432908
RPAB1_HUMANPOLR2Ephysical
27432908
PP4C_HUMANPPP4Cphysical
27432908
RPAP2_HUMANRPAP2physical
27432908
LY65B_HUMANLY6G5Bphysical
27432908
CSK22_HUMANCSNK2A2physical
27432908
BRX1_HUMANBRIX1physical
27432908
RL36L_HUMANRPL36ALphysical
27432908
CLU_HUMANCLUHphysical
27432908
AROS_HUMANRPS19BP1physical
27432908
CSK21_HUMANCSNK2A1physical
27432908
G45IP_HUMANGADD45GIP1physical
27432908
SPF27_HUMANBCAS2physical
27432908
HNRH3_HUMANHNRNPH3physical
27432908
RPB2_HUMANPOLR2Bphysical
27432908
RL37A_HUMANRPL37Aphysical
27432908
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 MCE1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-210, AND MASSSPECTROMETRY.

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