MTRR_HUMAN - dbPTM
MTRR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTRR_HUMAN
UniProt AC Q9UBK8
Protein Name Methionine synthase reductase
Gene Name MTRR
Organism Homo sapiens (Human).
Sequence Length 725
Subcellular Localization Isoform B: Cytoplasm.
Isoform C: Cytoplasm.
Isoform A: Cytoplasm .
Protein Description Involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. Necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects..
Protein Sequence MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS
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
101UbiquitinationDTARKFVKEIQNQTL
HHHHHHHHHHHCCCC		52.83-
171PhosphorylationLVVEPWIAGLWPALR
HHHHHHHCCHHHHHH		11.8023186163
177PhosphorylationIAGLWPALRKHFRSS
HCCHHHHHHHHHHHC		7.0332645325
181UbiquitinationWPALRKHFRSSRGQE
HHHHHHHHHHCCCCH		10.1922817900
183PhosphorylationALRKHFRSSRGQEEI
HHHHHHHHCCCCHHH		24.3630278072
184PhosphorylationLRKHFRSSRGQEEIS
HHHHHHHCCCCHHHC		35.8530278072
189PhosphorylationRSSRGQEEISGALPV
HHCCCCHHHCCCCCC		34.2723186163
191PhosphorylationSRGQEEISGALPVAS
CCCCHHHCCCCCCCC		22.6930278072
198PhosphorylationSGALPVASPASSRTD
CCCCCCCCCCCCCHH		22.6429255136
201PhosphorylationLPVASPASSRTDLVK
CCCCCCCCCCHHHHH		24.6023663014
202PhosphorylationPVASPASSRTDLVKS
CCCCCCCCCHHHHHH		41.1129255136
204PhosphorylationASPASSRTDLVKSEL
CCCCCCCHHHHHHHH		35.3230619164
208 (in isoform 2)Ubiquitination-45.5721906983
208UbiquitinationSSRTDLVKSELLHIE
CCCHHHHHHHHHCHH		45.5722817900
209PhosphorylationSRTDLVKSELLHIES
CCHHHHHHHHHCHHH		26.4627251275
216PhosphorylationSELLHIESQVELLRF
HHHHCHHHHEEEEEC		38.6321712546
226PhosphorylationELLRFDDSGRKDSEV
EEEECCCCCCCCHHH		42.2029214152
231PhosphorylationDDSGRKDSEVLKQNA
CCCCCCCHHHHHHHC		32.4125159151
235 (in isoform 1)Ubiquitination-46.8321906983
235UbiquitinationRKDSEVLKQNAVNSN
CCCHHHHHHHCCCCC		46.832190698
241PhosphorylationLKQNAVNSNQSNVVI
HHHHCCCCCCCCEEE		29.6421712546
244PhosphorylationNAVNSNQSNVVIEDF
HCCCCCCCCEEEECH		35.5221712546
371AcetylationREHCVLLKIKADTKK
HHCEEEEEEEECCCC		37.6926051181
3982-HydroxyisobutyrylationCSLQFIFTWCLEIRA
CCHHHHHHHHHHHHC		15.51-
407UbiquitinationCLEIRAIPKKAFLRA
HHHHHCCCHHHHHHH		30.9833845483
419PhosphorylationLRALVDYTSDSAEKR
HHHHCCCCCCHHHHH		22.92-
420PhosphorylationRALVDYTSDSAEKRR
HHHCCCCCCHHHHHH		24.28-
434UbiquitinationRLQELCSKQGAADYS
HHHHHHHHCCHHHHH		52.32-
548PhosphorylationKALAPKISISPRTTN
CCCCCEEEECCCCCC		24.1223186163
550PhosphorylationLAPKISISPRTTNSF
CCCEEEECCCCCCCC		11.0923186163
625AcetylationKELRHFLKHGILTHL
HHHHHHHHHCHHHHE		38.5526051181
633AcetylationHGILTHLKVSFSRDA
HCHHHHEEEEECCCC		28.3825953088
650UbiquitinationGEEEAPAKYVQDNIQ
CCCCCCHHHHHHHHH		44.91-
650AcetylationGEEEAPAKYVQDNIQ
CCCCCCHHHHHHHHH		44.9126051181
676UbiquitinationQENGHIYVCGDAKNM
HCCCEEEEECCHHHH		2.6629967540
681UbiquitinationIYVCGDAKNMAKDVH
EEEECCHHHHHHHHH		52.5829967540
696PhosphorylationDALVQIISKEVGVEK
HHHHHHHHHHHCHHH		25.1324719451
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 MTRR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTRR_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 MTRR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GMCL1_HUMANGMCL1physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
236270Homocystinuria-megaloblastic anemia, cblE complementation type (HMAE)
601634Neural tube defects, folate-sensitive (NTDFS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00115Cyanocobalamin
DB00200Hydroxocobalamin
DB00134L-Methionine
Regulatory Network of MTRR_HUMAN

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Related Literatures of Post-Translational Modification

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