MTNA_HUMAN - dbPTM
MTNA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTNA_HUMAN
UniProt AC Q9BV20
Protein Name Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119}
Gene Name MRI1 {ECO:0000255|HAMAP-Rule:MF_03119}
Organism Homo sapiens (Human).
Sequence Length 369
Subcellular Localization Nucleus . Cytoplasm . Cell projection . Primarily nuclear, but cytoplasmic in cancer cells, with enrichment at leading edge of the plasma membrane in late stage tumor cells.
Protein Description Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Independently from catalytic activity, promotes cell invasion in response to constitutive RhoA activation by promoting FAK tyrosine phosphorylation and stress fiber turnover..
Protein Sequence MTLEAIRYSRGSLQILDQLLLPKQSRYEAVGSVHQAWEAIRAMKVRGAPAIALVGCLSLAVELQAGAGGPGLAALVAFVRDKLSFLVTARPTAVNMARAARDLADVAAREAEREGATEEAVRERVICCTEDMLEKDLRDNRSIGDLGARHLLERVAPSGGKVTVLTHCNTGALATAGYGTALGVIRSLHSLGRLEHAFCTETRPYNQGARLTAFELVYEQIPATLITDSMVAAAMAHRGVSAVVVGADRVVANGDTANKVGTYQLAIVAKHHGIPFYVAAPSSSCDLRLETGKEIIIEERPGQELTDVNGVRIAAPGIGVWNPAFDVTPHDLITGGIITELGVFAPEELRTALTTTISSRDGTLDGPQM
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
1Acetylation-------MTLEAIRY
-------CCHHHHHH
9.7122814378
12PhosphorylationAIRYSRGSLQILDQL
HHHHHHHHHHHHHHH
18.9128857561
23UbiquitinationLDQLLLPKQSRYEAV
HHHHHCCCCCHHHHH
61.96-
32PhosphorylationSRYEAVGSVHQAWEA
CHHHHHHHHHHHHHH
15.1628857561
132SulfoxidationVICCTEDMLEKDLRD
EEEECHHHHHHHCCC
4.1921406390
135UbiquitinationCTEDMLEKDLRDNRS
ECHHHHHHHCCCCCC
59.0924816145
142PhosphorylationKDLRDNRSIGDLGAR
HHCCCCCCHHHHHHH
36.8628857561
200PhosphorylationRLEHAFCTETRPYNQ
CCEEEEECCCCCCCC
33.6628857561
241PhosphorylationAMAHRGVSAVVVGAD
HHHHCCCCEEEECCC
20.4028857561
246UbiquitinationGVSAVVVGADRVVAN
CCCEEEECCCEEEEC
15.3421963094
249MethylationAVVVGADRVVANGDT
EEEECCCEEEECCCC
25.03115483681
259UbiquitinationANGDTANKVGTYQLA
ECCCCCCCCCCEEEE
39.31-
259AcetylationANGDTANKVGTYQLA
ECCCCCCCCCCEEEE
39.3125953088
264UbiquitinationANKVGTYQLAIVAKH
CCCCCCEEEEEEHHH
25.0221963094
282PhosphorylationPFYVAAPSSSCDLRL
CEEEECCCCCCCEEE
30.1127251275
283PhosphorylationFYVAAPSSSCDLRLE
EEEECCCCCCCEEEC
33.6527251275
284PhosphorylationYVAAPSSSCDLRLET
EEECCCCCCCEEECC
18.9127251275
293UbiquitinationDLRLETGKEIIIEER
CEEECCCCEEEEEEC
53.8321963094
293AcetylationDLRLETGKEIIIEER
CEEECCCCEEEEEEC
53.8326051181
355PhosphorylationELRTALTTTISSRDG
HHHHHHHHCCCCCCC
24.0028857561
356PhosphorylationLRTALTTTISSRDGT
HHHHHHHCCCCCCCC
17.3928857561
358PhosphorylationTALTTTISSRDGTLD
HHHHHCCCCCCCCCC
19.7529214152
359PhosphorylationALTTTISSRDGTLDG
HHHHCCCCCCCCCCC
30.4629214152
363PhosphorylationTISSRDGTLDGPQM-
CCCCCCCCCCCCCC-
26.4329214152

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 MTNA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTNA_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 MTNA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTNA_HUMANMRI1physical
16189514
PP2BA_HUMANPPP3CAphysical
22939629
RPE_HUMANRPEphysical
22939629
MTNA_HUMANMRI1physical
19447967
MTNA_HUMANMRI1physical
25416956
MTND_HUMANADI1physical
26344197

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MTNA_HUMAN

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Related Literatures of Post-Translational Modification

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