MTNB_HUMAN - dbPTM
MTNB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTNB_HUMAN
UniProt AC Q96GX9
Protein Name Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03116}
Gene Name APIP {ECO:0000255|HAMAP-Rule:MF_03116}
Organism Homo sapiens (Human).
Sequence Length 242
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death..
Protein Sequence MSGCDAREGDCCSRRCGAQDKEHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLKKSQCTPLFMNAYTMRGAGAVIHTHSKAAVMATLLFPGREFKITHQEMIKGIKKCTSGGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGLDPSQLPVGENGIV
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
13PhosphorylationAREGDCCSRRCGAQD
CCCCCCCCCCCCCCC
29.1420068231
19 (in isoform 3)Phosphorylation-47.8227642862
21AcetylationRRCGAQDKEHPRYLI
CCCCCCCCCCHHHHH
45.9323749302
26PhosphorylationQDKEHPRYLIPELCK
CCCCCHHHHHHHHHH
17.2728152594
57PhosphorylationLKHGDEIYIAPSGVQ
CCCCCEEEECCCCCC
6.7528796482
61PhosphorylationDEIYIAPSGVQKERI
CEEEECCCCCCCCCC
42.4429978859
65UbiquitinationIAPSGVQKERIQPED
ECCCCCCCCCCCCCC
46.7029967540
84PhosphorylationDINEKDISGPSPSKK
ECCCCCCCCCCCCCC
55.5830266825
87PhosphorylationEKDISGPSPSKKLKK
CCCCCCCCCCCCCCH
45.3829255136
89PhosphorylationDISGPSPSKKLKKSQ
CCCCCCCCCCCCHHC
46.9229255136
90AcetylationISGPSPSKKLKKSQC
CCCCCCCCCCCHHCC
66.5625953088
94AcetylationSPSKKLKKSQCTPLF
CCCCCCCHHCCCHHE
57.0820167786
95PhosphorylationPSKKLKKSQCTPLFM
CCCCCCHHCCCHHEE
28.9723663014
98PhosphorylationKLKKSQCTPLFMNAY
CCCHHCCCHHEECHH
18.5223663014
105PhosphorylationTPLFMNAYTMRGAGA
CHHEECHHHHCCCCE
8.9623663014
106PhosphorylationPLFMNAYTMRGAGAV
HHEECHHHHCCCCEE
9.6623663014
125PhosphorylationSKAAVMATLLFPGRE
CCHHHHHHHHCCCCE
13.0920068231
142UbiquitinationITHQEMIKGIKKCTS
ECHHHHHHCHHHCCC
53.9629967540
146UbiquitinationEMIKGIKKCTSGGYY
HHHHCHHHCCCCCCC
40.6029967540
188GlutathionylationMNEYPDSCAVLVRRH
HHHCCCCEEEEEHHH
3.8622555962
206AcetylationVWGETWEKAKTMCEC
EEEHHHHHHHHHHHH
46.9019608861
209PhosphorylationETWEKAKTMCECYDY
HHHHHHHHHHHHHHH
31.7326552605
214PhosphorylationAKTMCECYDYLFDIA
HHHHHHHHHHHHHHH
5.8226552605
216PhosphorylationTMCECYDYLFDIAVS
HHHHHHHHHHHHHHH
5.2526552605
223PhosphorylationYLFDIAVSMKKVGLD
HHHHHHHHHHHHCCC
18.8326552605
225UbiquitinationFDIAVSMKKVGLDPS
HHHHHHHHHHCCCHH
36.4832015554
226UbiquitinationDIAVSMKKVGLDPSQ
HHHHHHHHHCCCHHH
32.6629967540

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 MTNB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTNB_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 MTNB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUD18_HUMANNUDT18physical
16189514
VPS25_HUMANVPS25physical
16189514
LNX1_HUMANLNX1physical
16189514
MTNB_HUMANAPIPphysical
16189514
APAF_HUMANAPAF1physical
15262985
MTNB_HUMANAPIPphysical
19060904
MTNB_HUMANAPIPphysical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
PDZD4_HUMANPDZD4physical
25416956
T22D4_HUMANTSC22D4physical
25416956
LNX1_HUMANLNX1physical
25416956
CF206_HUMANC6orf165physical
25416956
HPHL1_HUMANHEPHL1physical
26186194
LYG2_HUMANLYG2physical
26186194
UBA3_HUMANUBA3physical
26186194
DSG4_HUMANDSG4physical
26186194
FAKD2_HUMANFASTKD2physical
26186194
FAKD2_HUMANFASTKD2physical
28514442
LYG2_HUMANLYG2physical
28514442
HPHL1_HUMANHEPHL1physical
28514442
UBA3_HUMANUBA3physical
28514442
DSG4_HUMANDSG4physical
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 MTNB_HUMAN

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Related Literatures of Post-Translational Modification

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