MARC1_HUMAN - dbPTM
MARC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARC1_HUMAN
UniProt AC Q5VT66
Protein Name Mitochondrial amidoxime-reducing component 1
Gene Name 1-Mar
Organism Homo sapiens (Human).
Sequence Length 337
Subcellular Localization Mitochondrion outer membrane
Single-pass type II membrane protein . Membrane
Lipid-anchor . Mitochondrial import is mediated by AA 1-40 and requires ATP.
Protein Description As a component of an N-hydroxylated prodrug-converting complex required to reduce N-hydroxylated prodrugs, such as benzamidoxime. Also able to reduce N(omega)-hydroxy-L-arginine (NOHA) and N(omega)-hydroxy-N(delta)-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively..
Protein Sequence MGAAGSSALARFVLLAQSRPGWLGVAALGLTAVALGAVAWRRAWPTRRRRLLQQVGTVAQLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVINQEGNMVTARQEPRLVLISLTCDGDTLTLSAAYTKDLLLPIKTPTTNAVHKCRVHGLEIEGRDCGEATAQWITSFLKSQPYRLVHFEPHMRPRRPHQIADLFRPKDQIAYSDTSPFLILSEASLADLNSRLEKKVKATNFRPNIVISGCDVYAEDSWDELLIGDVELKRVMACSRCILTTVDPDTGVMSRKEPLETLKSYRQCDPSERKLYGKSPLFGQYFVLENPGTIKVGDPVYLLGQ
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
2Myristoylation------MGAAGSSAL
------CCCCHHHHH
25807930
6Phosphorylation--MGAAGSSALARFV
--CCCCHHHHHHHHH
20068231
7Phosphorylation-MGAAGSSALARFVL
-CCCCHHHHHHHHHH
20068231
18PhosphorylationRFVLLAQSRPGWLGV
HHHHHHHCCCCHHHH
20068231
46UbiquitinationAWRRAWPTRRRRLLQ
HHHHHCHHHHHHHHH
21963094
65UbiquitinationVAQLWIYPVKSCKGV
EEEEEEEECCCCCCC
21963094
67MalonylationQLWIYPVKSCKGVPV
EEEEEECCCCCCCCC
26320211
67AcetylationQLWIYPVKSCKGVPV
EEEEEECCCCCCCCC
26051181
67UbiquitinationQLWIYPVKSCKGVPV
EEEEEECCCCCCCCC
21963094
70UbiquitinationIYPVKSCKGVPVSEA
EEECCCCCCCCCCHH
21963094
72UbiquitinationPVKSCKGVPVSEAEC
ECCCCCCCCCCHHHH
21963094
91UbiquitinationLRSGNLRDRFWLVIN
CCCCCCCCCEEEEEE
21963094
100UbiquitinationFWLVINQEGNMVTAR
EEEEEECCCCEEECC
21963094
111MethylationVTARQEPRLVLISLT
EECCCCCCEEEEEEE
54557407
119UbiquitinationLVLISLTCDGDTLTL
EEEEEEEECCCEEEE
21963094
139UbiquitinationKDLLLPIKTPTTNAV
CCCEEECCCCCCCCC
29967540
140PhosphorylationDLLLPIKTPTTNAVH
CCEEECCCCCCCCCC
25159151
148UbiquitinationPTTNAVHKCRVHGLE
CCCCCCCCCEECCEE
21963094
163UbiquitinationIEGRDCGEATAQWIT
EECCCCHHHHHHHHH
21963094
171PhosphorylationATAQWITSFLKSQPY
HHHHHHHHHHHCCCE
24719451
174UbiquitinationQWITSFLKSQPYRLV
HHHHHHHHCCCEEEE
21963094
180UbiquitinationLKSQPYRLVHFEPHM
HHCCCEEEEEECCCC
22817900
182UbiquitinationSQPYRLVHFEPHMRP
CCCEEEEEECCCCCC
21963094
186UbiquitinationRLVHFEPHMRPRRPH
EEEEECCCCCCCCCC
21963094
193UbiquitinationHMRPRRPHQIADLFR
CCCCCCCCHHHHHCC
21963094
199UbiquitinationPHQIADLFRPKDQIA
CCHHHHHCCCHHHCC
22817900
202UbiquitinationIADLFRPKDQIAYSD
HHHHCCCHHHCCCCC
21963094
202 (in isoform 2)Ubiquitination--
203UbiquitinationADLFRPKDQIAYSDT
HHHCCCHHHCCCCCC
21963094
204UbiquitinationDLFRPKDQIAYSDTS
HHCCCHHHCCCCCCC
21963094
205UbiquitinationLFRPKDQIAYSDTSP
HCCCHHHCCCCCCCC
21963094
208UbiquitinationPKDQIAYSDTSPFLI
CHHHCCCCCCCCEEE
21890473
210UbiquitinationDQIAYSDTSPFLILS
HHCCCCCCCCEEEEE
21963094
212UbiquitinationIAYSDTSPFLILSEA
CCCCCCCCEEEEEHH
21963094
221UbiquitinationLILSEASLADLNSRL
EEEEHHHHHHHHHHH
21963094
222UbiquitinationILSEASLADLNSRLE
EEEHHHHHHHHHHHH
21963094
223UbiquitinationLSEASLADLNSRLEK
EEHHHHHHHHHHHHH
21963094
225 (in isoform 3)Ubiquitination-21890473
225UbiquitinationEASLADLNSRLEKKV
HHHHHHHHHHHHHHH
21890473
227UbiquitinationSLADLNSRLEKKVKA
HHHHHHHHHHHHHHH
21890473
229UbiquitinationADLNSRLEKKVKATN
HHHHHHHHHHHHHCC
21963094
230UbiquitinationDLNSRLEKKVKATNF
HHHHHHHHHHHHCCC
29967540
240UbiquitinationKATNFRPNIVISGCD
HHCCCCCCEEEECCE
21963094
242UbiquitinationTNFRPNIVISGCDVY
CCCCCCEEEECCEEE
22817900
244UbiquitinationFRPNIVISGCDVYAE
CCCCEEEECCEEEEC
21890473
261UbiquitinationWDELLIGDVELKRVM
CCCCEECCHHHHHHH
22817900
265UbiquitinationLIGDVELKRVMACSR
EECCHHHHHHHCCCC
21963094
271PhosphorylationLKRVMACSRCILTTV
HHHHHCCCCEEEEEE
22210691
276PhosphorylationACSRCILTTVDPDTG
CCCCEEEEEECCCCC
22210691
277PhosphorylationCSRCILTTVDPDTGV
CCCEEEEEECCCCCC
22210691
282UbiquitinationLTTVDPDTGVMSRKE
EEEECCCCCCCCCCC
22817900
288UbiquitinationDTGVMSRKEPLETLK
CCCCCCCCCCHHHHH
21963094
295UbiquitinationKEPLETLKSYRQCDP
CCCHHHHHHHHCCCH
21963094
296PhosphorylationEPLETLKSYRQCDPS
CCHHHHHHHHCCCHH
-
297PhosphorylationPLETLKSYRQCDPSE
CHHHHHHHHCCCHHH
-
303PhosphorylationSYRQCDPSERKLYGK
HHHCCCHHHHHHHCC
-
305UbiquitinationRQCDPSERKLYGKSP
HCCCHHHHHHHCCCC
21963094
306UbiquitinationQCDPSERKLYGKSPL
CCCHHHHHHHCCCCC
21963094
310UbiquitinationSERKLYGKSPLFGQY
HHHHHHCCCCCCCCE
21890473
310 (in isoform 1)Ubiquitination-21890473
310UbiquitinationSERKLYGKSPLFGQY
HHHHHHCCCCCCCCE
21963094
312UbiquitinationRKLYGKSPLFGQYFV
HHHHCCCCCCCCEEE
21963094
312 (in isoform 2)Ubiquitination--
317PhosphorylationKSPLFGQYFVLENPG
CCCCCCCEEEEECCC
-
323UbiquitinationQYFVLENPGTIKVGD
CEEEEECCCEEECCC
21963094
327UbiquitinationLENPGTIKVGDPVYL
EECCCEEECCCCEEE
21890473
344UbiquitinationQ--------------
C--------------
22817900

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 MARC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MARC1_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 MARC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB6C_HUMANRAB6Cphysical
22939629
RM39_HUMANMRPL39physical
22939629
VATB1_HUMANATP6V1B1physical
22939629
NDUBA_HUMANNDUFB10physical
22939629
NDUB4_HUMANNDUFB4physical
22939629
ZC3H4_HUMANZC3H4physical
22939629
NDUS4_HUMANNDUFS4physical
22939629
RM15_HUMANMRPL15physical
22939629
S2546_HUMANSLC25A46physical
22939629
ODPX_HUMANPDHXphysical
22939629
TFB2M_HUMANTFB2Mphysical
27173435
MCATL_HUMANSLC25A29physical
27173435
AGM1_HUMANPGM3physical
27173435
MBB1A_HUMANMYBBP1Aphysical
27173435
BDH_HUMANBDH1physical
27173435

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 MARC1_HUMAN

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Related Literatures of Post-Translational Modification

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