RPOM_HUMAN - dbPTM
RPOM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPOM_HUMAN
UniProt AC O00411
Protein Name DNA-directed RNA polymerase, mitochondrial
Gene Name POLRMT
Organism Homo sapiens (Human).
Sequence Length 1230
Subcellular Localization Mitochondrion .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates..
Protein Sequence MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHVELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCGRWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTRQAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLPLAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYAAALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSLPPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKPTLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVVRMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASDAEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSSRLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHSGAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQLFQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEALYRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDWLKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCMEVANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVAAQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQPYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILEASQLKETLQAVPKPGAFDLEQVKRSTYFFS
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
8MethylationMSALCWGRGAAGLKR
CCCCCCCCCHHHHHH
13.69115488221
28MethylationGRPGLPGKEGTAGGV
CCCCCCCCCCCCCCC
51.5423644510
77PhosphorylationVRQLQAESVSEVVVN
HHHHHHCCCCEEEEC
33.6819691289
79PhosphorylationQLQAESVSEVVVNRV
HHHHCCCCEEEECCC
33.6720860994
115PhosphorylationQMGAKDATPVPCGRW
CCCCCCCCCCCCHHH
34.6519007248
146SulfoxidationRLKAKLQMPFQSGEF
HHHHHHCCCCCCCHH
5.3521406390
150PhosphorylationKLQMPFQSGEFKALT
HHCCCCCCCHHHHHH
40.4420860994
154UbiquitinationPFQSGEFKALTRRLQ
CCCCCHHHHHHHHHC
37.88-
201UbiquitinationLLQEAPGKLSLDVEQ
HHHHCCCCCEEEHHC
33.57-
211PhosphorylationLDVEQAPSGQHSQAQ
EEHHCCCCCCCCCHH
54.8520860994
215PhosphorylationQAPSGQHSQAQLSGQ
CCCCCCCCCHHHCHH
21.2320860994
220PhosphorylationQHSQAQLSGQQQRLL
CCCCHHHCHHHHHHH
23.6020860994
299PhosphorylationLTPDLLSYAAALQCM
CCHHHHHHHHHHHHC
10.55-
315PhosphorylationRQDQDAGTIERCLEQ
CCCCCHHHHHHHHHH
22.76-
370PhosphorylationQLPPPVNTSKLLRDV
CCCCCCCHHHHHHHH
27.7222468782
371PhosphorylationLPPPVNTSKLLRDVY
CCCCCCHHHHHHHHH
18.9929759185
385PhosphorylationYAKDGRVSYPKLHLP
HCCCCCCCCCCCCCC
34.0624719451
386PhosphorylationAKDGRVSYPKLHLPL
CCCCCCCCCCCCCCH
11.09-
394UbiquitinationPKLHLPLKTLQCLFE
CCCCCCHHHHHHHHH
45.29-
394AcetylationPKLHLPLKTLQCLFE
CCCCCCHHHHHHHHH
45.2926051181
402AcetylationTLQCLFEKQLHMELA
HHHHHHHHHHHHHHH
51.3125825284
410PhosphorylationQLHMELASRVCVVSV
HHHHHHHHCEEEEEE
37.5622210691
419AcetylationVCVVSVEKPTLPSKE
EEEEEECCCCCCHHH
40.9426822725
424PhosphorylationVEKPTLPSKEVKHAR
ECCCCCCHHHHHHHH
44.5624719451
425AcetylationEKPTLPSKEVKHARK
CCCCCCHHHHHHHHH
65.6726051181
436PhosphorylationHARKTLKTLRDQWEK
HHHHHHHHHHHHHHH
30.09-
443AcetylationTLRDQWEKALCRALR
HHHHHHHHHHHHHHH
43.6426051181
532UbiquitinationALQNHYRKYLCLLAS
HHHHHHHHHHHHHHC
35.09-
595AcetylationQMPCSLDKPHRSSRL
CCCCCCCCCCHHCCH
48.2825953088
622AcetylationVQQIGILKPHPAYVQ
CEEEEECCCCHHHHH
39.0823236377
666PhosphorylationHSGAFLLSPTKLMRT
CCCCEECCHHHHHHH
32.4424719451
993PhosphorylationTRKVVKQTVMTVVYG
HHHHHHHHHHHHHHH
13.41-
999PhosphorylationQTVMTVVYGVTRYGG
HHHHHHHHHHHHCCC
11.09-
1004PhosphorylationVVYGVTRYGGRLQIE
HHHHHHHCCCHHHHH
17.99-
1101PhosphorylationGIQSITYTHNGDISR
CEEEEEEECCCCCCC
10.5428464451
1197UbiquitinationRFCSEPQKILEASQL
HHCCCHHHHHHHHHH
61.0321890473
1197AcetylationRFCSEPQKILEASQL
HHCCCHHHHHHHHHH
61.0326051181
1205UbiquitinationILEASQLKETLQAVP
HHHHHHHHHHHHCCC
40.80-
1205AcetylationILEASQLKETLQAVP
HHHHHHHHHHHHCCC
40.8026051181
1212UbiquitinationKETLQAVPKPGAFDL
HHHHHCCCCCCCCCH
39.8921890473
1213UbiquitinationETLQAVPKPGAFDLE
HHHHCCCCCCCCCHH
49.86-

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 RPOM_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPOM_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 RPOM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RPOM_HUMAN !!

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 RPOM_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115, AND MASSSPECTROMETRY.

TOP