MIRO1_HUMAN - dbPTM
MIRO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIRO1_HUMAN
UniProt AC Q8IXI2
Protein Name Mitochondrial Rho GTPase 1
Gene Name RHOT1
Organism Homo sapiens (Human).
Sequence Length 618
Subcellular Localization Mitochondrion outer membrane
Single-pass type IV membrane protein . Colocalizes with MGARP and RHOT2 at the mitochondria.
Protein Description Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution..
Protein Sequence MKKDVRILLVGEPRVGKTSLIMSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLINERTDKDSRLPLILVGNKSDLVEYSSMETILPIMNQYTEIETCVECSAKNLKNISELFYYAQKAVLHPTGPLYCPEEKEMKPACIKALTRIFKISDQDNDGTLNDAELNFFQRICFNTPLAPQALEDVKNVVRKHISDGVADSGLTLKGFLFLHTLFIQRGRHETTWTVLRRFGYDDDLDLTPEYLFPLLKIPPDCTTELNHHAYLFLQSTFDKHDLDRDCALSPDELKDLFKVFPYIPWGPDVNNTVCTNERGWITYQGFLSQWTLTTYLDVQRCLEYLGYLGYSILTEQESQASAVTVTRDKKIDLQKKQTQRNVFRCNVIGVKNCGKSGVLQALLGRNLMRQKKIREDHKSYYAINTVYVYGQEKYLLLHDISESEFLTEAEIICDVVCLVYDVSNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMPPPQAFTCNTADAPSKDIFVKLTTMAMYPHVTQADLKSSTFWLRASFGATVFAVLGFAMYKALLKQR
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
92UbiquitinationNNKHSIDKVTSRWIP
CCCCCCHHHHHCEEH		45.82-
92AcetylationNNKHSIDKVTSRWIP
CCCCCCHHHHHCEEH		45.8219608861
107UbiquitinationLINERTDKDSRLPLI
HHCCCCCCCCCCCEE		57.92-
153UbiquitinationECSAKNLKNISELFY
HHCCCCCCCHHHHHH		62.7221890473
153 (in isoform 2)Ubiquitination-62.7221890473
153 (in isoform 3)Ubiquitination-62.7221890473
153 (in isoform 1)Ubiquitination-62.7221890473
153 (in isoform 4)Ubiquitination-62.7221890473
153 (in isoform 5)Ubiquitination-62.7221890473
153 (in isoform 6)Ubiquitination-62.7221890473
156PhosphorylationAKNLKNISELFYYAQ
CCCCCCHHHHHHHHH		37.3322078885
160PhosphorylationKNISELFYYAQKAVL
CCHHHHHHHHHHHHC		15.54-
182UbiquitinationCPEEKEMKPACIKAL
CCCHHHCHHHHHHHH		30.47-
187 (in isoform 4)Ubiquitination-36.9121890473
187 (in isoform 5)Ubiquitination-36.9121890473
187 (in isoform 2)Ubiquitination-36.9121890473
187 (in isoform 1)Ubiquitination-36.9121890473
187 (in isoform 3)Ubiquitination-36.9121890473
187 (in isoform 6)Ubiquitination-36.9121890473
187UbiquitinationEMKPACIKALTRIFK
HCHHHHHHHHHHHHH		36.912189047
194UbiquitinationKALTRIFKISDQDND
HHHHHHHHCCCCCCC		38.64-
194 (in isoform 2)Ubiquitination-38.64-
230UbiquitinationPQALEDVKNVVRKHI
HHHHHHHHHHHHHHH		57.24-
235UbiquitinationDVKNVVRKHISDGVA
HHHHHHHHHHCCCCC		33.41-
235 (in isoform 2)Ubiquitination-33.41-
276PhosphorylationTVLRRFGYDDDLDLT
HHHHHHCCCCCCCCC		17.3118452278
283PhosphorylationYDDDLDLTPEYLFPL
CCCCCCCCHHHHHHH		17.4618452278
298PhosphorylationLKIPPDCTTELNHHA
HCCCCCCCCCCCHHH		30.5922078885
299PhosphorylationKIPPDCTTELNHHAY
CCCCCCCCCCCHHHE		44.8222078885
325PhosphorylationLDRDCALSPDELKDL
CCCCCCCCHHHHHHH		16.2724076635
330UbiquitinationALSPDELKDLFKVFP
CCCHHHHHHHHHHCC		50.79-
427UbiquitinationRCNVIGVKNCGKSGV
ECEEEEEECCCHHHH		41.11-
461PhosphorylationKSYYAINTVYVYGQE
HHEEEEEEEEEECCE		13.7028442448
463PhosphorylationYYAINTVYVYGQEKY
EEEEEEEEEECCEEE		5.9628152594
465PhosphorylationAINTVYVYGQEKYLL
EEEEEEEECCEEEEE		8.7328152594
512 (in isoform 3)Ubiquitination-40.26-
512MalonylationEYCARIFKQHFMDSR
HHHHHHHHHHCCCCC		40.2626320211
512AcetylationEYCARIFKQHFMDSR
HHHHHHHHHHCCCCC		40.2625953088
512 (in isoform 3)Malonylation-40.2626320211
512UbiquitinationEYCARIFKQHFMDSR
HHHHHHHHHHCCCCC		40.26-
535UbiquitinationKSDLHEVKQEYSISP
CCCHHHHHHHHCCCH		34.13-
558PhosphorylationMPPPQAFTCNTADAP
CCCCCCEECCCCCCC		14.09-
561PhosphorylationPQAFTCNTADAPSKD
CCCEECCCCCCCCCC		28.23-
566PhosphorylationCNTADAPSKDIFVKL
CCCCCCCCCCEEEHH		44.68-
572 (in isoform 2)Ubiquitination-29.39-
572UbiquitinationPSKDIFVKLTTMAMY
CCCCEEEHHHHHHHC		29.39-
579PhosphorylationKLTTMAMYPHVTQAD
HHHHHHHCCCCCHHH		4.8129116813
589 (in isoform 3)Phosphorylation-41.7428348404
589 (in isoform 2)Phosphorylation-41.7428348404
589PhosphorylationVTQADLKSSTFWLRA
CCHHHHCCCCCHHHH		41.7427251275
590PhosphorylationTQADLKSSTFWLRAS
CHHHHCCCCCHHHHH		26.4927251275
591PhosphorylationQADLKSSTFWLRASF
HHHHCCCCCHHHHHH		26.3927251275
597PhosphorylationSTFWLRASFGATVFA
CCCHHHHHHCHHHHH		20.1327251275
601PhosphorylationLRASFGATVFAVLGF
HHHHHCHHHHHHHHH		19.2827251275
611PhosphorylationAVLGFAMYKALLKQR
HHHHHHHHHHHHHCC		6.95-
613 (in isoform 5)Ubiquitination-10.7121890473
645 (in isoform 3)Ubiquitination-21890473
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
156SPhosphorylationKinasePINK1Q9BXM7
PSP
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:26254304
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIRO1_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 MIRO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PINK1_HUMANPINK1physical
22396657
PRKN_HUMANPARK2physical
22396657
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 MIRO1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND MASS SPECTROMETRY.

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