CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017056
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitochondrial Rho GTPase 2 
Protein Synonyms/Alias
 MIRO-2; hMiro-2; Ras homolog gene family member T2 
Gene Name
 RHOT2 
Gene Synonyms/Alias
 ARHT2; C16orf39 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
96TIEKIRTKWIPLVNGubiquitination[1]
119PIILVGNKSDLRSGSubiquitination[1, 2, 3, 4, 5, 6]
164ELFYYAQKAVLHPTAubiquitination[1, 5]
179PLYDPEAKQLRPACAubiquitination[1, 2, 5, 6]
214EELNAFQKSCFGHPLubiquitination[1, 5, 7, 8]
230PQALEDVKTVVCRNVubiquitination[1]
409EKRLDQEKGQTQRSVubiquitination[5]
420QRSVLLCKVVGARGVubiquitination[1, 2, 6, 9]
429VGARGVGKSAFLQAFubiquitination[1, 2, 6, 7]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). 
Sequence Annotation
 DOMAIN 1 142 Miro 1.
 DOMAIN 184 219 EF-hand 1.
 DOMAIN 304 339 EF-hand 2.
 DOMAIN 410 618 Miro 2.
 NP_BIND 11 18 GTP 1 (Potential).
 NP_BIND 57 61 GTP 1 (Potential).
 NP_BIND 118 121 GTP 1 (Potential).
 NP_BIND 423 430 GTP 2 (Potential).
 NP_BIND 459 463 GTP 2 (Potential).
 NP_BIND 524 527 GTP 2 (Potential).  
Keyword
 Alternative splicing; Calcium; Complete proteome; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 618 AA 
Protein Sequence
MRRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPPRAEEI TIPADVTPEK VPTHIVDYSE 60
AEQTDEELRE EIHKANVVCV VYDVSEEATI EKIRTKWIPL VNGGTTQGPR VPIILVGNKS 120
DLRSGSSMEA VLPIMSQFPE IETCVECSAK NLRNISELFY YAQKAVLHPT APLYDPEAKQ 180
LRPACAQALT RIFRLSDQDL DQALSDEELN AFQKSCFGHP LAPQALEDVK TVVCRNVAGG 240
VREDRLTLDG FLFLNTLFIQ RGRHETTWTI LRRFGYSDAL ELTADYLSPL IHVPPGCSTE 300
LNHLGYQFVQ RVFEKHDQDR DGALSPVELQ SLFSVFPAAP WGPELPRTVR TEAGRLPLHG 360
YLCQWTLVTY LDVRSCLGHL GYLGYPTLCE QDQAHAITVT REKRLDQEKG QTQRSVLLCK 420
VVGARGVGKS AFLQAFLGRG LGHQDTREQP PGYAIDTVQV NGQEKYLILC EVGTDGLLAT 480
SLDATCDVAC LMFDGSDPKS FAHCASVYKH HYMDGQTPCL FVSSKADLPE GVAVSGPSPA 540
EFCRKHRLPA PVPFSCAGPA EPSTTIFTQL ATMAAFPHLV HAELHPSSFW LRGLLGVVGA 600
AVAAVLSFSL YRVLVKSQ 618 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031307; C:integral to mitochondrial outer membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0019725; P:cellular homeostasis; IMP:UniProtKB.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0097345; P:mitochondrial outer membrane permeabilization; IMP:UniProtKB.
 GO:0047497; P:mitochondrion transport along microtubule; IMP:UniProtKB.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR013566; EF_hand_assoc_1.
 IPR013567; EF_hand_assoc_2.
 IPR002048; EF_hand_dom.
 IPR020860; MIRO.
 IPR013684; MIRO-like.
 IPR027417; P-loop_NTPase.
 IPR001806; Small_GTPase.
 IPR021181; Small_GTPase_Miro. 
Pfam
 PF08355; EF_assoc_1
 PF08356; EF_assoc_2
 PF08477; Miro
 PF00071; Ras 
SMART
 SM00054; EFh 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS51423; MIRO 
PRINTS
 PR00449; RASTRNSFRMNG.