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Q8IXI1

- MIRO2_HUMAN

UniProt

Q8IXI1 - MIRO2_HUMAN

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Protein

Mitochondrial Rho GTPase 2

Gene
RHOT2, ARHT2, C16orf39
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution By similarity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188GTP 1 Reviewed prediction
Nucleotide bindingi57 – 615GTP 1 Reviewed prediction
Nucleotide bindingi118 – 1214GTP 1 Reviewed prediction
Calcium bindingi197 – 208121 Reviewed predictionAdd
BLAST
Calcium bindingi317 – 328122 Reviewed predictionAdd
BLAST
Nucleotide bindingi423 – 4308GTP 2 Reviewed prediction
Nucleotide bindingi459 – 4635GTP 2 Reviewed prediction
Nucleotide bindingi524 – 5274GTP 2 Reviewed prediction

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. GTPase activity Source: InterPro
  3. GTP binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular homeostasis Source: UniProtKB
  2. mitochondrial outer membrane permeabilization Source: UniProtKB
  3. mitochondrion transport along microtubule Source: UniProtKB
  4. regulation of small GTPase mediated signal transduction Source: Reactome
  5. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, GTP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial Rho GTPase 2 (EC:3.6.5.-)
Short name:
MIRO-2
Short name:
hMiro-2
Alternative name(s):
Ras homolog gene family member T2
Gene namesi
Name:RHOT2
Synonyms:ARHT2, C16orf39
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:21169. RHOT2.

Subcellular locationi

Mitochondrion outer membrane; Single-pass type IV membrane protein
Note: Colocalizes with MGARP and RHOT2 at the mitochondria.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 592592Mitochondrial intermembrane Reviewed predictionAdd
BLAST
Transmembranei593 – 61523Helical; Anchor for type IV membrane protein; Reviewed predictionAdd
BLAST
Topological domaini616 – 6183Cytoplasmic Reviewed prediction

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of mitochondrial outer membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131A → V: Causes constitutive activation inducing an aggregation of the mitochondrial network. 2 Publications
Mutagenesisi18 – 181T → N: Induces an aggregation of the mitochondrial network. 1 Publication

Organism-specific databases

PharmGKBiPA134889674.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 618618Mitochondrial Rho GTPase 2PRO_0000239318Add
BLAST

Proteomic databases

MaxQBiQ8IXI1.
PaxDbiQ8IXI1.
PRIDEiQ8IXI1.

PTM databases

PhosphoSiteiQ8IXI1.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in heart, liver, skeletal muscle, kidney and pancreas.2 Publications

Gene expression databases

ArrayExpressiQ8IXI1.
BgeeiQ8IXI1.
CleanExiHS_RHOT2.
GenevestigatoriQ8IXI1.

Organism-specific databases

HPAiHPA012624.
HPA012895.

Interactioni

Subunit structurei

Interacts with the kinesin-binding proteins TRAK1/OIP106 and TRAK2/GRIF1, forming a link between mitochondria and the trafficking apparatus of the microtubules By similarity.1 Publication

Protein-protein interaction databases

BioGridi124646. 27 interactions.
IntActiQ8IXI1. 6 interactions.
MINTiMINT-1191538.
STRINGi9606.ENSP00000321971.

Structurei

3D structure databases

ProteinModelPortaliQ8IXI1.
SMRiQ8IXI1. Positions 5-167, 180-578.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 142142Miro 1Add
BLAST
Domaini184 – 21936EF-hand 1Add
BLAST
Domaini304 – 33936EF-hand 2Add
BLAST
Domaini410 – 618209Miro 2Add
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.
Contains 2 Miro domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1100.
HOVERGENiHBG079778.
InParanoidiQ8IXI1.
KOiK07871.
OMAiVLPQITI.
OrthoDBiEOG7PK8Z0.
PhylomeDBiQ8IXI1.
TreeFamiTF300814.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
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.
IPR029506. Rho_GTPase_2.
IPR021181. Rho_GTPase_Mt.
IPR001806. Small_GTPase.
[Graphical view]
PANTHERiPTHR24072:SF70. PTHR24072:SF70. 1 hit.
PfamiPF08355. EF_assoc_1. 1 hit.
PF08356. EF_assoc_2. 1 hit.
PF08477. Miro. 1 hit.
PF00071. Ras. 1 hit.
[Graphical view]
PIRSFiPIRSF037488. Mt_Rho_GTPase. 1 hit.
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS51423. MIRO. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IXI1-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MRRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPPRAEEI TIPADVTPEK    50
VPTHIVDYSE AEQTDEELRE EIHKANVVCV VYDVSEEATI EKIRTKWIPL 100
VNGGTTQGPR VPIILVGNKS DLRSGSSMEA VLPIMSQFPE IETCVECSAK 150
NLRNISELFY YAQKAVLHPT APLYDPEAKQ LRPACAQALT RIFRLSDQDL 200
DQALSDEELN AFQKSCFGHP LAPQALEDVK TVVCRNVAGG VREDRLTLDG 250
FLFLNTLFIQ RGRHETTWTI LRRFGYSDAL ELTADYLSPL IHVPPGCSTE 300
LNHLGYQFVQ RVFEKHDQDR DGALSPVELQ SLFSVFPAAP WGPELPRTVR 350
TEAGRLPLHG YLCQWTLVTY LDVRSCLGHL GYLGYPTLCE QDQAHAITVT 400
REKRLDQEKG QTQRSVLLCK VVGARGVGKS AFLQAFLGRG LGHQDTREQP 450
PGYAIDTVQV NGQEKYLILC EVGTDGLLAT SLDATCDVAC LMFDGSDPKS 500
FAHCASVYKH HYMDGQTPCL FVSSKADLPE GVAVSGPSPA EFCRKHRLPA 550
PVPFSCAGPA EPSTTIFTQL ATMAAFPHLV HAELHPSSFW LRGLLGVVGA 600
AVAAVLSFSL YRVLVKSQ 618
Length:618
Mass (Da):68,118
Last modified:June 13, 2006 - v2
Checksum:iC72ECBCA33D04B6B
GO
Isoform 2 (identifier: Q8IXI1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.
     251-340: FLFLNTLFIQ...SLFSVFPAAP → EAGCPPVPGE...PWLPVCAESV
     341-618: Missing.

Show »
Length:213
Mass (Da):23,077
Checksum:i76722819B54E29DE
GO

Sequence cautioni

The sequence BAB15740.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC03407.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAK61240.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti245 – 2451R → Q.1 Publication
Corresponds to variant rs1139897 [ dbSNP | Ensembl ].
VAR_026637
Natural varianti425 – 4251R → C.1 Publication
Corresponds to variant rs3177338 [ dbSNP | Ensembl ].
VAR_026638

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 127127Missing in isoform 2. VSP_019162Add
BLAST
Alternative sequencei251 – 34090FLFLN…FPAAP → EAGCPPVPGECGEGAVPGAP PALSRCRFPLPEHALHPARP ARDHLDHPAALRLQRCPGAD CGLSLPSDPRAPRLQHGAQP PWLPVCAESV in isoform 2. VSP_019163Add
BLAST
Alternative sequencei341 – 618278Missing in isoform 2. VSP_019164Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391P → S in CAD56957. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ517413 mRNA. Translation: CAD56957.1.
AY207375 mRNA. Translation: AAP46090.1.
AK024450 mRNA. Translation: BAB15740.1. Different initiation.
AK090426 mRNA. Translation: BAC03407.1. Different initiation.
AE006464 Genomic DNA. Translation: AAK61240.1. Sequence problems.
Z92544 Genomic DNA. Translation: CAM26351.1.
CH471112 Genomic DNA. Translation: EAW85763.1.
BC004327 mRNA. Translation: AAH04327.1.
BC014942 mRNA. Translation: AAH14942.1.
CCDSiCCDS10417.1. [Q8IXI1-1]
RefSeqiNP_620124.1. NM_138769.2. [Q8IXI1-1]
UniGeneiHs.513242.

Genome annotation databases

EnsembliENST00000315082; ENSP00000321971; ENSG00000140983. [Q8IXI1-1]
GeneIDi89941.
KEGGihsa:89941.
UCSCiuc002cip.3. human. [Q8IXI1-1]

Polymorphism databases

DMDMi108860798.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ517413 mRNA. Translation: CAD56957.1 .
AY207375 mRNA. Translation: AAP46090.1 .
AK024450 mRNA. Translation: BAB15740.1 . Different initiation.
AK090426 mRNA. Translation: BAC03407.1 . Different initiation.
AE006464 Genomic DNA. Translation: AAK61240.1 . Sequence problems.
Z92544 Genomic DNA. Translation: CAM26351.1 .
CH471112 Genomic DNA. Translation: EAW85763.1 .
BC004327 mRNA. Translation: AAH04327.1 .
BC014942 mRNA. Translation: AAH14942.1 .
CCDSi CCDS10417.1. [Q8IXI1-1 ]
RefSeqi NP_620124.1. NM_138769.2. [Q8IXI1-1 ]
UniGenei Hs.513242.

3D structure databases

ProteinModelPortali Q8IXI1.
SMRi Q8IXI1. Positions 5-167, 180-578.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124646. 27 interactions.
IntActi Q8IXI1. 6 interactions.
MINTi MINT-1191538.
STRINGi 9606.ENSP00000321971.

PTM databases

PhosphoSitei Q8IXI1.

Polymorphism databases

DMDMi 108860798.

Proteomic databases

MaxQBi Q8IXI1.
PaxDbi Q8IXI1.
PRIDEi Q8IXI1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315082 ; ENSP00000321971 ; ENSG00000140983 . [Q8IXI1-1 ]
GeneIDi 89941.
KEGGi hsa:89941.
UCSCi uc002cip.3. human. [Q8IXI1-1 ]

Organism-specific databases

CTDi 89941.
GeneCardsi GC16P000826.
HGNCi HGNC:21169. RHOT2.
HPAi HPA012624.
HPA012895.
MIMi 613889. gene.
neXtProti NX_Q8IXI1.
PharmGKBi PA134889674.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
HOVERGENi HBG079778.
InParanoidi Q8IXI1.
KOi K07871.
OMAi VLPQITI.
OrthoDBi EOG7PK8Z0.
PhylomeDBi Q8IXI1.
TreeFami TF300814.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.

Miscellaneous databases

GeneWikii RHOT2.
GenomeRNAii 89941.
NextBioi 76445.
PROi Q8IXI1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IXI1.
Bgeei Q8IXI1.
CleanExi HS_RHOT2.
Genevestigatori Q8IXI1.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
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.
IPR029506. Rho_GTPase_2.
IPR021181. Rho_GTPase_Mt.
IPR001806. Small_GTPase.
[Graphical view ]
PANTHERi PTHR24072:SF70. PTHR24072:SF70. 1 hit.
Pfami PF08355. EF_assoc_1. 1 hit.
PF08356. EF_assoc_2. 1 hit.
PF08477. Miro. 1 hit.
PF00071. Ras. 1 hit.
[Graphical view ]
PIRSFi PIRSF037488. Mt_Rho_GTPase. 1 hit.
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00054. EFh. 2 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS51423. MIRO. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis."
    Fransson A., Ruusala A., Aspenstroem P.
    J. Biol. Chem. 278:6495-6502(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS GLN-245 AND CYS-425.
  2. "Cloning and characterization of the mouse Arht2 gene which encodes a putative atypical GTPase."
    Shan Y., Hexige S., Guo Z., Wan B., Chen K., Chen X., Ma L., Huang C., Zhao S., Yu L.
    Cytogenet. Genome Res. 106:91-97(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Spleen.
  4. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
    Jikuya H., Takano J., Kikuno R., Nagase T., Ohara O.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Spleen.
  5. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta and Skin.
  9. "Rho GTPases have diverse effects on the organization of the actin filament system."
    Aspenstroem P., Fransson A., Saras J.
    Biochem. J. 377:327-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-13.
  10. "The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking."
    Fransson S., Ruusala A., Aspenstroem P.
    Biochem. Biophys. Res. Commun. 344:500-510(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRAK1 AND TRAK2, MUTAGENESIS OF ALA-13 AND THR-18.
  11. "HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport."
    Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.
    J. Cell Biol. 185:1065-1081(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMIRO2_HUMAN
AccessioniPrimary (citable) accession number: Q8IXI1
Secondary accession number(s): A2IDC2
, Q8NF53, Q96C13, Q96S17, Q9BT60, Q9H7M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: September 3, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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