Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8IXI2

- MIRO1_HUMAN

UniProt

Q8IXI2 - MIRO1_HUMAN

Protein

Mitochondrial Rho GTPase 1

Gene

RHOT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 188GTP 1
    Nucleotide bindingi57 – 615GTP 1Sequence Analysis
    Nucleotide bindingi118 – 1214GTP 1Sequence Analysis
    Calcium bindingi197 – 208121CuratedAdd
    BLAST
    Calcium bindingi317 – 328122CuratedAdd
    BLAST
    Nucleotide bindingi425 – 4328GTP 2
    Nucleotide bindingi463 – 4675GTP 2Sequence Analysis
    Nucleotide bindingi527 – 5304GTP 2Sequence Analysis

    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

    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 1 (EC:3.6.5.-)
    Short name:
    MIRO-1
    Short name:
    hMiro-1
    Alternative name(s):
    Rac-GTP-binding protein-like protein
    Ras homolog gene family member T1
    Gene namesi
    Name:RHOT1
    Synonyms:ARHT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:21168. RHOT1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. integral component of mitochondrial outer membrane Source: UniProtKB
    3. membrane Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131P → V: Causes constitutive activation inducing an aggregation of the mitochondrial network. 3 Publications
    Mutagenesisi18 – 181T → N: Causes constitutive inactivation. 2 Publications
    Mutagenesisi208 – 2081E → K: Abolishes the formation of thread-like mitochondria. 1 Publication
    Mutagenesisi328 – 3281E → K: Abolishes the formation of thread-like mitochondria. 1 Publication
    Mutagenesisi427 – 4271K → V: No effect. 1 Publication
    Mutagenesisi432 – 4321S → N: No effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA134906318.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 618618Mitochondrial Rho GTPase 1PRO_0000239313Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ8IXI2.
    PaxDbiQ8IXI2.
    PRIDEiQ8IXI2.

    PTM databases

    PhosphoSiteiQ8IXI2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Expressed at high level in heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ8IXI2.
    BgeeiQ8IXI2.
    CleanExiHS_RHOT1.
    GenevestigatoriQ8IXI2.

    Organism-specific databases

    HPAiHPA010687.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KIF5CO602822EBI-1396430,EBI-717170
    Kif5cP565365EBI-1396430,EBI-994504From a different organism.
    PARK2O602603EBI-1396430,EBI-716346
    PINK1Q9BXM73EBI-1396430,EBI-2846068
    TRAK1Q9UPV93EBI-1396430,EBI-1105048

    Protein-protein interaction databases

    BioGridi120576. 8 interactions.
    DIPiDIP-39114N.
    IntActiQ8IXI2. 9 interactions.
    MINTiMINT-3972897.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IXI2.
    SMRiQ8IXI2. Positions 6-159, 180-581.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 592592Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini616 – 6183CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei593 – 61523Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 177177Miro 1Add
    BLAST
    Domaini184 – 21936EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini304 – 33936EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini412 – 561150Miro 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the mitochondrial Rho GTPase family.Curated
    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 2 Miro domains.Curated

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG079778.
    KOiK07870.
    OMAiHEISQAN.
    OrthoDBiEOG7PK8Z0.
    PhylomeDBiQ8IXI2.
    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.
    IPR021181. Rho_GTPase_Mt.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    [Graphical view]
    PfamiPF13405. EF-hand_6. 1 hit.
    PF08355. 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.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    PS51423. MIRO. 2 hits.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IXI2-1) [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

    MKKDVRILLV GEPRVGKTSL IMSLVSEEFP EEVPPRAEEI TIPADVTPER    50
    VPTHIVDYSE AEQSDEQLHQ EISQANVICI VYAVNNKHSI DKVTSRWIPL 100
    INERTDKDSR LPLILVGNKS DLVEYSSMET ILPIMNQYTE IETCVECSAK 150
    NLKNISELFY YAQKAVLHPT GPLYCPEEKE MKPACIKALT RIFKISDQDN 200
    DGTLNDAELN FFQRICFNTP LAPQALEDVK NVVRKHISDG VADSGLTLKG 250
    FLFLHTLFIQ RGRHETTWTV LRRFGYDDDL DLTPEYLFPL LKIPPDCTTE 300
    LNHHAYLFLQ STFDKHDLDR DCALSPDELK DLFKVFPYIP WGPDVNNTVC 350
    TNERGWITYQ GFLSQWTLTT YLDVQRCLEY LGYLGYSILT EQESQASAVT 400
    VTRDKKIDLQ KKQTQRNVFR CNVIGVKNCG KSGVLQALLG RNLMRQKKIR 450
    EDHKSYYAIN TVYVYGQEKY LLLHDISESE FLTEAEIICD VVCLVYDVSN 500
    PKSFEYCARI FKQHFMDSRI PCLIVAAKSD LHEVKQEYSI SPTDFCRKHK 550
    MPPPQAFTCN TADAPSKDIF VKLTTMAMYP HVTQADLKSS TFWLRASFGA 600
    TVFAVLGFAM YKALLKQR 618
    Length:618
    Mass (Da):70,784
    Last modified:June 13, 2006 - v2
    Checksum:iFE47AC3A4AF6F6C2
    GO
    Isoform 2 (identifier: Q8IXI2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-580: P → PEDHYRDRLSRDMGHTDRIENLRKIWVFLKTAL

    Show »
    Length:650
    Mass (Da):74,752
    Checksum:i9E2A92E79F9160E1
    GO
    Isoform 3 (identifier: Q8IXI2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-580: P → PEDHYRDRLSRDMGHTDRIENLRKIWVFLKTAFHARLRCMCTCNRCTFCICQNFLNSDLLQSVKNKIFTAVLNR

    Show »
    Length:691
    Mass (Da):79,547
    Checksum:i478FF7C2F8DD1986
    GO
    Isoform 4 (identifier: Q8IXI2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         581-618: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:580
    Mass (Da):66,541
    Checksum:iEC42DCCD95811BC3
    GO
    Isoform 5 (identifier: Q8IXI2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         582-618: VTQADLKSST...AMYKALLKQR → ARLRCMCTCN...TAVLNRIISA

    Note: No experimental confirmation available.

    Show »
    Length:625
    Mass (Da):71,687
    Checksum:i3968C61EE9945024
    GO
    Isoform 6 (identifier: Q8IXI2-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         224-247: QALEDVKNVVRKHISDGVADSGLT → RFGFEQVLVLLFLQFWALLCTKHY
         248-618: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:247
    Mass (Da):28,265
    Checksum:i3802160B22935376
    GO
    Isoform 7 (identifier: Q8IXI2-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-580: P → PHARLRCMCTCNRCTFCICQNFLNSDLLQSVKNKIFTAVLNR

    Note: No experimental confirmation available.

    Show »
    Length:659
    Mass (Da):75,546
    Checksum:i82C8A91A753D656F
    GO

    Sequence cautioni

    The sequence AAH41114.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH68463.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91969.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14185.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751A → V in AAM15734. 1 PublicationCurated
    Sequence conflicti246 – 2461L → F in AAH60781. (PubMed:15489334)Curated
    Sequence conflicti246 – 2461L → F in BAA91969. (PubMed:14702039)Curated
    Sequence conflicti331 – 3311D → G in AAH60781. (PubMed:15489334)Curated
    Sequence conflicti587 – 5871L → P in CAD56956. (PubMed:12482879)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei224 – 24724QALED…DSGLT → RFGFEQVLVLLFLQFWALLC TKHY in isoform 6. 1 PublicationVSP_019153Add
    BLAST
    Alternative sequencei248 – 618371Missing in isoform 6. 1 PublicationVSP_019154Add
    BLAST
    Alternative sequencei580 – 5801P → PEDHYRDRLSRDMGHTDRIE NLRKIWVFLKTAL in isoform 2. 2 PublicationsVSP_019155
    Alternative sequencei580 – 5801P → PEDHYRDRLSRDMGHTDRIE NLRKIWVFLKTAFHARLRCM CTCNRCTFCICQNFLNSDLL QSVKNKIFTAVLNR in isoform 3. 3 PublicationsVSP_019156
    Alternative sequencei580 – 5801P → PHARLRCMCTCNRCTFCICQ NFLNSDLLQSVKNKIFTAVL NR in isoform 7. CuratedVSP_047651
    Alternative sequencei581 – 61838Missing in isoform 4. 1 PublicationVSP_019157Add
    BLAST
    Alternative sequencei582 – 61837VTQAD…LLKQR → ARLRCMCTCNRCTFCICQNF LNSDLLQSVKNKIFTAVLNR IISA in isoform 5. 1 PublicationVSP_019158Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ496730 mRNA. Translation: CAD43139.1.
    AJ517412 mRNA. Translation: CAD56956.1.
    AY094972 mRNA. Translation: AAM15734.1.
    AL136929 mRNA. Translation: CAB66863.1.
    AK001902 mRNA. Translation: BAA91969.1. Different initiation.
    AK022695 mRNA. Translation: BAB14185.1. Different initiation.
    AK294407 mRNA. Translation: BAG57659.1.
    AC116407 Genomic DNA. No translation available.
    AC026620 Genomic DNA. No translation available.
    BC015698 mRNA. Translation: AAH15698.1.
    BC041114 mRNA. Translation: AAH41114.1. Different initiation.
    BC051818 mRNA. Translation: AAH51818.1.
    BC060781 mRNA. Translation: AAH60781.2.
    BC068463 mRNA. Translation: AAH68463.1. Different initiation.
    BC125104 mRNA. Translation: AAI25105.1.
    BC125105 mRNA. Translation: AAI25106.1.
    CCDSiCCDS32610.1. [Q8IXI2-3]
    CCDS32611.1. [Q8IXI2-7]
    CCDS32612.1. [Q8IXI2-1]
    RefSeqiNP_001028738.1. NM_001033566.2. [Q8IXI2-7]
    NP_001028739.2. NM_001033567.2.
    NP_001028740.1. NM_001033568.2. [Q8IXI2-3]
    NP_001275683.1. NM_001288754.1. [Q8IXI2-2]
    NP_001275684.1. NM_001288755.1.
    NP_001275687.1. NM_001288758.1.
    NP_060777.3. NM_018307.4. [Q8IXI2-1]
    UniGeneiHs.655325.

    Genome annotation databases

    GeneIDi55288.
    KEGGihsa:55288.
    UCSCiuc002hgv.3. human. [Q8IXI2-1]
    uc002hgw.3. human. [Q8IXI2-3]
    uc010wby.2. human. [Q8IXI2-2]

    Polymorphism databases

    DMDMi108860796.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ496730 mRNA. Translation: CAD43139.1 .
    AJ517412 mRNA. Translation: CAD56956.1 .
    AY094972 mRNA. Translation: AAM15734.1 .
    AL136929 mRNA. Translation: CAB66863.1 .
    AK001902 mRNA. Translation: BAA91969.1 . Different initiation.
    AK022695 mRNA. Translation: BAB14185.1 . Different initiation.
    AK294407 mRNA. Translation: BAG57659.1 .
    AC116407 Genomic DNA. No translation available.
    AC026620 Genomic DNA. No translation available.
    BC015698 mRNA. Translation: AAH15698.1 .
    BC041114 mRNA. Translation: AAH41114.1 . Different initiation.
    BC051818 mRNA. Translation: AAH51818.1 .
    BC060781 mRNA. Translation: AAH60781.2 .
    BC068463 mRNA. Translation: AAH68463.1 . Different initiation.
    BC125104 mRNA. Translation: AAI25105.1 .
    BC125105 mRNA. Translation: AAI25106.1 .
    CCDSi CCDS32610.1. [Q8IXI2-3 ]
    CCDS32611.1. [Q8IXI2-7 ]
    CCDS32612.1. [Q8IXI2-1 ]
    RefSeqi NP_001028738.1. NM_001033566.2. [Q8IXI2-7 ]
    NP_001028739.2. NM_001033567.2.
    NP_001028740.1. NM_001033568.2. [Q8IXI2-3 ]
    NP_001275683.1. NM_001288754.1. [Q8IXI2-2 ]
    NP_001275684.1. NM_001288755.1.
    NP_001275687.1. NM_001288758.1.
    NP_060777.3. NM_018307.4. [Q8IXI2-1 ]
    UniGenei Hs.655325.

    3D structure databases

    ProteinModelPortali Q8IXI2.
    SMRi Q8IXI2. Positions 6-159, 180-581.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120576. 8 interactions.
    DIPi DIP-39114N.
    IntActi Q8IXI2. 9 interactions.
    MINTi MINT-3972897.

    PTM databases

    PhosphoSitei Q8IXI2.

    Polymorphism databases

    DMDMi 108860796.

    Proteomic databases

    MaxQBi Q8IXI2.
    PaxDbi Q8IXI2.
    PRIDEi Q8IXI2.

    Protocols and materials databases

    DNASUi 55288.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 55288.
    KEGGi hsa:55288.
    UCSCi uc002hgv.3. human. [Q8IXI2-1 ]
    uc002hgw.3. human. [Q8IXI2-3 ]
    uc010wby.2. human. [Q8IXI2-2 ]

    Organism-specific databases

    CTDi 55288.
    GeneCardsi GC17P030470.
    HGNCi HGNC:21168. RHOT1.
    HPAi HPA010687.
    MIMi 613888. gene.
    neXtProti NX_Q8IXI2.
    PharmGKBi PA134906318.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG079778.
    KOi K07870.
    OMAi HEISQAN.
    OrthoDBi EOG7PK8Z0.
    PhylomeDBi Q8IXI2.
    TreeFami TF300814.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi RHOT1. human.
    GeneWikii RHOT1.
    GenomeRNAii 55288.
    NextBioi 59462.
    PROi Q8IXI2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IXI2.
    Bgeei Q8IXI2.
    CleanExi HS_RHOT1.
    Genevestigatori Q8IXI2.

    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.
    IPR021181. Rho_GTPase_Mt.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    [Graphical view ]
    Pfami PF13405. EF-hand_6. 1 hit.
    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.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    PS51423. MIRO. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete physical map and gene content of the human NF1 tumor suppressor region in human and mouse."
      Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K., Kehrer-Sawatzki H.
      Genes Chromosomes Cancer 37:111-120(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. "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), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-13 AND THR-18.
    3. "Cloning a novel Rac-GTP binding protein-like gene from human fetal brain."
      Zeng L., Xie Y., Mao Y.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Fetal brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Uterus.
    5. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-618 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-618 (ISOFORM 3).
      Tissue: Amygdala, Placenta and Teratocarcinoma.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-618 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-550 (ISOFORM 6).
      Tissue: Brain, Lung, Testis and Uterus.
    8. "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 PRO-13.
    9. "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 PRO-13; THR-18; GLU-208; GLU-328; LYS-427 AND SER-432.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy."
      Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q., Foreman O., Kirkpatrick D.S., Sheng M.
      Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION.

    Entry informationi

    Entry nameiMIRO1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IXI2
    Secondary accession number(s): A4FVB6
    , A6NFV0, B4DG48, J9JIH9, Q6NUR3, Q6P9F8, Q6PJG1, Q6YMW8, Q86UB0, Q8IW28, Q8IXJ7, Q9H067, Q9H9N8, Q9NUZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 114 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3