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Q9H0F7

- ARL6_HUMAN

UniProt

Q9H0F7 - ARL6_HUMAN

Protein

ADP-ribosylation factor-like protein 6

Gene

ARL6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia. Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade. Isoform 2 may be required for proper retinal function and organization.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi31 – 311Magnesium1 Publication
    Metal bindingi50 – 501Magnesium1 Publication
    Binding sitei50 – 501GTP1 Publication
    Binding sitei72 – 721GTP; via amide nitrogen1 Publication
    Binding sitei164 – 1641GTP; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 318GTP1 Publication
    Nucleotide bindingi69 – 735GTPBy similarity
    Nucleotide bindingi130 – 1334GTP1 Publication

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. phospholipid binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cilium assembly Source: UniProtKB
    2. determination of left/right symmetry Source: BHF-UCL
    3. fat cell differentiation Source: Ensembl
    4. melanosome transport Source: BHF-UCL
    5. protein polymerization Source: UniProtKB
    6. protein targeting to membrane Source: UniProtKB
    7. small GTPase mediated signal transduction Source: InterPro
    8. visual perception Source: UniProtKB-KW
    9. Wnt signaling pathway Source: UniProtKB

    Keywords - Biological processi

    Cilium biogenesis/degradation, Protein transport, Sensory transduction, Transport, Vision

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-ribosylation factor-like protein 6
    Alternative name(s):
    Bardet-Biedl syndrome 3 protein
    Gene namesi
    Name:ARL6
    Synonyms:BBS3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:13210. ARL6.

    Subcellular locationi

    Cell projectioncilium membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeletoncilium axoneme. Cytoplasmcytoskeletoncilium basal body
    Note: Appears in a pattern of punctae flanking the microtubule axoneme that likely correspond to small membrane-associated patches. Localizes to the so-called ciliary gate where vesicles carrying ciliary cargo fuse with the membrane.

    GO - Cellular componenti

    1. axonemal microtubule Source: UniProtKB
    2. axoneme Source: UniProtKB
    3. ciliary membrane Source: UniProtKB-SubCell
    4. cytoplasm Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. membrane Source: UniProtKB
    7. membrane coat Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Bardet-Biedl syndrome 3 (BBS3) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311T → M in BBS3; abrogates the GTP-binding ability without affecting GDP-binding/dissociating properties; increased proteasomal degradation. 1 Publication
    VAR_027643
    Natural varianti31 – 311T → R in BBS3; locked in a GDP-bound state that differs from its wild-type counterpart which is mainly GTP-bound; increased proteasomal degradation. 1 Publication
    VAR_027644
    Natural varianti169 – 1691G → A in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 1 Publication
    VAR_027645
    Natural varianti170 – 1701L → W in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 1 Publication
    VAR_027646
    Retinitis pigmentosa 55 (RP55) [MIM:613575]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891A → V in RP55. 1 Publication
    VAR_064184

    Keywords - Diseasei

    Bardet-Biedl syndrome, Ciliopathy, Disease mutation, Mental retardation, Obesity, Retinitis pigmentosa

    Organism-specific databases

    MIMi209900. phenotype.
    613575. phenotype.
    Orphaneti110. Bardet-Biedl syndrome.
    791. Retinitis pigmentosa.
    PharmGKBiPA134931939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedSequence Analysis
    Chaini2 – 186185ADP-ribosylation factor-like protein 6PRO_0000207472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineSequence Analysis

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    MaxQBiQ9H0F7.
    PaxDbiQ9H0F7.
    PRIDEiQ9H0F7.

    PTM databases

    PhosphoSiteiQ9H0F7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H0F7.
    BgeeiQ9H0F7.
    CleanExiHS_ARL6.
    GenevestigatoriQ9H0F7.

    Organism-specific databases

    HPAiHPA019361.

    Interactioni

    Subunit structurei

    Interacts with SEC61B, ARL6IP1, ARL6IP2, ARL6IP3, ARL6IP4 ARL6IP5 and ARL6IP6. Interacts (GTP-bound form) with the BBSome a complex that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BBS1Q8NFJ94EBI-2891949,EBI-1805484

    Protein-protein interaction databases

    BioGridi123889. 7 interactions.
    IntActiQ9H0F7. 15 interactions.
    STRINGi9606.ENSP00000337722.

    Structurei

    Secondary structure

    1
    186
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 247
    Helixi30 – 367
    Helixi40 – 423
    Beta strandi51 – 599
    Beta strandi64 – 707
    Turni74 – 763
    Helixi77 – 8610
    Beta strandi88 – 958
    Helixi99 – 11416
    Turni116 – 1205
    Beta strandi125 – 1306
    Helixi140 – 1478
    Helixi149 – 1513
    Beta strandi157 – 1615
    Turni164 – 1674
    Helixi170 – 18011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H57X-ray2.00A/B/C16-186[»]
    ProteinModelPortaliQ9H0F7.
    SMRiQ9H0F7. Positions 16-182.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H0F7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Arf family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000163691.
    HOVERGENiHBG002073.
    InParanoidiQ9H0F7.
    KOiK07951.
    OMAiDIKHRRL.
    OrthoDBiEOG78WKTS.
    PhylomeDBiQ9H0F7.
    TreeFamiTF105466.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view]
    PfamiPF00025. Arf. 1 hit.
    [Graphical view]
    PRINTSiPR00328. SAR1GTPBP.
    SMARTiSM00177. ARF. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51417. ARF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H0F7-1) [UniParc]FASTAAdd to Basket

    Also known as: BBS3

    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

    MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT    50
    IGFSIEKFKS SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL 100
    RMVVAKEELD TLLNHPDIKH RRIPILFFAN KMDLRDAVTS VKVSQLLCLE 150
    NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT 186
    Length:186
    Mass (Da):21,097
    Last modified:March 1, 2001 - v1
    Checksum:i42E37FC7886BF1F0
    GO
    Isoform 2 (identifier: Q9H0F7-2) [UniParc]FASTAAdd to Basket

    Also known as: BBS3L

    The sequence of this isoform differs from the canonical sequence as follows:
         179-186: DQIQTVKT → EKTIQSDPDCEDMKR

    Note: Gene prediction based on EST data.

    Show »
    Length:193
    Mass (Da):21,960
    Checksum:i4C6C43101CE360C1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311T → M in BBS3; abrogates the GTP-binding ability without affecting GDP-binding/dissociating properties; increased proteasomal degradation. 1 Publication
    VAR_027643
    Natural varianti31 – 311T → R in BBS3; locked in a GDP-bound state that differs from its wild-type counterpart which is mainly GTP-bound; increased proteasomal degradation. 1 Publication
    VAR_027644
    Natural varianti89 – 891A → V in RP55. 1 Publication
    VAR_064184
    Natural varianti169 – 1691G → A in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 1 Publication
    VAR_027645
    Natural varianti170 – 1701L → W in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 1 Publication
    VAR_027646

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei179 – 1868DQIQTVKT → EKTIQSDPDCEDMKR in isoform 2. CuratedVSP_040511

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136815 mRNA. Translation: CAB66749.1.
    AK292958 mRNA. Translation: BAF85647.1.
    AC110491 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79880.1.
    CH471052 Genomic DNA. Translation: EAW79881.1.
    CH471052 Genomic DNA. Translation: EAW79882.1.
    CH471052 Genomic DNA. Translation: EAW79883.1.
    CH471052 Genomic DNA. Translation: EAW79884.1.
    BC024239 mRNA. Translation: AAH24239.1.
    CCDSiCCDS2928.1. [Q9H0F7-1]
    RefSeqiNP_001265222.1. NM_001278293.1. [Q9H0F7-1]
    NP_115522.1. NM_032146.4. [Q9H0F7-1]
    NP_816931.1. NM_177976.2. [Q9H0F7-1]
    XP_006713842.1. XM_006713779.1. [Q9H0F7-2]
    XP_006713843.1. XM_006713780.1. [Q9H0F7-2]
    XP_006713844.1. XM_006713781.1. [Q9H0F7-2]
    XP_006713845.1. XM_006713782.1. [Q9H0F7-2]
    UniGeneiHs.373801.

    Genome annotation databases

    EnsembliENST00000335979; ENSP00000337722; ENSG00000113966. [Q9H0F7-1]
    ENST00000394206; ENSP00000377756; ENSG00000113966. [Q9H0F7-1]
    ENST00000463745; ENSP00000419619; ENSG00000113966. [Q9H0F7-1]
    ENST00000493990; ENSP00000418057; ENSG00000113966. [Q9H0F7-1]
    GeneIDi84100.
    KEGGihsa:84100.
    UCSCiuc003dru.3. human. [Q9H0F7-1]

    Polymorphism databases

    DMDMi14547903.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136815 mRNA. Translation: CAB66749.1 .
    AK292958 mRNA. Translation: BAF85647.1 .
    AC110491 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79880.1 .
    CH471052 Genomic DNA. Translation: EAW79881.1 .
    CH471052 Genomic DNA. Translation: EAW79882.1 .
    CH471052 Genomic DNA. Translation: EAW79883.1 .
    CH471052 Genomic DNA. Translation: EAW79884.1 .
    BC024239 mRNA. Translation: AAH24239.1 .
    CCDSi CCDS2928.1. [Q9H0F7-1 ]
    RefSeqi NP_001265222.1. NM_001278293.1. [Q9H0F7-1 ]
    NP_115522.1. NM_032146.4. [Q9H0F7-1 ]
    NP_816931.1. NM_177976.2. [Q9H0F7-1 ]
    XP_006713842.1. XM_006713779.1. [Q9H0F7-2 ]
    XP_006713843.1. XM_006713780.1. [Q9H0F7-2 ]
    XP_006713844.1. XM_006713781.1. [Q9H0F7-2 ]
    XP_006713845.1. XM_006713782.1. [Q9H0F7-2 ]
    UniGenei Hs.373801.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H57 X-ray 2.00 A/B/C 16-186 [» ]
    ProteinModelPortali Q9H0F7.
    SMRi Q9H0F7. Positions 16-182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123889. 7 interactions.
    IntActi Q9H0F7. 15 interactions.
    STRINGi 9606.ENSP00000337722.

    PTM databases

    PhosphoSitei Q9H0F7.

    Polymorphism databases

    DMDMi 14547903.

    Proteomic databases

    MaxQBi Q9H0F7.
    PaxDbi Q9H0F7.
    PRIDEi Q9H0F7.

    Protocols and materials databases

    DNASUi 84100.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335979 ; ENSP00000337722 ; ENSG00000113966 . [Q9H0F7-1 ]
    ENST00000394206 ; ENSP00000377756 ; ENSG00000113966 . [Q9H0F7-1 ]
    ENST00000463745 ; ENSP00000419619 ; ENSG00000113966 . [Q9H0F7-1 ]
    ENST00000493990 ; ENSP00000418057 ; ENSG00000113966 . [Q9H0F7-1 ]
    GeneIDi 84100.
    KEGGi hsa:84100.
    UCSCi uc003dru.3. human. [Q9H0F7-1 ]

    Organism-specific databases

    CTDi 84100.
    GeneCardsi GC03P097483.
    GeneReviewsi ARL6.
    HGNCi HGNC:13210. ARL6.
    HPAi HPA019361.
    MIMi 209900. phenotype.
    608845. gene.
    613575. phenotype.
    neXtProti NX_Q9H0F7.
    Orphaneti 110. Bardet-Biedl syndrome.
    791. Retinitis pigmentosa.
    PharmGKBi PA134931939.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000163691.
    HOVERGENi HBG002073.
    InParanoidi Q9H0F7.
    KOi K07951.
    OMAi DIKHRRL.
    OrthoDBi EOG78WKTS.
    PhylomeDBi Q9H0F7.
    TreeFami TF105466.

    Miscellaneous databases

    ChiTaRSi ARL6. human.
    EvolutionaryTracei Q9H0F7.
    GeneWikii ARL6.
    GenomeRNAii 84100.
    NextBioi 73343.
    PROi Q9H0F7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0F7.
    Bgeei Q9H0F7.
    CleanExi HS_ARL6.
    Genevestigatori Q9H0F7.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR024156. Small_GTPase_ARF.
    IPR006689. Small_GTPase_ARF/SAR.
    [Graphical view ]
    Pfami PF00025. Arf. 1 hit.
    [Graphical view ]
    PRINTSi PR00328. SAR1GTPBP.
    SMARTi SM00177. ARF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51417. ARF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    2. "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].
      Tissue: Trachea.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Testis.
    6. "Comparative genomic analysis identifies an ADP-ribosylation factor-like gene as the cause of Bardet-Biedl Syndrome (BBS3)."
      Chiang A.P., Nishimura D., Searby C., Elbedour K., Carmi R., Ferguson A.L., Secrist J., Braun T., Casavant T., Stone E.M., Sheffield V.C.
      Am. J. Hum. Genet. 75:475-484(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN BBS3.
    7. "The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia."
      Jin H., White S.R., Shida T., Schulz S., Aguiar M., Gygi S.P., Bazan J.F., Nachury M.V.
      Cell 141:1208-1219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE BBSOME.
    8. "Identification and functional analysis of the vision-specific BBS3 (ARL6) long isoform."
      Pretorius P.R., Baye L.M., Nishimura D.Y., Searby C.C., Bugge K., Yang B., Mullins R.F., Stone E.M., Sheffield V.C., Slusarski D.C.
      PLoS Genet. 6:E1000884-E1000884(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened."
      Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., Sheffield V.C.
      PLoS Genet. 7:E1002358-E1002358(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Bardet-Biedl syndrome-associated small GTPase ARL6 (BBS3) functions at or near the ciliary gate and modulates Wnt signaling."
      Wiens C.J., Tong Y., Esmail M.A., Oh E., Gerdes J.M., Wang J., Tempel W., Rattner J.B., Katsanis N., Park H.W., Leroux M.R.
      J. Biol. Chem. 285:16218-16230(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-186 IN COMPLEX WITH GTP AND MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS MET-31; ARG-31; ALA-169 AND TRP-170.
    12. Cited for: VARIANTS BBS3 ARG-31; MET-31; ALA-169 AND TRP-170.
    13. "Biochemical characterization of missense mutations in the Arf/Arl-family small GTPase Arl6 causing Bardet-Biedl syndrome."
      Kobayashi T., Hori Y., Ueda N., Kajiho H., Muraoka S., Shima F., Kataoka T., Kontani K., Katada T.
      Biochem. Biophys. Res. Commun. 381:439-442(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS MET-31; ARG-31; ALA-169 AND TRP-170.
    14. "Molecular characterization of retinitis pigmentosa in Saudi Arabia."
      Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H., Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.
      Mol. Vis. 15:2464-2469(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT RP55 VAL-89.

    Entry informationi

    Entry nameiARL6_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0F7
    Secondary accession number(s): A8KA93, D3DN31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3