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Q9H0F7

- ARL6_HUMAN

UniProt

Q9H0F7 - ARL6_HUMAN

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Protein
ADP-ribosylation factor-like protein 6
Gene
ARL6, BBS3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 311Magnesium
Metal bindingi50 – 501Magnesium
Binding sitei50 – 501GTP
Binding sitei72 – 721GTP; via amide nitrogen
Binding sitei164 – 1641GTP; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 318GTP
Nucleotide bindingi69 – 735GTP By similarity
Nucleotide bindingi130 – 1334GTP

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

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.2 Publications

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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. 3 Publications
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. 3 Publications
VAR_027644
Natural varianti169 – 1691G → A in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 3 Publications
VAR_027645
Natural varianti170 – 1701L → W in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 3 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 11Removed Reviewed prediction
Chaini2 – 186185ADP-ribosylation factor-like protein 6
PRO_0000207472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine Reviewed prediction

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 BBIP10.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9H0F7.

Family & Domainsi

Sequence similaritiesi

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. 3 Publications
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. 3 Publications
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. 3 Publications
VAR_027645
Natural varianti170 – 1701L → W in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. 3 Publications
VAR_027646

Alternative sequence

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 126 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

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