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Q9H0F7 (ARL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ADP-ribosylation factor-like protein 6
Alternative name(s):
Bardet-Biedl syndrome 3 protein
Gene names
Name:ARL6
Synonyms:BBS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length186 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.10 Ref.11

Subunit structure

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. Ref.7

Subcellular location

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. Ref.7 Ref.11

Involvement in disease

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. Ref.6 Ref.12

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. Ref.14

Sequence similarities

Belongs to the small GTPase superfamily. Arf family.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Protein transport
Sensory transduction
Transport
Vision
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseBardet-Biedl syndrome
Ciliopathy
Disease mutation
Mental retardation
Obesity
Retinitis pigmentosa
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   PTMLipoprotein
Myristate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cilium assembly

Inferred from mutant phenotype Ref.11. Source: UniProtKB

determination of left/right symmetry

Inferred from sequence or structural similarity. Source: BHF-UCL

fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

melanosome transport

Inferred from sequence or structural similarity. Source: BHF-UCL

protein polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaxonemal microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

axoneme

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane coat

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipid binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7PubMed 22139371. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BBS1Q8NFJ94EBI-2891949,EBI-1805484

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H0F7-1)

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.
Isoform 2 (identifier: Q9H0F7-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 186185ADP-ribosylation factor-like protein 6
PRO_0000207472

Regions

Nucleotide binding24 – 318GTP
Nucleotide binding69 – 735GTP By similarity
Nucleotide binding130 – 1334GTP

Sites

Metal binding311Magnesium
Metal binding501Magnesium
Binding site501GTP
Binding site721GTP; via amide nitrogen
Binding site1641GTP; via amide nitrogen

Amino acid modifications

Lipidation21N-myristoyl glycine Potential

Natural variations

Alternative sequence179 – 1868DQIQTVKT → EKTIQSDPDCEDMKR in isoform 2.
VSP_040511
Natural variant311T → M in BBS3; abrogates the GTP-binding ability without affecting GDP-binding/dissociating properties; increased proteasomal degradation. Ref.11 Ref.12 Ref.13
VAR_027643
Natural variant311T → R in BBS3; locked in a GDP-bound state that differs from its wild-type counterpart which is mainly GTP-bound; increased proteasomal degradation. Ref.11 Ref.12 Ref.13
VAR_027644
Natural variant891A → V in RP55. Ref.14
VAR_064184
Natural variant1691G → A in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. Ref.11 Ref.12 Ref.13
VAR_027645
Natural variant1701L → W in BBS3; abrogates the GTP-binding ability; increased proteasomal degradation. Ref.11 Ref.12 Ref.13
VAR_027646

Secondary structure

................................ 186
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BBS3) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 42E37FC7886BF1F0

FASTA18621,097
        10         20         30         40         50         60 
MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS 

        70         80         90        100        110        120 
SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH 

       130        140        150        160        170        180 
RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ 


IQTVKT 

« Hide

Isoform 2 (BBS3L) [UniParc].

Checksum: 4C6C43101CE360C1
Show »

FASTA19321,960

References

« Hide 'large scale' references
[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in a member of the Ras superfamily of small GTP-binding proteins causes Bardet-Biedl syndrome."
Fan Y., Esmail M.A., Ansley S.J., Blacque O.E., Boroevich K., Ross A.J., Moore S.J., Badano J.L., May-Simera H., Compton D.S., Green J.S., Lewis R.A., van Haelst M.M., Parfrey P.S., Baillie D.L., Beales P.L., Katsanis N., Davidson W.S., Leroux M.R.
Nat. Genet. 36:989-993(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2928.1. [Q9H0F7-1]
RefSeqNP_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]
UniGeneHs.373801.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H57X-ray2.00A/B/C16-186[»]
ProteinModelPortalQ9H0F7.
SMRQ9H0F7. Positions 16-182.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123889. 7 interactions.
IntActQ9H0F7. 15 interactions.
STRING9606.ENSP00000337722.

PTM databases

PhosphoSiteQ9H0F7.

Polymorphism databases

DMDM14547903.

Proteomic databases

MaxQBQ9H0F7.
PaxDbQ9H0F7.
PRIDEQ9H0F7.

Protocols and materials databases

DNASU84100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335979; ENSP00000337722; ENSG00000113966. [Q9H0F7-1]
ENST00000394206; ENSP00000377756; ENSG00000113966. [Q9H0F7-1]
ENST00000463745; ENSP00000419619; ENSG00000113966. [Q9H0F7-1]
ENST00000493990; ENSP00000418057; ENSG00000113966. [Q9H0F7-1]
GeneID84100.
KEGGhsa:84100.
UCSCuc003dru.3. human. [Q9H0F7-1]

Organism-specific databases

CTD84100.
GeneCardsGC03P097483.
GeneReviewsARL6.
HGNCHGNC:13210. ARL6.
HPAHPA019361.
MIM209900. phenotype.
608845. gene.
613575. phenotype.
neXtProtNX_Q9H0F7.
Orphanet110. Bardet-Biedl syndrome.
791. Retinitis pigmentosa.
PharmGKBPA134931939.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000163691.
HOVERGENHBG002073.
InParanoidQ9H0F7.
KOK07951.
OMADIKHRRL.
OrthoDBEOG78WKTS.
PhylomeDBQ9H0F7.
TreeFamTF105466.

Gene expression databases

ArrayExpressQ9H0F7.
BgeeQ9H0F7.
CleanExHS_ARL6.
GenevestigatorQ9H0F7.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR024156. Small_GTPase_ARF.
IPR006689. Small_GTPase_ARF/SAR.
[Graphical view]
PfamPF00025. Arf. 1 hit.
[Graphical view]
PRINTSPR00328. SAR1GTPBP.
SMARTSM00177. ARF. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51417. ARF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARL6. human.
EvolutionaryTraceQ9H0F7.
GeneWikiARL6.
GenomeRNAi84100.
NextBio73343.
PROQ9H0F7.
SOURCESearch...

Entry information

Entry nameARL6_HUMAN
AccessionPrimary (citable) accession number: Q9H0F7
Secondary accession number(s): A8KA93, D3DN31
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM