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Q8N157 (AHI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Jouberin
Alternative name(s):
Abelson helper integration site 1 protein homolog
Short name=AHI-1
Gene names
Name:AHI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes By similarity.

Subunit structure

Part of the tectonic-like complex (also named B9 complex). Interacts with MKS1 By similarity. Interacts with NPHP1. Interacts (via SH3 domain) with the dynamin GTPase DNM2. Ref.11 Ref.13

Subcellular location

Cytoplasmcytoskeletoncilium basal body By similarity. Cell junctionadherens junction Ref.11.

Tissue specificity

Highly expressed in the most primitive normal hematopoietic cells. Expressed in brain, particularly in neurons that give rise to the crossing axons of the corticospinal tract and superior cerebellar peduncles. Expressed in kidney (renal collecting duct cells) (at protein level). Ref.8 Ref.9 Ref.11

Induction

Down-regulated during early differentiation of normal hematopoietic cells. Up-regulated in leukemic cells at all stages of differentiation from patients with chronic myeloid leukemia. Ref.8

Involvement in disease

Joubert syndrome 3 (JBTS3) [MIM:608629]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease. Joubert syndrome type 3 shows minimal extra central nervous system involvement and appears not to be associated with renal dysfunction.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.14 Ref.15 Ref.16

Sequence similarities

Contains 1 SH3 domain.

Contains 7 WD repeats.

Sequence caution

The sequence AAH29417.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH65712.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence CAI20201.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI20387.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI22523.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCell junction
Cell projection
Cilium
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DiseaseCiliopathy
Disease mutation
Joubert syndrome
   DomainCoiled coil
Repeat
SH3 domain
WD repeat
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processKupffer's vesicle development

Inferred from sequence or structural similarity. Source: UniProtKB

cellular protein localization

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

cilium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cloaca development

Inferred from sequence or structural similarity. Source: UniProtKB

heart looping

Inferred from sequence or structural similarity. Source: UniProtKB

hindbrain development

Inferred from sequence or structural similarity. Source: UniProtKB

left/right axis specification

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of a polarized epithelium

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

otic vesicle development

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor cell outer segment organization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of polarized epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of receptor internalization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

pronephric duct morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

pronephric nephron tubule morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to organelle

Inferred from electronic annotation. Source: Ensembl

regulation of behavior

Inferred from sequence or structural similarity. Source: UniProtKB

retina layer formation

Inferred from sequence or structural similarity. Source: UniProtKB

specification of axis polarity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle targeting

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentTCTN-B9D complex

Inferred from sequence or structural similarity. Source: UniProtKB

adherens junction

Inferred from direct assay Ref.11. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.11. Source: UniProtKB

centriole

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Inferred from direct assay Ref.11. Source: UniProtKB

ciliary basal body

Inferred from direct assay Ref.11. Source: UniProtKB

cilium

Inferred from sequence or structural similarity. Source: UniProtKB

nonmotile primary cilium

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

primary cilium

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DNM2P505702EBI-1049056,EBI-346547

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N157-1)

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: Q8N157-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1037-1053: GIISIERKPCNHQVDTA → DSHFAEFNTCILWWKKH
     1054-1196: Missing.
Isoform 3 (identifier: Q8N157-3)

The sequence of this isoform differs from the canonical sequence as follows:
     594-609: ACRIPNKHLFSLNAGE → ENEDVFVLISPTMEEY
     610-1196: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11961196Jouberin
PRO_0000050838

Regions

Repeat607 – 64943WD 1
Repeat652 – 69140WD 2
Repeat695 – 73541WD 3
Repeat742 – 78140WD 4
Repeat797 – 83741WD 5
Repeat841 – 88040WD 6
Repeat885 – 92642WD 7
Domain1051 – 111161SH3
Coiled coil13 – 4533 Potential
Compositional bias234 – 2396Poly-Lys

Natural variations

Alternative sequence594 – 60916ACRIP…LNAGE → ENEDVFVLISPTMEEY in isoform 3.
VSP_015353
Alternative sequence610 – 1196587Missing in isoform 3.
VSP_015354
Alternative sequence1037 – 105317GIISI…QVDTA → DSHFAEFNTCILWWKKH in isoform 2.
VSP_015355
Alternative sequence1054 – 1196143Missing in isoform 2.
VSP_015356
Natural variant491I → N. Ref.15
VAR_037892
Natural variant4431V → D in JBTS3. Ref.9 Ref.14
VAR_023391
Natural variant5481R → H. Ref.15
Corresponds to variant rs35433555 [ dbSNP | Ensembl ].
VAR_037893
Natural variant7231R → Q in JBTS3. Ref.15
VAR_037894
Natural variant7611S → L. Ref.15
VAR_037895
Natural variant8301R → W. Ref.15
Corresponds to variant rs13312995 [ dbSNP | Ensembl ].
VAR_037896
Natural variant8561T → S. Ref.15
Corresponds to variant rs199736888 [ dbSNP | Ensembl ].
VAR_037897
Natural variant9331Y → C. Ref.15
Corresponds to variant rs41288013 [ dbSNP | Ensembl ].
VAR_037898
Natural variant10181Q → P.
Corresponds to variant rs6940875 [ dbSNP | Ensembl ].
VAR_037899
Natural variant10861E → G in JBTS3. Ref.16
Corresponds to variant rs148000791 [ dbSNP | Ensembl ].
VAR_068171
Natural variant11231S → F. Ref.15
Corresponds to variant rs117447608 [ dbSNP | Ensembl ].
VAR_037900
Natural variant11401P → S. Ref.15
VAR_037901

Experimental info

Sequence conflict181E → K in CAB66731. Ref.3
Sequence conflict5531L → P in AAY99645. Ref.2

Secondary structure

............ 1196
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: 16A237C915DABF0F

FASTA1,196137,115
        10         20         30         40         50         60 
MPTAESEAKV KTKVRFEELL KTHSDLMREK KKLKKKLVRS EENISPDTIR SNLHYMKETT 

        70         80         90        100        110        120 
SDDPDTIRSN LPHIKETTSD DVSAANTNNL KKSTRVTKNK LRNTQLATEN PNGDASVEED 

       130        140        150        160        170        180 
KQGKPNKKVI KTVPQLTTQD LKPETPENKV DSTHQKTHTK PQPGVDHQKS EKANEGREET 

       190        200        210        220        230        240 
DLEEDEELMQ AYQCHVTEEM AKEIKRKIRK KLKEQLTYFP SDTLFHDDKL SSEKRKKKKE 

       250        260        270        280        290        300 
VPVFSKAETS TLTISGDTVE GEQKKESSVR SVSSDSHQDD EISSMEQSTE DSMQDDTKPK 

       310        320        330        340        350        360 
PKKTKKKTKA VADNNEDVDG DGVHEITSRD SPVYPKCLLD DDLVLGVYIH RTDRLKSDFM 

       370        380        390        400        410        420 
ISHPMVKIHV VDEHTGQYVK KDDSGRPVSS YYEKENVDYI LPIMTQPYDF KQLKSRLPEW 

       430        440        450        460        470        480 
EEQIVFNENF PYLLRGSDES PKVILFFEIL DFLSVDEIKN NSEVQNQECG FRKIAWAFLK 

       490        500        510        520        530        540 
LLGANGNANI NSKLRLQLYY PPTKPRSPLS VVEAFEWWSK CPRNHYPSTL YVTVRGLKVP 

       550        560        570        580        590        600 
DCIKPSYRSM MALQEEKGKP VHCERHHESS SVDTEPGLEE SKEVIKWKRL PGQACRIPNK 

       610        620        630        640        650        660 
HLFSLNAGER GCFCLDFSHN GRILAAACAS RDGYPIILYE IPSGRFMREL CGHLNIIYDL 

       670        680        690        700        710        720 
SWSKDDHYIL TSSSDGTARI WKNEINNTNT FRVLPHPSFV YTAKFHPAVR ELVVTGCYDS 

       730        740        750        760        770        780 
MIRIWKVEMR EDSAILVRQF DVHKSFINSL CFDTEGHHMY SGDCTGVIVV WNTYVKINDL 

       790        800        810        820        830        840 
EHSVHHWTIN KEIKETEFKG IPISYLEIHP NGKRLLIHTK DSTLRIMDLR ILVARKFVGA 

       850        860        870        880        890        900 
ANYREKIHST LTPCGTFLFA GSEDGIVYVW NPETGEQVAM YSDLPFKSPI RDISYHPFEN 

       910        920        930        940        950        960 
MVAFCAFGQN EPILLYIYDF HVAQQEAEMF KRYNGTFPLP GIHQSQDALC TCPKLPHQGS 

       970        980        990       1000       1010       1020 
FQIDEFVHTE SSSTKMQLVK QRLETVTEVI RSCAAKVNKN LSFTSPPAVS SQQSKLKQSN 

      1030       1040       1050       1060       1070       1080 
MLTAQEILHQ FGFTQTGIIS IERKPCNHQV DTAPTVVALY DYTANRSDEL TIHRGDIIRV 

      1090       1100       1110       1120       1130       1140 
FFKDNEDWWY GSIGKGQEGY FPANHVASET LYQELPPEIK ERSPPLSPEE KTKIEKSPAP 

      1150       1160       1170       1180       1190 
QKQSINKNKS QDFRLGSESM THSEMRKEQS HEDQGHIMDT RMRKNKQAGR KVTLIE 

« Hide

Isoform 2 [UniParc].

Checksum: 65D1BBEC361F9728
Show »

FASTA1,053120,853
Isoform 3 [UniParc].

Checksum: 42CE037DC5397F84
Show »

FASTA60970,047

References

« Hide 'large scale' references
[1]"Genome annotation of a 1.5 Mb region of human chromosome 6q23 encompassing a quantitative trait locus for fetal hemoglobin expression in adults."
Close J.P., Game L., Clark B., Bergounioux J., Gerovassili A., Thein S.L.
BMC Genomics 5:33-33(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Small intestine.
[2]"Full sequence of DKFZp686J1653."
Westin E.H., Zhang Y.
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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] (ISOFORM 1).
Tissue: Testis.
[4]"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] (ISOFORM 1).
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-301.
Tissue: Bone marrow and Testis.
[8]"Deregulated expression in Ph+ human leukemias of AHI-1, a gene activated by insertional mutagenesis in mouse models of leukemia."
Jiang X., Zhao Y., Chan W.-Y., Vercauteren S., Pang E., Kennedy S., Nicolini F., Eaves A., Eaves C.
Blood 103:3897-3904(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[9]"Abnormal cerebellar development and axonal decussation due to mutations in AHI1 in Joubert syndrome."
Ferland R.J., Eyaid W., Collura R.V., Tully L.D., Hill R.S., Al-Nouri D., Al-Rumayyan A., Topcu M., Gascon G., Bodell A., Shugart Y.Y., Ruvolo M., Walsh C.A.
Nat. Genet. 36:1008-1013(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANT JBTS3 ASP-443.
[10]Erratum
Ferland R.J., Eyaid W., Collura R.V., Tully L.D., Hill R.S., Al-Nouri D., Al-Rumayyan A., Topcu M., Gascon G., Bodell A., Shugart Y.Y., Ruvolo M., Walsh C.A.
Nat. Genet. 36:1126-1126(2004)
[11]"Jouberin localizes to collecting ducts and interacts with nephrocystin-1."
Eley L., Gabrielides C., Adams M., Johnson C.A., Hildebrandt F., Sayer J.A.
Kidney Int. 74:1139-1149(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NPHP1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Molecular and structural characterization of the SH3 domain of AHI-1 in regulation of cellular resistance of BCR-ABL(+) chronic myeloid leukemia cells to tyrosine kinase inhibitors."
Liu X., Chen M., Lobo P., An J., Grace Cheng S.W., Moradian A., Morin G.B., Van Petegem F., Jiang X.
Proteomics 12:2094-2106(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 1048-1116, INTERACTION WITH DNM2.
[14]"Mutations in the AHI1 gene, encoding jouberin, cause Joubert syndrome with cortical polymicrogyria."
Dixon-Salazar T., Silhavy J.L., Marsh S.E., Louie C.M., Scott L.C., Gururaj A., Al-Gazali L., Al-Tawari A.A., Kayserili H., Sztriha L., Gleeson J.G.
Am. J. Hum. Genet. 75:979-987(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JBTS3 ASP-443.
[15]"AHI1 gene mutations cause specific forms of Joubert syndrome-related disorders."
International JSRD study group
Valente E.M., Brancati F., Silhavy J.L., Castori M., Marsh S.E., Barrano G., Bertini E., Boltshauser E., Zaki M.S., Abdel-Aleem A., Abdel-Salam G.M.H., Bellacchio E., Battini R., Cruse R.P., Dobyns W.B., Krishnamoorthy K.S., Lagier-Tourenne C., Magee A. expand/collapse author list , Pascual-Castroviejo I., Salpietro C.D., Sarco D., Dallapiccola B., Gleeson J.G.
Ann. Neurol. 59:527-534(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JBTS3 GLN-723, VARIANTS ASN-49; HIS-548; LEU-761; TRP-830; SER-856; CYS-933; PHE-1123 AND SER-1140.
[16]"Mutations in C5ORF42 cause Joubert syndrome in the French Canadian population."
Srour M., Schwartzentruber J., Hamdan F.F., Ospina L.H., Patry L., Labuda D., Massicotte C., Dobrzeniecka S., Capo-Chichi J.M., Papillon-Cavanagh S., Samuels M.E., Boycott K.M., Shevell M.I., Laframboise R., Desilets V., Maranda B., Rouleau G.A., Majewski J., Michaud J.L.
Am. J. Hum. Genet. 90:693-700(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JBTS3 GLY-1086.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ459824 mRNA. Translation: CAD30871.1.
AJ459825 mRNA. Translation: CAD30872.1.
AJ606362 mRNA. Translation: CAE54481.1.
DQ090887 mRNA. Translation: AAY99645.1.
AL136797 mRNA. Translation: CAB66731.1.
AK092262 mRNA. Translation: BAC03840.1.
AL023693, AL049552, AL133544 Genomic DNA. Translation: CAI20201.1. Sequence problems.
AL049552, AL023693, AL133544 Genomic DNA. Translation: CAI20387.1. Sequence problems.
AL133544, AL023693, AL049552 Genomic DNA. Translation: CAI22523.1. Sequence problems.
CH471051 Genomic DNA. Translation: EAW47962.1.
CH471051 Genomic DNA. Translation: EAW47963.1.
BC029417 mRNA. Translation: AAH29417.1. Sequence problems.
BC065712 mRNA. Translation: AAH65712.1. Sequence problems.
BC094800 mRNA. Translation: AAH94800.1.
RefSeqNP_001128302.1. NM_001134830.1.
NP_001128303.1. NM_001134831.1.
NP_001128304.1. NM_001134832.1.
NP_060121.3. NM_017651.4.
UniGeneHs.386684.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ESRX-ray1.53A/B1048-1116[»]
ProteinModelPortalQ8N157.
SMRQ8N157. Positions 1052-1116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120163. 3 interactions.
IntActQ8N157. 3 interactions.
MINTMINT-4716361.
STRING9606.ENSP00000356774.

PTM databases

PhosphoSiteQ8N157.

Polymorphism databases

DMDM73921659.

Proteomic databases

PaxDbQ8N157.
PRIDEQ8N157.

Protocols and materials databases

DNASU54806.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265602; ENSP00000265602; ENSG00000135541. [Q8N157-1]
ENST00000327035; ENSP00000322478; ENSG00000135541. [Q8N157-2]
ENST00000367800; ENSP00000356774; ENSG00000135541. [Q8N157-1]
ENST00000457866; ENSP00000388650; ENSG00000135541. [Q8N157-1]
ENST00000531788; ENSP00000432167; ENSG00000135541. [Q8N157-3]
GeneID54806.
KEGGhsa:54806.
UCSCuc003qgh.3. human. [Q8N157-1]
uc003qgl.3. human. [Q8N157-2]

Organism-specific databases

CTD54806.
GeneCardsGC06M135646.
HGNCHGNC:21575. AHI1.
HPAHPA046684.
MIM608629. phenotype.
608894. gene.
neXtProtNX_Q8N157.
Orphanet220493. Joubert syndrome with ocular defect.
PharmGKBPA134874587.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG080824.
InParanoidQ8N157.
KOK16740.
OMALIHTKDS.
OrthoDBEOG7ZPNJZ.
PhylomeDBQ8N157.
TreeFamTF329226.

Enzyme and pathway databases

SignaLinkQ8N157.

Gene expression databases

ArrayExpressQ8N157.
BgeeQ8N157.
CleanExHS_AHI1.
GenevestigatorQ8N157.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR001452. SH3_domain.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00018. SH3_1. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50978. SSF50978. 1 hit.
PROSITEPS50002. SH3. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAHI1. human.
GeneWikiAHI1.
GenomeRNAi54806.
NextBio57511.
PROQ8N157.
SOURCESearch...

Entry information

Entry nameAHI1_HUMAN
AccessionPrimary (citable) accession number: Q8N157
Secondary accession number(s): E1P584 expand/collapse secondary AC list , Q4FD35, Q504T3, Q5TCP9, Q6P098, Q6PIT6, Q8NDX0, Q9H0H2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 110 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 6

Human chromosome 6: entries, gene names and cross-references to MIM