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Q8K3E5 (AHI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Jouberin
Alternative name(s):
Abelson helper integration site 1 protein
Short name=AHI-1
Gene names
Name:Ahi1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1047 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. Ref.7

Subunit structure

Interacts (via SH3 domain) with the dynamin GTPase DNM2 By similarity. Part of the tectonic-like complex (also named B9 complex). Interacts with NPHP1. Interacts with MKS1. Ref.5 Ref.6 Ref.7

Subcellular location

Cytoplasmcytoskeletoncilium basal body. Cell junctionadherens junction By similarity Ref.5.

Tissue specificity

Highly expressed in the brain and testis. Weakly expressed in the liver. Strongly expressed during periods of both cortical and cerebellar development. Ref.1 Ref.4

Developmental stage

First detected at embryonic days 7 (E7) and is also present at E11, E15 and E17 with the most high level at E15. Expression in whole brain is detected from E14 to adult. Expression in cerebellum appears maximal at E18 and postnatal days 5 (P5), whereas expression in cerebral cortex appears maximal at E16 and E18. Ref.4

Miscellaneous

Is targeted by provirus integrations. This deregulation contributes to tumor development.

Sequence similarities

Contains 1 SH3 domain.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
   Cellular componentCell junction
Cell projection
Cilium
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
WD repeat
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processKupffer's vesicle development

Inferred from sequence or structural similarity. Source: UniProtKB

cellular protein localization

Inferred from genetic interaction PubMed 20081859. Source: UniProtKB

central nervous system development

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

cilium assembly

Inferred from mutant phenotype PubMed 21959375. Source: UniProtKB

cilium morphogenesis

Inferred from mutant phenotype PubMed 19625297. Source: UniProtKB

cloaca development

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

heart looping

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

hindbrain development

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

left/right axis specification

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of a polarized epithelium

Inferred from mutant phenotype PubMed 21959375. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 20081859. Source: UniProtKB

otic vesicle development

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

photoreceptor cell outer segment organization

Inferred from genetic interaction PubMed 20081859. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 20592197. Source: MGI

positive regulation of polarized epithelial cell differentiation

Inferred from mutant phenotype PubMed 21959375. Source: UniProtKB

positive regulation of receptor internalization

Inferred from mutant phenotype PubMed 20956301. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20956301. Source: UniProtKB

pronephric duct morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

pronephric nephron tubule morphogenesis

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

protein localization to organelle

Inferred from mutant phenotype PubMed 19625297. Source: UniProtKB

regulation of behavior

Inferred from mutant phenotype PubMed 20956301. Source: UniProtKB

retina development in camera-type eye

Inferred from mutant phenotype PubMed 20592197. Source: MGI

retina layer formation

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

specification of axis polarity

Inferred from genetic interaction PubMed 21959375. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from mutant phenotype PubMed 20956301. Source: UniProtKB

vesicle targeting

Inferred from mutant phenotype PubMed 20592197. Source: MGI

vesicle-mediated transport

Inferred from mutant phenotype PubMed 19625297. Source: UniProtKB

   Cellular_componentTCTN-B9D complex

Inferred from direct assay Ref.7. Source: UniProtKB

adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from sequence or structural similarity. Source: UniProtKB

centriole

Inferred from direct assay PubMed 19625297. Source: UniProtKB

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary basal body

Inferred from direct assay PubMed 19625297PubMed 19718039PubMed 20081859. Source: UniProtKB

cilium

Inferred from direct assay PubMed 20081859. Source: UniProtKB

nonmotile primary cilium

Inferred from direct assay PubMed 19625297PubMed 19718039. Source: UniProtKB

photoreceptor outer segment

Inferred from direct assay PubMed 20592197. Source: MGI

primary cilium

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hap1O356682EBI-4280729,EBI-473704

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K3E5-1)

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: Q8K3E5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     994-1005: QSLSKGRPLDPR → GGHEEETKSQTN
     1006-1047: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10471047Jouberin
PRO_0000050839

Regions

Repeat457 – 49943WD 1
Repeat502 – 54140WD 2
Repeat545 – 58541WD 3
Repeat592 – 63140WD 4
Repeat648 – 68740WD 5
Repeat691 – 73040WD 6
Repeat735 – 77642WD 7
Domain902 – 96261SH3
Compositional bias87 – 948Poly-Lys

Natural variations

Alternative sequence994 – 100512QSLSK…PLDPR → GGHEEETKSQTN in isoform 2.
VSP_015357
Alternative sequence1006 – 104742Missing in isoform 2.
VSP_015358

Experimental info

Sequence conflict481Q → T in AAM94175. Ref.1
Sequence conflict1941V → L in AAM94175. Ref.1
Sequence conflict227 – 2348QYVKKDDS → H in BAB24355. Ref.3
Sequence conflict6321T → H in AAH55400. Ref.2

Sequences

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

Last modified August 30, 2005. Version 2.
Checksum: 91908C847218D4C0

FASTA1,047119,650
        10         20         30         40         50         60 
MEPETPEKVD SAQEKVRGKT PTADDSDDSR EKTGIEEKGE LTDAYQLQVA EEMAKEIKKK 

        70         80         90        100        110        120 
IRKKLKEQLT YFPPDTLLHD DKLASEKRKK KKKKVPVPTK PESSPSDVCD SAVEGEQKKE 

       130        140        150        160        170        180 
GTPEDSQHME GICSREQDVD ATVPENAKPK PKKTKKKTKA VSNDNEDTNG DGVHEITSRD 

       190        200        210        220        230        240 
SPVHPKCLLD DDLVMGVYIH RTDRLKSDFM ISHPMVKIHV VDEHTGQYVK KDDSERPVSS 

       250        260        270        280        290        300 
YYEKDNVDYI LPIMTQPYDF KKLKSRLPEW EEQVIFNENF PYLLREFEEC PKVILFFEIL 

       310        320        330        340        350        360 
DFLSMDEIKN NSEVQNQECG FRKIAWAFLK LLGANGNANI NSKLRLQLYY PPTKPRSQLN 

       370        380        390        400        410        420 
VVEVFEWWSK CPRNRYPSTL YVTVRGLKVP DCIKPSYRSM MALQEERGTP VYCERHRETS 

       430        440        450        460        470        480 
SVDTEPGLED SKEEVKWKRL PGQACRIPNK HLFSLNAGER GCFCLDFSHN GRILAAACAS 

       490        500        510        520        530        540 
RDGYPIILYE IPSGRFMREL CGHLNIIYDL DWSKDDRYLV TSSSDGTARV WKNEINSTST 

       550        560        570        580        590        600 
FRVLPHPSFV YTAKFHPATR ELVVTGCYDS MIRIWKIDAR EDAAILVRQL DVHKSFVNSI 

       610        620        630        640        650        660 
CFDDEGHHMY SGDCIGVIVV WDTYVKVNDV QTSVRHWTIN KEIKETEFRG VPISYLEVHP 

       670        680        690        700        710        720 
NGKRLLIHTK DSTLRIMDLR ILAARKFVGA ANYREKIHST LTPCGTLLFS GSEDGIVYVW 

       730        740        750        760        770        780 
NPETGEQVAM YSDLPFKSTI RDISYHPLEN MVAFCAFGQS EPILLYIYDF QVAQQEAEML 

       790        800        810        820        830        840 
KRYSGTLPLP GIHQSEDALC TCPKLPQQGS FQIDEFVNTE NSSSRKIQLV KQRLETVTEV 

       850        860        870        880        890        900 
IRSCAAKVNK NLSMTSPPPG PAKKPRVKQS FVLTTDEIIH QFGLPQTAFI SIERGPFVRH 

       910        920        930        940        950        960 
VDPPPMVVAL YDYTASRSDE LTIHRGDIIR VYFKDNEDWW YGSVRKGQEG FFPANHVASE 

       970        980        990       1000       1010       1020 
TLYRDSPPKV KERSPPLTPK EKTKPEKPLA SQKQSLSKGR PLDPRLGPQP VGHSEKGKDQ 

      1030       1040 
NVEDRGHKVD METKKSEPVV RKVTLIE 

« Hide

Isoform 2 [UniParc].

Checksum: 63388F7CA53AE454
Show »

FASTA1,005114,935

References

« Hide 'large scale' references
[1]"Ahi-1, a novel gene encoding a modular protein with WD40-repeat and SH3 domains, is targeted by the Ahi-1 and Mis-2 provirus integrations."
Jiang X., Hanna Z., Kaouass M., Girard L., Jolicoeur P.
J. Virol. 76:9046-9059(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Strain: C3H.
[2]"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 2).
Tissue: Eye.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322.
Strain: C57BL/6J.
Tissue: Testis.
[4]"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: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[5]"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, SUBCELLULAR LOCATION.
[6]"Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways."
Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A., Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K., Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D., O'Toole J.F. expand/collapse author list , Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A., Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B., Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.
Cell 145:513-528(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKS1.
[7]"A ciliopathy complex at the transition zone protects the cilia as a privileged membrane domain."
Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E., Sandoval W., Peterson A.S.
Nat. Cell Biol. 14:61-72(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY133241 mRNA. Translation: AAM94175.1.
BC055400 mRNA. Translation: AAH55400.1.
AK005991 mRNA. Translation: BAB24355.1.
CCDSCCDS35860.1. [Q8K3E5-1]
RefSeqXP_006512862.1. XM_006512799.1.
UniGeneMm.253280.
Mm.486431.

3D structure databases

ProteinModelPortalQ8K3E5.
SMRQ8K3E5. Positions 430-801, 905-967.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8K3E5. 18 interactions.

PTM databases

PhosphoSiteQ8K3E5.

Proteomic databases

MaxQBQ8K3E5.
PaxDbQ8K3E5.
PRIDEQ8K3E5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID52906.
KEGGmmu:52906.

Organism-specific databases

CTD54806.
MGIMGI:87971. Ahi1.

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000033864.
HOVERGENHBG080824.
InParanoidQ8K3E5.
KOK16740.
PhylomeDBQ8K3E5.

Gene expression databases

CleanExMM_AHI1.
GenevestigatorQ8K3E5.

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. 5 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
SM00320. WD40. 7 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

PROQ8K3E5.
SOURCESearch...

Entry information

Entry nameAHI1_MOUSE
AccessionPrimary (citable) accession number: Q8K3E5
Secondary accession number(s): Q7TNV2, Q9CVY1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot