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Q495M9 (USH1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 91. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Usher syndrome type-1G protein
Alternative name(s):
Scaffold protein containing ankyrin repeats and SAM domain
Gene names
Name:USH1G
Synonyms:SANS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal development and maintenance of cochlear hair cell bundles. Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. Ref.4 Ref.7

Subunit structure

Interacts with CDH23 and PCDH15; these interactions may recruit USH1G to the plasma membrane By similarity. Interacts with USH1C (via the first PDZ domain) and with USH1G. Interacts with PDZD7. Interacts with MYO7A. Part of a complex composed of USH1C, USH1G and MYO7A. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Cytoplasmcytosol. Cytoplasmcytoskeleton. Cell membrane; Peripheral membrane protein By similarity. Note: Detected at the tip of cochlear hair cell stereocilia. Recruited to the cell membrane via interaction with CDH23 or PCDH15 By similarity. Ref.4 Ref.5

Tissue specificity

Expressed in vestibule of the inner ear, eye and small intestine. Ref.7

Involvement in disease

Usher syndrome 1G (USH1G) [MIM:606943]: USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by profound congenital sensorineural deafness, absent vestibular function and prepubertal onset of progressive retinitis pigmentosa leading to blindness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.5 Ref.7 Ref.8

Sequence similarities

Contains 3 ANK repeats.

Contains 1 SAM (sterile alpha motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Usher syndrome type-1G protein
PRO_0000067077

Regions

Repeat31 – 6030ANK 1
Repeat64 – 9330ANK 2
Repeat97 – 12630ANK 3
Domain385 – 44763SAM
Compositional bias444 – 4474Poly-Arg

Natural variations

Natural variant481L → P in USH1G. Ref.7
VAR_023739
Natural variant4581D → V in USH1G; atypical form with mild retinitis pigmentosa and normal vestibular function; also found in patients with autosomal recessive non-syndromic deafness; strongly reduced affinity for USH1C. Ref.5 Ref.8
VAR_060468

Experimental info

Mutagenesis3071F → E: Reduced affinity for MYO7A. Ref.6
Mutagenesis3171F → E: Reduced affinity for MYO7A. Ref.6
Mutagenesis3741W → Q: Strongly reduced affinity for MYO7A. Ref.6
Sequence conflict3001D → N in BAC03619. Ref.1
Sequence conflict4021E → G in BAC03619. Ref.1

Secondary structure

.................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q495M9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: B0ABB9F5711A5095

FASTA46151,489
        10         20         30         40         50         60 
MNDQYHRAAR DGYLELLKEA TRKELNAPDE DGMTPTLWAA YHGNLESLRL IVSRGGDPDK 

        70         80         90        100        110        120 
CDIWGNTPLH LAASNGHLHC LSFLVSFGAN IWCLDNDYHT PLDMAAMKGH MECVRYLDSI 

       130        140        150        160        170        180 
AAKQSSLNPK LVGKLKDKAF REAERRIREC AKLQRRHHER MERRYRRELA ERSDTLSFSS 

       190        200        210        220        230        240 
LTSSTLSRRL QHLALGSHLP YSQATLHGTA RGKTKMQKKL ERRKQGGEGT FKVSEDGRKS 

       250        260        270        280        290        300 
ARSLSGLQLG SDVMFVRQGT YANPKEWGRA PLRDMFLSDE DSVSRATLAA EPAHSEVSTD 

       310        320        330        340        350        360 
SGHDSLFTRP GLGTMVFRRN YLSSGLHGLG REDGGLDGVG APRGRLQSSP SLDDDSLGSA 

       370        380        390        400        410        420 
NSLQDRSCGE ELPWDELDLG LDEDLEPETS PLETFLASLH MEDFAALLRQ EKIDLEALML 

       430        440        450        460 
CSDLDLRSIS VPLGPRKKIL GAVRRRRQAM ERPPALEDTE L 

« Hide

References

« Hide 'large scale' references
[1]"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: Tongue.
[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].
[3]"Homozygous disruption of PDZD7 by reciprocal translocation in a consanguineous family: a new member of the Usher syndrome protein interactome causing congenital hearing impairment."
Schneider E., Marker T., Daser A., Frey-Mahn G., Beyer V., Farcas R., Schneider-Ratzke B., Kohlschmidt N., Grossmann B., Bauss K., Napiontek U., Keilmann A., Bartsch O., Zechner U., Wolfrum U., Haaf T.
Hum. Mol. Genet. 18:655-666(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZD7.
[4]"Myosin VIIa and sans localization at stereocilia upper tip-link density implicates these Usher syndrome proteins in mechanotransduction."
Grati M., Kachar B.
Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH MYO7A; USH1C AND USH1G.
[5]"The structure of the harmonin/sans complex reveals an unexpected interaction mode of the two Usher syndrome proteins."
Yan J., Pan L., Chen X., Wu L., Zhang M.
Proc. Natl. Acad. Sci. U.S.A. 107:4040-4045(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 388-461 IN COMPLEX WITH USH1C, INTERACTION WITH USH1C, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT USH1G VAL-458.
[6]"Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo."
Wu L., Pan L., Wei Z., Zhang M.
Science 331:757-760(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 295-390 IN COMPLEX WITH MYO7A, STRUCTURE BY NMR OF 370-380, INTERACTION WITH MYO7A, MUTAGENESIS OF PHE-307; PHE-317 AND TRP-374.
[7]"Usher syndrome type I G (USH1G) is caused by mutations in the gene encoding SANS, a protein that associates with the USH1C protein, harmonin."
Weil D., El-Amraoui A., Masmoudi S., Mustapha M., Kikkawa Y., Laine S., Delmaghani S., Adato A., Nadifi S., Zina Z.B., Hamel C., Gal A., Ayadi H., Yonekawa H., Petit C.
Hum. Mol. Genet. 12:463-471(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT USH1G PRO-48, INTERACTION WITH USH1C, TISSUE SPECIFICITY, POSSIBLE FUNCTION.
[8]"A novel D458V mutation in the SANS PDZ binding motif causes atypical Usher syndrome."
Kalay E., de Brouwer A.P.M., Caylan R., Nabuurs S.B., Wollnik B., Karaguzel A., Heister J.G.A.M., Erdol H., Cremers F.P.M., Cremers C.W.R.J., Brunner H.G., Kremer H.
J. Mol. Med. 83:1025-1032(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT USH1G VAL-458.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK091243 mRNA. Translation: BAC03619.1.
BC101096 mRNA. Translation: AAI01097.1.
BC101097 mRNA. Translation: AAI01098.1.
BC101098 mRNA. Translation: AAI01099.1.
BC101099 mRNA. Translation: AAI01100.1.
RefSeqNP_001269418.1. NM_001282489.1.
NP_775748.2. NM_173477.3.
UniGeneHs.376688.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L7TNMR-A370-380[»]
3K1RX-ray2.30B388-461[»]
3PVLX-ray2.80B295-390[»]
ProteinModelPortalQ495M9.
SMRQ495M9. Positions 3-178, 388-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-41617N.
MINTMINT-257481.
STRING9606.ENSP00000320076.

PTM databases

PhosphoSiteQ495M9.

Polymorphism databases

DMDM81175048.

Proteomic databases

PaxDbQ495M9.
PRIDEQ495M9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319642; ENSP00000320076; ENSG00000182040.
GeneID124590.
KEGGhsa:124590.
UCSCuc002jme.1. human.

Organism-specific databases

CTD124590.
GeneCardsGC17M072912.
HGNCHGNC:16356. USH1G.
HPAHPA024360.
MIM276900. phenotype.
606943. phenotype.
607696. gene.
neXtProtNX_Q495M9.
Orphanet231169. Usher syndrome type 1.
PharmGKBPA38126.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000007847.
HOVERGENHBG051882.
InParanoidQ495M9.
OMAMKGHMEC.
OrthoDBEOG70GMFR.
PhylomeDBQ495M9.
TreeFamTF324946.

Enzyme and pathway databases

SignaLinkQ495M9.

Gene expression databases

ArrayExpressQ495M9.
BgeeQ495M9.
CleanExHS_USH1G.
GenevestigatorQ495M9.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ495M9.
GeneWikiUSH1G.
GenomeRNAi124590.
NextBio81331.
PROQ495M9.
SOURCESearch...

Entry information

Entry nameUSH1G_HUMAN
AccessionPrimary (citable) accession number: Q495M9
Secondary accession number(s): Q8N251
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: September 13, 2005
Last modified: March 19, 2014
This is version 91 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 17

Human chromosome 17: entries, gene names and cross-references to MIM