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O75445 (USH2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Usherin
Alternative name(s):
Usher syndrome type IIa protein
Usher syndrome type-2A protein
Gene names
Name:USH2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length5202 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 hearing and vision.

Subunit structure

Interacts with collagen IV and fibronectin via its laminin EGF-like domains. Interaction with collagen may be required for stable integration into the basement membrane. Interacts with USH1C and WHRN. Interacts with NINL. Interacts with PDZD7. Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

Cell projectionstereocilium membrane; Single-pass type I membrane protein. Note: Probable component of the interstereocilia ankle links in the inner ear sensory cells. Ref.8

Isoform 2: Secreted Ref.8.

Tissue specificity

Present in the basement membrane of many, but not all tissues. Expressed in retina, cochlea, small and large intestine, pancreas, bladder, prostate, esophagus, trachea, thymus, salivary glands, placenta, ovary, fallopian tube, uterus and testis. Absent in many other tissues such as heart, lung, liver, kidney and brain. In the retina, it is present in the basement membranes in the Bruch's layer choroid capillary basement membranes, where it localizes just beneath the retinal pigment epithelial cells (at protein level). Weakly expressed. Isoform 2 is expressed in fetal eye, cochlea and heart, and at very low level in brain, CNS, intestine, skeleton, tongue, kidney and lung. Isoform 2 is not expressed in stomach and liver. In adult tissues, isoform 2 is expressed in neural retina and testis, and at low level in brain, heart, kidney and liver. Isoform 1 displays a similar pattern of expression but is expressed at very low level in fetal cochlea. Ref.1 Ref.4 Ref.6 Ref.7

Domain

The PDZ-binding motif probably mediates the association with some of the PDZ domains of USH1C and WHRN By similarity.

Involvement in disease

Usher syndrome 2A (USH2A) [MIM:276901]: 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). USH2 is characterized by congenital mild hearing impairment with normal vestibular responses.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.4 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31 Ref.32

Retinitis pigmentosa 39 (RP39) [MIM:613809]: 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.16 Ref.20 Ref.21 Ref.26 Ref.28 Ref.30 Ref.35

Sequence similarities

Contains 35 fibronectin type-III domains.

Contains 10 laminin EGF-like domains.

Contains 2 laminin G-like domains.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processHearing
Sensory transduction
Vision
   Cellular componentCell membrane
Cell projection
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
Retinitis pigmentosa
Usher syndrome
   DomainLaminin EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhair cell differentiation

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

inner ear receptor cell differentiation

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

maintenance of organ identity

Inferred from mutant phenotype PubMed 15671307. Source: HGNC

photoreceptor cell maintenance

Inferred from mutant phenotype PubMed 10090909. Source: HGNC

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

sensory perception of light stimulus

Inferred from mutant phenotype PubMed 10090909. Source: HGNC

sensory perception of sound

Inferred from mutant phenotype PubMed 10090909. Source: HGNC

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical plasma membrane

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

basement membrane

Inferred from direct assay Ref.7. Source: HGNC

cytoplasm

Inferred from direct assay Ref.12. Source: HGNC

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

stereocilia ankle link complex

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

stereocilium bundle

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

stereocilium membrane

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

   Molecular_functioncollagen binding

Inferred from direct assay Ref.8. Source: HGNC

myosin binding

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

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75445-1)

Also known as: b;

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: O75445-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1544-1546: IKA → KCV
     1547-5202: Missing.
Isoform 3 (identifier: O75445-3)

The sequence of this isoform differs from the canonical sequence as follows:
     5099-5099: M → MFDSVADISDVSSNVTLKSYTMHFE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 52025171Usherin
PRO_0000229804

Regions

Topological domain32 – 50425011Extracellular Potential
Transmembrane5043 – 506321Helical; Potential
Topological domain5064 – 5202139Cytoplasmic Potential
Domain271 – 517247Laminin N-terminal
Domain518 – 57457Laminin EGF-like 1
Domain575 – 64066Laminin EGF-like 2
Domain641 – 69353Laminin EGF-like 3
Domain694 – 74653Laminin EGF-like 4
Domain747 – 79448Laminin EGF-like 5
Domain795 – 84652Laminin EGF-like 6
Domain847 – 89953Laminin EGF-like 7
Domain900 – 95051Laminin EGF-like 8
Domain951 – 100151Laminin EGF-like 9
Domain1002 – 105251Laminin EGF-like 10
Domain1058 – 114689Fibronectin type-III 1
Domain1148 – 124497Fibronectin type-III 2
Domain1245 – 1363119Fibronectin type-III 3
Domain1364 – 1468105Fibronectin type-III 4
Domain1517 – 1709193Laminin G-like 1
Domain1714 – 1891178Laminin G-like 2
Domain1869 – 195587Fibronectin type-III 5
Domain1957 – 205498Fibronectin type-III 6
Domain2055 – 214490Fibronectin type-III 7
Domain2145 – 223995Fibronectin type-III 8
Domain2243 – 233088Fibronectin type-III 9
Domain2331 – 2433103Fibronectin type-III 10
Domain2437 – 253195Fibronectin type-III 11
Domain2535 – 262288Fibronectin type-III 12
Domain2624 – 272299Fibronectin type-III 13
Domain2726 – 281994Fibronectin type-III 14
Domain2820 – 2923104Fibronectin type-III 15
Domain2927 – 301892Fibronectin type-III 16
Domain3022 – 311291Fibronectin type-III 17
Domain3113 – 320997Fibronectin type-III 18
Domain3403 – 349795Fibronectin type-III 19
Domain3501 – 358989Fibronectin type-III 20
Domain3592 – 368291Fibronectin type-III 21
Domain3684 – 377087Fibronectin type-III 22
Domain3774 – 386592Fibronectin type-III 23
Domain3866 – 396398Fibronectin type-III 24
Domain3964 – 4067104Fibronectin type-III 25
Domain4068 – 415386Fibronectin type-III 26
Domain4157 – 4261105Fibronectin type-III 27
Domain4262 – 435796Fibronectin type-III 28
Domain4358 – 444588Fibronectin type-III 29
Domain4446 – 453085Fibronectin type-III 30
Domain4534 – 463097Fibronectin type-III 31
Domain4636 – 473398Fibronectin type-III 32
Domain4734 – 482794Fibronectin type-III 33
Domain4828 – 4927100Fibronectin type-III 34
Motif5200 – 52023PDZ-binding

Amino acid modifications

Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential
Glycosylation5871N-linked (GlcNAc...) Potential
Glycosylation6111N-linked (GlcNAc...) Potential
Glycosylation6501N-linked (GlcNAc...) Potential
Glycosylation6971N-linked (GlcNAc...) Potential
Glycosylation8391N-linked (GlcNAc...) Potential
Glycosylation8561N-linked (GlcNAc...) Potential
Glycosylation8621N-linked (GlcNAc...) Potential
Glycosylation8881N-linked (GlcNAc...) Potential
Glycosylation9441N-linked (GlcNAc...) Potential
Glycosylation10111N-linked (GlcNAc...) Potential
Glycosylation10711N-linked (GlcNAc...) Potential
Glycosylation11511N-linked (GlcNAc...) Potential
Glycosylation11741N-linked (GlcNAc...) Potential
Glycosylation13791N-linked (GlcNAc...) Potential
Glycosylation13881N-linked (GlcNAc...) Potential
Glycosylation14791N-linked (GlcNAc...) Potential
Glycosylation16351N-linked (GlcNAc...) Potential
Glycosylation17791N-linked (GlcNAc...) Potential
Glycosylation19031N-linked (GlcNAc...) Potential
Glycosylation20111N-linked (GlcNAc...) Potential
Glycosylation20141N-linked (GlcNAc...) Potential
Glycosylation20481N-linked (GlcNAc...) Potential
Glycosylation21301N-linked (GlcNAc...) Potential
Glycosylation21821N-linked (GlcNAc...) Potential
Glycosylation21951N-linked (GlcNAc...) Potential
Glycosylation22581N-linked (GlcNAc...) Potential
Glycosylation22851N-linked (GlcNAc...) Potential
Glycosylation23221N-linked (GlcNAc...) Potential
Glycosylation23771N-linked (GlcNAc...) Potential
Glycosylation23821N-linked (GlcNAc...) Potential
Glycosylation24071N-linked (GlcNAc...) Potential
Glycosylation24131N-linked (GlcNAc...) Potential
Glycosylation25811N-linked (GlcNAc...) Potential
Glycosylation25841N-linked (GlcNAc...) Potential
Glycosylation26561N-linked (GlcNAc...) Potential
Glycosylation27101N-linked (GlcNAc...) Potential
Glycosylation27701N-linked (GlcNAc...) Potential
Glycosylation27881N-linked (GlcNAc...) Potential
Glycosylation29301N-linked (GlcNAc...) Potential
Glycosylation29371N-linked (GlcNAc...) Potential
Glycosylation29701N-linked (GlcNAc...) Potential
Glycosylation30321N-linked (GlcNAc...) Potential
Glycosylation30991N-linked (GlcNAc...) Potential
Glycosylation32171N-linked (GlcNAc...) Potential
Glycosylation33301N-linked (GlcNAc...) Potential
Glycosylation34191N-linked (GlcNAc...) Potential
Glycosylation34331N-linked (GlcNAc...) Potential
Glycosylation36531N-linked (GlcNAc...) Potential
Glycosylation36941N-linked (GlcNAc...) Potential
Glycosylation37331N-linked (GlcNAc...) Potential
Glycosylation37801N-linked (GlcNAc...) Potential
Glycosylation38491N-linked (GlcNAc...) Potential
Glycosylation39841N-linked (GlcNAc...) Potential
Glycosylation42021N-linked (GlcNAc...) Potential
Glycosylation42261N-linked (GlcNAc...) Potential
Glycosylation43171N-linked (GlcNAc...) Potential
Glycosylation44181N-linked (GlcNAc...) Potential
Glycosylation45641N-linked (GlcNAc...) Potential
Glycosylation45831N-linked (GlcNAc...) Potential
Glycosylation46911N-linked (GlcNAc...) Potential
Glycosylation47541N-linked (GlcNAc...) Potential
Glycosylation48001N-linked (GlcNAc...) Potential
Glycosylation49431N-linked (GlcNAc...) Potential
Glycosylation49501N-linked (GlcNAc...) Potential
Disulfide bond518 ↔ 527 By similarity
Disulfide bond520 ↔ 536 By similarity
Disulfide bond538 ↔ 549 By similarity
Disulfide bond552 ↔ 572 By similarity
Disulfide bond575 ↔ 584 By similarity
Disulfide bond577 ↔ 605 By similarity
Disulfide bond608 ↔ 617 By similarity
Disulfide bond620 ↔ 638 By similarity
Disulfide bond641 ↔ 655 By similarity
Disulfide bond643 ↔ 662 By similarity
Disulfide bond664 ↔ 673 By similarity
Disulfide bond676 ↔ 691 By similarity
Disulfide bond694 ↔ 708 By similarity
Disulfide bond696 ↔ 715 By similarity
Disulfide bond717 ↔ 726 By similarity
Disulfide bond729 ↔ 744 By similarity
Disulfide bond747 ↔ 759 By similarity
Disulfide bond749 ↔ 766 By similarity
Disulfide bond768 ↔ 777 By similarity
Disulfide bond780 ↔ 792 By similarity
Disulfide bond795 ↔ 808 By similarity
Disulfide bond797 ↔ 815 By similarity
Disulfide bond817 ↔ 826 By similarity
Disulfide bond829 ↔ 844 By similarity
Disulfide bond847 ↔ 861 By similarity
Disulfide bond849 ↔ 868 By similarity
Disulfide bond870 ↔ 879 By similarity
Disulfide bond882 ↔ 897 By similarity
Disulfide bond900 ↔ 913 By similarity
Disulfide bond902 ↔ 920 By similarity
Disulfide bond922 ↔ 931 By similarity
Disulfide bond934 ↔ 948 By similarity
Disulfide bond951 ↔ 963 By similarity
Disulfide bond953 ↔ 970 By similarity
Disulfide bond972 ↔ 982 By similarity
Disulfide bond985 ↔ 999 By similarity
Disulfide bond1002 ↔ 1014 By similarity
Disulfide bond1004 ↔ 1021 By similarity
Disulfide bond1023 ↔ 1032 By similarity
Disulfide bond1035 ↔ 1050 By similarity
Disulfide bond1672 ↔ 1709 By similarity
Disulfide bond1862 ↔ 1891 By similarity
Disulfide bond3371 ↔ 3444 By similarity
Disulfide bond3399 ↔ 3425 By similarity

Natural variations

Alternative sequence1544 – 15463IKA → KCV in isoform 2.
VSP_017771
Alternative sequence1547 – 52023656Missing in isoform 2.
VSP_017772
Alternative sequence50991M → MFDSVADISDVSSNVTLKSY TMHFE in isoform 3.
VSP_017773
Natural variant1251A → T. Ref.26 Ref.28 Ref.30 Ref.32
Corresponds to variant rs10779261 [ dbSNP | Ensembl ].
VAR_025760
Natural variant1631C → Y in USH2A. Ref.17 Ref.32
VAR_025761
Natural variant2181V → E in USH2A. Ref.19 Ref.31
VAR_025762
Natural variant2301V → M in USH2A; may be a common polymorphism. Ref.17 Ref.19 Ref.26 Ref.32
Corresponds to variant rs45500891 [ dbSNP | Ensembl ].
VAR_025763
Natural variant2681G → R in USH2A; unknown pathological significance. Ref.26 Ref.32
VAR_054557
Natural variant2801L → F in USH2A. Ref.31
VAR_054558
Natural variant2841E → K in USH2A. Ref.31
VAR_054559
Natural variant3031R → C in USH2A. Ref.32
VAR_054560
Natural variant3031R → S in USH2A. Ref.25
VAR_054561
Natural variant3071S → I in USH2A; unknown pathological significance. Ref.26
VAR_054562
Natural variant3191C → Y in USH2A. Ref.2
VAR_025764
Natural variant3341R → Q in USH2A. Ref.31
VAR_054563
Natural variant3341R → W in USH2A. Ref.18 Ref.23 Ref.31 Ref.32
VAR_025765
Natural variant3461N → H in USH2A. Ref.2 Ref.23 Ref.27 Ref.31 Ref.32
VAR_025766
Natural variant3521T → I in USH2A. Ref.31 Ref.32
VAR_054564
Natural variant3571N → T in USH2A. Ref.23
VAR_054565
Natural variant3651L → F. Ref.26
VAR_054566
Natural variant3911S → I in USH2A; unknown pathological significance. Ref.26
VAR_054567
Natural variant4191C → F in USH2A and RP39. Ref.2 Ref.26 Ref.27 Ref.35
VAR_025767
Natural variant4531T → I Found in a renal cell carcinoma sample; somatic mutation. Ref.34
VAR_064761
Natural variant4641R → C in USH2A; unknown pathological significance. Ref.26
VAR_054568
Natural variant4781E → D in RP39 and USH2A; unknown pathological significance. Ref.18 Ref.26 Ref.28 Ref.30 Ref.32
Corresponds to variant rs35730265 [ dbSNP | Ensembl ].
VAR_025768
Natural variant4791F → S. Ref.1 Ref.23
VAR_054569
Natural variant5161G → V in USH2A; unknown pathological significance. Ref.26
VAR_054570
Natural variant5171R → T in USH2A; unknown pathological significance. Ref.26
VAR_054571
Natural variant5361C → R in USH2A; abolishes interaction with collagen IV. Ref.17 Ref.27 Ref.32
VAR_025769
Natural variant5551L → V in USH2A. Ref.19
Corresponds to variant rs35818432 [ dbSNP | Ensembl ].
VAR_025770
Natural variant5751C → S in USH2A; unknown pathological significance. Ref.26
VAR_054572
Natural variant5871Missing in USH2A; unknown pathological significance. Ref.26
VAR_054573
Natural variant5951F → S. Ref.32
Corresponds to variant rs200496467 [ dbSNP | Ensembl ].
VAR_054574
Natural variant6101H → P in USH2A. Ref.22
VAR_025771
Natural variant6441D → V. Ref.18 Ref.23 Ref.26 Ref.28 Ref.30 Ref.32
Corresponds to variant rs1805048 [ dbSNP | Ensembl ].
VAR_025772
Natural variant7031D → E. Ref.28
VAR_025773
Natural variant7131G → R in USH2A; abolishes interaction with collagen IV; unknown pathological significance. Ref.17 Ref.21 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32
Corresponds to variant rs696723 [ dbSNP | Ensembl ].
VAR_025774
Natural variant7391F → L in RP39; unknown pathological significance. Ref.26
VAR_054575
Natural variant7591C → F in RP39 and USH2A. Ref.16 Ref.20 Ref.21 Ref.25 Ref.26 Ref.28 Ref.31 Ref.32 Ref.35
Corresponds to variant rs80338902 [ dbSNP | Ensembl ].
VAR_025775
Natural variant7611P → R in USH2A. Ref.22
VAR_025776
Natural variant8411S → Y. Ref.28
Corresponds to variant rs111033282 [ dbSNP | Ensembl ].
VAR_025777
Natural variant9111T → N in RP39; unknown pathological significance. Ref.26
VAR_054576
Natural variant10471L → V. Ref.26
VAR_054577
Natural variant10591P → L in USH2A; unknown pathological significance. Ref.26
VAR_054578
Natural variant12121P → L in USH2A. Ref.32
VAR_054579
Natural variant13491S → P. Ref.32
VAR_054580
Natural variant14701L → R in RP39; unknown pathological significance. Ref.26
VAR_054581
Natural variant14861R → K. Ref.1 Ref.2 Ref.18 Ref.26 Ref.28 Ref.30 Ref.32
Corresponds to variant rs1805049 [ dbSNP | Ensembl ].
VAR_025778
Natural variant15151T → M in USH2A. Ref.18
VAR_025779
Natural variant15721L → F. Ref.29 Ref.31 Ref.32
Corresponds to variant rs111033333 [ dbSNP | Ensembl ].
VAR_054582
Natural variant16651I → T. Ref.29 Ref.30 Ref.32
Corresponds to variant rs56222536 [ dbSNP | Ensembl ].
VAR_038362
Natural variant17571Y → C. Ref.32
VAR_054583
Natural variant18331V → E in USH2A. Ref.31
VAR_054584
Natural variant18591F → C in RP39. Ref.35
VAR_068354
Natural variant20801K → N. Ref.32
Corresponds to variant rs114402911 [ dbSNP | Ensembl ].
VAR_054585
Natural variant20861T → N. Ref.32
Corresponds to variant rs149202379 [ dbSNP | Ensembl ].
VAR_054586
Natural variant21061I → T. Ref.29 Ref.30 Ref.32
Corresponds to variant rs6657250 [ dbSNP | Ensembl ].
VAR_038363
Natural variant21691I → T. Ref.29 Ref.30 Ref.32
Corresponds to variant rs10864219 [ dbSNP | Ensembl ].
VAR_038364
Natural variant22381E → A. Ref.29 Ref.32
Corresponds to variant rs41277212 [ dbSNP | Ensembl ].
VAR_054587
Natural variant22491A → D in USH2A. Ref.29
VAR_054588
Natural variant2265 – 22662EY → D in USH2A. Ref.32
VAR_054589
Natural variant22921R → H. Ref.32
Corresponds to variant rs41277210 [ dbSNP | Ensembl ].
VAR_054590
Natural variant23541R → H in USH2A. Ref.29
VAR_054591
Natural variant24601R → H in RP39. Ref.35
VAR_068355
Natural variant25621V → A. Ref.32
Corresponds to variant rs56385601 [ dbSNP | Ensembl ].
VAR_054592
Natural variant27951A → S in USH2A. Ref.31
VAR_054593
Natural variant28201V → I.
Corresponds to variant rs59174500 [ dbSNP | Ensembl ].
VAR_061350
Natural variant28751R → Q. Ref.29 Ref.30 Ref.32
Corresponds to variant rs12118814 [ dbSNP | Ensembl ].
VAR_038365
Natural variant28861L → F. Ref.29 Ref.32
Corresponds to variant rs41277200 [ dbSNP | Ensembl ].
VAR_054594
Natural variant30881E → K. Ref.32
Corresponds to variant rs56056328 [ dbSNP | Ensembl ].
VAR_054595
Natural variant30991N → S. Ref.29 Ref.30 Ref.32
Corresponds to variant rs41277194 [ dbSNP | Ensembl ].
VAR_038366
Natural variant31151T → A. Ref.32
Corresponds to variant rs56032526 [ dbSNP | Ensembl ].
VAR_054596
Natural variant31241R → G in USH2A; unknown pathological significance. Ref.32
VAR_054597
Natural variant31441D → N. Ref.29 Ref.30 Ref.32
Corresponds to variant rs11120645 [ dbSNP | Ensembl ].
VAR_038367
Natural variant31991N → D. Ref.32
Corresponds to variant rs4129843 [ dbSNP | Ensembl ].
VAR_034064
Natural variant32511C → R in USH2A. Ref.29
VAR_054598
Natural variant32671C → R in USH2A. Ref.29
VAR_054599
Natural variant32821C → R in USH2A. Ref.31
VAR_054600
Natural variant33351I → M. Ref.30
VAR_038368
Natural variant33581C → Y in RP39. Ref.35
VAR_068356
Natural variant34111E → A. Ref.29 Ref.32
Corresponds to variant rs10864198 [ dbSNP | Ensembl ].
VAR_050087
Natural variant34721Y → YY in USH2A. Ref.29
VAR_054601
Natural variant35041P → T in USH2A. Ref.32
VAR_054602
Natural variant35211W → R in USH2A. Ref.32
VAR_054603
Natural variant35711T → M in USH2A. Ref.29 Ref.31
VAR_054604
Natural variant35901P → L. Ref.32
Corresponds to variant rs115403785 [ dbSNP | Ensembl ].
VAR_054605
Natural variant36691S → R in RP39. Ref.35
VAR_068357
Natural variant38351T → I. Ref.32
Corresponds to variant rs11120616 [ dbSNP | Ensembl ].
VAR_050088
Natural variant38681M → V. Ref.29 Ref.32
Corresponds to variant rs35309576 [ dbSNP | Ensembl ].
VAR_054606
Natural variant38931P → T. Ref.32
Corresponds to variant rs41303285 [ dbSNP | Ensembl ].
VAR_054607
Natural variant38951G → E in USH2A. Ref.31
VAR_054608
Natural variant39761T → M in USH2A. Ref.31
VAR_054609
Natural variant40541S → I in USH2A. Ref.32
VAR_054610
Natural variant41151R → C in USH2A and RP39; associated with M-4425. Ref.4 Ref.31 Ref.32 Ref.35
VAR_025780
Natural variant41921R → H in RP39. Ref.35
Corresponds to variant rs199605265 [ dbSNP | Ensembl ].
VAR_068358
Natural variant42031Q → R Found in a patient with spinocerebellar ataxia. Ref.33
Corresponds to variant rs148556640 [ dbSNP | Ensembl ].
VAR_066665
Natural variant42321P → R in USH2A. Ref.32
VAR_054611
Natural variant43371T → M in USH2A. Ref.29
VAR_054612
Natural variant44251T → M in USH2Aand RP39; associated with C-4115. Ref.4 Ref.31 Ref.35
Corresponds to variant rs201238640 [ dbSNP | Ensembl ].
VAR_025781
Natural variant44331V → L. Ref.32
Corresponds to variant rs111033381 [ dbSNP | Ensembl ].
VAR_054613
Natural variant44391T → I in USH2A. Ref.15 Ref.32
VAR_054614
Natural variant44871Y → C in USH2A. Ref.32
VAR_054615
Natural variant45921Q → H in USH2A. Ref.32
VAR_054616
Natural variant46241F → V. Ref.32
VAR_054617
Natural variant46741R → G in RP39. Ref.30
VAR_038369
Natural variant46921G → R.
Corresponds to variant rs45549044 [ dbSNP | Ensembl ].
VAR_061351
Natural variant47391R → K.
Corresponds to variant rs12085354 [ dbSNP | Ensembl ].
VAR_050089
Natural variant47951L → R in USH2A. Ref.32
VAR_054618
Natural variant48181P → L in USH2A. Ref.29
Corresponds to variant rs143344549 [ dbSNP | Ensembl ].
VAR_054619
Natural variant48381G → E.
Corresponds to variant rs41315587 [ dbSNP | Ensembl ].
VAR_061352
Natural variant50311R → W. Ref.32
Corresponds to variant rs56038610 [ dbSNP | Ensembl ].
VAR_054620

Experimental info

Sequence conflict2371F → C in AAC23748. Ref.1
Sequence conflict2371F → C in AAF75819. Ref.2

Sequences

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

Last modified April 4, 2006. Version 3.
Checksum: 06A123CA9C0F7F1D

FASTA5,202575,600
        10         20         30         40         50         60 
MNCPVLSLGS GFLFQVIEML IFAYFASISL TESRGLFPRL ENVGAFKKVS IVPTQAVCGL 

        70         80         90        100        110        120 
PDRSTFCHSS AAAESIQFCT QRFCIQDCPY RSSHPTYTAL FSAGLSSCIT PDKNDLHPNA 

       130        140        150        160        170        180 
HSNSASFIFG NHKSCFSSPP SPKLMASFTL AVWLKPEQQG VMCVIEKTVD GQIVFKLTIS 

       190        200        210        220        230        240 
EKETMFYYRT VNGLQPPIKV MTLGRILVKK WIHLSVQVHQ TKISFFINGV EKDHTPFNAR 

       250        260        270        280        290        300 
TLSGSITDFA SGTVQIGQSL NGLEQFVGRM QDFRLYQVAL TNREILEVFS GDLLRLHAQS 

       310        320        330        340        350        360 
HCRCPGSHPR VHPLAQRYCI PNDAGDTADN RVSRLNPEAH PLSFVNDNDV GTSWVSNVFT 

       370        380        390        400        410        420 
NITQLNQGVT ISVDLENGQY QVFYIIIQFF SPQPTEIRIQ RKKENSLDWE DWQYFARNCG 

       430        440        450        460        470        480 
AFGMKNNGDL EKPDSVNCLQ LSNFTPYSRG NVTFSILTPG PNYRPGYNNF YNTPSLQEFV 

       490        500        510        520        530        540 
KATQIRFHFH GQYYTTETAV NLRHRYYAVD EITISGRCQC HGHADNCDTT SQPYRCLCSQ 

       550        560        570        580        590        600 
ESFTEGLHCD RCLPLYNDKP FRQGDQVYAF NCKPCQCNSH SKSCHYNISV DPFPFEHFRG 

       610        620        630        640        650        660 
GGGVCDDCEH NTTGRNCELC KDYFFRQVGA DPSAIDVCKP CDCDTVGTRN GSILCDQIGG 

       670        680        690        700        710        720 
QCNCKRHVSG RQCNQCQNGF YNLQELDPDG CSPCNCNTSG TVDGDITCHQ NSGQCKCKAN 

       730        740        750        760        770        780 
VIGLRCDHCN FGFKFLRSFN DVGCEPCQCN LHGSVNKFCN PHSGQCECKK EAKGLQCDTC 

       790        800        810        820        830        840 
RENFYGLDVT NCKACDCDTA GSLPGTVCNA KTGQCICKPN VEGRQCNKCL EGNFYLRQNN 

       850        860        870        880        890        900 
SFLCLPCNCD KTGTINGSLL CNKSTGQCPC KLGVTGLRCN QCEPHRYNLT IDNFQHCQMC 

       910        920        930        940        950        960 
ECDSLGTLPG TICDPISGQC LCVPNRQGRR CNQCQPGFYI SPGNATGCLP CSCHTTGAVN 

       970        980        990       1000       1010       1020 
HICNSLTGQC VCQDASIAGQ RCDQCKDHYF GFDPQTGRCQ PCNCHLSGAL NETCHLVTGQ 

      1030       1040       1050       1060       1070       1080 
CFCKQFVTGS KCDACVPSAS HLDVNNLLGC SKTPFQQPPP RGQVQSSSAI NLSWSPPDSP 

      1090       1100       1110       1120       1130       1140 
NAHWLTYSLL RDGFEIYTTE DQYPYSIQYF LDTDLLPYTK YSYYIETTNV HGSTRSVAVT 

      1150       1160       1170       1180       1190       1200 
YKTKPGVPEG NLTLSYIIPI GSDSVTLTWT TLSNQSGPIE KYILSCAPLA GGQPCVSYEG 

      1210       1220       1230       1240       1250       1260 
HETSATIWNL VPFAKYDFSV QACTSGGCLH SLPITVTTAQ APPQRLSPPK MQKISSTELH 

      1270       1280       1290       1300       1310       1320 
VEWSPPAELN GIIIRYELYM RRLRSTKETT SEESRVFQSS GWLSPHSFVE SANENALKPP 

      1330       1340       1350       1360       1370       1380 
QTMTTITGLE PYTKYEFRVL AVNMAGSVSS AWVSERTGES APVFMIPPSV FPLSSYSLNI 

      1390       1400       1410       1420       1430       1440 
SWEKPADNVT RGKVVGYDIN MLSEQSPQQS IPMAFSQLLH TAKSQELSYT VEGLKPYRIY 

      1450       1460       1470       1480       1490       1500 
EFTITLCNSV GCVTSASGAG QTLAAAPAQL RPPLVKGINS TTIHLRWFPP EELNGPSPIY 

      1510       1520       1530       1540       1550       1560 
QLERRESSLP ALMTTMMKGI RFIGNGYCKF PSSTHPVNTD FTGIKASFRT KVPEGLIVFA 

      1570       1580       1590       1600       1610       1620 
ASPGNQEEYF ALQLKKGRLY FLFDPQGSPV EVTTTNDHGK QYSDGKWHEI IAIRHQAFGQ 

      1630       1640       1650       1660       1670       1680 
ITLDGIYTGS SAILNGSTVI GDNTGVFLGG LPRSYTILRK DPEIIQKGFV GCLKDVHFMK 

      1690       1700       1710       1720       1730       1740 
NYNPSAIWEP LDWQSSEEQI NVYNSWEGCP ASLNEGAQFL GAGFLELHPY MFHGGMNFEI 

      1750       1760       1770       1780       1790       1800 
SFKFRTDQLN GLLLFVYNKD GPDFLAMELK SGILTFRLNT SLAFTQVDLL LGLSYCNGKW 

      1810       1820       1830       1840       1850       1860 
NKVIIKKEGS FISASVNGLM KHASESGDQP LVVNSPVYVG GIPQELLNSY QHLCLEQGFG 

      1870       1880       1890       1900       1910       1920 
GCMKDVKFTR GAVVNLASVS SGAVRVNLDG CLSTDSAVNC RGNDSILVYQ GKEQSVYEGG 

      1930       1940       1950       1960       1970       1980 
LQPFTEYLYR VIASHEGGSV YSDWSRGRTT GAAPQSVPTP SRVRSLNGYS IEVTWDEPVV 

      1990       2000       2010       2020       2030       2040 
RGVIEKYILK AYSEDSTRPP RMPSASAEFV NTSNLTGILT GLLPFKNYAV TLTACTLAGC 

      2050       2060       2070       2080       2090       2100 
TESSHALNIS TPQEAPQEVQ PPVAKSLPSS LLLSWNPPKK ANGIITQYCL YMDGRLIYSG 

      2110       2120       2130       2140       2150       2160 
SEENYIVTDL AVFTPHQFLL SACTHVGCTN SSWVLLYTAQ LPPEHVDSPV LTVLDSRTIH 

      2170       2180       2190       2200       2210       2220 
IQWKQPRKIS GILERYVLYM SNHTHDFTIW SVIYNSTELF QDHMLQYVLP GNKYLIKLGA 

      2230       2240       2250       2260       2270       2280 
CTGGGCTVSE ASEALTDEDI PEGVPAPKAH SYSPDSFNVS WTEPEYPNGV ITSYGLYLDG 

      2290       2300       2310       2320       2330       2340 
ILIHNSSELS YRAYGFAPWS LHSFRVQACT AKGCALGPLV ENRTLEAPPE GTVNVFVKTQ 

      2350       2360       2370       2380       2390       2400 
GSRKAHVRWE APFRPNGLLT HSVLFTGIFY VDPVGNNYTL LNVTKVMYSG EETNLWVLID 

      2410       2420       2430       2440       2450       2460 
GLVPFTNYTV QVNISNSQGS LITDPITIAM PPGAPDGVLP PRLSSATPTS LQVVWSTPAR 

      2470       2480       2490       2500       2510       2520 
NNAPGSPRYQ LQMRSGDSTH GFLELFSNPS ASLSYEVSDL QPYTEYMFRL VASNGFGSAH 

      2530       2540       2550       2560       2570       2580 
SSWIPFMTAE DKPGPVVPPI LLDVKSRMML VTWQHPRKSN GVITHYNIYL HGRLYLRTPG 

      2590       2600       2610       2620       2630       2640 
NVTNCTVMHL HPYTAYKFQV EACTSKGCSL SPESQTVWTL PGAPEGIPSP ELFSDTPTSV 

      2650       2660       2670       2680       2690       2700 
IISWQPPTHP NGLVENFTIE RRVKGKEEVT TLVTLPRSHS MRFIDKTSAL SPWTKYEYRV 

      2710       2720       2730       2740       2750       2760 
LMSTLHGGTN SSAWVEVTTR PSRPAGVQPP VVTVLEPDAV QVTWKPPLIQ NGDILSYEIH 

      2770       2780       2790       2800       2810       2820 
MPDPHITLTN VTSAVLSQKV THLIPFTNYS VTIVACSGGN GYLGGCTESL PTYVTTHPTV 

      2830       2840       2850       2860       2870       2880 
PQNVGPLSVI PLSESYVVIS WQPPSKPNGP NLRYELLRRK IQQPLASNPP EDLNRWHNIY 

      2890       2900       2910       2920       2930       2940 
SGTQWLYEDK GLSRFTTYEY MLFVHNSVGF TPSREVTVTT LAGLPERGAN LTASVLNHTA 

      2950       2960       2970       2980       2990       3000 
IDVRWAKPTV QDLQGEVEYY TLFWSSATSN DSLKILPDVN SHVIGHLKPN TEYWIFISVF 

      3010       3020       3030       3040       3050       3060 
NGVHSINSAG LHATTCDGEP QGMLPPEVVI INSTAVRVIW TSPSNPNGVV TEYSIYVNNK 

      3070       3080       3090       3100       3110       3120 
LYKTGMNVPG SFILRDLSPF TIYDIQVEVC TIYACVKSNG TQITTVEDTP SDIPTPTIRG 

      3130       3140       3150       3160       3170       3180 
ITSRSLQIDW VSPRKPNGII LGYDLLWKTW YPCAKTQKLV QDQSDELCKA VRCQKPESIC 

      3190       3200       3210       3220       3230       3240 
GHICYSSEAK VCCNGVLYNP KPGHRCCEEK YIPFVLNSTG VCCGGRIQEA QPNHQCCSGY 

      3250       3260       3270       3280       3290       3300 
YARILPGEVC CPDEQHNRVS VGIGDSCCGR MPYSTSGNQI CCAGRLHDGH GQKCCGRQIV 

      3310       3320       3330       3340       3350       3360 
SNDLECCGGE EGVVYNRLPG MFCCGQDYVN MSDTICCSAS SGESKAHIKK NDPVPVKCCE 

      3370       3380       3390       3400       3410       3420 
TELIPKSQKC CNGVGYNPLK YVCSDKISTG MMMKETKECR ILCPASMEAT EHCGRCDFNF 

      3430       3440       3450       3460       3470       3480 
TSHICTVIRG SHNSTGKASI EEMCSSAEET IHTGSVNTYS YTDVNLKPYM TYEYRISAWN 

      3490       3500       3510       3520       3530       3540 
SYGRGLSKAV RARTKEDVPQ GVSPPTWTKI DNLEDTIVLN WRKPIQSNGP IIYYILLRNG 

      3550       3560       3570       3580       3590       3600 
IERFRGTSLS FSDKEGIQPF QEYSYQLKAC TVAGCATSSK VVAATTQGVP ESILPPSITA 

      3610       3620       3630       3640       3650       3660 
LSAVALHLSW SVPEKSNGVI KEYQIRQVGK GLIHTDTTDR RQHTVTGLQP YTNYSFTLTA 

      3670       3680       3690       3700       3710       3720 
CTSAGCTSSE PFLGQTLQAA PEGVWVTPRH IIINSTTVEL YWSLPEKPNG LVSQYQLSRN 

      3730       3740       3750       3760       3770       3780 
GNLLFLGGSE EQNFTDKNLE PNSRYTYKLE VKTGGGSSAS DDYIVQTPMS TPEEIYPPYN 

      3790       3800       3810       3820       3830       3840 
ITVIGPYSIF VAWIPPGILI PEIPVEYNVL LNDGSVTPLA FSVGHHQSTL LENLTPFTQY 

      3850       3860       3870       3880       3890       3900 
EIRIQACQNG SCGVSSRMFV KTPEAAPMDL NSPVLKALGS ACIEIKWMPP EKPNGIIINY 

      3910       3920       3930       3940       3950       3960 
FIYRRPAGIE EESVLFVWSE GALEFMDEGD TLRPFTLYEY RVRACNSKGS VESLWSLTQT 

      3970       3980       3990       4000       4010       4020 
LEAPPQDFPA PWAQATSAHS VLLNWTKPES PNGIISHYRV VYQERPDDPT FNSPTVHAFT 

      4030       4040       4050       4060       4070       4080 
VKGTSHQAHL YGLEPFTTYR IGVVAANHAG EILSPWTLIQ TLESSPSGLR NFIVEQKENG 

      4090       4100       4110       4120       4130       4140 
RALLLQWSEP MRTNGVIKTY NIFSDGFLEY SGLNRQFLFR RLDPFTLYTL TLEACTRAGC 

      4150       4160       4170       4180       4190       4200 
AHSAPQPLWT DEAPPDSQLA PTVHSVKSTS VELSWSEPVN PNGKIIRYEV IRRCFEGKAW 

      4210       4220       4230       4240       4250       4260 
GNQTIQADEK IVFTEYNTER NTFMYNDTGL QPWTQCEYKI YTWNSAGHTC SSWNVVRTLQ 

      4270       4280       4290       4300       4310       4320 
APPEGLSPPV ISYVSMNPQK LLISWIPPEQ SNGIIQSYRL QRNEMLYPFS FDPVTFNYTD 

      4330       4340       4350       4360       4370       4380 
EELLPFSTYS YALQACTSGG CSTSKPTSIT TLEAAPSEVS PPDLWAVSAT QMNVCWSPPT 

      4390       4400       4410       4420       4430       4440 
VQNGKITKYL VRYDNKESLA GQGLCLLVSH LQPYSQYNFS LVACTNGGCT ASVSKSAWTM 

      4450       4460       4470       4480       4490       4500 
EALPENMDSP TLQVTGSESI EITWKPPRNP NGQIRSYELR RDGTIVYTGL ETRYRDFTLT 

      4510       4520       4530       4540       4550       4560 
PGVEYSYTVT ASNSQGGILS PLVKDRTSPS APSGMEPPKL QARGPQEILV NWDPPVRTNG 

      4570       4580       4590       4600       4610       4620 
DIINYTLFIR ELFERETKII HINTTHNSFG MQSYIVNQLK PFHRYEIRIQ ACTTLGCASS 

      4630       4640       4650       4660       4670       4680 
DWTFIQTPEI APLMQPPPHL EVQMAPGGFQ PTVSLLWTGP LQPNGKVLYY ELYRRQIATQ 

      4690       4700       4710       4720       4730       4740 
PRKSNPVLIY NGSSTSFIDS ELLPFTEYEY QVWAVNSAGK APSSWTWCRT GPAPPEGLRA 

      4750       4760       4770       4780       4790       4800 
PTFHVISSTQ AVVNISAPGK PNGIVSLYRL FSSSAHGAET VLSEGMATQQ TLHGLQAFTN 

      4810       4820       4830       4840       4850       4860 
YSIGVEACTC FNCCSKGPTA ELRTHPAPPS GLSSPQIGTL ASRTASFRWS PPMFPNGVIH 

      4870       4880       4890       4900       4910       4920 
SYELQFHVAC PPDSALPCTP SQIETKYTGL GQKASLGGLQ PYTTYKLRVV AHNEVGSTAS 

      4930       4940       4950       4960       4970       4980 
EWISFTTQKE LPQYRAPFSV DSNLSVVCVN WSDTFLLNGQ LKEYVLTDGG RRVYSGLDTT 

      4990       5000       5010       5020       5030       5040 
LYIPRTADKT FFFQVICTTD EGSVKTPLIQ YDTSTGLGLV LTTPGKKKGS RSKSTEFYSE 

      5050       5060       5070       5080       5090       5100 
LWFIVLMAML GLILLAIFLS LILQRKIHKE PYIRERPPLV PLQKRMSPLN VYPPGENHMG 

      5110       5120       5130       5140       5150       5160 
LADTKIPRSG TPVSIRSNRS ACVLRIPSQN QTSLTYSQGS LHRSVSQLMD IQDKKVLMDN 

      5170       5180       5190       5200 
SLWEAIMGHN SGLYVDEEDL MNAIKDFSSV TKERTTFTDT HL 

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Isoform 2 [UniParc].

Checksum: 434CD024FE19C0D6
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FASTA1,546171,074
Isoform 3 [UniParc].

Checksum: 9E201BC41FA9FC0E
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FASTA5,226578,275

References

« Hide 'large scale' references
[1]"Mutation of a gene encoding a protein with extracellular matrix motifs in Usher syndrome type IIa."
Eudy J.D., Weston M.D., Yao S.F., Hoover D.M., Rehm H.L., Ahmad I., Ma-Edmonds M., Yan D., Cheng J.J., Beisel K.W., Ayuso C., Cremers C., Davenport S., Moller C., Talmadge C.B., Tamayo M., Swaroop A., Morton C.C., Kimberling W.J., Sumegi J.
Science 280:1753-1757(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN USH2A, TISSUE SPECIFICITY, VARIANTS SER-479 AND LYS-1486.
[2]"Genomic structure and identification of novel mutations in usherin, the gene responsible for Usher syndrome type IIa."
Weston M.D., Eudy J.D., Fugita S., Yao S.-F., Usami S., Cremers C., Greenberg J., Ramesar R., Martini A., Moller C., Smith R.J., Sumegi J., Kimberling W.J.
Am. J. Hum. Genet. 66:1199-1210(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-1486, VARIANTS USH2A TYR-319; HIS-346 AND PHE-419.
[3]Erratum
Weston M.D., Eudy J.D., Fugita S., Yao S.-F., Usami S., Cremers C., Greenberg J., Ramesar R., Martini A., Moller C., Smith R.J., Sumegi J., Kimberling W.J.
Am. J. Hum. Genet. 66:2020-2020(2000)
[4]"Identification of 51 novel exons of the Usher syndrome type 2A (USH2A) gene that encode multiple conserved functional domains and that are mutated in patients with Usher syndrome type II."
Van Wijk E., Pennings R.J.E., Te Brinke H., Claassen A., Yntema H.G., Hoefsloot L.H., Cremers F.P.M., Cremers C.W.R.J., Kremer H.
Am. J. Hum. Genet. 74:738-744(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS USH2A CYS-4115 AND MET-4425.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Localization and expression of usherin: a novel basement membrane protein defective in people with Usher's syndrome type IIa."
Bhattacharya G., Miller C., Kimberling W.J., Jablonski M.M., Cosgrove D.
Hear. Res. 163:1-11(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Usherin expression is highly conserved in mouse and human tissues."
Pearsall N., Bhattacharya G., Wisecarver J., Adams J., Cosgrove D., Kimberling W.
Hear. Res. 174:55-63(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"A domain-specific usherin/collagen IV interaction may be required for stable integration into the basement membrane superstructure."
Bhattacharya G., Kalluri R., Orten D.J., Kimberling W.J., Cosgrove D.
J. Cell Sci. 117:233-242(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH COLLAGEN.
[9]"Evidence for functional importance of usherin/fibronectin interactions in retinal basement membranes."
Bhattacharya G., Cosgrove D.
Biochemistry 44:11518-11524(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FIBRONECTIN.
[10]"Usherin, the defective protein in Usher syndrome type IIA, is likely to be a component of interstereocilia ankle links in the inner ear sensory cells."
Adato A., Lefevre G., Delprat B., Michel V., Michalski N., Chardenoux S., Weil D., El-Amraoui A., Petit C.
Hum. Mol. Genet. 14:3921-3932(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3).
[11]"Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2."
Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K., te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H., Wolfrum U.
Hum. Mol. Genet. 14:3933-3943(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USH1C.
[12]"The DFNB31 gene product whirlin connects to the Usher protein network in the cochlea and retina by direct association with USH2A and VLGR1."
van Wijk E., van der Zwaag B., Peters T., Zimmermann U., Te Brinke H., Kersten F.F.J., Maerker T., Aller E., Hoefsloot L.H., Cremers C.W.R.J., Cremers F.P.M., Wolfrum U., Knipper M., Roepman R., Kremer H.
Hum. Mol. Genet. 15:751-765(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WHRN.
[13]"The molecular genetics of Usher syndrome."
Ahmed Z.M., Riazuddin S., Riazuddin S., Wilcox E.R.
Clin. Genet. 63:431-444(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[14]"Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein."
van Wijk E., Kersten F.F.J., Kartono A., Mans D.A., Brandwijk K., Letteboer S.J.F., Peters T.A., Maerker T., Yan X., Cremers C.W.R.J., Cremers F.P.M., Wolfrum U., Roepman R., Kremer H.
Hum. Mol. Genet. 18:51-64(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NINL.
[15]"PDZD7 is a modifier of retinal disease and a contributor to digenic Usher syndrome."
Ebermann I., Phillips J.B., Liebau M.C., Koenekoop R.K., Schermer B., Lopez I., Schafer E., Roux A.F., Dafinger C., Bernd A., Zrenner E., Claustres M., Blanco B., Nurnberg G., Nurnberg P., Ruland R., Westerfield M., Benzing T., Bolz H.J.
J. Clin. Invest. 120:1812-1823(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZD7, VARIANT USH2A ILE-4439.
[16]"Missense mutation in the USH2A gene: association with recessive retinitis pigmentosa without hearing loss."
Rivolta C., Sweklo E.A., Berson E.L., Dryja T.P.
Am. J. Hum. Genet. 66:1975-1978(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP39 PHE-759.
[17]"Identification of novel USH2A mutations: implications for the structure of USH2A protein."
Dreyer B., Tranebjaerg L., Rosenberg T., Weston M.D., Kimberling W.J., Nilssen O.
Eur. J. Hum. Genet. 8:500-506(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A TYR-163; MET-230; ARG-536 AND ARG-713.
[18]"Three novel mutations and twelve polymorphisms identified in the USH2A gene in Israeli USH2 families."
Adato A., Weston M.D., Berry A., Kimberling W.J., Bonne-Tamir A.
Hum. Mutat. 15:388-388(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A TRP-334 AND MET-1515, VARIANTS ASP-478; VAL-644 AND LYS-1486.
[19]"Spectrum of mutations in USH2A in British patients with Usher syndrome type II."
Leroy B.P., Aragon-Martin J.A., Weston M.D., Bessant D.A.R., Willis C., Webster A.R., Bird A.C., Kimberling W.J., Payne A.M., Bhattacharya S.S.
Exp. Eye Res. 72:503-509(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A GLU-218; MET-230 AND VAL-555.
[20]"Paternal uniparental heterodisomy with partial isodisomy of chromosome 1 in a patient with retinitis pigmentosa without hearing loss and a missense mutation in the Usher syndrome type II gene USH2A."
Rivolta C., Berson E.L., Dryja T.P.
Arch. Ophthalmol. 120:1566-1571(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP39 PHE-759.
[21]"Mutations in myosin VIIA (MYO7A) and usherin (USH2A) in Spanish patients with Usher syndrome types I and II, respectively."
Najera C., Beneyto M., Blanca J., Aller E., Fontcuberta A., Millan J.M., Ayuso C.
Hum. Mutat. 20:76-77(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT USH2A ARG-713, VARIANT RP39 PHE-759.
[22]"Mutations in USH2A in Spanish patients with autosomal recessive retinitis pigmentosa: high prevalence and phenotypic variation."
Bernal S., Ayuso C., Antinolo G., Gimenez A., Borrego S., Trujillo M.J., Marcos I., Calaf M., Del Rio E., Baiget M.
J. Med. Genet. 40:E8-E8(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A PRO-610 AND ARG-761.
[23]"Mutational spectrum in Usher syndrome type II."
Ouyang X.M., Yan D., Hejtmancik J.F., Jacobson S.G., Li A.R., Du L.L., Angeli S., Kaiser M., Balkany T., Liu X.Z.
Clin. Genet. 65:288-293(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A TRP-334; HIS-346 AND THR-357, VARIANTS SER-479 AND VAL-644.
[24]Erratum
Ouyang X.M., Yan D., Hejtmancik J.F., Jacobson S.G., Li A.R., Du L.L., Angeli S., Kaiser M., Balkany T., Liu X.Z.
Clin. Genet. 65:433-433(2004)
[25]"Genetic analysis of 2299delG and C759F mutations (USH2A) in patients with visual and/or auditory impairments."
Aller E., Najera C., Millan J.M., Oltra J.S., Perez-Garrigues H., Vilela C., Navea A., Beneyto M.
Eur. J. Hum. Genet. 12:407-410(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT USH2A SER-303, VARIANT RP PHE-759.
[26]"Comprehensive screening of the USH2A gene in Usher syndrome type II and non-syndromic recessive retinitis pigmentosa."
Seyedahmadi B.J., Rivolta C., Keene J.A., Berson E.L., Dryja T.P.
Exp. Eye Res. 79:167-173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A ILE-307; ILE-391; PHE-419; CYS-464; VAL-516 THR-517; SER-575; ASN-587 DEL AND LEU-1059, VARIANTS RP39/USH2A ASP-478 AND PHE-759, VARIANTS RP39 LEU-739; ASN-911 AND ARG-1470, VARIANTS THR-125; MET-230; ARG-268; PHE-365; VAL-644; ARG-713; VAL-1047 AND LYS-1486.
[27]"USH2A mutation analysis in 70 Dutch families with Usher syndrome type II."
Pennings R.J.E., Te Brinke H., Weston M.D., Claassen A., Orten D.J., Weekamp H., Van Aarem A., Huygen P.L.M., Deutman A.F., Hoefsloot L.H., Cremers F.P.M., Cremers C.W.R.J., Kimberling W.J., Kremer H.
Hum. Mutat. 24:185-185(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A HIS-346; PHE-419; ARG-536 AND ARG-713.
[28]"Clinical and genetic studies in Spanish patients with Usher syndrome type II: description of new mutations and evidence for a lack of genotype-phenotype correlation."
Bernal S., Meda C., Solans T., Ayuso C., Garcia-Sandoval B., Valverde D., Del Rio E., Baiget M.
Clin. Genet. 68:204-214(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP39 PHE-759, VARIANTS THR-125; ASP-478; VAL-644; GLU-703; TYR-841 AND LYS-1486.
[29]"Identification of 14 novel mutations in the long isoform of USH2A in Spanish patients with Usher syndrome type II."
Aller E., Jaijo T., Beneyto M., Najera C., Oltra S., Ayuso C., Baiget M., Carballo M., Antinolo G., Valverde D., Moreno F., Vilela C., Collado D., Perez-Garrigues H., Navea A., Millan J.M.
J. Med. Genet. 43:E55-E55(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A ASP-2249; HIS-2354; ARG-3251; ARG-3267; TYR-3472 INS; MET-3571; MET-4337 AND LEU-4818, VARIANTS ARG-713; PHE-1572; THR-1665; THR-2106; THR-2169; ALA-2238; GLN-2875; PHE-2886; SER-3099; ASN-3144; ALA-3411 AND VAL-3868.
[30]"Novel USH2A mutations in Israeli patients with retinitis pigmentosa and Usher syndrome type 2."
Kaiserman N., Obolensky A., Banin E., Sharon D.
Arch. Ophthalmol. 125:219-224(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP39 GLY-4674, VARIANTS THR-125; ASP-478; VAL-644; ARG-713; LYS-1486; THR-1665; THR-2106; THR-2169; GLN-2875; SER-3099; ASN-3144 AND MET-3335.
[31]"Molecular and in silico analyses of the full-length isoform of usherin identify new pathogenic alleles in Usher type II patients."
Baux D., Larrieu L., Blanchet C., Hamel C., Ben Salah S., Vielle A., Gilbert-Dussardier B., Holder M., Calvas P., Philip N., Edery P., Bonneau D., Claustres M., Malcolm S., Roux A.-F.
Hum. Mutat. 28:781-789(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A GLU-218; PHE-280; LYS-284; TRP-334; GLN-334; HIS-346; ILE-352; PHE-759; GLU-1833; SER-2795; ARG-3282; MET-3571; GLU-3895; MET-3976; CYS-4115 AND MET-4425, VARIANT PHE-1572.
[32]"Spectrum of USH2A mutations in Scandinavian patients with Usher syndrome type II."
Dreyer B., Brox V., Tranebjaerg L., Rosenberg T., Sadeghi A.M., Moeller C., Nilssen O.
Hum. Mutat. 29:451-451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS USH2A TYR-163; ARG-268; CYS-303; TRP-334; HIS-346; ILE-352; ARG-536; PHE-759; LEU-1212; ASP-2265-ASP-TYR-2266 DELINS ASP; GLY-3124; THR-3504; ARG-3521; ILE-4054; ARG-4232; ILE-4439; CYS-4487; HIS-4592 AND ARG-4795, VARIANTS THR-125; MET-230; ASP-478; SER-595; VAL-644; ARG-713; PRO-1349; LYS-1486; PHE-1572; THR-1665; CYS-1757; ASN-2080; ASN-2086; THR-2106; THR-2169; ALA-2238; HIS-2292; ALA-2562; GLN-2875; PHE-2886; LYS-3088; SER-3099; ALA-3115; ASN-3144; ASP-3199; ALA-3411; LEU-3590; ILE-3835; VAL-3868; THR-3893; CYS-4115; LEU-4433; VAL-4624 AND TRP-5031.
[33]"Exome sequencing reveals a homozygous SYT14 mutation in adult-onset, autosomal-recessive spinocerebellar ataxia with psychomotor retardation."
Doi H., Yoshida K., Yasuda T., Fukuda M., Fukuda Y., Morita H., Ikeda S., Kato R., Tsurusaki Y., Miyake N., Saitsu H., Sakai H., Miyatake S., Shiina M., Nukina N., Koyano S., Tsuji S., Kuroiwa Y., Matsumoto N.
Am. J. Hum. Genet. 89:320-327(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-4203.
[34]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-453.
[35]"Next-generation genetic testing for retinitis pigmentosa."
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. expand/collapse author list , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.
Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RP39 PHE-419; PHE-759; CYS-1859; HIS-2460; TYR-3358; ARG-3669; CYS-4115; HIS-4192 AND MET-4425.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055580 mRNA. Translation: AAC23748.2.
AF091889 expand/collapse EMBL AC list , AF091873, AF091875, AF091876, AF091874, AF091877, AF091879, AF091881, AF091883, AF091888, AF091887, AF091886, AF091885, AF091884, AF091882, AF091880, AF091878 Genomic DNA. Translation: AAF75819.1.
AY481573 mRNA. Translation: AAS47698.1.
AL445650, AC138024, AL358858 Genomic DNA. Translation: CAH70620.1.
AL358858, AC138024, AL445650 Genomic DNA. Translation: CAH71587.1.
AL358858 expand/collapse EMBL AC list , AC092799, AC093581, AC119429, AC138024, AL139259, AL358452, AL445650, AL513305 Genomic DNA. Translation: CAH71588.1.
AL513305 expand/collapse EMBL AC list , AC138024, AC119429, AC093581, AC092799, AL445650, AL358858, AL358452, AL139259 Genomic DNA. Translation: CAH73621.1.
AL139259 expand/collapse EMBL AC list , AL513305, AL445650, AL358858, AL358452, AC138024, AC119429, AC093581, AC092799 Genomic DNA. Translation: CAI23041.1.
AL358452 expand/collapse EMBL AC list , AL513305, AL445650, AL358858, AL139259, AC138024, AC119429, AC093581, AC092799 Genomic DNA. Translation: CAI19189.1.
AL445650 expand/collapse EMBL AC list , AC092799, AC093581, AC119429, AC138024, AL139259, AL513305, AL358858, AL358452 Genomic DNA. Translation: CAH70621.1.
RefSeqNP_009054.5. NM_007123.5.
NP_996816.2. NM_206933.2.
UniGeneHs.655974.

3D structure databases

ProteinModelPortalO75445.
SMRO75445. Positions 326-1052, 1522-1903, 2500-2718, 3415-3574, 3729-4057, 4262-4675.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113242. 1 interaction.
STRING9606.ENSP00000305941.

PTM databases

PhosphoSiteO75445.

Proteomic databases

PaxDbO75445.
PRIDEO75445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307340; ENSP00000305941; ENSG00000042781. [O75445-1]
ENST00000366942; ENSP00000355909; ENSG00000042781. [O75445-2]
ENST00000366943; ENSP00000355910; ENSG00000042781. [O75445-3]
GeneID7399.
KEGGhsa:7399.
UCSCuc001hku.1. human. [O75445-1]
uc001hkv.3. human. [O75445-2]

Organism-specific databases

CTD7399.
GeneCardsGC01M215796.
H-InvDBHIX0028527.
HGNCHGNC:12601. USH2A.
MIM276901. phenotype.
608400. gene.
613809. phenotype.
neXtProtNX_O75445.
Orphanet791. Retinitis pigmentosa.
231178. Usher syndrome type 2.
PharmGKBPA37228.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245744.
HOGENOMHOG000124780.
HOVERGENHBG094138.
OMAEIRIQAC.
OrthoDBEOG783MTD.
PhylomeDBO75445.
TreeFamTF330287.

Gene expression databases

BgeeO75445.
CleanExHS_USH2A.
GenevestigatorO75445.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
2.60.40.10. 35 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR002049. EGF_laminin.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR006558. LamG-like.
IPR001791. Laminin_G.
IPR008211. Laminin_N.
IPR026915. USH2A.
[Graphical view]
PANTHERPTHR10574:SF170. PTHR10574:SF170. 1 hit.
PfamPF00041. fn3. 20 hits.
PF00053. Laminin_EGF. 10 hits.
PF02210. Laminin_G_2. 2 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 10 hits.
SM00060. FN3. 33 hits.
SM00282. LamG. 2 hits.
SM00560. LamGL. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 23 hits.
SSF49899. SSF49899. 3 hits.
PROSITEPS00022. EGF_1. 7 hits.
PS01248. EGF_LAM_1. 7 hits.
PS50027. EGF_LAM_2. 10 hits.
PS50853. FN3. 35 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUSH2A.
GenomeRNAi7399.
NextBio28962.
PROO75445.
SOURCESearch...

Entry information

Entry nameUSH2A_HUMAN
AccessionPrimary (citable) accession number: O75445
Secondary accession number(s): Q5VVM9, Q6S362, Q9NS27
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 114 of the entry and version 3 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM