O75445 (USH2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Usherin

Alternative name(s):
Usher syndrome type IIa protein
Usher syndrome type-2A protein

Gene names

Name:

USH2A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	5202 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 projection › stereocilium 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 process	Hearing Sensory transduction Vision
Cellular component	Cell membrane Cell projection Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness Disease mutation Retinitis pigmentosa Usher syndrome
Domain	Laminin EGF-like domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	hair 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 sound Inferred from mutant phenotype PubMed 10090909. Source: HGNC
Cellular_component	apical 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW stereocilia ankle link complex Inferred from sequence or structural similarity. Source: BHF-UCL stereocilium membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	collagen 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 5202	5171	Usherin		PRO_0000229804
Regions
	Topological domain	32 – 5042	5011	Extracellular Potential
	Transmembrane	5043 – 5063	21	Helical; Potential
	Topological domain	5064 – 5202	139	Cytoplasmic Potential
	Domain	271 – 517	247	Laminin N-terminal
	Domain	518 – 574	57	Laminin EGF-like 1
	Domain	575 – 640	66	Laminin EGF-like 2
	Domain	641 – 693	53	Laminin EGF-like 3
	Domain	694 – 746	53	Laminin EGF-like 4
	Domain	747 – 794	48	Laminin EGF-like 5
	Domain	795 – 846	52	Laminin EGF-like 6
	Domain	847 – 899	53	Laminin EGF-like 7
	Domain	900 – 950	51	Laminin EGF-like 8
	Domain	951 – 1001	51	Laminin EGF-like 9
	Domain	1002 – 1052	51	Laminin EGF-like 10
	Domain	1058 – 1143	86	Fibronectin type-III 1
	Domain	1145 – 1238	94	Fibronectin type-III 2
	Domain	1242 – 1357	116	Fibronectin type-III 3
	Domain	1367 – 1462	96	Fibronectin type-III 4
	Domain	1517 – 1709	193	Laminin G-like 1
	Domain	1714 – 1891	178	Laminin G-like 2
	Domain	1871 – 1949	79	Fibronectin type-III 5
	Domain	1954 – 2051	98	Fibronectin type-III 6
	Domain	2052 – 2138	87	Fibronectin type-III 7
	Domain	2142 – 2236	95	Fibronectin type-III 8
	Domain	2241 – 2325	85	Fibronectin type-III 9
	Domain	2328 – 2432	105	Fibronectin type-III 10
	Domain	2435 – 2528	94	Fibronectin type-III 11
	Domain	2533 – 2619	87	Fibronectin type-III 12
	Domain	2621 – 2718	98	Fibronectin type-III 13
	Domain	2724 – 2812	89	Fibronectin type-III 14
	Domain	2821 – 2920	100	Fibronectin type-III 15
	Domain	2925 – 3015	91	Fibronectin type-III 16
	Domain	3020 – 3105	86	Fibronectin type-III 17
	Domain	3110 – 3200	91	Fibronectin type-III 18
	Domain	3404 – 3494	91	Fibronectin type-III 19
	Domain	3499 – 3585	87	Fibronectin type-III 20
	Domain	3590 – 3676	87	Fibronectin type-III 21
	Domain	3677 – 3767	91	Fibronectin type-III 22
	Domain	3768 – 3862	95	Fibronectin type-III 23
	Domain	3863 – 3960	98	Fibronectin type-III 24
	Domain	3961 – 4062	102	Fibronectin type-III 25
	Domain	4066 – 4150	85	Fibronectin type-III 26
	Domain	4154 – 4258	105	Fibronectin type-III 27
	Domain	4265 – 4351	87	Fibronectin type-III 28
	Domain	4356 – 4439	84	Fibronectin type-III 29
	Domain	4444 – 4528	85	Fibronectin type-III 30
	Domain	4529 – 4627	99	Fibronectin type-III 31
	Domain	4633 – 4730	98	Fibronectin type-III 32
	Domain	4732 – 4825	94	Fibronectin type-III 33
	Domain	4826 – 4927	102	Fibronectin type-III 34
	Domain	4928 – 5014	87	Fibronectin type-III 35
	Motif	5200 – 5202	3	PDZ-binding
Amino acid modifications
	Glycosylation	361	1	N-linked (GlcNAc...) Potential
	Glycosylation	451	1	N-linked (GlcNAc...) Potential
	Glycosylation	587	1	N-linked (GlcNAc...) Potential
	Glycosylation	611	1	N-linked (GlcNAc...) Potential
	Glycosylation	650	1	N-linked (GlcNAc...) Potential
	Glycosylation	697	1	N-linked (GlcNAc...) Potential
	Glycosylation	839	1	N-linked (GlcNAc...) Potential
	Glycosylation	856	1	N-linked (GlcNAc...) Potential
	Glycosylation	862	1	N-linked (GlcNAc...) Potential
	Glycosylation	888	1	N-linked (GlcNAc...) Potential
	Glycosylation	944	1	N-linked (GlcNAc...) Potential
	Glycosylation	1011	1	N-linked (GlcNAc...) Potential
	Glycosylation	1071	1	N-linked (GlcNAc...) Potential
	Glycosylation	1151	1	N-linked (GlcNAc...) Potential
	Glycosylation	1174	1	N-linked (GlcNAc...) Potential
	Glycosylation	1379	1	N-linked (GlcNAc...) Potential
	Glycosylation	1388	1	N-linked (GlcNAc...) Potential
	Glycosylation	1479	1	N-linked (GlcNAc...) Potential
	Glycosylation	1635	1	N-linked (GlcNAc...) Potential
	Glycosylation	1779	1	N-linked (GlcNAc...) Potential
	Glycosylation	1903	1	N-linked (GlcNAc...) Potential
	Glycosylation	2011	1	N-linked (GlcNAc...) Potential
	Glycosylation	2014	1	N-linked (GlcNAc...) Potential
	Glycosylation	2048	1	N-linked (GlcNAc...) Potential
	Glycosylation	2130	1	N-linked (GlcNAc...) Potential
	Glycosylation	2182	1	N-linked (GlcNAc...) Potential
	Glycosylation	2195	1	N-linked (GlcNAc...) Potential
	Glycosylation	2258	1	N-linked (GlcNAc...) Potential
	Glycosylation	2285	1	N-linked (GlcNAc...) Potential
	Glycosylation	2322	1	N-linked (GlcNAc...) Potential
	Glycosylation	2377	1	N-linked (GlcNAc...) Potential
	Glycosylation	2382	1	N-linked (GlcNAc...) Potential
	Glycosylation	2407	1	N-linked (GlcNAc...) Potential
	Glycosylation	2413	1	N-linked (GlcNAc...) Potential
	Glycosylation	2581	1	N-linked (GlcNAc...) Potential
	Glycosylation	2584	1	N-linked (GlcNAc...) Potential
	Glycosylation	2656	1	N-linked (GlcNAc...) Potential
	Glycosylation	2710	1	N-linked (GlcNAc...) Potential
	Glycosylation	2770	1	N-linked (GlcNAc...) Potential
	Glycosylation	2788	1	N-linked (GlcNAc...) Potential
	Glycosylation	2930	1	N-linked (GlcNAc...) Potential
	Glycosylation	2937	1	N-linked (GlcNAc...) Potential
	Glycosylation	2970	1	N-linked (GlcNAc...) Potential
	Glycosylation	3032	1	N-linked (GlcNAc...) Potential
	Glycosylation	3099	1	N-linked (GlcNAc...) Potential
	Glycosylation	3217	1	N-linked (GlcNAc...) Potential
	Glycosylation	3330	1	N-linked (GlcNAc...) Potential
	Glycosylation	3419	1	N-linked (GlcNAc...) Potential
	Glycosylation	3433	1	N-linked (GlcNAc...) Potential
	Glycosylation	3653	1	N-linked (GlcNAc...) Potential
	Glycosylation	3694	1	N-linked (GlcNAc...) Potential
	Glycosylation	3733	1	N-linked (GlcNAc...) Potential
	Glycosylation	3780	1	N-linked (GlcNAc...) Potential
	Glycosylation	3849	1	N-linked (GlcNAc...) Potential
	Glycosylation	3984	1	N-linked (GlcNAc...) Potential
	Glycosylation	4202	1	N-linked (GlcNAc...) Potential
	Glycosylation	4226	1	N-linked (GlcNAc...) Potential
	Glycosylation	4317	1	N-linked (GlcNAc...) Potential
	Glycosylation	4418	1	N-linked (GlcNAc...) Potential
	Glycosylation	4564	1	N-linked (GlcNAc...) Potential
	Glycosylation	4583	1	N-linked (GlcNAc...) Potential
	Glycosylation	4691	1	N-linked (GlcNAc...) Potential
	Glycosylation	4754	1	N-linked (GlcNAc...) Potential
	Glycosylation	4800	1	N-linked (GlcNAc...) Potential
	Glycosylation	4943	1	N-linked (GlcNAc...) Potential
	Glycosylation	4950	1	N-linked (GlcNAc...) Potential
	Disulfide bond	518 ↔ 527		By similarity
	Disulfide bond	520 ↔ 536		By similarity
	Disulfide bond	538 ↔ 549		By similarity
	Disulfide bond	552 ↔ 572		By similarity
	Disulfide bond	575 ↔ 584		By similarity
	Disulfide bond	577 ↔ 605		By similarity
	Disulfide bond	608 ↔ 617		By similarity
	Disulfide bond	620 ↔ 638		By similarity
	Disulfide bond	641 ↔ 655		By similarity
	Disulfide bond	643 ↔ 662		By similarity
	Disulfide bond	664 ↔ 673		By similarity
	Disulfide bond	676 ↔ 691		By similarity
	Disulfide bond	694 ↔ 708		By similarity
	Disulfide bond	696 ↔ 715		By similarity
	Disulfide bond	717 ↔ 726		By similarity
	Disulfide bond	729 ↔ 744		By similarity
	Disulfide bond	747 ↔ 759		By similarity
	Disulfide bond	749 ↔ 766		By similarity
	Disulfide bond	768 ↔ 777		By similarity
	Disulfide bond	780 ↔ 792		By similarity
	Disulfide bond	795 ↔ 808		By similarity
	Disulfide bond	797 ↔ 815		By similarity
	Disulfide bond	817 ↔ 826		By similarity
	Disulfide bond	829 ↔ 844		By similarity
	Disulfide bond	847 ↔ 861		By similarity
	Disulfide bond	849 ↔ 868		By similarity
	Disulfide bond	870 ↔ 879		By similarity
	Disulfide bond	882 ↔ 897		By similarity
	Disulfide bond	900 ↔ 913		By similarity
	Disulfide bond	902 ↔ 920		By similarity
	Disulfide bond	922 ↔ 931		By similarity
	Disulfide bond	934 ↔ 948		By similarity
	Disulfide bond	951 ↔ 963		By similarity
	Disulfide bond	953 ↔ 970		By similarity
	Disulfide bond	972 ↔ 982		By similarity
	Disulfide bond	985 ↔ 999		By similarity
	Disulfide bond	1002 ↔ 1014		By similarity
	Disulfide bond	1004 ↔ 1021		By similarity
	Disulfide bond	1023 ↔ 1032		By similarity
	Disulfide bond	1035 ↔ 1050		By similarity
	Disulfide bond	1672 ↔ 1709		By similarity
	Disulfide bond	1862 ↔ 1891		By similarity
	Disulfide bond	3371 ↔ 3444		By similarity
	Disulfide bond	3399 ↔ 3425		By similarity
Natural variations
	Alternative sequence	1544 – 1546	3	IKA → KCV in isoform 2.		VSP_017771
	Alternative sequence	1547 – 5202	3656	Missing in isoform 2.		VSP_017772
	Alternative sequence	5099	1	M → MFDSVADISDVSSNVTLKSY TMHFE in isoform 3.		VSP_017773
	Natural variant	125	1	A → T. Ref.26 Ref.28 Ref.30 Ref.32 Corresponds to variant rs10779261 [ dbSNP | Ensembl ].		VAR_025760
	Natural variant	163	1	C → Y in USH2A. Ref.17 Ref.32		VAR_025761
	Natural variant	218	1	V → E in USH2A. Ref.19 Ref.31		VAR_025762
	Natural variant	230	1	V → 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 variant	268	1	G → R in USH2A; uncertain pathogenicity. Ref.26 Ref.32		VAR_054557
	Natural variant	280	1	L → F in USH2A. Ref.31		VAR_054558
	Natural variant	284	1	E → K in USH2A. Ref.31		VAR_054559
	Natural variant	303	1	R → C in USH2A. Ref.32		VAR_054560
	Natural variant	303	1	R → S in USH2A. Ref.25		VAR_054561
	Natural variant	307	1	S → I in USH2A; uncertain pathogenicity. Ref.26		VAR_054562
	Natural variant	319	1	C → Y in USH2A. Ref.2		VAR_025764
	Natural variant	334	1	R → Q in USH2A. Ref.31		VAR_054563
	Natural variant	334	1	R → W in USH2A. Ref.18 Ref.23 Ref.31 Ref.32		VAR_025765
	Natural variant	346	1	N → H in USH2A. Ref.2 Ref.23 Ref.27 Ref.31 Ref.32		VAR_025766
	Natural variant	352	1	T → I in USH2A. Ref.31 Ref.32		VAR_054564
	Natural variant	357	1	N → T in USH2A. Ref.23		VAR_054565
	Natural variant	365	1	L → F. Ref.26		VAR_054566
	Natural variant	391	1	S → I in USH2A; uncertain pathogenicity. Ref.26		VAR_054567
	Natural variant	419	1	C → F in USH2A and RP39. Ref.2 Ref.26 Ref.27 Ref.35		VAR_025767
	Natural variant	453	1	T → I Found in a renal cell carcinoma sample; somatic mutation. Ref.34		VAR_064761
	Natural variant	464	1	R → C in USH2A; uncertain pathogenicity. Ref.26		VAR_054568
	Natural variant	478	1	E → D in RP39 and USH2A; uncertain pathogenicity. Ref.18 Ref.26 Ref.28 Ref.30 Ref.32 Corresponds to variant rs35730265 [ dbSNP | Ensembl ].		VAR_025768
	Natural variant	479	1	F → S. Ref.1 Ref.23		VAR_054569
	Natural variant	516	1	G → V in USH2A; uncertain pathogenicity. Ref.26		VAR_054570
	Natural variant	517	1	R → T in USH2A; uncertain pathogenicity. Ref.26		VAR_054571
	Natural variant	536	1	C → R in USH2A; abolishes interaction with collagen IV. Ref.17 Ref.27 Ref.32		VAR_025769
	Natural variant	555	1	L → V in USH2A. Ref.19 Corresponds to variant rs35818432 [ dbSNP | Ensembl ].		VAR_025770
	Natural variant	575	1	C → S in USH2A; uncertain pathogenicity. Ref.26		VAR_054572
	Natural variant	587	1	Missing in USH2A; uncertain pathogenicity. Ref.26		VAR_054573
	Natural variant	595	1	F → S. Ref.32		VAR_054574
	Natural variant	610	1	H → P in USH2A. Ref.22		VAR_025771
	Natural variant	644	1	D → V. Ref.18 Ref.23 Ref.26 Ref.28 Ref.30 Ref.32 Corresponds to variant rs1805048 [ dbSNP | Ensembl ].		VAR_025772
	Natural variant	703	1	D → E. Ref.28		VAR_025773
	Natural variant	713	1	G → R in USH2A; abolishes interaction with collagen IV; uncertain pathogenicity. Ref.17 Ref.21 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32 Corresponds to variant rs696723 [ dbSNP | Ensembl ].		VAR_025774
	Natural variant	739	1	F → L in RP39; uncertain pathogenicity. Ref.26		VAR_054575
	Natural variant	759	1	C → F in RP39 and USH2A. Ref.16 Ref.20 Ref.21 Ref.25 Ref.26 Ref.28 Ref.31 Ref.32 Ref.35		VAR_025775
	Natural variant	761	1	P → R in USH2A. Ref.22		VAR_025776
	Natural variant	841	1	S → Y. Ref.28		VAR_025777
	Natural variant	911	1	T → N in RP39; uncertain pathogenicity. Ref.26		VAR_054576
	Natural variant	1047	1	L → V. Ref.26		VAR_054577
	Natural variant	1059	1	P → L in USH2A; uncertain pathogenicity. Ref.26		VAR_054578
	Natural variant	1212	1	P → L in USH2A. Ref.32		VAR_054579
	Natural variant	1349	1	S → P. Ref.32		VAR_054580
	Natural variant	1470	1	L → R in RP39; uncertain pathogenicity. Ref.26		VAR_054581
	Natural variant	1486	1	R → K. Ref.1 Ref.2 Ref.18 Ref.26 Ref.28 Ref.30 Ref.32 Corresponds to variant rs1805049 [ dbSNP | Ensembl ].		VAR_025778
	Natural variant	1515	1	T → M in USH2A. Ref.18		VAR_025779
	Natural variant	1572	1	L → F. Ref.29 Ref.31 Ref.32		VAR_054582
	Natural variant	1665	1	I → T. Ref.29 Ref.30 Ref.32 Corresponds to variant rs56222536 [ dbSNP | Ensembl ].		VAR_038362
	Natural variant	1757	1	Y → C. Ref.32		VAR_054583
	Natural variant	1833	1	V → E in USH2A. Ref.31		VAR_054584
	Natural variant	1859	1	F → C in RP39. Ref.35		VAR_068354
	Natural variant	2080	1	K → N. Ref.32		VAR_054585
	Natural variant	2086	1	T → N. Ref.32		VAR_054586
	Natural variant	2106	1	I → T. Ref.29 Ref.30 Ref.32 Corresponds to variant rs6657250 [ dbSNP | Ensembl ].		VAR_038363
	Natural variant	2169	1	I → T. Ref.29 Ref.30 Ref.32 Corresponds to variant rs10864219 [ dbSNP | Ensembl ].		VAR_038364
	Natural variant	2238	1	E → A. Ref.29 Ref.32 Corresponds to variant rs41277212 [ dbSNP | Ensembl ].		VAR_054587
	Natural variant	2249	1	A → D in USH2A. Ref.29		VAR_054588
	Natural variant	2265 – 2266	2	EY → D in USH2A. Ref.32		VAR_054589
	Natural variant	2292	1	R → H. Ref.32 Corresponds to variant rs41277210 [ dbSNP | Ensembl ].		VAR_054590
	Natural variant	2354	1	R → H in USH2A. Ref.29		VAR_054591
	Natural variant	2460	1	R → H in RP39. Ref.35		VAR_068355
	Natural variant	2562	1	V → A. Ref.32 Corresponds to variant rs56385601 [ dbSNP | Ensembl ].		VAR_054592
	Natural variant	2795	1	A → S in USH2A. Ref.31		VAR_054593
	Natural variant	2820	1	V → I. Corresponds to variant rs59174500 [ dbSNP | Ensembl ].		VAR_061350
	Natural variant	2875	1	R → Q. Ref.29 Ref.30 Ref.32 Corresponds to variant rs12118814 [ dbSNP | Ensembl ].		VAR_038365
	Natural variant	2886	1	L → F. Ref.29 Ref.32 Corresponds to variant rs41277200 [ dbSNP | Ensembl ].		VAR_054594
	Natural variant	3088	1	E → K. Ref.32 Corresponds to variant rs56056328 [ dbSNP | Ensembl ].		VAR_054595
	Natural variant	3099	1	N → S. Ref.29 Ref.30 Ref.32 Corresponds to variant rs41277194 [ dbSNP | Ensembl ].		VAR_038366
	Natural variant	3115	1	T → A. Ref.32 Corresponds to variant rs56032526 [ dbSNP | Ensembl ].		VAR_054596
	Natural variant	3124	1	R → G in USH2A; uncertain pathogenicity. Ref.32		VAR_054597
	Natural variant	3144	1	D → N. Ref.29 Ref.30 Ref.32 Corresponds to variant rs11120645 [ dbSNP | Ensembl ].		VAR_038367
	Natural variant	3199	1	N → D. Ref.32 Corresponds to variant rs4129843 [ dbSNP | Ensembl ].		VAR_034064
	Natural variant	3251	1	C → R in USH2A. Ref.29		VAR_054598
	Natural variant	3267	1	C → R in USH2A. Ref.29		VAR_054599
	Natural variant	3282	1	C → R in USH2A. Ref.31		VAR_054600
	Natural variant	3335	1	I → M. Ref.30		VAR_038368
	Natural variant	3358	1	C → Y in RP39. Ref.35		VAR_068356
	Natural variant	3411	1	E → A. Ref.29 Ref.32 Corresponds to variant rs10864198 [ dbSNP | Ensembl ].		VAR_050087
	Natural variant	3472	1	Y → YY in USH2A. Ref.29		VAR_054601
	Natural variant	3504	1	P → T in USH2A. Ref.32		VAR_054602
	Natural variant	3521	1	W → R in USH2A. Ref.32		VAR_054603
	Natural variant	3571	1	T → M in USH2A. Ref.29 Ref.31		VAR_054604
	Natural variant	3590	1	P → L. Ref.32		VAR_054605
	Natural variant	3669	1	S → R in RP39. Ref.35		VAR_068357
	Natural variant	3835	1	T → I. Ref.32 Corresponds to variant rs11120616 [ dbSNP | Ensembl ].		VAR_050088
	Natural variant	3868	1	M → V. Ref.29 Ref.32 Corresponds to variant rs35309576 [ dbSNP | Ensembl ].		VAR_054606
	Natural variant	3893	1	P → T. Ref.32 Corresponds to variant rs41303285 [ dbSNP | Ensembl ].		VAR_054607
	Natural variant	3895	1	G → E in USH2A. Ref.31		VAR_054608
	Natural variant	3976	1	T → M in USH2A. Ref.31		VAR_054609
	Natural variant	4054	1	S → I in USH2A. Ref.32		VAR_054610
	Natural variant	4115	1	R → C in USH2A and RP39; associated with M-4425. Ref.4 Ref.31 Ref.32 Ref.35		VAR_025780
	Natural variant	4192	1	R → H in RP39. Ref.35		VAR_068358
	Natural variant	4203	1	Q → R Found in a patient with spinocerebellar ataxia. Ref.33		VAR_066665
	Natural variant	4232	1	P → R in USH2A. Ref.32		VAR_054611
	Natural variant	4337	1	T → M in USH2A. Ref.29		VAR_054612
	Natural variant	4425	1	T → M in USH2Aand RP39; associated with C-4115. Ref.4 Ref.31 Ref.35		VAR_025781
	Natural variant	4433	1	V → L. Ref.32		VAR_054613
	Natural variant	4439	1	T → I in USH2A. Ref.15 Ref.32		VAR_054614
	Natural variant	4487	1	Y → C in USH2A. Ref.32		VAR_054615
	Natural variant	4592	1	Q → H in USH2A. Ref.32		VAR_054616
	Natural variant	4624	1	F → V. Ref.32		VAR_054617
	Natural variant	4674	1	R → G in RP39. Ref.30		VAR_038369
	Natural variant	4692	1	G → R. Corresponds to variant rs45549044 [ dbSNP | Ensembl ].		VAR_061351
	Natural variant	4739	1	R → K. Corresponds to variant rs12085354 [ dbSNP | Ensembl ].		VAR_050089
	Natural variant	4795	1	L → R in USH2A. Ref.32		VAR_054618
	Natural variant	4818	1	P → L in USH2A. Ref.29		VAR_054619
	Natural variant	4838	1	G → E. Corresponds to variant rs41315587 [ dbSNP | Ensembl ].		VAR_061352
	Natural variant	5031	1	R → W. Ref.32		VAR_054620
Experimental info
	Sequence conflict	237	1	F → C in AAC23748. Ref.1
	Sequence conflict	237	1	F → C in AAF75819. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (b) [UniParc]. Last modified April 4, 2006. Version 3. Checksum: 06A123CA9C0F7F1D	FASTA	5,202	575,600
	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
	Isoform 2 [UniParc]. Checksum: 434CD024FE19C0D6	FASTA	1,546	171,074
	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 QLERRESSLP ALMTTMMKGI RFIGNGYCKF PSSTHPVNTD FTGKCV
	Isoform 3 [UniParc]. Checksum: 9E201BC41FA9FC0E	FASTA	5,226	578,275
	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 VYPPGENHMF 5110 5120 5130 5140 5150 5160 DSVADISDVS SNVTLKSYTM HFEGLADTKI PRSGTPVSIR SNRSACVLRI PSQNQTSLTY 5170 5180 5190 5200 5210 5220 SQGSLHRSVS QLMDIQDKKV LMDNSLWEAI MGHNSGLYVD EEDLMNAIKD FSSVTKERTT FTDTHL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF055580 mRNA. Translation: AAC23748.2. AF091889 , 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 , AC092799, AC093581, AC119429, AC138024, AL139259, AL358452, AL445650, AL513305 Genomic DNA. Translation: CAH71588.1. AL513305 , AC138024, AC119429, AC093581, AC092799, AL445650, AL358858, AL358452, AL139259 Genomic DNA. Translation: CAH73621.1. AL139259 , AL513305, AL445650, AL358858, AL358452, AC138024, AC119429, AC093581, AC092799 Genomic DNA. Translation: CAI23041.1. AL358452 , AL513305, AL445650, AL358858, AL139259, AC138024, AC119429, AC093581, AC092799 Genomic DNA. Translation: CAI19189.1. AL445650 , AC092799, AC093581, AC119429, AC138024, AL139259, AL513305, AL358858, AL358452 Genomic DNA. Translation: CAH70621.1.
IPI	IPI00289540. IPI00410150. IPI00741527.
RefSeq	NP_009054.5. NM_007123.5. NP_996816.2. NM_206933.2.
UniGene	Hs.655974.
3D structure databases
ProteinModelPortal	O75445.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000305941.
PTM databases
PhosphoSite	O75445.
Proteomic databases
PaxDb	O75445.
PRIDE	O75445.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307340; ENSP00000305941; ENSG00000042781. ENST00000366942; ENSP00000355909; ENSG00000042781. ENST00000366943; ENSP00000355910; ENSG00000042781.
GeneID	7399.
KEGG	hsa:7399.
UCSC	uc001hku.1. human. uc001hkv.3. human.
Organism-specific databases
CTD	7399.
GeneCards	GC01M215796.
H-InvDB	HIX0028527.
HGNC	HGNC:12601. USH2A.
MIM	276901. phenotype. 608400. gene. 613809. phenotype.
neXtProt	NX_O75445.
Orphanet	791. Retinitis pigmentosa. 231178. Usher syndrome type 2.
PharmGKB	PA37228.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG245744.
HOGENOM	HOG000124780.
HOVERGEN	HBG094138.
OMA	EIRIQAC.
OrthoDB	EOG4B5P57.
Gene expression databases
Bgee	O75445.
CleanEx	HS_USH2A.
Genevestigator	O75445.
GermOnline	ENSG00000042781. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 3 hits. 2.60.40.10. 35 hits.
InterPro	IPR008985. 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]
PANTHER	PTHR10574:SF53. PTHR10574:SF53. 1 hit.
Pfam	PF00041. fn3. 20 hits. PF00053. Laminin_EGF. 9 hits. PF02210. Laminin_G_2. 2 hits. PF00055. Laminin_N. 1 hit. [Graphical view]
SMART	SM00180. EGF_Lam. 10 hits. SM00060. FN3. 33 hits. SM00282. LamG. 2 hits. SM00560. LamGL. 1 hit. SM00136. LamNT. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 3 hits. SSF49265. FN_III-like. 33 hits.
PROSITE	PS00022. 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]
ProtoNet	Search...
Other
GenomeRNAi	7399.
NextBio	28962.
SOURCE	Search...

Entry information

Entry name

USH2A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.