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Q99502 (EYA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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:
Eyes absent homolog 1

EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:EYA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Has also phosphatase activity with proteins phosphorylated on Ser and Thr residues (in vitro). Required for normal embryonic development of the craniofacial and trunk skeleton, kidneys and ears. Together with SIX1, it plays an important role in hypaxial muscle development; in this it is functionally redundant with EYA2. Ref.12

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.12

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.12

Cofactor

Binds 1 Mg2+ ion per subunit By similarity.

Subunit structure

Probably interacts with SIX2, SIX4 and SIX5. Interacts with H2AX in response to DNA damage By similarity.

Subcellular location

Cytoplasm. Nucleus. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs). Ref.9 Ref.12

Tissue specificity

In the embryo, highly expressed in kidney with lower levels in brain. Weakly expressed in lung. In the adult, highly expressed in heart and skeletal muscle. Weakly expressed in brain and liver. No expression in eye or kidney.

Developmental stage

Detected in cytoplasm of somite cells at the beginning of fourth week of development. Detected in cytoplasm of limb bud cell between the sixth and eighth week of development. Ref.9

Post-translational modification

Sumoylated with SUMO1 By similarity.

Involvement in disease

Branchiootorenal syndrome 1 (BOR1) [MIM:113650]: A syndrome characterized by branchial cleft fistulas or cysts, sensorineural and/or conductive hearing loss, pre-auricular pits, structural defects of the outer, middle or inner ear, and renal malformations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18

Otofaciocervical syndrome 1 (OFC1) [MIM:166780]: A disorder characterized by facial dysmorphism, cup-shaped low-set ears, preauricular fistulas, hearing loss, branchial defects, skeletal anomalies including vertebral defects, low-set clavicles, winged scapulae, sloping shoulders, and mild intellectual disability.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.10

Branchiootic syndrome 1 (BOS1) [MIM:602588]: A syndrome characterized by usually bilateral branchial cleft fistulas or cysts, sensorineural and/or conductive hearing loss, pre-auricular pits, and structural defects of the outer, middle or inner ear. Otic defects include malformed and hypoplastic pinnae, a narrowed external ear canal, bulbous internal auditory canal, stapes fixation, malformed and hypoplastic cochlea. Branchial and otic anomalies overlap with those seen in individuals with the branchiootorenal syndrome. However renal anomalies are absent in branchiootic syndrome patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.11 Ref.17

Anterior segment anomalies with or without cataract (ASA) [MIM:602588]: A disease characterized by various types of developmental eye anomalies, in the absence of other abnormalities. The phenotypic spectrum of anterior segment anomalies include central corneal opacity, Peters anomaly, and bilateral persistence of the pupillary membrane. Some patients have cataract.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. EYA family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
Mental retardation
   LigandMagnesium
Metal-binding
   Molecular functionActivator
Chromatin regulator
Developmental protein
Hydrolase
Protein phosphatase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement Ref.2. Source: ProtInc

aorta morphogenesis

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

cochlea morphogenesis

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from mutant phenotype Ref.12. Source: UniProtKB

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

establishment of mitotic spindle orientation

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of apical/basal cell polarity

Inferred from electronic annotation. Source: Ensembl

histone dephosphorylation

Inferred from direct assay Ref.12. Source: UniProtKB

lung epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

metanephros development

Inferred from electronic annotation. Source: Ensembl

middle ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

neuron fate specification

Inferred from electronic annotation. Source: Ensembl

otic vesicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

outer ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

outflow tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

pattern specification process

Inferred from electronic annotation. Source: Ensembl

pharyngeal system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA repair

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of Notch signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of secondary heart field cardioblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from direct assay Ref.12. Source: UniProtKB

semicircular canal morphogenesis

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Traceable author statement Ref.2. Source: ProtInc

striated muscle tissue development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19497856. Source: UniProtKB

nucleus

Inferred from direct assay Ref.12PubMed 19497856. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine phosphatase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform EYA1A (identifier: Q99502-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform EYA1B (identifier: Q99502-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MEMQDLTSPHSRLSGSSESPSGPKLGNSHINSNSMTPNGTE → MLLFPQVA
Isoform EYA1D (identifier: Q99502-3)

The sequence of this isoform differs from the canonical sequence as follows:
     140-144: Missing.
     351-380: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Eyes absent homolog 1
PRO_0000218643

Sites

Active site3281Nucleophile Probable
Active site3301Proton donor By similarity
Metal binding3281Magnesium By similarity
Metal binding3301Magnesium By similarity
Metal binding5561Magnesium By similarity

Natural variations

Alternative sequence1 – 4141MEMQD…PNGTE → MLLFPQVA in isoform EYA1B.
VSP_001486
Alternative sequence140 – 1445Missing in isoform EYA1D.
VSP_045793
Alternative sequence351 – 38030Missing in isoform EYA1D.
VSP_045794
Natural variant201P → A.
Corresponds to variant rs1445404 [ dbSNP | Ensembl ].
VAR_024439
Natural variant411E → K Found in a patient with congenital cataract. Ref.19
VAR_070033
Natural variant951P → S in BOR1. Ref.18
VAR_064942
Natural variant1401G → S in BOR1. Ref.18
VAR_064943
Natural variant2421S → G in BOS1. Ref.17
Corresponds to variant rs191838840 [ dbSNP | Ensembl ].
VAR_044452
Natural variant3631E → K in ASA. Ref.14
VAR_016864
Natural variant3631E → V in BOR1. Ref.18
VAR_064944
Natural variant4261G → S in BOR1; with cataract. Ref.14
VAR_016865
Natural variant4291D → G in BOR1. Ref.16
VAR_016866
Natural variant4401R → Q in BOR1. Ref.13 Ref.18
VAR_016867
Natural variant4871S → P in BOR1. Ref.1
VAR_005203
Natural variant5051L → R in BOR1. Ref.1
VAR_005204
Natural variant5141L → P in BOR1. Ref.18
VAR_064945
Natural variant5271Y → C in BOR1. Ref.18
VAR_064946
Natural variant5471R → G in ASA; with cataract. Ref.14
VAR_016868
Natural variant5691M → T in BOR1. Ref.18
VAR_064947
Natural variant5831L → P in BOR1. Ref.15
VAR_016869

Experimental info

Mutagenesis3281D → A: Loss of tyrosine phosphatase activity toward H2AX. Ref.12
Sequence conflict331N → D in AAL73437. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform EYA1A [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: D62365F81EB692E2

FASTA59264,593
        10         20         30         40         50         60 
MEMQDLTSPH SRLSGSSESP SGPKLGNSHI NSNSMTPNGT EVKTEPMSSS ETASTTADGS 

        70         80         90        100        110        120 
LNNFSGSAIG SSSFSPRPTH QFSPPQIYPS NRPYPHILPT PSSQTMAAYG QTQFTTGMQQ 

       130        140        150        160        170        180 
ATAYATYPQP GQPYGISSYG ALWAGIKTEG GLSQSQSPGQ TGFLSYGTSF STPQPGQAPY 

       190        200        210        220        230        240 
SYQMQGSSFT TSSGIYTGNN SLTNSSGFNS SQQDYPSYPS FGQGQYAQYY NSSPYPAHYM 

       250        260        270        280        290        300 
TSSNTSPTTP STNATYQLQE PPSGITSQAV TDPTAEYSTI HSPSTPIKDS DSDRLRRGSD 

       310        320        330        340        350        360 
GKSRGRGRRN NNPSPPPDSD LERVFIWDLD ETIIVFHSLL TGSYANRYGR DPPTSVSLGL 

       370        380        390        400        410        420 
RMEEMIFNLA DTHLFFNDLE ECDQVHIDDV SSDDNGQDLS TYNFGTDGFP AAATSANLCL 

       430        440        450        460        470        480 
ATGVRGGVDW MRKLAFRYRR VKEIYNTYKN NVGGLLGPAK REAWLQLRAE IEALTDSWLT 

       490        500        510        520        530        540 
LALKALSLIH SRTNCVNILV TTTQLIPALA KVLLYGLGIV FPIENIYSAT KIGKESCFER 

       550        560        570        580        590 
IIQRFGRKVV YVVIGDGVEE EQGAKKHAMP FWRISSHSDL MALHHALELE YL 

« Hide

Isoform EYA1B [UniParc].

Checksum: 6B638C22438309A8
Show »

FASTA55961,211
Isoform EYA1D [UniParc].

Checksum: 7AAB97F0AAE440CC
Show »

FASTA55760,660

References

« Hide 'large scale' references
[1]"Clustering of mutations responsible for branchio-oto-renal (BOR) syndrome in the eyes absent homologous region (eyaHR) of EYA1."
Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D., Vincent C., Levi-Acobas F., Cruaud C., le Merrer M., Mathieu M., Koenig R., Vigneron J., Weissenbach J., Petit C., Weil D.
Hum. Mol. Genet. 6:2247-2255(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, VARIANTS BOR1 PRO-487 AND ARG-505.
Tissue: Embryo.
[2]"A human homologue of the Drosophila eyes absent gene underlies branchio-oto-renal (BOR) syndrome and identifies a novel gene family."
Abdelhak S., Kalatzis V., Heilig R., Compain S., Samson D., Vincent C., Weil D., Cruaud C., Sahly I., Leibovici M., Bitner-Glindzicz M., Francis M., Lacombe D., Vigneron J., Charachon R., Boven K., Bedbeder P., van Regemorter N., Weissenbach J., Petit C.
Nat. Genet. 15:157-164(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM EYA1A).
Tissue: Embryo.
[3]"EYA1D, a novel EYA1 isoform."
Vervoort V.S., Schwartz C.E.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EYA1D), ALTERNATIVE SPLICING.
Tissue: Kidney.
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"BOR and BO syndromes are allelic defects of EYA1."
Vincent C., Kalatzis V., Abdelhak S., Chaib H., Compain S., Helias J., Vaneecloo F.M., Petit C.
Eur. J. Hum. Genet. 5:242-246(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BOS1.
[8]"Oto-facio-cervical (OFC) syndrome is a contiguous gene deletion syndrome involving EYA1: molecular analysis confirms allelism with BOR syndrome and further narrows the Duane syndrome critical region to 1 cM."
Rickard S., Parker M., van't Hoff W., Barnicoat A., Russell-Eggitt I., Winter R.M., Bitner-Glindzicz M.
Hum. Genet. 108:398-403(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN OFC1.
[9]"Six and Eya expression during human somitogenesis and MyoD gene family activation."
Fougerousse F., Durand M., Lopez S., Suel L., Demignon J., Thornton C., Ozaki H., Kawakami K., Barbet P., Beckmann J.S., Maire P.
J. Muscle Res. Cell Motil. 23:255-264(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[10]"Point mutation of an EYA1-gene splice site in a patient with oto-facio-cervical syndrome."
Estefania E., Ramirez-Camacho R., Gomar M., Trinidad A., Arellano B., Garcia-Berrocal J.R., Verdaguer J.M., Vilches C.
Ann. Hum. Genet. 70:140-144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN OFC1.
[11]"Identification of a novel EYA1 mutation presenting in a newborn with laryngomalacia, glossoptosis, retrognathia, and pectus excavatum."
Spruijt L., Hoefsloot L.H., van Schaijk G.H.W.H., van Waardenburg D., Kremer B., Brackel H.J.L., de Die-Smulders C.E.M.
Am. J. Med. Genet. A 140:1343-1345(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BOS1.
[12]"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-328.
[13]"Branchio-oto-renal syndrome: identification of novel mutations, molecular characterization, mutation distribution, and prospects for genetic testing."
Kumar S., Deffenbacher K., Cremers C.W.R.J., Van Camp G., Kimberling W.J.
Genet. Test. 1:243-251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BOR1 GLN-440.
[14]"Mutations of a human homologue of the Drosophila eyes absent gene (EYA1) detected in patients with congenital cataracts and ocular anterior segment anomalies."
Azuma N., Hirakiyama A., Inoue T., Asaka A., Yamada M.
Hum. Mol. Genet. 9:363-366(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASA LYS-363 AND GLY-547, VARIANT BOR1 SER-426.
[15]"Importance of clinical evaluation and molecular testing in the branchio-oto-renal (BOR) syndrome and overlapping phenotypes."
Rickard S., Boxer M., Trompeter R., Bitner-Glindzicz M.
J. Med. Genet. 37:623-627(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BOR1 PRO-583.
[16]"Genetic features of hearing loss associated with ear anomalies: PDS and EYA1 mutation analysis."
Namba A., Abe S., Shinkawa H., Kimberling W.J., Usami S.
J. Hum. Genet. 46:518-521(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BOR1 GLY-429.
[17]"Mutation of the EYA1 gene in patients with branchio-oto syndrome."
Yashima T., Noguchi Y., Ishikawa K., Mizusawa H., Kitamura K.
Acta Oto-Laryngol. 123:279-282(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BOS1 GLY-242.
[18]"Mutation screening of the EYA1, SIX1, and SIX5 genes in a large cohort of patients harboring branchio-oto-renal syndrome calls into question the pathogenic role of SIX5 mutations."
Krug P., Moriniere V., Marlin S., Koubi V., Gabriel H.D., Colin E., Bonneau D., Salomon R., Antignac C., Heidet L.
Hum. Mutat. 32:183-190(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BOR1 SER-95; SER-140; VAL-363; GLN-440; PRO-514; CYS-527 AND THR-569.
[19]"Whole exome sequencing in dominant cataract identifies a new causative factor, CRYBA2, and a variety of novel alleles in known genes."
Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P., Costakos D., Yonath H., Hall S., Power P., Semina E.V.
Hum. Genet. 132:761-770(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-41.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10260 Genomic DNA. Translation: CAA71309.1.
AJ000097 mRNA. Translation: CAA03922.1.
AJ000098 mRNA. Translation: CAA03923.1.
AF467247 mRNA. Translation: AAL73437.1.
AC016465 Genomic DNA. No translation available.
AC022858 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86976.1.
BC121799 mRNA. Translation: AAI21800.1.
RefSeqNP_000494.2. NM_000503.5.
NP_001275503.1. NM_001288574.1.
NP_001275504.1. NM_001288575.1.
NP_742055.1. NM_172058.3.
NP_742056.1. NM_172059.3.
NP_742057.1. NM_172060.3.
UniGeneHs.491997.

3D structure databases

ProteinModelPortalQ99502.
SMRQ99502. Positions 322-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108439. 4 interactions.
DIPDIP-60446N.
STRING9606.ENSP00000342626.

PTM databases

PhosphoSiteQ99502.

Polymorphism databases

DMDM3183005.

Proteomic databases

PaxDbQ99502.
PRIDEQ99502.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340726; ENSP00000342626; ENSG00000104313. [Q99502-1]
ENST00000388740; ENSP00000373392; ENSG00000104313. [Q99502-2]
ENST00000388742; ENSP00000373394; ENSG00000104313. [Q99502-1]
ENST00000419131; ENSP00000410176; ENSG00000104313. [Q99502-3]
GeneID2138.
KEGGhsa:2138.
UCSCuc003xyr.4. human.
uc003xys.4. human. [Q99502-1]
uc003xyt.4. human. [Q99502-2]

Organism-specific databases

CTD2138.
GeneCardsGC08M072159.
HGNCHGNC:3519. EYA1.
MIM113650. phenotype.
166780. phenotype.
601653. gene.
602588. phenotype.
neXtProtNX_Q99502.
Orphanet107. BOR syndrome.
52429. Branchio-otic syndrome.
2792. Otofaciocervical syndrome.
PharmGKBPA27931.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297494.
HOGENOMHOG000293149.
HOVERGENHBG002447.
InParanoidQ99502.
KOK15616.
OMAGQPYGIS.
OrthoDBEOG7DNNTZ.
PhylomeDBQ99502.
TreeFamTF319337.

Gene expression databases

ArrayExpressQ99502.
BgeeQ99502.
CleanExHS_EYA1.
GenevestigatorQ99502.

Family and domain databases

InterProIPR006545. EYA_dom.
IPR028472. EYA_fam.
IPR028471. Eyes_absent_h1.
[Graphical view]
PANTHERPTHR10190. PTHR10190. 1 hit.
PTHR10190:SF11. PTHR10190:SF11. 1 hit.
TIGRFAMsTIGR01658. EYA-cons_domain. 1 hit.
ProtoNetSearch...

Other

GeneWikiEYA1.
GenomeRNAi2138.
NextBio8639.
PROQ99502.
SOURCESearch...

Entry information

Entry nameEYA1_HUMAN
AccessionPrimary (citable) accession number: Q99502
Secondary accession number(s): A6NHQ0 expand/collapse secondary AC list , G5E9R4, Q0P516, Q8WX80
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 125 of the entry and version 2 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 8

Human chromosome 8: entries, gene names and cross-references to MIM