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P14679 (TYRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosinase

EC=1.14.18.1
Alternative name(s):
LB24-AB
Monophenol monooxygenase
SK29-AB
Tumor rejection antigen AB
Gene names
Name:TYR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.

Catalytic activity

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit.

Subcellular location

Melanosome membrane; Single-pass type I membrane protein Ref.14 Ref.15.

Induction

Increased expression after UVB irradiation.

Polymorphism

Genetic variants in TYR define the skin/hair/eye pigmentation variation locus 3 (SHEP3) [MIM:601800]. Hair, eye and skin pigmentation are among the most visible examples of human phenotypic variation, with a broad normal range that is subject to substantial geographic stratification. In the case of skin, individuals tend to have lighter pigmentation with increasing distance from the equator. By contrast, the majority of variation in human eye and hair color is found among individuals of European ancestry, with most other human populations fixed for brown eyes and black hair.

Compound heterozygosity for the R402Q polymorphism and a mutant allele of TYR is a common cause of autosomal recessive ocular albinism. The R402Q polymorphism is also found in Waardenburg syndrome type II with ocular albinism (WS2-OA) in association with a deletion in the MITF gene.

Involvement in disease

Albinism, oculocutaneous, 1A (OCA1A) [MIM:203100]: An autosomal recessive disorder in which the biosynthesis of melanin pigment is absent in skin, hair, and eyes. It is characterized by complete lack of tyrosinase activity due to production of an inactive enzyme. Patients present with a life-long absence of melanin pigment after birth, and manifest increased sensitivity to ultraviolet radiation with predisposition to skin cancer. Visual anomalies include decreased acuity, nystagmus, strabismus and photophobia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38

Albinism, oculocutaneous, 1B (OCA1B) [MIM:606952]: An autosomal recessive disorder in which the biosynthesis of melanin pigment is reduced in skin, hair, and eyes. It is characterized by partial lack of tyrosinase activity. Patients have white hair at birth that rapidly turns yellow or blond. They manifest the development of minimal-to-moderate amounts of cutaneous and ocular pigment. Some patients may have with white hair in the warmer areas (scalp and axilla) and progressively darker hair in the cooler areas (extremities). This variant phenotype is due to a loss of tyrosinase activity above 35-37 degrees C.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.22 Ref.26 Ref.30 Ref.31 Ref.33

Sequence similarities

Belongs to the tyrosinase family.

Sequence caution

The sequence AAA61241.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA68756.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processMelanin biosynthesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAlbinism
Deafness
Disease mutation
Waardenburg syndrome
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
Tumor antigen
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

eye pigment biosynthetic process

Traceable author statement PubMed 7704033. Source: ProtInc

melanin biosynthetic process from tyrosine

Traceable author statement PubMed 7704033. Source: ProtInc

thymus development

Inferred from electronic annotation. Source: Ensembl

visual perception

Traceable author statement PubMed 7704033. Source: ProtInc

   Cellular_componentGolgi-associated vesicle

Traceable author statement PubMed 10823941. Source: ProtInc

cytoplasm

Inferred from direct assay PubMed 11092760. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Traceable author statement PubMed 11092760. Source: UniProtKB

melanosome

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 11092760. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from mutant phenotype PubMed 11092760. Source: UniProtKB

monophenol monooxygenase activity

Inferred from direct assay PubMed 11092760. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16162817. Source: UniProtKB

protein heterodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14679-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P14679-2)

The sequence of this isoform differs from the canonical sequence as follows:
     346-377: GFASPLTGIADASQSSMHNALHIYMNGTMSQV → EMGFLHVGWAGLKLLTSRDPPPWPPKMLGLQA
     378-529: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 529511Tyrosinase
PRO_0000035879

Regions

Topological domain19 – 476458Lumenal, melanosome Potential
Transmembrane477 – 49721Helical; Potential
Topological domain498 – 52932Cytoplasmic Potential

Sites

Metal binding1801Copper A By similarity
Metal binding2021Copper A By similarity
Metal binding2111Copper A By similarity
Metal binding3631Copper B By similarity
Metal binding3671Copper B By similarity
Metal binding3901Copper B By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence346 – 37732GFASP…TMSQV → EMGFLHVGWAGLKLLTSRDP PPWPPKMLGLQA in isoform 2.
VSP_006701
Alternative sequence378 – 529152Missing in isoform 2.
VSP_006702
Natural variant191H → Q in OCA1A.
VAR_007649
Natural variant211P → S in OCA1A. Ref.20
VAR_007650
Natural variant361C → Y in OCA1A. Ref.33
VAR_021683
Natural variant421D → G in OCA1A. Ref.23
Corresponds to variant rs28940878 [ dbSNP | Ensembl ].
VAR_007651
Natural variant441S → G in OCA1A. Ref.38
VAR_021684
Natural variant441S → R in OCA1A. Ref.38
VAR_021685
Natural variant471G → D in OCA1A. Ref.26 Ref.36 Ref.38
Corresponds to variant rs61753180 [ dbSNP | Ensembl ].
VAR_007652
Natural variant471G → V in OCA1A. Ref.38
VAR_021686
Natural variant521R → I in OCA1.
VAR_007653
Natural variant551C → Y in OCA1A. Ref.23 Ref.35
Corresponds to variant rs28940879 [ dbSNP | Ensembl ].
VAR_007654
Natural variant681Q → H in OCA1A. Ref.38
VAR_021687
Natural variant771R → Q in OCA1A. Ref.33 Ref.36 Ref.38
Corresponds to variant rs61753185 [ dbSNP | Ensembl ].
VAR_007655
Natural variant771R → RR in OCA1A. Ref.35
VAR_009236
Natural variant771R → W in OCA1A. Ref.33
Corresponds to variant rs61753184 [ dbSNP | Ensembl ].
VAR_007656
Natural variant791S → L in OCA1A. Ref.38
VAR_021688
Natural variant801W → R in OCA1A.
VAR_007657
Natural variant811P → L in OCA1A. Ref.17 Ref.33 Ref.38
Corresponds to variant rs28940876 [ dbSNP | Ensembl ].
VAR_007658
Natural variant891C → R in OCA1A. Ref.21
Corresponds to variant rs28940877 [ dbSNP | Ensembl ].
VAR_007659
Natural variant971G → R in OCA1A. Ref.33
VAR_007660
Natural variant1091G → R in OCA1A. Ref.36
VAR_021689
Natural variant1341F → C.
Corresponds to variant rs33955261 [ dbSNP | Ensembl ].
VAR_034576
Natural variant1421K → N.
Corresponds to variant rs11545463 [ dbSNP | Ensembl ].
VAR_042665
Natural variant1521P → S in OCA1B. Ref.26
VAR_007925
Natural variant1551T → S in OCA1A. Ref.38
VAR_021690
Natural variant1761F → I in OCA1A. Ref.24
VAR_007661
Natural variant1771V → F in OCA1A. Ref.38
Corresponds to variant rs138487695 [ dbSNP | Ensembl ].
VAR_021691
Natural variant1791M → L in OCA1A. Ref.38
VAR_021692
Natural variant1801H → N in OCA1A. Ref.38
VAR_021693
Natural variant1921S → Y Associated with SHEP3; light/dark skin. Ref.7 Ref.11 Ref.16 Ref.33 Ref.38 Ref.39 Ref.40
Corresponds to variant rs1042602 [ dbSNP | Ensembl ].
VAR_007662
Natural variant1991D → N in OCA1A. Ref.38
VAR_021694
Natural variant2011A → S in OCA1A. Ref.38
VAR_021695
Natural variant2051P → T in OCA1A. Ref.36
Corresponds to variant rs61754362 [ dbSNP | Ensembl ].
VAR_021696
Natural variant2061A → T in OCA1A. Ref.23
Corresponds to variant rs28940880 [ dbSNP | Ensembl ].
VAR_007663
Natural variant2161L → M in OCA1A.
VAR_007664
Natural variant2171R → G in OCA1A.
VAR_007665
Natural variant2171R → Q in OCA1A. Ref.24 Ref.33
VAR_007667
Natural variant2171R → S in OCA1A. Ref.38
VAR_021697
Natural variant2171R → W in OCA1A. Ref.20 Ref.33
VAR_007666
Natural variant2171Missing in OCA1A.
VAR_007926
Natural variant2271Missing in OCA1A.
VAR_021698
Natural variant2361W → L in OCA1A. Ref.38
VAR_021699
Natural variant2361W → S in OCA1A. Ref.33
VAR_021700
Natural variant2391R → W in OCA1A. Ref.37
VAR_021701
Natural variant2401D → V in OCA1A. Ref.38
VAR_021702
Natural variant2431K → T in OCA1A. Ref.38
VAR_021703
Natural variant2531G → R in OCA1A.
VAR_007668
Natural variant2561H → Y in OCA1A. Ref.36 Ref.38
VAR_021704
Natural variant2721W → C in OCA1A. Ref.33
VAR_021705
Natural variant2751V → F in OCA1B. Ref.18 Ref.36
Corresponds to variant rs104894314 [ dbSNP | Ensembl ].
VAR_007669
Natural variant2881L → S in OCA1A.
VAR_007927
Natural variant2891C → G in OCA1A. Ref.35
VAR_009237
Natural variant2891C → R in OCA1A. Ref.33 Ref.38
VAR_007670
Natural variant2941E → G in OCA1A. Ref.33
VAR_021706
Natural variant2941E → K in OCA1A and OCA1B. Ref.26 Ref.33 Ref.36
VAR_007928
Natural variant2991R → H in OCA1A. Ref.20 Ref.26 Ref.35
Corresponds to variant rs61754375 [ dbSNP | Ensembl ].
VAR_007671
Natural variant2991R → S in OCA1A. Ref.35
VAR_007672
Natural variant3081R → T.
Corresponds to variant rs1042608 [ dbSNP | Ensembl ].
VAR_011825
Natural variant3121L → V in OCA1.
VAR_007673
Natural variant3131P → R in OCA1.
VAR_007674
Natural variant3181V → E in OCA1A. Ref.38
VAR_021707
Natural variant3251T → A in OCA1B.
VAR_007675
Natural variant3281E → Q in OCA1A. Ref.25
VAR_007929
Natural variant3291S → P in OCA1A. Ref.38
VAR_021708
Natural variant3321M → T in OCA1A. Ref.38
VAR_021709
Natural variant3391S → G in OCA1A. Ref.36
VAR_007676
Natural variant3401F → L in OCA1.
VAR_007677
Natural variant3451E → G in OCA1A. Ref.38
VAR_021710
Natural variant3461G → E in OCA1A.
VAR_007930
Natural variant3551A → E in OCA1A.
VAR_007931
Natural variant3551A → P in OCA1A. Ref.33 Ref.36 Ref.38
VAR_007678
Natural variant3611S → R in OCA1A. Ref.28
VAR_007932
Natural variant3671H → Y in OCA1A. Ref.27
VAR_007933
Natural variant3701M → T in OCA1A. Ref.27
VAR_007934
Natural variant3711N → T in OCA1A.
VAR_007679
Natural variant3711N → Y in OCA1A. Ref.28 Ref.33
VAR_007935
Natural variant3731T → K in OCA1A. Ref.16 Ref.26 Ref.27 Ref.33 Ref.36 Ref.38
VAR_007680
Natural variant3781Q → K in OCA1A. Ref.38
VAR_021711
Natural variant3801S → P in OCA1B.
VAR_007681
Natural variant3821N → K in OCA1A.
VAR_007682
Natural variant3831D → N in OCA1A. Ref.16 Ref.36 Ref.38
VAR_007683
Natural variant3901H → D in OCA1B.
VAR_007684
Natural variant3931V → F in OCA1A. Ref.38
VAR_007936
Natural variant3951S → N in OCA1A.
VAR_007685
Natural variant3951S → R in OCA1A. Ref.38
VAR_021712
Natural variant3981E → A in OCA1A. Ref.38
VAR_021713
Natural variant3981E → V in OCA1A. Ref.38
VAR_021714
Natural variant4001W → L in OCA1A. Ref.35
VAR_009238
Natural variant4021R → G in OCA1B.
VAR_007937
Natural variant4021R → L in OCA1A. Ref.38
VAR_021715
Natural variant4021R → Q. Ref.16 Ref.27 Ref.29 Ref.33 Ref.38
Corresponds to variant rs1126809 [ dbSNP | Ensembl ].
VAR_007686
Natural variant4031R → S in OCA1A and OCA1B. Ref.20 Ref.33 Ref.38
VAR_007687
Natural variant4041H → N in OCA1A. Ref.38
VAR_021716
Natural variant4041H → P in OCA-I.
VAR_007688
Natural variant4051R → L in OCA1A. Ref.38
VAR_021717
Natural variant4061P → L in OCA1A and OCA1B. Ref.18 Ref.33 Ref.38
VAR_007689
Natural variant4081Q → H in OCA1A. Ref.38
VAR_021718
Natural variant4091E → D in OCA1A. Ref.38
VAR_021719
Natural variant4161A → S in OCA1A. Ref.38
VAR_021720
Natural variant4171P → H in OCA1A. Ref.38
VAR_021721
Natural variant4191G → R in OCA1A. Ref.23 Ref.25 Ref.33 Ref.38
VAR_007690
Natural variant4221R → Q in OCA1A and OCA1B; temperature sensitive variant. Ref.22 Ref.33 Ref.38
VAR_007691
Natural variant4241S → F in OCA1A. Ref.38
VAR_021722
Natural variant4261M → K in OCA1A. Ref.38
VAR_021723
Natural variant4271V → G in OCA1A. Ref.38
VAR_021724
Natural variant4311P → L in OCA1A. Ref.25
VAR_007938
Natural variant4341R → I in OCA1A. Ref.38
VAR_021725
Natural variant4351N → D in OCA1A. Ref.38
VAR_021726
Natural variant4391F → V in OCA1A. Ref.33
VAR_021727
Natural variant4441D → G in OCA1A. Ref.38
VAR_021728
Natural variant4461G → S in OCA1A. Ref.20 Ref.33 Ref.36
VAR_007692
Natural variant4481D → N in OCA1A. Ref.20 Ref.33 Ref.38
VAR_007693

Experimental info

Sequence conflict42 – 454DRSP → TGV in AAA61241. Ref.2
Sequence conflict1791M → I in CAA68756. Ref.4
Sequence conflict373 – 3786TMSQVQ → HVPGT in AAA61241. Ref.2
Sequence conflict4951L → P in AAA61241. Ref.2
Sequence conflict4951L → P in AAA61244. Ref.2
Sequence conflict520 – 5234DYHS → GLPQ Ref.2
Sequence conflict525 – 5284YQSH → VSEPFIKGLGNRVGPKSPDL TLTQSNVQVPENICWYFL Ref.2

Sequences

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

Last modified July 1, 1993. Version 3.
Checksum: 67211A91608A59E1

FASTA52960,393
        10         20         30         40         50         60 
MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS GRGSCQNILL 

        70         80         90        100        110        120 
SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFWGP NCTERRLLVR 

       130        140        150        160        170        180 
RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH 

       190        200        210        220        230        240 
YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD 

       250        260        270        280        290        300 
AEKCDICTDE YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLRRN 

       310        320        330        340        350        360 
PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS 

       370        380        390        400        410        420 
SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLQEV YPEANAPIGH 

       430        440        450        460        470        480 
NRESYMVPFI PLYRNGDFFI SSKDLGYDYS YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG 

       490        500        510        520 
AAMVGAVLTA LLAGLVSLLC RHKRKQLPEE KQPLLMEKED YHSLYQSHL 

« Hide

Isoform 2 [UniParc].

Checksum: E4E415B71C60359B
Show »

FASTA37742,914

References

« Hide 'large scale' references
[1]"Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment."
Giebel L.B., Strunk K.M., Spritz R.A.
Genomics 9:435-445(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]"Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus."
Kwon B.S., Haq A.K., Pomerantz S.H., Halaban R.
Proc. Natl. Acad. Sci. U.S.A. 84:7473-7477(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Erratum
Kwon B.S., Haq A.K., Pomerantz S.H., Halaban R.
Proc. Natl. Acad. Sci. U.S.A. 85:6352-6352(1988)
Cited for: SEQUENCE REVISION TO 384-398.
[4]"Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA."
Bouchard B., Fuller B.B., Vijayasaradhi S., Houghton A.N.
J. Exp. Med. 169:2029-2042(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Melanoma.
[5]"A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism."
Chintamaneni C.D., Halaban R., Kobayashi Y., Witkop C.J., Kwon B.S.
Proc. Natl. Acad. Sci. U.S.A. 88:5272-5276(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"The tyrosinase gene codes for an antigen recognized by autologous cytolytic T lymphocytes on HLA-A2 melanomas."
Brichard V., van Pel A., Woelfel T., Woelfel C., de Plaen E., Lethe B.G., Coulie P., Boon T.
J. Exp. Med. 178:489-495(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
Tissue: Melanoma and T-cell.
[7]"The tyrosinase gene in gorillas and the albinism of 'Snowflake'."
Martinez-Arias R., Comas D., Andres A., Abello M.-T., Domingo-Roura X., Bertranpetit J.
Pigment Cell Res. 13:467-470(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT TYR-192.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Skin.
[9]"Characteristic sequences in the upstream region of the human tyrosinase gene."
Kikuchi H., Miura H., Yamamoto H., Takeuchi T., Dei T., Watanabe M.
Biochim. Biophys. Acta 1009:283-286(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-272.
Tissue: Liver.
[10]"Functional analysis of the cDNA encoding human tyrosinase precursor."
Takeda A., Tomita Y., Okinaga S., Tagami H., Shibahara S.
Biochem. Biophys. Res. Commun. 162:984-990(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-32.
[11]"Molecular phylogenetics and the origins of placental mammals."
Murphy W.J., Eizirik E., Johnson W.E., Zhang Y.-P., Ryder O.A., O'Brien S.J.
Nature 409:614-618(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-195, VARIANT TYR-192.
[12]"Molecular basis of type I (tyrosinase-related) oculocutaneous albinism: mutations and polymorphisms of the human tyrosinase gene."
Oetting W.S., King R.A.
Hum. Mutat. 2:1-6(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON OCA VARIANTS.
[13]"Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism."
Oetting W.S., King R.A.
Hum. Mutat. 13:99-115(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON OCA1 VARIANTS.
[14]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[15]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[16]"Detection of mutations in the tyrosinase gene in a patient with type IA oculocutaneous albinism."
Spritz R.A., Strunk K.M., Giebel L.B., King R.A.
N. Engl. J. Med. 322:1724-1728(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A LYS-373 AND ASN-383, VARIANTS TYR-192 AND GLN-402.
[17]"A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism."
Giebel L.B., Strunk K.M., King R.A., Hanifin J.M., Spritz R.A.
Proc. Natl. Acad. Sci. U.S.A. 87:3255-3258(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OCA1A LEU-81.
[18]"Tyrosinase gene mutations associated with type IB ('yellow') oculocutaneous albinism."
Giebel L.B., Tripathi R.K., Strunk K.M., Hanifin J.M., Jackson C.E., King R.A., Spritz R.A.
Am. J. Hum. Genet. 48:1159-1167(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1B PHE-275 AND LEU-406.
[19]Erratum
Giebel L.B., Tripathi R.K., Strunk K.M., Hanifin J.M., Jackson C.E., King R.A., Spritz R.A.
Am. J. Hum. Genet. 49:696-696(1991)
[20]"Tyrosinase gene mutations in type I (tyrosinase-deficient) oculocutaneous albinism define two clusters of missense substitutions."
Tripathi R.K., Strunk K.M., Giebel L.B., Weleber R.G., Spritz R.A.
Am. J. Med. Genet. 43:865-871(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A SER-21; TRP-217; HIS-299; SER-403; SER-446 AND ASN-448.
[21]"Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism."
Spritz R.A., Strunk K.M., Hsieh C.-L., Sekhon G.S., Francke U.
Am. J. Hum. Genet. 48:318-324(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OCA1A ARG-89.
[22]"A tyrosinase gene missense mutation in temperature-sensitive type I oculocutaneous albinism. A human homologue to the Siamese cat and the Himalayan mouse."
Giebel L.B., Tripathi R.K., King R.A., Spritz R.A.
J. Clin. Invest. 87:1119-1122(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OCA1B GLN-422.
[23]"Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism."
King R.A., Mentink M.M., Oetting W.S.
Mol. Biol. Med. 8:19-29(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A GLY-42; TYR-55; THR-206 AND ARG-419.
[24]"Molecular analysis of type I-A (tyrosinase negative) oculocutaneous albinism."
Oetting W.S., King R.A.
Hum. Genet. 90:258-262(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A ILE-176 AND GLN-217.
[25]"Mutations of the tyrosinase gene in Indo-Pakistani patients with type I (tyrosinase-deficient) oculocutaneous albinism (OCA)."
Tripathi R.K., Bundey S., Musarella M.A., Droetto S., Strunk K.M., Holmes S.A., Spritz R.A.
Am. J. Hum. Genet. 53:1173-1179(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A GLN-328; ARG-419 AND LEU-431.
[26]"Mutations of the tyrosinase gene in patients with oculocutaneous albinism from various ethnic groups in Israel."
Gershoni-Baruch R., Rosenmann A., Droetto S., Holmes S.A., Tripathi R.K., Spritz R.A.
Am. J. Hum. Genet. 54:586-594(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A ASP-47; CYS-217 DEL; HIS-299 AND LYS-373, VARIANTS OCA1B SER-152 AND LYS-294.
[27]"Initiation codon mutation of the tyrosinase gene as a cause of human albinism."
Breimer L.H., Winder A.F., Jay B., Jay M.
Clin. Chim. Acta 227:17-22(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A TYR-367; THR-370 AND LYS-373, VARIANT GLN-402.
[28]"Diagnosis of oculocutaneous albinism with molecular analysis."
Summers C.G., Oetting W.S., King R.A.
Am. J. Ophthalmol. 121:724-726(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A ARG-361 AND TYR-371.
[29]"Apparent digenic inheritance of Waardenburg syndrome type 2 (WS2) and autosomal recessive ocular albinism (AROA)."
Morell R., Spritz R.A., Ho L., Pierpont J., Guo W., Friedman T.B., Asher J.H. Jr.
Hum. Mol. Genet. 6:659-664(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-402.
[30]"Novel mutations of the tyrosinase (TYR) gene in type I oculocutaneous albinism (OCA1)."
Spritz R.A., Oh J., Fukai K., Holmes S.A., Ho L., Chitayat D., France T.D., Musarella M.A., Orlow S.J., Schnur R.E., Weleber R.G., Levin A.V.
Hum. Mutat. 10:171-174(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A AND OCA1B.
[31]"Mutations of the human tyrosinase gene associated with tyrosinase related oculocutaneous albinism (OCA1)."
Oetting W.S., Fryer J.P., King R.A.
Hum. Mutat. 12:433-434(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A AND OCA1B.
[32]Erratum
Oetting W.S., Fryer J.P., King R.A.
Hum. Mutat. 13:83-83(1999)
[33]"Novel and recurrent mutations in the tyrosinase gene and the P gene in the German albino population."
Passmore L.A., Kaesmann-Kellner B., Weber B.H.F.
Hum. Genet. 105:200-210(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A TYR-36; GLN-77; TRP-77; LEU-81; ARG-97; GLN-217; TRP-217; SER-236; CYS-272; ARG-289; GLY-294; LYS-294; PRO-355; TYR-371; LYS-373; LEU-406; ARG-419; GLN-422; VAL-439; SER-446 AND ASN-448, VARIANT OCA1B SER-403, VARIANTS TYR-192 AND GLN-402.
[34]Erratum
Passmore L.A., Kaesmann-Kellner B., Weber B.H.F.
Hum. Genet. 108:208-208(2001)
[35]"Insertion/deletion mutations of type I oculocutaneous albinism in Chinese patients from Taiwan."
Tsai C.-H., Tsai F.-J., Wu J.-Y., Lin S.-P., Chang J.-G., Yang C.-F., Lee C.-C.
Hum. Mutat. 14:542-542(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A TYR-55; ARG-77 INS; GLY-289; HIS-299; SER-299 AND LEU-400.
[36]"Mutation analysis of the tyrosinase gene in oculocutaneous albinism."
Camand O., Marchant D., Boutboul S., Pequignot M., Odent S., Dollfus H., Sutherland J., Levin A., Menasche M., Marsac C., Dufier J.-L., Heon E., Abitbol M.
Hum. Mutat. 17:352-352(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A ASP-47; GLN-77; ARG-109; THR-205; TYR-256; PHE-275; LYS-294; GLY-339; PRO-355; LYS-373; ASN-383 AND SER-446.
[37]"A novel mutation of the tyrosinase gene causing oculocutaneous albinism type 1 (OCA1)."
Nakamura E., Miyamura Y., Matsunaga J., Kano Y., Dakeishi-Hara M., Tanita M., Kono M., Tomita Y.
J. Dermatol. Sci. 28:102-105(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OCA1A TRP-239.
[38]"Detection of 53 novel DNA variations within the tyrosinase gene and accumulation of mutations in 17 patients with albinism."
Opitz S., Kaesmann-Kellner B., Kaufmann M., Schwinger E., Zuehlke C.
Hum. Mutat. 23:630-631(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OCA1A ARG-44; GLY-44; ASP-47; VAL-47; HIS-68; GLN-77; LEU-79; LEU-81; SER-155; PHE-177; LEU-179; ASN-180; ASN-199; SER-201; SER-217; LEU-236; VAL-240; THR-243; TYR-256; ARG-289; GLU-318; PRO-329; THR-332; GLY-345; PRO-355; LYS-373; LYS-378; ASN-383; PHE-393; ARG-395; VAL-398; ALA-398; LEU-402; SER-403; ASN-404; LEU-405; LEU-406; HIS-408; ASP-409; SER-416; HIS-417; ARG-419; GLN-422; PHE-424; LYS-426; GLY-427; ILE-434; ASP-435; GLY-444 AND ASN-448, VARIANTS TYR-192 AND GLN-402.
[39]"A genomewide association study of skin pigmentation in a South Asian population."
Stokowski R.P., Pant P.V.K., Dadd T., Fereday A., Hinds D.A., Jarman C., Filsell W., Ginger R.S., Green M.R., van der Ouderaa F.J., Cox D.R.
Am. J. Hum. Genet. 81:1119-1132(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-192, ASSOCIATION WITH SHEP3.
[40]"Genetic determinants of hair, eye and skin pigmentation in Europeans."
Sulem P., Gudbjartsson D.F., Stacey S.N., Helgason A., Rafnar T., Magnusson K.P., Manolescu A., Karason A., Palsson A., Thorleifsson G., Jakobsdottir M., Steinberg S., Palsson S., Jonasson F., Sigurgeirsson B., Thorisdottir K., Ragnarsson R., Benediktsdottir K.R. expand/collapse author list , Aben K.K., Kiemeney L.A., Olafsson J.H., Gulcher J., Kong A., Thorsteinsdottir U., Stefansson K.
Nat. Genet. 39:1443-1452(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-192, ASSOCIATION WITH SHEP3.
+Additional computationally mapped references.

Web resources

Mutations of the TYR gene

Retina International's Scientific Newsletter

Albinism database (ADB)

TYR mutations

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Wikipedia

Tyrosinase entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27160 mRNA. Translation: AAB37227.1.
M63239 expand/collapse EMBL AC list , M63235, M63236, M63237, M63238 Genomic DNA. Translation: AAA61242.1.
J03581 mRNA. Translation: AAA61241.1. Different initiation.
Y00819 mRNA. Translation: CAA68756.1. Different initiation.
U01873 mRNA. Translation: AAB60319.1. Sequence problems.
M74314 mRNA. Translation: AAA61244.1.
X16073 Genomic DNA. Translation: CAA34205.1.
AF237811 expand/collapse EMBL AC list , AF237807, AF237808, AF237809, AF237810 Genomic DNA. Translation: AAK00805.1.
BC027179 mRNA. Translation: AAH27179.1.
AY012019 Genomic DNA. Translation: AAG38762.1.
CCDSCCDS8284.1. [P14679-1]
PIRYRHU1. A38444.
RefSeqNP_000363.1. NM_000372.4. [P14679-1]
UniGeneHs.503555.

3D structure databases

ProteinModelPortalP14679.
SMRP14679. Positions 172-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113150. 2 interactions.
STRING9606.ENSP00000263321.

Chemistry

BindingDBP14679.
ChEMBLCHEMBL1973.
DrugBankDB00548. Azelaic Acid.
DB01055. Mimosine.
DB00157. NADH.
GuidetoPHARMACOLOGY2643.

PTM databases

PhosphoSiteP14679.

Polymorphism databases

DMDM401235.

Proteomic databases

PaxDbP14679.
PRIDEP14679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263321; ENSP00000263321; ENSG00000077498. [P14679-1]
GeneID7299.
KEGGhsa:7299.
UCSCuc001pcs.3. human. [P14679-1]

Organism-specific databases

CTD7299.
GeneCardsGC11P088911.
GeneReviewsTYR.
HGNCHGNC:12442. TYR.
HPACAB000079.
MIM103470. phenotype.
203100. phenotype.
601800. phenotype.
606933. gene.
606952. phenotype.
neXtProtNX_P14679.
Orphanet352734. Minimal pigment oculocutaneous albinism type 1.
352740. Ocular albinism with congenital sensorineural deafness.
79431. Oculocutaneous albinism type 1A.
79434. Oculocutaneous albinism type 1B.
352737. Temperature-sensitive oculocutaneous albinism type 1.
PharmGKBPA37095.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG08919.
HOVERGENHBG003553.
InParanoidP14679.
KOK00505.
OMACLSLTQY.
OrthoDBEOG7TJ3HG.
PhylomeDBP14679.
TreeFamTF315865.

Enzyme and pathway databases

BioCycMetaCyc:HS01248-MONOMER.

Gene expression databases

BgeeP14679.
CleanExHS_TYR.
GenevestigatorP14679.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTyrosinase.
GenomeRNAi7299.
NextBio28547.
PROP14679.
SOURCESearch...

Entry information

Entry nameTYRO_HUMAN
AccessionPrimary (citable) accession number: P14679
Secondary accession number(s): Q15675 expand/collapse secondary AC list , Q15676, Q15680, Q8TAK4, Q9BYY0, Q9BZX1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 171 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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 11

Human chromosome 11: entries, gene names and cross-references to MIM