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Mutation Database
Mutations of the Tyrosinase Gene

Recent update from: 23.06.02


Phenotype Mutation Basechange Nucleotide Exon Restriction Site Classification
& Remarks
Mutation Database OMIM Reference






The sequence data are adjusted to a sequence given in a WORD file which can be downloaded here. Nucleotides are counted from the translation start site as used in most of the recent publications of TYR mutations.


OCA1A Deletion Exon1
0001 1

Compound:
  • 730delTG


(4)
AROA Met 1 Val ATG-GTG 0001 1

Compound:
  • R402Q
  • M320Q
  • Single

complete loss of activity
CM981972
(5)
(1)
OCA1A Met 1 Thr ATG-ACG 0002 1

CM981972
OCA1B 24delC TGC CTG-TG_ CTG 0024 1

No compound
CD972506
(23)
OCA1A 52delG GCT GGC-GCT G_C 0052 1

Heterozygous
No compound
CD982992
(13)
To online reference
OCA1A His 19 Gln CAT-CAA 0057 1

Heterozygous
No compound
CM981973
(13)
To online reference
OCA1A Pro 21 Ser CCT-TCT 0061 1

CM920692
(15)
(14)
(21)
(20)
OCA1 Cys 36 Tyr TGT-TAT 0107 1

CM992224
(18)
OCA1A Asp 42 Gly GAC-GGC 0125 1

CM910379
(15)
(14)
(21)
(20)
OCA1A Gly 47 Asp GGC-GAC 0140 1 -HaeIII
Homozygous
Compound:
  • T373K
  • L216M
  • P81L
  • 649del C
CM930711
(16)
(14)
(15)
(21)
(3)
(20)
OCA1A Ser 50 ter TCA-TGA 0149 1

Homozygous
CM941343
(6)
OCA1A Arg 52 Ile AGA-ATA 0155 1

Heterozygous
Compound:
  • D383N
CM981974
(13)
To online reference
AROA Cys 55 Tyr TGT-TAT 0164 1

Compound:
  • R402Q
CM910380
(5)
(14)
(20)
OCA1A Cys 55 Tyr TGT-TAT 0165 1

Disrupts disulfide bond or elminates copper binding
Compound:
  • R402Q
  • Single
CM910380
(15)
(21)
(30)
(2)
(5)
To online reference
OCA1B 223delG GTG GAT-GTG _AT 0222 1

Heterozygous
No compound
CD982993
(13)
To online reference
OCA2 Arg 77 Trp CGG-TGG 0229 1

Compound:
  • 1164delT
CM900220
(18)
OCA1B Arg 77 Trp CGG-TGG 0229 1

Heterozygous
Compound:
  • V275F

reported as R77C (CGG-TGT)
CM971542
(13)
(23)
To online reference
OCA2 Arg 77 Gln CGG-CAG 0230 1 -MspI
Compound:
  • IVS2-7t-a
CM900220
(18)
(3)
OCA1A Arg 77 Gln CGG-CAG 0230 1 -MspI
Compound:
  • 926insC
  • 731delGT
  • -959delg + -801ins gagagggaga + -691ins c + -682ins g + -658del c
  • R299H
CM900220
(15)
(14)
(21)
(20)
(26)
(17)
(18)
(12)
OCA1B Glu 78 ter GAG-TAG 0232 1

Compound:
  • G446S
CM971543
(23)
OCA1A Glu 78 ter GAG-TAG 0232 1

Compound:
  • G446S
CM971543
(23)
OCA1 232insGGG CGG GAG - CGG GGG GAG 0232 1



(30)
To online reference
OCA1A Trp 80 Arg TGG-CGG 0238 1

Compound:
  • G446S
  • R402Q
CM971544
(23)
OCA1A Trp 80 ter TGG-TGA 0240 1

Heterozygous
Compound:
  • G47D
CM981975
(13)
(3)
To online reference
OCA1A Pro 81 Leu CCT-CTT 0242 1

Homozygous
Compound:
  • R217G
  • N371T
  • G47D
  • G446S
CM900221
(8)
(23)
(16)
(14)
(18)
(15)
(21)
OCA1 Cys 89 Arg TGC-CGC 0265 1 -BsrI
Resides in critical domain (C-G-N-C) conserved in TYR of different species and in TRP1 and TRP2
unprocessed and misfolded glycoform
remains in ER
possibly involved in C-C bonds
CM910381
(24)
(20)
(14)
(15)
(21)
(10)
OCA1A 286insA TTC ATG- TTC AAT G 0286 1

CI910577
(15)
(14)
(21)
(20)
OCA1A Gly 97 Arg GGA-AGA 0289 1

Heterozygous
Compound:
  • 731delGT (affects EGF-like site)
  • T373K
CM981976
(13)
(18)
To online reference
OCA Gly 109 Arg GGA-AGA 0325 1

Possibly affects protein interactions and glycosylation
Compound:
  • T373K


(3)
To online reference
OCA 336delCA TGC ACA GGA-TG_ _CA 0336 1

Compound:
  • T373K
CD931054
(3)
To online reference
OCA1A 340delGA ACA GAG AGA CGA-ACA __G AGA CGA 0340 1

Homozygous
Compound:
  • R403S
CD931054
(15)
(21)
(18)
OCA1A Arg 116 ter CGA-TGA 0346 1

Heterozygous
No compound
CM981977
(13)
To online reference
OCA1 Pro 152 Ser CCC-TCC 0456 1

Compound:
  • A355A
CM941344
(6)
(21)
OCA1 459insT ATA GGG - ATT AGGG 0459 1

Compound:
  • IVS2-7t-a
  • T373K
CI992295
(18)
OCA1 Phe 176 Ile TTT-ATT 0526 1

CM930712
(16)
(14)
(15)
(21)
OCA1 Trp 178 ter TGG-TAG 0533 1 +XbaI
CM910382
(7)
(14)
(15)
(21)
(20)
OCA1A 571delG CTT GGG GGA-CTT _GG GGA 0568 1

CD910558
(15)
(14)
(21)
(20)
Polymorphism Ser 192 Tyr TCT-TAT 0575 1 -DpnI, +MspI
Compound:
  • R402Q - 27% activity at 37 C


(15)
(14)
(21)
(20)
(18)
OCA Pro 205 Thr CCA-ACA 0613 1

Impairs copper-binding


(3)
To online reference
OCA1 Ala 206 Thr GCT-ACT 0616 1 -AluI
CM910383
(11)
(14)
(15)
(20)
OCA1 Leu 216 Met TTG-ATG 0646 1

Compound:
  • G47D
CM930713
(16)
(14)
(15)
(21)
OCA 649delC TTG CGG-TTG _GG 0649 1

Compound:
  • R217W
CD941801
(21)
(18)
OCA1A Arg 217 Gly CGG-GGG 0649 1 -AciI
Compound:
  • P81L
CM971545
(23)
(22)
OCA2 Arg 217 Trp CGG-TGG 0649 1 -AciI
Compound:
  • 649delC
CM920693
(18)
(14)
(20)
OCA1 Arg 217 Trp CGG-TGG 0649 1 -AciI
Compound:
  • 649delC
CM920693
(29)
(15)
(14)
(21)
(18)
OCA1 Arg 217 Gln CGG-CAG 0650 1 -AciI
Compound:
  • E294K
CM930714
(14)
(15)
(21)
(18)
OCA 678delAGG ACA GGA-AC_ __A 0678 1

Compound:
  • T373K


(3)
To online reference
OCA1 Trp 236 ter TGG-TAG 0707 1

Homozygous
CM930715
(16)
(20)
(14)
(15)
(21)
OCA1 Trp 236 Ser TGG-TCG 0707 1

Compound:
  • F439V
CM930715
(18)
OCA1A 730delTG AAG TGT GAC-AAG __T GAC 0730 1

Compound:
  • IVS2-7t-a
  • R77Q
  • N371Y (OCA2)
  • Deletion exon 1
CD910559
(15)
(14)
(21)
(20)
(18)
(4)
OCA1A Gly 253 Arg GGA-AGA 0757 1 -MnlI
Homozygous
CM971546
(23)
OCA His 256 Tyr CAC-TAC 0766 1



(3)
To online reference
OCA1 Trp 272 Cys TGG-TGC 0816 1

Compound:
  • R422Q
CM992226
(18)
OCA1 IVS1-3c-g acag - agag 0820 2

Abberant splicing


(30)
To online reference
OCA1 Val 275 Phe GTC-TTC 0823 2

CM910384
(9)
(14)
(20)
OCA1B Val 275 Phe GTC-TTC 0825 2

Compound:

    R77W
    IVS2-1g-a
CM910384
(23)
(15)
(3)
OCA1 Arg 278 ter CGA-TGA 0832 2

CM930716
(28)
(6)
(21)
(20)
OCA1 840delG GAG GAG-GA_ GAG 0840 2

Homozygous
CD992281
(18)
OCA1 871delTT TCT TTA - TC_ _TA 0871 2



(30)
To online reference
OCA1A 871delT TCT TTA-TC_ TTA 0871 2

Compound:
  • no
CD931055
(17)
(20)
OCA1A Cys 289 Arg TGC-CGC 0875 2

Heterozygous
Compound:

    M1T
    G446S
CM992227
(13)
(18)
To online reference
OCA1 Cys 289 Gly TGC-GGC 0875 2

Disrupts disulfide bond, affecting protein folding and/or stability


(30)
To online reference
OCA1 Glu 294 Lys GAG-AAG 0890 2

Compound:
  • IVS2-7 t-a
  • R217Q
CM941345
(6)
(18)
(3)
OCA1 Glu 294 Gly GAG-GGG 0891 2

Compound:
  • R403S
CM9992227
(18)
OCA1 Arg 299 Ser CGT-AGT 0895 2

Homozygous
Disrupts copper binding
CM971547
(23)
(30)
(14)
(20)
To online reference
OCA1A Arg 299 His CGT-CAT 0896 2

Heterozygous
Compound:
  • 926insC

Disrupts copper binding
CM920694
(29)
(15)
(6)
(21)
(17)
(31)
To online reference
OCA1 Arg 299 His CGT-CAT 0896 2

CM920694
(17)
OCA1A 926insC AGA ACC CCA AGG-AGA ACC CCC AAG G 0926 2

Compound:
  • IVS2-10deltt-7t-a
  • R77Q
  • R299H
  • No compound
CI910578
(15)
(14)
(21)
(20)
(30)
(17)
(27)
(29)
OCA1A Leu 312 Val CTC-GTC 0934 2

Heterozygous
Compound:
  • P313R
CM981979
(13)
To online reference
OCA1A Pro 313 Arg CCC-CGC 0938 2

Heterozygous
Compound:
  • L312V
CM981980
(13)
To online reference
OCA1B Thr 325 Ala ACC-GCC 0973 2

No compound
CM971548
(23)
OCA1 Glu 328 Gln GAA-CAA 0982 2 -HinfI
CM930717
(28)
(21)
(20)
OCA1A Ser 339 Gly AGC-GGC 1015 2 -AluI
No compound
CM971549
(23)
(3)
OCA1B Phe 340 Leu TTT-CTT 1018 2

Heterozygous
No compound
CM981981
(13)
To online reference
OCA1B IVS2-10deltt-7t-a tttttaatgaa-ttt__aaagaa 1037 IVS2

Compound:
  • 928insC


(17)
OCA1B IVS2-7t-a ttttgt-tttagt 1037 IVS2

Compound:
  • S380P
  • H390D
  • 731delGT
CS930868
(23)
(21)
(18)
(20)
(19)
OCA1B IVS2-1g-a cagAT-caaAT 1037 IVS2

Compound:
  • V275F
CS971924
(23)
OCA1B Ala 355 Pro GCG-CCG 1063 3 -AciI
Compound:
  • D448N
  • P406L
  • R403S
CM971550
(23)
(21)
(20)
(18)
(3)
OCA1A Gln 359 ter CAA-TAA 1075 3

Compound:
  • T373K
CM971551
(23)
OCA1A Ser 361 Arg AGC-CGC 1081 3



(25)
OCA1A His 367 Arg CAC-CGC 1100 3



(15)
OCA1 His 367 Tyr CAC-TAC 1100 3

CM941346
(1)
OCA1 Met 370 Thr ATG-ACG 1109 3

No Activity
Compound:
  • M1V
  • R402Q
CM941347
(1)
OCA1A Asn 371 Tyr AAT-TAT 1111 3

Compound:
  • 731delGT
CM992228
(18)
(14)
(25)
OCA1A Asn 371 Thr AAT-ACT 1112 3

Compound:
  • P81L
CM930718
(16)
(15)
(21)
(20)
OCA1A Thr 373 Lys ACA-AAA 1118 3

Compound:
  • Q359X
  • S395N
  • 49insT
  • A355P
  • P406L
  • 336delCA
  • 678delAGG
  • G109R
  • R402Q
  • Homozygous

destroys glycosylation site at N371
retained in ER
CM900222
(23)
(20)
(16)
(14)
(15)
(18)
(6)
(21)
(3)
(10)
(1)
OCA1A Gln 376 ter CAG-TAG 1126 3 -MvaI
CM930719
(21)
(20)
OCA1A Gln 378 ter CAG-TAG 1132 3 -Csp6I
CM920695
(15)
(14)
(20)
OCA1B Ser 380 Pro TCT-CCT 1138 3 -DpnI
Compound:
  • IVS2-7t-a
CM971553
(23)
(20)
OCA1A Asn 382 Lys AAC-AAA 1146 3

CM920696
(15)
(21)
(14)
(20)
OCA1A Asp 383 Asn GAT-AAT 1147 3 -DpnI
CM900223
(15)
(21)
(3)
(20)
(17)
(14)
OCA1A 1161delT TTC CTT CTT-TTC C_T CTT 1160 3



(15)
OCA2 1163delT CTT CAC-C_T CAC 1163 3

CD920914
(29)
(18)
(20)
OCA1B His 390 Asp CAT-GAT 1168 3 -NlaIII
Compound:
  • IVS2-7t-a
CM971553
(23)
(21)
(20)
OCA1A Ser 395 Asp AGT-AAT 1183 4

Compound:
  • T373K
CM971554
(23)
OCA1 Trp 400 Leu TGG-TTG 1199 4

Disrupts copper binding


(30)
To online reference
OCA1A Arg 402 ter CGA-TGA 1204 4

Homozygous
CM941348
(6)
(21)
(18)
(20)
Polymorphism Arg 402 Gln CGA-CAA 1205 4

Temperature sensitive variant with permissive temperature at 32 C and non-permissive at 37 C
At non permissive temperature retained in the ER bound to calnexin
Compound:
  • No
CM971555
(15)
(21)
(20)
AROA Arg 402 Gln CGA-CAA 1205 4

Temperature sensitive variant with permissive T at 32 C and non-permissive T at 37 C (27% activity of WT)
Compound:
  • C55Y
  • M1V both on S195Y background
  • M370T
CM971555
(10)
(5)
(1)
(14)
(20)
OCA1B Arg 403 Ser AGG-AGT 1209 4

Compound:
  • A355P
  • R403S
  • E294G
  • 344delGA
CM981982
(15)
(14)
(21)
(20)
(18)
OCA1A His 404 Pro CAC-CCC 1211 4

Heterozygous
Compound:
  • Q452X
CM910385
(13)
To online reference
OCA1B Pro 406 Leu CCT-CTT 1217 4

CM910386
(15)
(14)
(21)
(20)
(18)
OCA1A Gly 419 Arg GGA-AGA 1255 4

Homozygous
CM910386
(15)
(14)
(21)
(20)
(18)
OCA1TS Arg 422 Gln CGG-CAG 1265 4

Compound:
  • W272C
CM910687
(15)
(14)
(21)
(20)
(18)
(2)
OCA1A Pro 431 Leu CCA-CTA 1292 4

CM930720
(21)
(20)
OCA1A 1314delCTTT TTC TTT ATT-TT_ ___ ATT 1314 4

CD920915
(15)
(14)
(21)
OCA1A 1315delTTTinsC TTC TTT ATT-TTC CAT T 1314 4

CD920915
(2)
OCA1 Phe 439 Val TTT-GTT 1315 5

Compound:
  • W236S
CM992229
(18)
OCA1A Gly 446 Ser GGC-AGC 1336 4

Compound:
  • E78S
  • W80R
  • C289R
CM920698
(23)
(20)
(15)
(14)
(18)
(3)
OCA1A Asp 448 Asn GAC-AAC 1342 4

Homozygous
Compound:
  • A355P
  • C289R
CM920699
(23)
(20)
(15)
(14)
(18)
OCA1A Gln 453 ter CAA-TAA 1357 4

CM920700
(15)
(14)
OCA1B IVS4+5a-g aaa gt-aag gt 1366 IVS4

No compound
CS971925
(23)
OCA1B IVS4+4a-g aaa gt-aga gt 1366 IVS4



(20)
OCA1A 1467insT ACT-ACTT 1467 5

CI910578
(15)
(20)
(14)
(21)
OCA1A 1501insC CGT-CCGT 1501 5

CI910579
(15)
(14)
(21)
(20)
Polymorphism -301c/t aacct-aatct -301 5'UTR



(14)
Polymorphism -199c/a tcgaa-tagaa -199 5'UTR



(14)
Polymorphism -658del c tgcag ctatc-tg_ag ctatc -658 5'UTR



(12)
Polymorphism -682ins g tgaac aaatc-tgaag caaatc -682 5'UTR



(12)
Polymorphism -691ins c tatcc cacaa-tatcc ccaca a -691 5'UTR



(12)
Polymorphism -801ins gagagggaga gaggg agagg-gaggg gagag ggaga agagg -801 5'UTR



(12)
Polymorphism -961del g gaggg ggaga-gaggg g_aga -961 5'UTR



(12)

References

  1. Breimer,L.H., Winder,A.F., Jay,B., and Jay,M. Initiation codon mutation of the tyrosinase gene as a cause of human albinism. 1994; Clin.Chim.Acta. 227: 17-22.
    Goto Top

  2. Breimer,L.H., Winder,A.F., Panayiotidis,P., Jay,M., Moore,A., and Jay,B. A trinucleotide deletion together with a base duplication event at codon 439 in the human tyrosinase gene identifies a mutational hotspot. 1995; Clin.Chim.Acta. 243: 35-42.
    Goto Top

  3. 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., and Abitbol,M. Mutation analysis of the tyrosinase gene in oculocutaneous albinism. 2001; Hum.Mutat. 17: 352
    Link to PubMed
    Human Mutation Online
    Goto Top

  4. Coupry,I., Taine,L., Goizet,C., Soriano,C., Mortemousque,B., Arveiler,B., and Lacombe,D. Leucodystrophy and oculocutaneous albinism in a child with an 11q14 deletion. 2001; J.Med.Genet. 38: 35-38.
    Link to PubMed
    Goto Top

  5. Fukai,K., Holmes,S.A., Lucchese,N.J., Siu,V.M., Weleber,R.G., Schnur,R.E., and Spritz,R.A. Autosomal recessive ocular albinism associated with a functionally significant tyrosinase gene polymorphism. 1995; Nat.Genet. 9: 92-95.
    Link to PubMed
    Goto Top

  6. Gershoni Baruch,R., Rosenmann,A., Droetto,S., Holmes,S., Tripathi,R.K., and Spritz,R.A. Mutations of the tyrosinase gene in patients with oculocutaneous albinism from various ethnic groups in Israel. 1994; Am.J.Hum.Genet. 54: 586-594.
    Goto Top

  7. Giebel,L.B., Musarella,M.A., and Spritz,R.A. A nonsense mutation in the tyrosinase gene of Afghan patients with tyrosinase negative (type IA) oculocutaneous albinism. 1991; J.Med.Genet. 28: 464-467.
    Link to PubMed
    Goto Top

  8. Giebel,L.B., Strunk,K.M., King,R.A., Hanifin,J.M., and Spritz,R.A. A frequent tyrosinase gene mutation in classic, tyrosinase- negative (type IA) oculocutaneous albinism. 1990; Proc.Natl.Acad.Sci.U.S.A. 87: 3255-3258.
    Goto Top

  9. Giebel,L.B., Tripathi,R.K., Strunk,K.M., Hanifin,J.M., Jackson,C.E., King,R.A., and Spritz,R.A. Tyrosinase gene mutations associated with type IB ("yellow") oculocutaneous albinism. 1991; Am.J.Hum.Genet. 48: 1159-1167.
    Link to PubMed
    Goto Top

  10. Halaban,R., Svedine,S., Cheng,E., Smicun,Y., Aron,R., and Hebert,D.N. Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism. 2000; Proc.Natl.Acad.Sci.U.S.A. 97: 5889-5894.
    Link to PubMed
    Goto Top

  11. King,R.A., Mentink,M.M., and Oetting,W.S. Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism. 1991; Mol.Biol.Med. 8: 19-29.
    Goto Top

  12. Matsunaga,J., Dakeishi,M., Miyamura,Y., and Tomita,Y. Sequence analysis of the human tyrosinase promoter from a patient with tyrosinase-negative oculocutaneous albinism. 1997; Pigment Cell Res. 10: 64-67.
    Goto Top

  13. Oetting,W.S., Fryer,J.P., and King,R.A. Mutations of the human tyrosinase gene associated with tyrosinase related oculocutaneous albinism (OCA1). 1998; Hum.Mutat. 12: 433-434.
    Link to PubMed
    Human Mutation Online
    Goto Top

  14. Oetting,W.S. and King,R.A. Molecular basis of type I (tyrosinase-related) oculocutaneous albinism: mutations and polymorphisms of the human tyrosinase gene. 1993; Hum.Mutat. 2: 1-6.
    Goto Top

  15. Oetting,W.S. and King,R.A. Analysis of tyrosinase mutations associated with tyrosinase- related oculocutaneous albinism (OCA1). 1994; Pigment Cell Res. 7: 285-290.
    Goto Top

  16. Oetting,W.S., Witkop,C.J., Jr., Brown,S.A., Colomer,R., Fryer,J.P., Bloom,K.E., and King,R.A. A frequent tyrosinase gene mutation associated with type I-A (tyrosinase-negative) oculocutaneous albinism in Puerto Rico. 1993; Am.J.Hum.Genet. 52: 17-23.
    Goto Top

  17. Park,S.K., Lee,K.H., Park,K.C., Lee,J.S., Spritz,R.A., and Lee,S.T. Prevalent and novel mutations of the tyrosinase gene in Korean patients with tyrosinase-deficient oculocutaneous albinism. 1997; Mol.Cells. 7: 187-191.
    Goto Top

  18. Passmore,L., Kaesmann-Kellner,B., and Weber,B.H.F. Novel and recurrent mutations in the tyrosinase gene and the P gene in the German albino population. 1999; Hum.Genet. 105: 200-210.
    Goto Top

  19. Schnur,R.E., Sellinger,B.T., Holmes,S.A., Wick,P.A., Tatsumura,Y.O., and Spritz,R.A. Type I oculocutaneous albinism associated with a full-length deletion of the tyrosinase gene. 1996; J.Invest.Dermatol. 106: 1137-1140.
    Goto Top

  20. Spritz,R.A. Molecular genetics of oculocutaneous albinism. 1993; Semin.Dermatol. 12: 167-172.
    Goto Top

  21. Spritz,R.A. Molecular genetics of oculocutaneous albinism. 1994; Hum.Mol.Genet. 3 Spec No: 1469-1475.
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  22. Spritz,R.A., Lee,S.T., Fukai,K., Brondum Nielsen,K., Chitayat,D., Lipson,M.H., Musarella,M.A., Rosenmann,A., and Weleber,R.G. Novel mutations of the P gene in type II oculocutaneous albinism (OCA2). 1997; Hum.Mutat. 10: 175-177.
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  23. 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., and Levin,A.V. Novel mutations of the tyrosinase (TYR) gene in type I oculocutaneous albinism (OCA1). 1997; Hum.Mutat. 10: 171-174.
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  24. Spritz,R.A., Strunk,K.M., Hsieh,C.L., Sekhon,G.S., and Francke,U. Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism. 1991; Am.J.Hum.Genet. 48: 318-324.
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  25. Summers,C.G., Oetting,W.S., and King,R.A. Diagnosis of oculocutaneous albinism with molecular analysis. 1996; Am.J.Ophthalmol. 121: 724-726.
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  26. Takeda,A., Tomita,Y., Matsunaga,J., Tagami,H., and Shibahara,S. Molecular basis of tyrosinase-negative oculocutaneous albinism. A single base mutation in the tyrosinase gene causing arginine to glutamine substitution at position 59. 1990; J.Biol.Chem. 265: 17792-17797.
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  27. Tomita,Y., Takeda,A., Okinaga,S., Tagami,H., and Shibahara,S. Human oculocutaneous albinism caused by single base insertion in the tyrosinase gene. 1989; Biochem.Biophys.Res.Commun. 164: 990-996.
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  28. Tripathi,R.K., Bundey,S., Musarella,M.A., Droetto,S., Strunk,K.M., Holmes,S.A., and Spritz,R.A. Mutations of the tyrosinase gene in Indo-Pakistani patients with type I (tyrosinase-deficient) oculocutaneous albinism (OCA). 1993; Am.J.Hum.Genet. 53: 1173-1179.
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  29. Tripathi,R.K., Strunk,K.M., Giebel,L.B., Weleber,R.G., and Spritz,R.A. Tyrosinase gene mutations in type I (tyrosinase-deficient) oculocutaneous albinism define two clusters of missense substitutions. 1992; Am.J.Med.Genet. 43: 865-871.
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  30. Tsai,C.H., Tsai,F.J., Wu,J.Y., Lin,S.P., Chang,J.G., Yang,C.F., and Lee,C.C. Insertion/deletion mutations of type I oculocutaneous albinism in chinese patients from Taiwan. 1999; Hum.Mutat.Online. 14: 542
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  31. Tsai,H.J., Ma,G.C., Wang,T.M., and Su,C.Y. Molecular Structures And Regulatory Elements Of The Commom Carp Rhodopsin Gene. 2000; Invest.Ophthalm.Vis.Sci. S389
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This site is maintained and edited by
Dr. rer. medic. Markus Preising, Dipl.Biol.
Molecular Genetics Laboratory
Department of Paediatric Ophthalmology, Strabismology and Ophthalmogenetics
University of Regensburg
Head: Prof. Dr. med. Birgit Lorenz