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Q99972 (MYOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myocilin
Alternative name(s):
Myocilin 55 kDa subunit
Trabecular meshwork-induced glucocorticoid response protein

Cleaved into the following 2 chains:

  1. Myocilin, N-terminal fragment
    Alternative name(s):
    Myocilin 20 kDa N-terminal fragment
  2. Myocilin, C-terminal fragment
    Alternative name(s):
    Myocilin 35 kDa N-terminal fragment
Gene names
Name:MYOC
Synonyms:GLC1A, TIGR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Subunit structure

Homodimer (via N-terminus). Interacts with OLFM3, FN1, NRCAM, GLDN and NFASC. Interacts (via N-terminus) with MYL2. Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt signaling. Interacts with SNTA1; regulates muscle hypertrophy. Interacts with ERBB2 and ERBB3; acivates ERBB2-ERBB3 signaling pathway. Interacts with SNCG; affects its secretion and its aggegation. Ref.11 Ref.16 Ref.17 Ref.18 Ref.27 Ref.31

Subcellular location

Secreted. Golgi apparatus. Cytoplasmic vesicle. Secretedextracellular space. Secretedextracellular spaceextracellular matrix. Secretedexosome. Mitochondrion. Mitochondrion intermembrane space. Mitochondrion inner membrane. Mitochondrion outer membrane. Rough endoplasmic reticulum. Cell projection. Cell projectioncilium. Note: Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum. It is only imported to mitochondria in the trabecular meshwork. Localizes to the Golgi apparatus in Schlemm's canal endothelial cells. Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles. Localizes in trabecular meshwork extracellular matrix. Ref.2 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.22 Ref.23 Ref.24

Myocilin, C-terminal fragment: Secreted Ref.2 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.22 Ref.23 Ref.24.

Myocilin, N-terminal fragment: Endoplasmic reticulum. Note: Remains retained in the endoplasmic reticulum. Ref.2 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.22 Ref.23 Ref.24

Tissue specificity

Expressed in large amounts in various types of muscle, ciliary body, papillary sphincter, skeletal muscle, heart, bone marrow-derived mesenchymal stem cells and other tissues. Expressed predominantly in the retina. In normal eyes, found in the inner uveal meshwork region and the anterior portion of the meshwork. In contrast, in many glaucomatous eyes, it is found in more regions of the meshwork and appeared more intensively than in normal eyes, regardless of the type or clinical severity of glaucoma. The myocilin 35 kDa fragment is detected in aqueous humor and at the less extend in iris and ciliary body. Ref.13

Post-translational modification

Different isoforms may arise by post-translational modifications.

Glycosylated. Ref.23

Palmitoylated By similarity.

Undergoes a calcium-dependent proteolytic cleavage at Arg-226 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper-like domain.

Involvement in disease

Glaucoma 1, open angle, A (GLC1A) [MIM:137750]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.4 Ref.13 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.62 Ref.63 Ref.64

Glaucoma 3, primary congenital, A (GLC3A) [MIM:231300]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor.
Note: The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (Ref.61). Ref.61

Sequence similarities

Contains 1 olfactomedin-like domain.

Sequence caution

The sequence BAA24532.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell projection
Cilium
Cytoplasmic vesicle
Endoplasmic reticulum
Extracellular matrix
Golgi apparatus
Membrane
Mitochondrion
Mitochondrion inner membrane
Mitochondrion outer membrane
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Glaucoma
   DomainCoiled coil
Signal
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERBB2-ERBB3 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

bone development

Inferred from sequence or structural similarity. Source: UniProtKB

clustering of voltage-gated sodium channels

Inferred from sequence or structural similarity. Source: UniProtKB

myelination in peripheral nervous system

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of Rho protein signal transduction

Inferred from direct assay Ref.25. Source: UniProtKB

negative regulation of cell-matrix adhesion

Inferred from direct assay Ref.25. Source: UniProtKB

negative regulation of stress fiber assembly

Inferred from direct assay Ref.25. Source: UniProtKB

neuron projection development

Inferred from mutant phenotype Ref.28. Source: UniProtKB

non-canonical Wnt signaling pathway via JNK cascade

Inferred from mutant phenotype Ref.27. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay Ref.30. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.29. Source: UniProtKB

positive regulation of focal adhesion assembly

Inferred from direct assay Ref.26. Source: UniProtKB

positive regulation of mitochondrial depolarization

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay Ref.29. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from direct assay Ref.29. Source: UniProtKB

positive regulation of stress fiber assembly

Inferred from direct assay Ref.27. Source: UniProtKB

positive regulation of substrate adhesion-dependent cell spreading

Inferred from direct assay Ref.26. Source: UniProtKB

regulation of MAPK cascade

Inferred from direct assay Ref.30. Source: UniProtKB

skeletal muscle hypertrophy

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.14. Source: UniProtKB

cilium

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle

Inferred from direct assay Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from direct assay Ref.17. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 17317787. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

mitochondrial inner membrane

Inferred from direct assay Ref.24. Source: UniProtKB

mitochondrial intermembrane space

Inferred from direct assay Ref.24. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay Ref.24. Source: UniProtKB

node of Ranvier

Inferred from sequence or structural similarity. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

rough endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfibronectin binding

Inferred from physical interaction Ref.17. Source: UniProtKB

frizzled binding

Inferred from physical interaction Ref.27. Source: UniProtKB

myosin light chain binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16Ref.27Ref.31. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.12
Chain33 – 504472Myocilin
PRO_0000020084
Chain33 – 226194Myocilin, N-terminal fragment
PRO_0000428749
Chain227 – 504278Myocilin, C-terminal fragment
PRO_0000428750

Regions

Domain244 – 503260Olfactomedin-like
Coiled coil74 – 184111 Potential
Motif502 – 5043Microbody targeting signal Potential

Sites

Site226 – 2272Cleavage; by CAPN2

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Probable
Disulfide bond245 ↔ 433

Natural variations

Natural variant41F → S.
VAR_009665
Natural variant91C → S.
VAR_009666
Natural variant121G → R. Ref.48 Ref.54
Corresponds to variant rs199752860 [ dbSNP | Ensembl ].
VAR_009667
Natural variant161P → L. Ref.54
VAR_054269
Natural variant171A → S. Ref.54
VAR_054270
Natural variant191Q → H. Ref.47
Corresponds to variant rs2234925 [ dbSNP | Ensembl ].
VAR_009668
Natural variant251C → R in GLC1A. Ref.56
VAR_054271
Natural variant481Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. Ref.58 Ref.61
VAR_054272
Natural variant531V → A in GLC1A. Ref.46
Corresponds to variant rs200208925 [ dbSNP | Ensembl ].
VAR_008969
Natural variant571N → D. Ref.44
VAR_054273
Natural variant571N → S Loss of higher molecular weight isoform. Ref.21 Ref.57
VAR_054274
Natural variant731N → S.
VAR_009669
Natural variant761R → K. Ref.38 Ref.44 Ref.47 Ref.48 Ref.52 Ref.53 Ref.54 Ref.57 Ref.58
Corresponds to variant rs2234926 [ dbSNP | Ensembl ].
VAR_009670
Natural variant771D → E. Ref.52
VAR_054275
Natural variant821R → C in GLC1A.
VAR_009671
Natural variant821R → H.
VAR_009672
Natural variant951L → P. Ref.54
VAR_054276
Natural variant1261R → W in GLC1A. Ref.52
Corresponds to variant rs200120115 [ dbSNP | Ensembl ].
VAR_054277
Natural variant1581R → Q in GLC1A. Ref.47
Corresponds to variant rs199746824 [ dbSNP | Ensembl ].
VAR_054278
Natural variant1891R → Q.
VAR_009673
Natural variant2031S → F.
VAR_009674
Natural variant2081D → E in GLC1A; unknown pathological significance. Ref.47 Ref.48 Ref.54
Corresponds to variant rs2234927 [ dbSNP | Ensembl ].
VAR_014943
Natural variant2151L → P. Ref.54
VAR_054279
Natural variant2441G → V in GLC1A; unknown pathological significance. Ref.64
VAR_054280
Natural variant2451C → Y in GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly. Ref.62
VAR_054281
Natural variant2461G → R in GLC1A. Ref.3
VAR_005468
Natural variant2511V → A in GLC1A. Ref.53
VAR_054282
Natural variant2521G → R in GLC1A. Ref.44 Ref.45 Ref.51 Ref.64
VAR_054283
Natural variant2611E → K in GLC1A. Ref.50
VAR_054284
Natural variant2721R → G in GLC1A; unknown pathological significance. Ref.44
VAR_054285
Natural variant2741P → R in GLC1A. Ref.60
VAR_054286
Natural variant2861W → R in GLC1A.
VAR_009675
Natural variant2931T → K in GLC1A. Ref.51 Ref.52
VAR_009676
Natural variant3001E → K in GLC1A; unknown pathological significance. Ref.54
VAR_054287
Natural variant3231E → K in GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. Ref.13 Ref.44
VAR_054288
Natural variant3291V → M. Ref.44
Corresponds to variant rs146391864 [ dbSNP | Ensembl ].
VAR_009677
Natural variant3371Q → E in GLC1A. Ref.50
VAR_054289
Natural variant3371Q → R in GLC1A. Ref.34
VAR_005469
Natural variant3411S → P in GLC1A. Ref.33
VAR_054290
Natural variant3421R → K in GLC1A. Ref.55
VAR_054291
Natural variant3451I → M in GLC1A. Ref.53
VAR_054292
Natural variant3521E → K in GLC1A; unknown pathological significance. Ref.35 Ref.52
Corresponds to variant rs61745146 [ dbSNP | Ensembl ].
VAR_009678
Natural variant3531T → I in GLC1A; unknown pathological significance. Ref.41 Ref.48 Ref.54
Corresponds to variant rs137853277 [ dbSNP | Ensembl ].
VAR_009679
Natural variant3601I → N in GLC1A. Ref.47 Ref.59
VAR_054293
Natural variant3611P → S in GLC1A.
VAR_009680
Natural variant3631A → T in GLC1A. Ref.47 Ref.59
VAR_054294
Natural variant3641G → V in GLC1A. Ref.4
VAR_005470
Natural variant3671G → R in GLC1A. Ref.32 Ref.36 Ref.37 Ref.51 Ref.52 Ref.53 Ref.57
VAR_005471
Natural variant3691F → L in GLC1A. Ref.59
VAR_054295
Natural variant3701P → L in GLC1A; severe form; inhibits endoproteolytic processing; produced the highest inhibition of the endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum; inhibits neurite outgrowth. Ref.3 Ref.13 Ref.32 Ref.35 Ref.36 Ref.38 Ref.44 Ref.51 Ref.53
VAR_005472
Natural variant3771T → K in GLC1A. Ref.51
VAR_054296
Natural variant3771T → M in GLC1A. Ref.35 Ref.44
VAR_009681
Natural variant3801D → A in GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. Ref.38
VAR_009682
Natural variant3801D → G in GLC1A. Ref.13
VAR_009683
Natural variant3801D → H in GLC1A. Ref.63
VAR_054297
Natural variant3801D → N in GLC1A. Ref.55
VAR_054298
Natural variant3931S → N in GLC1A. Ref.53
VAR_054299
Natural variant3931S → R in GLC1A.
VAR_009684
Natural variant3981K → R. Ref.44 Ref.50 Ref.51 Ref.52 Ref.57
Corresponds to variant rs56314834 [ dbSNP | Ensembl ].
VAR_009685
Natural variant3991G → V in GLC1A. Ref.51
Corresponds to variant rs28936694 [ dbSNP | Ensembl ].
VAR_054300
Natural variant4021V → I.
VAR_009686
Natural variant4141E → K. Ref.54
VAR_054301
Natural variant4221R → C.
VAR_009687
Natural variant4221R → H in GLC1A.
VAR_009688
Natural variant4231K → E in GLC1A; heterozygote specific phenotype. Ref.39 Ref.52 Ref.56
VAR_009689
Natural variant4251S → P.
VAR_009690
Natural variant4261V → F in GLC1A. Ref.37 Ref.44
VAR_005473
Natural variant4271A → T in GLC1A. Ref.52
VAR_054302
Natural variant4331C → R in GLC1A; severe form. Ref.49
VAR_008970
Natural variant4341G → S in GLC1A. Ref.53
VAR_054303
Natural variant4371Y → H in GLC1A. Ref.4 Ref.35
VAR_005474
Natural variant4381T → I in GLC1A. Ref.57
VAR_054304
Natural variant4451A → V in GLC1A. Ref.51 Ref.52
Corresponds to variant rs140967767 [ dbSNP | Ensembl ].
VAR_009691
Natural variant4481T → P in GLC1A. Ref.43 Ref.59
VAR_054305
Natural variant4501N → D in GLC1A. Ref.53
VAR_054306
Natural variant4651I → M in GLC1A.
VAR_009692
Natural variant4701R → C in GLC1A. Ref.53
VAR_009693
Natural variant4701R → H. Ref.47
VAR_054307
Natural variant4711Y → C in GLC1A; unknown pathological significance. Ref.54
VAR_054308
Natural variant4731Y → C.
VAR_009694
Natural variant4771I → N in GLC1A; induces stress fiber formation in only 5% of cells. Ref.27 Ref.44
VAR_009695
Natural variant4771I → S in GLC1A. Ref.3
VAR_005475
Natural variant4801N → K in GLC1A. Ref.3 Ref.57
VAR_005476
Natural variant4811P → L in GLC1A. Ref.52
VAR_009696
Natural variant4811P → T in GLC1A.
VAR_009697
Natural variant4951V → I.
VAR_009698
Natural variant4991I → F in GLC1A. Ref.3 Ref.57
VAR_005477
Natural variant4991I → S in GLC1A. Ref.44
VAR_054309
Natural variant5001K → R.
Corresponds to variant rs145977437 [ dbSNP | Ensembl ].
VAR_009699
Natural variant5021S → P in GLC1A. Ref.38
VAR_009700

Experimental info

Mutagenesis226 – 2305Missing: Impairs endoproteolytic processing. Ref.23
Mutagenesis2261R → A: Reduced processing. Impairs endoproteolytic processing; when associated with A-229 or A-230. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-229 or A-230. Ref.23
Mutagenesis2261R → Q: Slightly increases endoproteolytic processing. Ref.23
Mutagenesis2271I → G: Reduced processing. Ref.23
Mutagenesis2291K → A: Completely blocks endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226. Ref.23
Mutagenesis2301E → A: Impairs endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and released a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226. Ref.23

Sequences

Sequence LengthMass (Da)Tools
Q99972 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 9588C04F1D227623

FASTA50456,972
        10         20         30         40         50         60 
MRFFCARCCS FGPEMPAVQL LLLACLVWDV GARTAQLRKA NDQSGRCQYT FSVASPNESS 

        70         80         90        100        110        120 
CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH QLTLDQAARP QETQEGLQRE 

       130        140        150        160        170        180 
LGTLRRERDQ LETQTRELET AYSNLLRDKS VLEEEKKRLR QENENLARRL ESSSQEVARL 

       190        200        210        220        230        240 
RRGQCPQTRD TARAVPPGSR EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE 

       250        260        270        280        290        300 
GDTGCGELVW VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE 

       310        320        330        340        350        360 
YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN TETVKAEKEI 

       370        380        390        400        410        420 
PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA IVLSKLNPEN LELEQTWETN 

       430        440        450        460        470        480 
IRKQSVANAF IICGTLYTVS SYTSADATVN FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN 

       490        500 
PLEKKLFAWD NLNMVTYDIK LSKM 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of subtracted cDNAs from a human ciliary body library encoding TIGR, a protein involved in juvenile open angle glaucoma with homology to myosin and olfactomedin."
Ortego J., Escribano J., Coca-Prados M.
FEBS Lett. 413:349-353(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A novel myosin-like protein (myocilin) expressed in the connecting cilium of the photoreceptor: molecular cloning, tissue expression, and chromosomal mapping."
Kubota R., Noda S., Wang Y., Minoshima S., Asakawa S., Kudoh J., Mashima Y., Oguchi Y., Shimizu N.
Genomics 41:360-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Retina.
[3]"Recurrent mutations in a single exon encoding the evolutionarily conserved olfactomedin-homology domain of TIGR in familial open-angle glaucoma."
Adam M.F., Belmouden A., Binisti P., Brezin A.P., Valtot F., Bechetoille A., Dascotte J.-C., Copin B., Gomez L., Chaventre A., Bach J.-F., Garchon H.-J.
Hum. Mol. Genet. 6:2091-2097(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLC1A ARG-246; LEU-370; SER-477; LYS-480 AND PHE-499.
Tissue: Leukocyte.
[4]"Identification of a gene that causes primary open angle glaucoma."
Stone E.M., Fingert J.H., Alward W.L.M., Nguyen T.D., Polansky J.R., Sunden S.L.F., Nishimura D., Clark A.F., Nystuen A., Nichols B.E., Mackey D.A., Ritch R., Kalenak J.W., Craven E.R., Sheffield V.C.
Science 275:668-670(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS GLC1A VAL-364 AND HIS-437.
[5]"Genomic organization of the human myocilin gene (MYOC) responsible for primary open angle glaucoma (GLC1A)."
Kubota R., Kudoh J., Mashima Y., Asakawa S., Minoshima S., Hejtmancik J.F., Oguchi Y., Shimizu N.
Biochem. Biophys. Res. Commun. 242:396-400(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Characterization and comparison of the human and mouse GLC1A glaucoma genes."
Fingert J.H., Ying L., Swiderski R.E., Nystuen A.M., Arbour N.C., Alward W.L.M., Sheffield V.C., Stone E.M.
Genome Res. 8:377-384(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[8]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.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].
[10]"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].
Tissue: Brain.
[11]"Gene structure and properties of TIGR, an olfactomedin-related glycoprotein cloned from glucocorticoid-induced trabecular meshwork cells."
Nguyen T.D., Chen P., Huang W.D., Chen H., Johnson D., Polansky J.R.
J. Biol. Chem. 273:6341-6350(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-6 AND 33-37, SEQUENCE REVISION, OLIGOMERIZATION.
[12]"Dual localization of wild-type myocilin in the endoplasmic reticulum and extracellular compartment likely occurs due to its incomplete secretion."
Sohn S., Joe M.K., Kim T.E., Im J.E., Choi Y.R., Park H., Kee C.
Mol. Vis. 15:545-556(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-37, SUBCELLULAR LOCATION.
[13]"Myocilin mutations causing glaucoma inhibit the intracellular endoproteolytic cleavage of myocilin between amino acids Arg226 and Ile227."
Aroca-Aguilar J.D., Sanchez-Sanchez F., Ghosh S., Coca-Prados M., Escribano J.
J. Biol. Chem. 280:21043-21051(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 227-233, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANTS GLC1A LYS-323; LEU-370 AND GLY-380, PROTEOLYTIC PROCESSING.
[14]"Localization of myocilin to the golgi apparatus in Schlemm's canal cells."
O'Brien E.T., Ren X., Wang Y.
Invest. Ophthalmol. Vis. Sci. 41:3842-3849(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"Glucocorticoid induction of the glaucoma gene MYOC in human and monkey trabecular meshwork cells and tissues."
Clark A.F., Steely H.T., Dickerson J.E. Jr., English-Wright S., Stropki K., McCartney M.D., Jacobson N., Shepard A.R., Clark J.I., Matsushima H., Peskind E.R., Leverenz J.B., Wilkinson C.W., Swiderski R.E., Fingert J.H., Sheffield V.C., Stone E.M.
Invest. Ophthalmol. Vis. Sci. 42:1769-1780(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Optimedin: a novel olfactomedin-related protein that interacts with myocilin."
Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.
Hum. Mol. Genet. 11:1291-1301(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OLFM3.
[17]"In vitro localization of TIGR/MYOC in trabecular meshwork extracellular matrix and binding to fibronectin."
Filla M.S., Liu X., Nguyen T.D., Polansky J.R., Brandt C.R., Kaufman P.L., Peters D.M.
Invest. Ophthalmol. Vis. Sci. 43:151-161(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FN1, SUBCELLULAR LOCATION.
[18]"Protein interactions with myocilin."
Wentz-Hunter K., Ueda J., Yue B.Y.
Invest. Ophthalmol. Vis. Sci. 43:176-182(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYL2.
[19]"Distribution of myocilin and extracellular matrix components in the juxtacanalicular tissue of human eyes."
Ueda J., Wentz-Hunter K., Yue B.Y.
Invest. Ophthalmol. Vis. Sci. 43:1068-1076(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Expression and characterization of the olfactomedin domain of human myocilin."
Nagy I., Trexler M., Patthy L.
Biochem. Biophys. Res. Commun. 302:554-561(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND AT 245-CYS--CYS-433.
[21]"Characterization of rabbit myocilin: implications for human myocilin glycosylation and signal peptide usage."
Shepard A.R., Jacobson N., Sui R., Steely H.T., Lotery A.J., Stone E.M., Clark A.F.
BMC Genet. 4:5-5(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SER-57.
[22]"Extracellular trafficking of myocilin in human trabecular meshwork cells."
Hardy K.M., Hoffman E.A., Gonzalez P., McKay B.S., Stamer W.D.
J. Biol. Chem. 280:28917-28926(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"Characterization of the intracellular proteolytic cleavage of myocilin and identification of calpain II as a myocilin-processing protease."
Sanchez-Sanchez F., Martinez-Redondo F., Aroca-Aguilar J.D., Coca-Prados M., Escribano J.
J. Biol. Chem. 282:27810-27824(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY CAPN2, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF 226-ARG--GLU-230; ARG-226; ILE-227; LYS-229 AND GLU-230.
[24]"Mitochondrial association of myocilin, product of a glaucoma gene, in human trabecular meshwork cells."
Sakai H., Shen X., Koga T., Park B.C., Noskina Y., Tibudan M., Yue B.Y.
J. Cell. Physiol. 213:775-784(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MITOCHONDRIAL DEPOLARIZATION, SUBCELLULAR LOCATION.
[25]"Rho GTPase and cAMP/protein kinase A signaling mediates myocilin-induced alterations in cultured human trabecular meshwork cells."
Shen X., Koga T., Park B.C., SundarRaj N., Yue B.Y.
J. Biol. Chem. 283:603-612(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL-MATRIX ADHESION.
[26]"Myocilin promotes substrate adhesion, spreading and formation of focal contacts in podocytes and mesangial cells."
Goldwich A., Scholz M., Tamm E.R.
Histochem. Cell Biol. 131:167-180(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL ADHESION.
[27]"Myocilin is a modulator of Wnt signaling."
Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.
Mol. Cell. Biol. 29:2139-2154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN STRESS FIBER ASSEMBLY, INTERACTION WITH FRZB; FZD7; FZD10; FZD1 AND WIF1, CHARACTERIZATION OF VARIANT ASN-477.
[28]"Differential effects of myocilin and optineurin, two glaucoma genes, on neurite outgrowth."
Koga T., Shen X., Park J.S., Qiu Y., Park B.C., Shyam R., Yue B.Y.
Am. J. Pathol. 176:343-352(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURITE OUTGROWTH.
[29]"Myocilin, a glaucoma-associated protein, promotes cell migration through activation of integrin-focal adhesion kinase-serine/threonine kinase signaling pathway."
Kwon H.S., Tomarev S.I.
J. Cell. Physiol. 226:3392-3402(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[30]"Myocilin stimulates osteogenic differentiation of mesenchymal stem cells through mitogen-activated protein kinase signaling."
Kwon H.S., Johnson T.V., Tomarev S.I.
J. Biol. Chem. 288:16882-16894(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION.
[31]"Myocilin mediates myelination in the peripheral nervous system through ErbB2/3 signaling."
Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C., Tomarev S.I.
J. Biol. Chem. 288:26357-26371(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MYELINATION, INTERACTION WITH NFASC; GLDN AND NRCAM.
[32]"Mutations in the TIGR gene in familial primary open-angle glaucoma in Japan."
Suzuki Y., Shirato S., Taniguchi F., Ohara K., Nishimaki K., Ohta S.
Am. J. Hum. Genet. 61:1202-1204(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-367 AND LEU-370.
[33]"TIGR gene in primary open-angle glaucoma and steroid-induced glaucoma."
Kee C., Ahn B.-H.
Korean J. Ophthalmol. 11:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A PRO-341.
[34]"Identification of a new 'TIGR' mutation in a family with juvenile-onset primary open angle glaucoma."
Stoilova D., Child A., Brice G., Crick R.P., Fleck B.W., Sarfarazi M.
Ophthalmic Genet. 18:109-118(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A ARG-337.
[35]"Prevalence of mutations in TIGR/Myocilin in patients with adult and juvenile primary open-angle glaucoma."
Wiggs J.L., Allingham R.R., Vollrath D., Jones K.H., De La Paz M., Kern J., Patterson K., Babb V.L., Del Bono E.A., Broomer B.W., Pericak-Vance M.A., Haines J.L.
Am. J. Hum. Genet. 63:1549-1552(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A LYS-352; LEU-370; MET-377 AND HIS-437.
[36]"Juvenile open angle glaucoma: fine mapping of the TIGR gene to 1q24.3-q25.2 and mutation analysis."
Michels-Rautenstrauss K.G., Mardin C.Y., Budde W.M., Liehr T., Polansky J.R., Nguyen T., Timmerman V., van Broeckhoven C., Naumann G.O.H., Pfeiffer R.A., Rautenstrauss B.W.
Hum. Genet. 102:103-106(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-367 AND LEU-370.
[37]"Novel mutations in the TIGR gene in early and late onset open angle glaucoma."
Mansergh F.C., Kenna P.F., Ayuso C., Kiang A.-S., Humphries P., Farrar G.J.
Hum. Mutat. 11:244-251(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-367 AND PHE-426.
[38]"Novel TIGR/MYOC mutations in families with juvenile onset primary open angle glaucoma."
Stoilova D., Child A., Brice G., Desai T., Barsoum-Homsy M., Ozdemir N., Chevrette L., Adam M.F., Garchon H.-J., Pitts Crick R., Sarfarazi M.
J. Med. Genet. 35:989-992(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A LEU-370; ALA-380 AND PRO-502, VARIANT LYS-76.
[39]"Homozygotes carrying an autosomal dominant TIGR mutation do not manifest glaucoma."
Morissette J., Clepet C., Moisan S., Dubois S., Winstall E., Vermeeren D., Nguyen T.D., Polansky J.R., Cote G., Anctil J.-L., Amyot M., Plante M., Falardeau P., Raymond V.
Nat. Genet. 19:319-321(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A GLU-423.
[40]"Clinical features associated with mutations in the chromosome 1 open-angle glaucoma gene."
Alward W.L.M., Fingert J.H., Coote M.A., Johnson A.T., Lerner S.F., Junqua D., Durcan F.J., McCartney P.J., Mackey D.A., Sheffield V.C., Stone E.M.
N. Engl. J. Med. 338:1022-1027(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A, VARIANTS.
[41]"Mutations of the TIGR/MYOC gene in primary open-angle glaucoma in Korea."
Yoon S.-J.K., Kim H.-S., Moon J.-I., Lim J.M., Joo C.-K.
Am. J. Hum. Genet. 64:1775-1778(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A ILE-353.
[42]"Analysis of myocilin mutations in 1703 glaucoma patients from five different populations."
Fingert J.H., Heon E., Liebmann J.M., Yamamoto T., Craig J.E., Rait J., Kawase K., Hoh S.-T., Buys Y.M., Dickinson J., Hockey R.R., Williams-Lyn D., Trope G., Kitazawa Y., Ritch R., Mackey D.A., Alward W.L.M., Sheffield V.C., Stone E.M.
Hum. Mol. Genet. 8:899-905(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A, VARIANTS.
[43]"Detection of a new TIGR gene mutation in a Japanese family with primary open angle glaucoma."
Yokoyama A., Nao-i N., Date Y., Nakazato M., Chumann H., Chihara E., Sawada A., Matsukura S.
Jpn. J. Ophthalmol. 43:85-88(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A PRO-448.
[44]"Age-dependent prevalence of mutations at the GLC1A locus in primary open-angle glaucoma."
Shimizu S., Lichter P.R., Johnson A.T., Zhou Z., Higashi M., Gottfredsdottir M., Othman M., Moroi S.E., Rozsa F.W., Schertzer R.M., Clarke M.S., Schwartz A.L., Downs C.A., Vollrath D., Richards J.E.
Am. J. Ophthalmol. 130:165-177(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-252; GLY-272; LYS-323; LEU-370; MET-377; PHE-426; ASN-477 AND SER-499, VARIANTS ASP-57; LYS-76; MET-329 AND ARG-398, CHARACTERIZATION OF VARIANTS GLC1A ARG-252; GLY-272; LYS-323; LEU-370; MET-377; PHE-426; ASN-477 AND SER-499, CHARACTERIZATION OF VARIANTS ASP-57; LYS-76; MET-329 AND ARG-398.
[45]"Genetic screening in a large family with juvenile onset primary open angle glaucoma."
Booth A.P., Anwar R., Chen H., Churchill A.J., Jay J., Polansky J., Nguyen T., Markham A.F.
Br. J. Ophthalmol. 84:722-726(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A ARG-252.
[46]"Novel TIGR sequence alteration Val53Ala."
Pang C.P., Leung Y.F., Chua J.K.H., Baum L., Fan D.S.P., Lam D.S.
Hum. Mutat. 15:122-122(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A ALA-53.
[47]"Novel mutations in the myocilin gene in Japanese glaucoma patients."
Kubota R., Mashima Y., Ohtake Y., Tanino T., Kimura T., Hotta Y., Kanai A., Tokuoka S., Azuma I., Tanihara H., Inatani M., Inoue Y., Kudoh J., Oguchi Y., Shimizu N.
Hum. Mutat. 16:270-270(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A GLN-158; ASN-360 AND THR-363, VARIANTS HIS-19; LYS-76; GLU-208 AND HIS-470.
[48]"Truncations in the TIGR gene in individuals with and without primary open-angle glaucoma."
Lam D.S.C., Leung Y.F., Chua J.K.H., Baum L., Fan D.S.P., Choy K.W., Pang C.P.
Invest. Ophthalmol. Vis. Sci. 41:1386-1391(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A GLU-208 AND ILE-353, VARIANTS ARG-12 AND LYS-76.
[49]"Novel mutation in the MYOC gene in primary open glaucoma patients."
Vasconcellos J.P.C., Melo M.B., Tsukumo D.M.L., Basseres D.S., Bordin S., Saad S.T.O., Costa F.F.
J. Med. Genet. 37:301-303(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A ARG-433.
[50]"Mutations in the third exon of the MYOC gene in Spanish patients with primary open angle glaucoma."
Vazquez C.M., Herrero O.M.V., Bastus B.M., Perez V.D.
Ophthalmic Genet. 21:109-115(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A LYS-261 AND GLU-337, VARIANT ARG-398.
[51]"Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene."
Vincent A.L., Billingsley G., Buys Y., Levin A.V., Priston M., Trope G., Williams-Lyn D., Heon E.
Am. J. Hum. Genet. 70:448-460(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-252; LYS-293; ARG-367; LEU-370; LYS-377; VAL-399 AND VAL-445, VARIANT ARG-398.
[52]"Founder TIGR/myocilin mutations for glaucoma in the Quebec population."
The Quebec glaucoma network
Faucher M., Anctil J.-L., Rodrigue M.-A., Duchesne A., Bergeron D., Blondeau P., Cote G., Dubois S., Bergeron J., Arseneault R., Morissette J., Raymond V.
Hum. Mol. Genet. 11:2077-2090(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A TRP-126; LYS-293; LYS-352; ARG-367; GLU-423; THR-427; VAL-445 AND LEU-481, VARIANTS LYS-76; GLU-77 AND ARG-398.
[53]"Novel mutations in the MYOC/GLC1A gene in a large group of glaucoma patients."
Michels-Rautenstrauss K., Mardin C., Wakili N., Juenemann A.M., Villalobos L., Mejia C., Soley G.C., Azofeifa J., Oezbey S., Naumann G.O.H., Reis A., Rautenstrauss B.
Hum. Mutat. 20:479-480(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ALA-251; MET-345; ARG-367; LEU-370; ASN-393; SER-434; ASP-450 AND CYS-470, VARIANT LYS-76.
[54]"TIGR/MYOC gene sequence alterations in individuals with and without primary open-angle glaucoma."
Pang C.P., Leung Y.F., Fan B., Baum L., Tong W.C., Lee W.S., Chua J.K.H., Fan D.S.P., Liu Y., Lam D.S.C.
Invest. Ophthalmol. Vis. Sci. 43:3231-3235(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A LYS-300 AND CYS-471, VARIANTS ARG-12; LEU-16; SER-17; LYS-76; PRO-95; GLU-208; PRO-215; ILE-353 AND LYS-414.
[55]"Prevalence of myocilin mutations in adults with primary open-angle glaucoma in Ghana, West Africa."
Challa P., Herndon L.W., Hauser M.A., Broomer B.W., Pericak-Vance M.A., Ababio-Danso B., Allingham R.R.
J. Glaucoma 11:416-420(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A LYS-342 AND ASN-380.
[56]"Mutations in the myocilin gene in families with primary open-angle glaucoma and juvenile open-angle glaucoma."
Bruttini M., Longo I., Frezzotti P., Ciappetta R., Randazzo A., Orzalesi N., Fumagalli E., Caporossi A., Frezzotti R., Renieri A.
Arch. Ophthalmol. 121:1034-1038(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-25 AND GLU-423.
[57]"Myocilin analysis by DHPLC in French POAG patients: increased prevalence of Q368X mutation."
Melki R., Belmouden A., Brezin A., Garchon H.-J.
Hum. Mutat. 22:179-179(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ARG-367; ILE-438; LYS-480 AND PHE-499, VARIANTS SER-57; LYS-76 AND ARG-398.
[58]"Low frequency of myocilin mutations in Indian primary open-angle glaucoma patients."
Sripriya S., Uthra S., Sangeetha R., George R.J., Hemamalini A., Paul P.G., Amali J., Vijaya L., Kumaramanickavel G.
Clin. Genet. 65:333-337(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A HIS-48, VARIANT LYS-76.
[59]"Novel MYOC gene mutation, Phe369Leu, in Japanese patients with primary open-angle glaucoma detected by denaturing high-performance liquid chromatography."
Ishikawa K., Funayama T., Ohtake Y., Tanino T., Kurosaka D., Suzuki K., Ideta H., Fujimaki T., Tanihara H., Asaoka R., Naoi N., Yasuda N., Iwata T., Mashima Y.
J. Glaucoma 13:466-471(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A ASN-360; THR-363; LEU-369 AND PRO-448.
[60]"Genetic analysis of an Indian family with members affected with juvenile-onset primary open-angle glaucoma."
Markandaya M., Ramesh T.K., Selvaraju V., Dorairaj S.K., Prakash R., Shetty J., Kumar A.
Ophthalmic Genet. 25:11-23(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A ARG-274.
[61]"Myocilin gene implicated in primary congenital glaucoma."
Kaur K., Reddy A.B.M., Mukhopadhyay A., Mandal A.K., Hasnain S.E., Ray K., Thomas R., Balasubramanian D., Chakrabarti S.
Clin. Genet. 67:335-340(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC3A HIS-48.
[62]"Novel myocilin mutation in a Chinese family with juvenile-onset open-angle glaucoma."
Fan B.J., Leung D.Y.L., Wang D.Y., Gobeil S., Raymond V., Tam P.O.S., Lam D.S.C., Pang C.P.
Arch. Ophthalmol. 124:102-106(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A TYR-245, CHARACTERIZATION OF VARIANT GLC1A TYR-245.
[63]"Clinical features associated with an Asp380His Myocilin mutation in a US family with primary open-angle glaucoma."
Wirtz M.K., Samples J.R., Choi D., Gaudette N.D.
Am. J. Ophthalmol. 144:75-80(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1A HIS-380.
[64]"Myocilin Gly252Arg mutation and glaucoma of intermediate severity in Caucasian individuals."
Hewitt A.W., Bennett S.L., Richards J.E., Dimasi D.P., Booth A.P., Inglehearn C., Anwar R., Yamamoto T., Fingert J.H., Heon E., Craig J.E., Mackey D.A.
Arch. Ophthalmol. 125:98-104(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1A VAL-244 AND ARG-252.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001620 mRNA. Translation: AAC51725.1.
D88214 mRNA. Translation: BAA23531.1.
Z97171, Z97177, Z97174 Genomic DNA. Translation: CAB09899.1.
U85257 mRNA. Translation: AAC52051.1.
AB006688 Genomic DNA. Translation: BAA24532.1. Different initiation.
AF049793, AF049791, AF049792 Genomic DNA. Translation: AAC14264.1.
AK315443 mRNA. Translation: BAG37831.1.
Z98750 Genomic DNA. Translation: CAD92590.2.
CH471067 Genomic DNA. Translation: EAW90903.1.
BC029261 mRNA. Translation: AAH29261.1.
CCDSCCDS1297.1.
PIRJC5830.
RefSeqNP_000252.1. NM_000261.1.
UniGeneHs.436037.

3D structure databases

ProteinModelPortalQ99972.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110736. 43 interactions.
STRING9606.ENSP00000037502.

PTM databases

PhosphoSiteQ99972.

Polymorphism databases

DMDM3024209.

Proteomic databases

PaxDbQ99972.
PRIDEQ99972.

Protocols and materials databases

DNASU4653.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000037502; ENSP00000037502; ENSG00000034971.
GeneID4653.
KEGGhsa:4653.
UCSCuc001ghu.3. human.

Organism-specific databases

CTD4653.
GeneCardsGC01M171604.
HGNCHGNC:7610. MYOC.
HPAHPA027364.
MIM137750. phenotype.
231300. phenotype.
601652. gene.
neXtProtNX_Q99972.
Orphanet98976. Congenital glaucoma.
98977. Juvenile glaucoma.
PharmGKBPA31415.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298097.
HOGENOMHOG000059654.
HOVERGENHBG105662.
InParanoidQ99972.
OMARYKYSSM.
OrthoDBEOG75F4CZ.
PhylomeDBQ99972.
TreeFamTF315964.

Gene expression databases

ArrayExpressQ99972.
BgeeQ99972.
CleanExHS_MYOC.
GenevestigatorQ99972.

Family and domain databases

InterProIPR003112. Olfac-like.
[Graphical view]
PfamPF02191. OLF. 1 hit.
[Graphical view]
SMARTSM00284. OLF. 1 hit.
[Graphical view]
PROSITEPS51132. OLF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMYOC.
GenomeRNAi4653.
NextBio17936.
PROQ99972.
SOURCESearch...

Entry information

Entry nameMYOC_HUMAN
AccessionPrimary (citable) accession number: Q99972
Secondary accession number(s): B2RD84, O00620, Q7Z6Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 141 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 1

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