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Q99972

- MYOC_HUMAN

UniProt

Q99972 - MYOC_HUMAN

Protein

Myocilin

Gene

MYOC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    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.8 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei226 – 2272Cleavage; by CAPN2

    GO - Molecular functioni

    1. fibronectin binding Source: UniProtKB
    2. frizzled binding Source: UniProtKB
    3. myosin light chain binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. bone development Source: UniProtKB
    2. clustering of voltage-gated sodium channels Source: UniProtKB
    3. ERBB2-ERBB3 signaling pathway Source: UniProtKB
    4. myelination in peripheral nervous system Source: UniProtKB
    5. negative regulation of cell-matrix adhesion Source: UniProtKB
    6. negative regulation of Rho protein signal transduction Source: UniProtKB
    7. negative regulation of stress fiber assembly Source: UniProtKB
    8. neuron projection development Source: UniProtKB
    9. non-canonical Wnt signaling pathway via JNK cascade Source: UniProtKB
    10. osteoblast differentiation Source: UniProtKB
    11. positive regulation of cell migration Source: UniProtKB
    12. positive regulation of focal adhesion assembly Source: UniProtKB
    13. positive regulation of mitochondrial depolarization Source: UniProtKB
    14. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    15. positive regulation of protein kinase B signaling Source: UniProtKB
    16. positive regulation of stress fiber assembly Source: UniProtKB
    17. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    18. regulation of MAPK cascade Source: UniProtKB
    19. skeletal muscle hypertrophy Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myocilin
    Alternative name(s):
    Myocilin 55 kDa subunit
    Trabecular meshwork-induced glucocorticoid response protein
    Cleaved into the following 2 chains:
    Alternative name(s):
    Myocilin 20 kDa N-terminal fragment
    Alternative name(s):
    Myocilin 35 kDa N-terminal fragment
    Gene namesi
    Name:MYOC
    Synonyms:GLC1A, TIGR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7610. MYOC.

    Subcellular locationi

    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.
    Chain Myocilin, N-terminal fragment : Endoplasmic reticulum
    Note: Remains retained in the endoplasmic reticulum.

    GO - Cellular componenti

    1. cilium Source: UniProtKB-SubCell
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. cytoplasmic vesicle Source: UniProtKB
    4. endoplasmic reticulum Source: UniProtKB
    5. extracellular matrix Source: UniProtKB
    6. extracellular space Source: MGI
    7. extracellular vesicular exosome Source: UniProtKB
    8. Golgi apparatus Source: UniProtKB
    9. mitochondrial inner membrane Source: UniProtKB
    10. mitochondrial intermembrane space Source: UniProtKB
    11. mitochondrial outer membrane Source: UniProtKB
    12. node of Ranvier Source: UniProtKB
    13. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    14. rough endoplasmic reticulum Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, Extracellular matrix, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.34 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251C → R in GLC1A. 1 Publication
    VAR_054271
    Natural varianti48 – 481Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. 2 Publications
    VAR_054272
    Natural varianti53 – 531V → A in GLC1A. 1 Publication
    Corresponds to variant rs200208925 [ dbSNP | Ensembl ].
    VAR_008969
    Natural varianti82 – 821R → C in GLC1A.
    VAR_009671
    Natural varianti126 – 1261R → W in GLC1A. 1 Publication
    Corresponds to variant rs200120115 [ dbSNP | Ensembl ].
    VAR_054277
    Natural varianti158 – 1581R → Q in GLC1A. 1 Publication
    Corresponds to variant rs199746824 [ dbSNP | Ensembl ].
    VAR_054278
    Natural varianti208 – 2081D → E in GLC1A; unknown pathological significance. 3 Publications
    Corresponds to variant rs2234927 [ dbSNP | Ensembl ].
    VAR_014943
    Natural varianti244 – 2441G → V in GLC1A; unknown pathological significance. 1 Publication
    VAR_054280
    Natural varianti245 – 2451C → Y in GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly. 1 Publication
    VAR_054281
    Natural varianti246 – 2461G → R in GLC1A. 1 Publication
    VAR_005468
    Natural varianti251 – 2511V → A in GLC1A. 1 Publication
    VAR_054282
    Natural varianti252 – 2521G → R in GLC1A. 4 Publications
    VAR_054283
    Natural varianti261 – 2611E → K in GLC1A. 1 Publication
    VAR_054284
    Natural varianti272 – 2721R → G in GLC1A; unknown pathological significance. 1 Publication
    VAR_054285
    Natural varianti274 – 2741P → R in GLC1A. 1 Publication
    VAR_054286
    Natural varianti286 – 2861W → R in GLC1A.
    VAR_009675
    Natural varianti293 – 2931T → K in GLC1A. 2 Publications
    VAR_009676
    Natural varianti300 – 3001E → K in GLC1A; unknown pathological significance. 1 Publication
    VAR_054287
    Natural varianti323 – 3231E → K in GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 1 Publication
    VAR_054288
    Natural varianti337 – 3371Q → E in GLC1A. 1 Publication
    VAR_054289
    Natural varianti337 – 3371Q → R in GLC1A. 1 Publication
    VAR_005469
    Natural varianti341 – 3411S → P in GLC1A. 1 Publication
    VAR_054290
    Natural varianti342 – 3421R → K in GLC1A. 1 Publication
    VAR_054291
    Natural varianti345 – 3451I → M in GLC1A. 1 Publication
    VAR_054292
    Natural varianti352 – 3521E → K in GLC1A; unknown pathological significance. 2 Publications
    Corresponds to variant rs61745146 [ dbSNP | Ensembl ].
    VAR_009678
    Natural varianti353 – 3531T → I in GLC1A; unknown pathological significance. 3 Publications
    Corresponds to variant rs137853277 [ dbSNP | Ensembl ].
    VAR_009679
    Natural varianti360 – 3601I → N in GLC1A. 2 Publications
    VAR_054293
    Natural varianti361 – 3611P → S in GLC1A.
    VAR_009680
    Natural varianti363 – 3631A → T in GLC1A. 2 Publications
    VAR_054294
    Natural varianti364 – 3641G → V in GLC1A. 1 Publication
    VAR_005470
    Natural varianti367 – 3671G → R in GLC1A. 7 Publications
    VAR_005471
    Natural varianti369 – 3691F → L in GLC1A. 1 Publication
    VAR_054295
    Natural varianti370 – 3701P → 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. 8 Publications
    VAR_005472
    Natural varianti377 – 3771T → K in GLC1A. 1 Publication
    VAR_054296
    Natural varianti377 – 3771T → M in GLC1A. 2 Publications
    VAR_009681
    Natural varianti380 – 3801D → A in GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 1 Publication
    VAR_009682
    Natural varianti380 – 3801D → G in GLC1A.
    VAR_009683
    Natural varianti380 – 3801D → H in GLC1A. 1 Publication
    VAR_054297
    Natural varianti380 – 3801D → N in GLC1A. 1 Publication
    VAR_054298
    Natural varianti393 – 3931S → N in GLC1A. 1 Publication
    VAR_054299
    Natural varianti393 – 3931S → R in GLC1A.
    VAR_009684
    Natural varianti399 – 3991G → V in GLC1A. 1 Publication
    Corresponds to variant rs28936694 [ dbSNP | Ensembl ].
    VAR_054300
    Natural varianti422 – 4221R → H in GLC1A.
    VAR_009688
    Natural varianti423 – 4231K → E in GLC1A; heterozygote specific phenotype. 3 Publications
    VAR_009689
    Natural varianti426 – 4261V → F in GLC1A. 2 Publications
    VAR_005473
    Natural varianti427 – 4271A → T in GLC1A. 1 Publication
    VAR_054302
    Natural varianti433 – 4331C → R in GLC1A; severe form. 1 Publication
    VAR_008970
    Natural varianti434 – 4341G → S in GLC1A. 1 Publication
    VAR_054303
    Natural varianti437 – 4371Y → H in GLC1A. 2 Publications
    VAR_005474
    Natural varianti438 – 4381T → I in GLC1A. 1 Publication
    VAR_054304
    Natural varianti445 – 4451A → V in GLC1A. 2 Publications
    Corresponds to variant rs140967767 [ dbSNP | Ensembl ].
    VAR_009691
    Natural varianti448 – 4481T → P in GLC1A. 2 Publications
    VAR_054305
    Natural varianti450 – 4501N → D in GLC1A. 1 Publication
    VAR_054306
    Natural varianti465 – 4651I → M in GLC1A.
    VAR_009692
    Natural varianti470 – 4701R → C in GLC1A. 1 Publication
    VAR_009693
    Natural varianti471 – 4711Y → C in GLC1A; unknown pathological significance. 1 Publication
    VAR_054308
    Natural varianti477 – 4771I → N in GLC1A; induces stress fiber formation in only 5% of cells. 1 Publication
    VAR_009695
    Natural varianti477 – 4771I → S in GLC1A. 1 Publication
    VAR_005475
    Natural varianti480 – 4801N → K in GLC1A. 2 Publications
    VAR_005476
    Natural varianti481 – 4811P → L in GLC1A. 1 Publication
    VAR_009696
    Natural varianti481 – 4811P → T in GLC1A.
    VAR_009697
    Natural varianti499 – 4991I → F in GLC1A. 2 Publications
    VAR_005477
    Natural varianti499 – 4991I → S in GLC1A. 1 Publication
    VAR_054309
    Natural varianti502 – 5021S → P in GLC1A. 1 Publication
    VAR_009700
    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.1 Publication
    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 (PubMed:15733270).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. 2 Publications
    VAR_054272

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi226 – 2305Missing: Impairs endoproteolytic processing. 1 Publication
    Mutagenesisi226 – 2261R → 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. 1 Publication
    Mutagenesisi226 – 2261R → Q: Slightly increases endoproteolytic processing. 1 Publication
    Mutagenesisi227 – 2271I → G: Reduced processing. 1 Publication
    Mutagenesisi229 – 2291K → 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. 1 Publication
    Mutagenesisi230 – 2301E → 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. 1 Publication

    Keywords - Diseasei

    Disease mutation, Glaucoma

    Organism-specific databases

    MIMi137750. phenotype.
    231300. phenotype.
    Orphaneti98976. Congenital glaucoma.
    98977. Juvenile glaucoma.
    PharmGKBiPA31415.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32322 PublicationsAdd
    BLAST
    Chaini33 – 504472MyocilinPRO_0000020084Add
    BLAST
    Chaini33 – 226194Myocilin, N-terminal fragmentPRO_0000428749Add
    BLAST
    Chaini227 – 504278Myocilin, C-terminal fragmentPRO_0000428750Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)1 Publication
    Disulfide bondi245 ↔ 4331 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Different isoforms may arise by post-translational modifications.
    Glycosylated.1 Publication
    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.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiQ99972.
    PRIDEiQ99972.

    PTM databases

    PhosphoSiteiQ99972.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ99972.
    BgeeiQ99972.
    CleanExiHS_MYOC.
    GenevestigatoriQ99972.

    Organism-specific databases

    HPAiHPA027364.

    Interactioni

    Subunit structurei

    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.5 Publications

    Protein-protein interaction databases

    BioGridi110736. 43 interactions.
    STRINGi9606.ENSP00000037502.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99972.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini244 – 503260Olfactomedin-likePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili74 – 184111Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi502 – 5043Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal

    Phylogenomic databases

    eggNOGiNOG298097.
    HOGENOMiHOG000059654.
    HOVERGENiHBG105662.
    InParanoidiQ99972.
    OMAiRYKYSSM.
    OrthoDBiEOG75F4CZ.
    PhylomeDBiQ99972.
    TreeFamiTF315964.

    Family and domain databases

    InterProiIPR003112. Olfac-like.
    [Graphical view]
    PfamiPF02191. OLF. 1 hit.
    [Graphical view]
    SMARTiSM00284. OLF. 1 hit.
    [Graphical view]
    PROSITEiPS51132. OLF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99972-1 [UniParc]FASTAAdd to Basket

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    MRFFCARCCS FGPEMPAVQL LLLACLVWDV GARTAQLRKA NDQSGRCQYT    50
    FSVASPNESS CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH 100
    QLTLDQAARP QETQEGLQRE LGTLRRERDQ LETQTRELET AYSNLLRDKS 150
    VLEEEKKRLR QENENLARRL ESSSQEVARL RRGQCPQTRD TARAVPPGSR 200
    EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE GDTGCGELVW 250
    VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE 300
    YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN 350
    TETVKAEKEI PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA 400
    IVLSKLNPEN LELEQTWETN IRKQSVANAF IICGTLYTVS SYTSADATVN 450
    FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN PLEKKLFAWD NLNMVTYDIK 500
    LSKM 504
    Length:504
    Mass (Da):56,972
    Last modified:January 1, 1998 - v2
    Checksum:i9588C04F1D227623
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41F → S.
    VAR_009665
    Natural varianti9 – 91C → S.
    VAR_009666
    Natural varianti12 – 121G → R.2 Publications
    Corresponds to variant rs199752860 [ dbSNP | Ensembl ].
    VAR_009667
    Natural varianti16 – 161P → L.1 Publication
    VAR_054269
    Natural varianti17 – 171A → S.1 Publication
    VAR_054270
    Natural varianti19 – 191Q → H.1 Publication
    Corresponds to variant rs2234925 [ dbSNP | Ensembl ].
    VAR_009668
    Natural varianti25 – 251C → R in GLC1A. 1 Publication
    VAR_054271
    Natural varianti48 – 481Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. 2 Publications
    VAR_054272
    Natural varianti53 – 531V → A in GLC1A. 1 Publication
    Corresponds to variant rs200208925 [ dbSNP | Ensembl ].
    VAR_008969
    Natural varianti57 – 571N → D.1 Publication
    VAR_054273
    Natural varianti57 – 571N → S Loss of higher molecular weight isoform. 1 Publication
    VAR_054274
    Natural varianti73 – 731N → S.
    VAR_009669
    Natural varianti76 – 761R → K.9 Publications
    Corresponds to variant rs2234926 [ dbSNP | Ensembl ].
    VAR_009670
    Natural varianti77 – 771D → E.1 Publication
    VAR_054275
    Natural varianti82 – 821R → C in GLC1A.
    VAR_009671
    Natural varianti82 – 821R → H.
    VAR_009672
    Natural varianti95 – 951L → P.1 Publication
    VAR_054276
    Natural varianti126 – 1261R → W in GLC1A. 1 Publication
    Corresponds to variant rs200120115 [ dbSNP | Ensembl ].
    VAR_054277
    Natural varianti158 – 1581R → Q in GLC1A. 1 Publication
    Corresponds to variant rs199746824 [ dbSNP | Ensembl ].
    VAR_054278
    Natural varianti189 – 1891R → Q.
    VAR_009673
    Natural varianti203 – 2031S → F.
    VAR_009674
    Natural varianti208 – 2081D → E in GLC1A; unknown pathological significance. 3 Publications
    Corresponds to variant rs2234927 [ dbSNP | Ensembl ].
    VAR_014943
    Natural varianti215 – 2151L → P.1 Publication
    VAR_054279
    Natural varianti244 – 2441G → V in GLC1A; unknown pathological significance. 1 Publication
    VAR_054280
    Natural varianti245 – 2451C → Y in GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly. 1 Publication
    VAR_054281
    Natural varianti246 – 2461G → R in GLC1A. 1 Publication
    VAR_005468
    Natural varianti251 – 2511V → A in GLC1A. 1 Publication
    VAR_054282
    Natural varianti252 – 2521G → R in GLC1A. 4 Publications
    VAR_054283
    Natural varianti261 – 2611E → K in GLC1A. 1 Publication
    VAR_054284
    Natural varianti272 – 2721R → G in GLC1A; unknown pathological significance. 1 Publication
    VAR_054285
    Natural varianti274 – 2741P → R in GLC1A. 1 Publication
    VAR_054286
    Natural varianti286 – 2861W → R in GLC1A.
    VAR_009675
    Natural varianti293 – 2931T → K in GLC1A. 2 Publications
    VAR_009676
    Natural varianti300 – 3001E → K in GLC1A; unknown pathological significance. 1 Publication
    VAR_054287
    Natural varianti323 – 3231E → K in GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 1 Publication
    VAR_054288
    Natural varianti329 – 3291V → M.1 Publication
    Corresponds to variant rs146391864 [ dbSNP | Ensembl ].
    VAR_009677
    Natural varianti337 – 3371Q → E in GLC1A. 1 Publication
    VAR_054289
    Natural varianti337 – 3371Q → R in GLC1A. 1 Publication
    VAR_005469
    Natural varianti341 – 3411S → P in GLC1A. 1 Publication
    VAR_054290
    Natural varianti342 – 3421R → K in GLC1A. 1 Publication
    VAR_054291
    Natural varianti345 – 3451I → M in GLC1A. 1 Publication
    VAR_054292
    Natural varianti352 – 3521E → K in GLC1A; unknown pathological significance. 2 Publications
    Corresponds to variant rs61745146 [ dbSNP | Ensembl ].
    VAR_009678
    Natural varianti353 – 3531T → I in GLC1A; unknown pathological significance. 3 Publications
    Corresponds to variant rs137853277 [ dbSNP | Ensembl ].
    VAR_009679
    Natural varianti360 – 3601I → N in GLC1A. 2 Publications
    VAR_054293
    Natural varianti361 – 3611P → S in GLC1A.
    VAR_009680
    Natural varianti363 – 3631A → T in GLC1A. 2 Publications
    VAR_054294
    Natural varianti364 – 3641G → V in GLC1A. 1 Publication
    VAR_005470
    Natural varianti367 – 3671G → R in GLC1A. 7 Publications
    VAR_005471
    Natural varianti369 – 3691F → L in GLC1A. 1 Publication
    VAR_054295
    Natural varianti370 – 3701P → 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. 8 Publications
    VAR_005472
    Natural varianti377 – 3771T → K in GLC1A. 1 Publication
    VAR_054296
    Natural varianti377 – 3771T → M in GLC1A. 2 Publications
    VAR_009681
    Natural varianti380 – 3801D → A in GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 1 Publication
    VAR_009682
    Natural varianti380 – 3801D → G in GLC1A.
    VAR_009683
    Natural varianti380 – 3801D → H in GLC1A. 1 Publication
    VAR_054297
    Natural varianti380 – 3801D → N in GLC1A. 1 Publication
    VAR_054298
    Natural varianti393 – 3931S → N in GLC1A. 1 Publication
    VAR_054299
    Natural varianti393 – 3931S → R in GLC1A.
    VAR_009684
    Natural varianti398 – 3981K → R.5 Publications
    Corresponds to variant rs56314834 [ dbSNP | Ensembl ].
    VAR_009685
    Natural varianti399 – 3991G → V in GLC1A. 1 Publication
    Corresponds to variant rs28936694 [ dbSNP | Ensembl ].
    VAR_054300
    Natural varianti402 – 4021V → I.
    VAR_009686
    Natural varianti414 – 4141E → K.1 Publication
    VAR_054301
    Natural varianti422 – 4221R → C.
    VAR_009687
    Natural varianti422 – 4221R → H in GLC1A.
    VAR_009688
    Natural varianti423 – 4231K → E in GLC1A; heterozygote specific phenotype. 3 Publications
    VAR_009689
    Natural varianti425 – 4251S → P.
    VAR_009690
    Natural varianti426 – 4261V → F in GLC1A. 2 Publications
    VAR_005473
    Natural varianti427 – 4271A → T in GLC1A. 1 Publication
    VAR_054302
    Natural varianti433 – 4331C → R in GLC1A; severe form. 1 Publication
    VAR_008970
    Natural varianti434 – 4341G → S in GLC1A. 1 Publication
    VAR_054303
    Natural varianti437 – 4371Y → H in GLC1A. 2 Publications
    VAR_005474
    Natural varianti438 – 4381T → I in GLC1A. 1 Publication
    VAR_054304
    Natural varianti445 – 4451A → V in GLC1A. 2 Publications
    Corresponds to variant rs140967767 [ dbSNP | Ensembl ].
    VAR_009691
    Natural varianti448 – 4481T → P in GLC1A. 2 Publications
    VAR_054305
    Natural varianti450 – 4501N → D in GLC1A. 1 Publication
    VAR_054306
    Natural varianti465 – 4651I → M in GLC1A.
    VAR_009692
    Natural varianti470 – 4701R → C in GLC1A. 1 Publication
    VAR_009693
    Natural varianti470 – 4701R → H.1 Publication
    VAR_054307
    Natural varianti471 – 4711Y → C in GLC1A; unknown pathological significance. 1 Publication
    VAR_054308
    Natural varianti473 – 4731Y → C.
    VAR_009694
    Natural varianti477 – 4771I → N in GLC1A; induces stress fiber formation in only 5% of cells. 1 Publication
    VAR_009695
    Natural varianti477 – 4771I → S in GLC1A. 1 Publication
    VAR_005475
    Natural varianti480 – 4801N → K in GLC1A. 2 Publications
    VAR_005476
    Natural varianti481 – 4811P → L in GLC1A. 1 Publication
    VAR_009696
    Natural varianti481 – 4811P → T in GLC1A.
    VAR_009697
    Natural varianti495 – 4951V → I.
    VAR_009698
    Natural varianti499 – 4991I → F in GLC1A. 2 Publications
    VAR_005477
    Natural varianti499 – 4991I → S in GLC1A. 1 Publication
    VAR_054309
    Natural varianti500 – 5001K → R.
    Corresponds to variant rs145977437 [ dbSNP | Ensembl ].
    VAR_009699
    Natural varianti502 – 5021S → P in GLC1A. 1 Publication
    VAR_009700

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1297.1.
    PIRiJC5830.
    RefSeqiNP_000252.1. NM_000261.1.
    UniGeneiHs.436037.

    Genome annotation databases

    EnsembliENST00000037502; ENSP00000037502; ENSG00000034971.
    GeneIDi4653.
    KEGGihsa:4653.
    UCSCiuc001ghu.3. human.

    Polymorphism databases

    DMDMi3024209.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1297.1.
    PIRi JC5830.
    RefSeqi NP_000252.1. NM_000261.1.
    UniGenei Hs.436037.

    3D structure databases

    ProteinModelPortali Q99972.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110736. 43 interactions.
    STRINGi 9606.ENSP00000037502.

    PTM databases

    PhosphoSitei Q99972.

    Polymorphism databases

    DMDMi 3024209.

    Proteomic databases

    PaxDbi Q99972.
    PRIDEi Q99972.

    Protocols and materials databases

    DNASUi 4653.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000037502 ; ENSP00000037502 ; ENSG00000034971 .
    GeneIDi 4653.
    KEGGi hsa:4653.
    UCSCi uc001ghu.3. human.

    Organism-specific databases

    CTDi 4653.
    GeneCardsi GC01M171604.
    HGNCi HGNC:7610. MYOC.
    HPAi HPA027364.
    MIMi 137750. phenotype.
    231300. phenotype.
    601652. gene.
    neXtProti NX_Q99972.
    Orphaneti 98976. Congenital glaucoma.
    98977. Juvenile glaucoma.
    PharmGKBi PA31415.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298097.
    HOGENOMi HOG000059654.
    HOVERGENi HBG105662.
    InParanoidi Q99972.
    OMAi RYKYSSM.
    OrthoDBi EOG75F4CZ.
    PhylomeDBi Q99972.
    TreeFami TF315964.

    Miscellaneous databases

    GeneWikii MYOC.
    GenomeRNAii 4653.
    NextBioi 17936.
    PROi Q99972.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99972.
    Bgeei Q99972.
    CleanExi HS_MYOC.
    Genevestigatori Q99972.

    Family and domain databases

    InterProi IPR003112. Olfac-like.
    [Graphical view ]
    Pfami PF02191. OLF. 1 hit.
    [Graphical view ]
    SMARTi SM00284. OLF. 1 hit.
    [Graphical view ]
    PROSITEi PS51132. OLF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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.
      , 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. 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. 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. 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. Cited for: VARIANTS GLC1A LEU-370; ALA-380 AND PRO-502, VARIANT LYS-76.
    39. Cited for: VARIANT GLC1A GLU-423.
    40. 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. 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. 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. Cited for: VARIANT GLC1A ALA-53.
    47. 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. 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. 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. 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. 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. Cited for: VARIANTS GLC1A VAL-244 AND ARG-252.

    Entry informationi

    Entry nameiMYOC_HUMAN
    AccessioniPrimary (citable) accession number: Q99972
    Secondary accession number(s): B2RD84, O00620, Q7Z6Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3