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Protein

Myocilin

Gene

MYOC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • fibronectin binding Source: UniProtKB
  • frizzled binding Source: UniProtKB
  • myosin light chain binding Source: UniProtKB

GO - Biological processi

  • bone development Source: UniProtKB
  • clustering of voltage-gated sodium channels Source: UniProtKB
  • ERBB2-ERBB3 signaling pathway Source: UniProtKB
  • myelination in peripheral nervous system Source: UniProtKB
  • negative regulation of cell-matrix adhesion Source: UniProtKB
  • negative regulation of Rho protein signal transduction Source: UniProtKB
  • negative regulation of stress fiber assembly Source: UniProtKB
  • neuron projection development Source: UniProtKB
  • non-canonical Wnt signaling pathway via JNK cascade Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of mitochondrial depolarization Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • regulation of MAPK cascade Source: UniProtKB
  • skeletal muscle hypertrophy Source: UniProtKB
Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7610. MYOC.

Subcellular locationi

Myocilin, N-terminal fragment :

GO - Cellular componenti

  • cilium Source: UniProtKB-SubCell
  • cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: MGI
  • Golgi apparatus Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrial outer membrane Source: UniProtKB
  • node of Ranvier Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • rough endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

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)34 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:137750
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. 2 Publications
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. 9 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. 1 Publication
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. 2 Publications
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)1 Publication

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).

Disease descriptionAn 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.

See also OMIM:231300
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.

Polymorphism and mutation databases

BioMutaiMYOC.
DMDMi3024209.

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 ↔ 433PROSITE-ProRule annotation1 Publication

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

BgeeiQ99972.
CleanExiHS_MYOC.
ExpressionAtlasiQ99972. baseline and differential.
GenevisibleiQ99972. HS.

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

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi248 – 2514Combined sources
Beta strandi255 – 2595Combined sources
Helixi263 – 2653Combined sources
Beta strandi266 – 2727Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi292 – 30312Combined sources
Helixi304 – 3096Combined sources
Beta strandi313 – 32210Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi333 – 3386Combined sources
Beta strandi341 – 3488Combined sources
Turni349 – 3524Combined sources
Beta strandi353 – 3597Combined sources
Beta strandi366 – 3694Combined sources
Turni375 – 3784Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi387 – 3926Combined sources
Turni395 – 3995Combined sources
Beta strandi400 – 4067Combined sources
Turni408 – 4103Combined sources
Beta strandi413 – 42210Combined sources
Helixi423 – 4253Combined sources
Beta strandi426 – 4327Combined sources
Beta strandi435 – 45420Combined sources
Turni455 – 4573Combined sources
Beta strandi460 – 4689Combined sources
Beta strandi474 – 4807Combined sources
Turni481 – 4844Combined sources
Beta strandi485 – 4906Combined sources
Beta strandi493 – 4975Combined sources
Beta strandi499 – 5013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WXQX-ray2.15A228-504[»]
4WXSX-ray1.90A228-504[»]
4WXUX-ray2.09A228-504[»]
ProteinModelPortaliQ99972.
SMRiQ99972. Positions 251-502.
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.
GeneTreeiENSGT00760000119005.
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

« Hide

        10         20         30         40         50
MRFFCARCCS FGPEMPAVQL LLLACLVWDV GARTAQLRKA NDQSGRCQYT
60 70 80 90 100
FSVASPNESS CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH
110 120 130 140 150
QLTLDQAARP QETQEGLQRE LGTLRRERDQ LETQTRELET AYSNLLRDKS
160 170 180 190 200
VLEEEKKRLR QENENLARRL ESSSQEVARL RRGQCPQTRD TARAVPPGSR
210 220 230 240 250
EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE GDTGCGELVW
260 270 280 290 300
VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE
310 320 330 340 350
YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN
360 370 380 390 400
TETVKAEKEI PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA
410 420 430 440 450
IVLSKLNPEN LELEQTWETN IRKQSVANAF IICGTLYTVS SYTSADATVN
460 470 480 490 500
FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN PLEKKLFAWD NLNMVTYDIK

LSKM
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.Curated

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. 2 Publications
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. 2 Publications
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. 9 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. 1 Publication
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. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WXQX-ray2.15A228-504[»]
4WXSX-ray1.90A228-504[»]
4WXUX-ray2.09A228-504[»]
ProteinModelPortaliQ99972.
SMRiQ99972. Positions 251-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110736. 43 interactions.
STRINGi9606.ENSP00000037502.

PTM databases

PhosphoSiteiQ99972.

Polymorphism and mutation databases

BioMutaiMYOC.
DMDMi3024209.

Proteomic databases

PaxDbiQ99972.
PRIDEiQ99972.

Protocols and materials databases

DNASUi4653.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4653.
GeneCardsiGC01M171604.
HGNCiHGNC:7610. MYOC.
HPAiHPA027364.
MIMi137750. phenotype.
231300. phenotype.
601652. gene.
neXtProtiNX_Q99972.
Orphaneti98976. Congenital glaucoma.
98977. Juvenile glaucoma.
PharmGKBiPA31415.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG298097.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000059654.
HOVERGENiHBG105662.
InParanoidiQ99972.
OMAiRYKYSSM.
OrthoDBiEOG75F4CZ.
PhylomeDBiQ99972.
TreeFamiTF315964.

Miscellaneous databases

GeneWikiiMYOC.
GenomeRNAii4653.
NextBioi17936.
PROiQ99972.
SOURCEiSearch...

Gene expression databases

BgeeiQ99972.
CleanExiHS_MYOC.
ExpressionAtlasiQ99972. baseline and differential.
GenevisibleiQ99972. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.,