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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.By similarity8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi380CalciumCombined sources1
Metal bindingi428CalciumCombined sources1
Metal bindingi429Calcium; via carbonyl oxygenCombined sources1
Metal bindingi477Calcium; via carbonyl oxygenCombined sources1
Metal bindingi478CalciumCombined sources1

GO - Molecular functioni

  • fibronectin binding Source: UniProtKB
  • frizzled binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • 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...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000034971-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Myocilin1 Publication
Alternative name(s):
Myocilin 55 kDa subunit
Trabecular meshwork-induced glucocorticoid response protein1 Publication
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, TIGR1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05427125C → R in GLC1A. 1 PublicationCorresponds to variant rs755246983dbSNPEnsembl.1
Natural variantiVAR_05427248Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. 2 PublicationsCorresponds to variant rs74315339dbSNPEnsembl.1
Natural variantiVAR_00896953V → A in GLC1A. 1 PublicationCorresponds to variant rs200208925dbSNPEnsembl.1
Natural variantiVAR_00967182R → C in GLC1A. Corresponds to variant rs764005392dbSNPEnsembl.1
Natural variantiVAR_054277126R → W in GLC1A. 1 PublicationCorresponds to variant rs200120115dbSNPEnsembl.1
Natural variantiVAR_054278158R → Q in GLC1A. 1 PublicationCorresponds to variant rs199746824dbSNPEnsembl.1
Natural variantiVAR_014943208D → E in GLC1A; unknown pathological significance. 3 PublicationsCorresponds to variant rs2234927dbSNPEnsembl.1
Natural variantiVAR_054280244G → V in GLC1A; unknown pathological significance. 1 PublicationCorresponds to variant rs757769997dbSNPEnsembl.1
Natural variantiVAR_054281245C → Y in GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly. 1 PublicationCorresponds to variant rs74315340dbSNPEnsembl.1
Natural variantiVAR_005468246G → R in GLC1A. 1 Publication1
Natural variantiVAR_054282251V → A in GLC1A. 1 Publication1
Natural variantiVAR_054283252G → R in GLC1A. 4 PublicationsCorresponds to variant rs74315341dbSNPEnsembl.1
Natural variantiVAR_054284261E → K in GLC1A. 1 Publication1
Natural variantiVAR_054285272R → G in GLC1A; unknown pathological significance. 1 Publication1
Natural variantiVAR_054286274P → R in GLC1A. 1 Publication1
Natural variantiVAR_009675286W → R in GLC1A. 1
Natural variantiVAR_009676293T → K in GLC1A; no effect on protein stability. 3 PublicationsCorresponds to variant rs139122673dbSNPEnsembl.1
Natural variantiVAR_054287300E → K in GLC1A; unknown pathological significance. 1 PublicationCorresponds to variant rs748621461dbSNPEnsembl.1
Natural variantiVAR_054288323E → K in GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 2 Publications1
Natural variantiVAR_054289337Q → E in GLC1A. 1 Publication1
Natural variantiVAR_005469337Q → R in GLC1A. 1 PublicationCorresponds to variant rs74315335dbSNPEnsembl.1
Natural variantiVAR_054290341S → P in GLC1A. 1 Publication1
Natural variantiVAR_054291342R → K in GLC1A. 1 Publication1
Natural variantiVAR_054292345I → M in GLC1A. 1 Publication1
Natural variantiVAR_009678352E → K in GLC1A; unknown pathological significance. 2 PublicationsCorresponds to variant rs61745146dbSNPEnsembl.1
Natural variantiVAR_009679353T → I in GLC1A; unknown pathological significance; no significant effect on protein stability. 4 PublicationsCorresponds to variant rs137853277dbSNPEnsembl.1
Natural variantiVAR_054293360I → N in GLC1A. 2 Publications1
Natural variantiVAR_009680361P → S in GLC1A. 1
Natural variantiVAR_054294363A → T in GLC1A. 2 Publications1
Natural variantiVAR_005470364G → V in GLC1A. 1 PublicationCorresponds to variant rs121909193dbSNPEnsembl.1
Natural variantiVAR_005471367G → R in GLC1A. 7 PublicationsCorresponds to variant rs74315334dbSNPEnsembl.1
Natural variantiVAR_054295369F → L in GLC1A. 1 Publication1
Natural variantiVAR_005472370P → 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 PublicationsCorresponds to variant rs74315330dbSNPEnsembl.1
Natural variantiVAR_054296377T → K in GLC1A. 1 Publication1
Natural variantiVAR_009681377T → M in GLC1A. 2 PublicationsCorresponds to variant rs566289099dbSNPEnsembl.1
Natural variantiVAR_009682380D → A in GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 1 Publication1
Natural variantiVAR_009683380D → G in GLC1A. 1 Publication1
Natural variantiVAR_054297380D → H in GLC1A. 1 PublicationCorresponds to variant rs121909194dbSNPEnsembl.1
Natural variantiVAR_054298380D → N in GLC1A. 1 Publication1
Natural variantiVAR_054299393S → N in GLC1A. 1 Publication1
Natural variantiVAR_009684393S → R in GLC1A. 1
Natural variantiVAR_054300399G → V in GLC1A. 1 PublicationCorresponds to variant rs28936694dbSNPEnsembl.1
Natural variantiVAR_009688422R → H in GLC1A. Corresponds to variant rs201573718dbSNPEnsembl.1
Natural variantiVAR_009689423K → E in GLC1A; heterozygote specific phenotype. 3 PublicationsCorresponds to variant rs74315336dbSNPEnsembl.1
Natural variantiVAR_005473426V → F in GLC1A. 2 Publications1
Natural variantiVAR_054302427A → T in GLC1A. 1 PublicationCorresponds to variant rs754237376dbSNPEnsembl.1
Natural variantiVAR_008970433C → R in GLC1A; severe form. 1 PublicationCorresponds to variant rs74315338dbSNPEnsembl.1
Natural variantiVAR_054303434G → S in GLC1A. 1 Publication1
Natural variantiVAR_005474437Y → H in GLC1A. 2 PublicationsCorresponds to variant rs74315328dbSNPEnsembl.1
Natural variantiVAR_054304438T → I in GLC1A. 1 Publication1
Natural variantiVAR_009691445A → V in GLC1A; no effect on protein stability. 3 PublicationsCorresponds to variant rs140967767dbSNPEnsembl.1
Natural variantiVAR_054305448T → P in GLC1A. 2 Publications1
Natural variantiVAR_054306450N → D in GLC1A. 1 Publication1
Natural variantiVAR_009692465I → M in GLC1A. 1
Natural variantiVAR_009693470R → C in GLC1A. 1 PublicationCorresponds to variant rs771122834dbSNPEnsembl.1
Natural variantiVAR_054308471Y → C in GLC1A; unknown pathological significance. 1 PublicationCorresponds to variant rs554235897dbSNPEnsembl.1
Natural variantiVAR_009695477I → N in GLC1A; induces stress fiber formation in only 5% of cells. 2 PublicationsCorresponds to variant rs74315331dbSNPEnsembl.1
Natural variantiVAR_005475477I → S in GLC1A. 1 PublicationCorresponds to variant rs74315331dbSNPEnsembl.1
Natural variantiVAR_005476480N → K in GLC1A. 2 PublicationsCorresponds to variant rs74315332dbSNPEnsembl.1
Natural variantiVAR_009696481P → L in GLC1A. 1 Publication1
Natural variantiVAR_009697481P → T in GLC1A. 1
Natural variantiVAR_005477499I → F in GLC1A. 2 Publications1
Natural variantiVAR_054309499I → S in GLC1A. 1 Publication1
Natural variantiVAR_009700502S → P in GLC1A. 1 Publication1
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).1 Publication
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05427248Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. 2 PublicationsCorresponds to variant rs74315339dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi226 – 230Missing : Impairs endoproteolytic processing. 1 Publication5
Mutagenesisi226R → 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 Publication1
Mutagenesisi226R → Q: Slightly increases endoproteolytic processing. 1 Publication1
Mutagenesisi227I → G: Reduced processing. 1 Publication1
Mutagenesisi229K → 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 Publication1
Mutagenesisi230E → 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 Publication1

Keywords - Diseasei

Disease mutation, Glaucoma

Organism-specific databases

DisGeNETi4653.
MalaCardsiMYOC.
MIMi137750. phenotype.
231300. phenotype.
OpenTargetsiENSG00000034971.
Orphaneti98976. Congenital glaucoma.
98977. Juvenile glaucoma.
PharmGKBiPA31415.

Polymorphism and mutation databases

BioMutaiMYOC.
DMDMi3024209.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 322 PublicationsAdd BLAST32
ChainiPRO_000002008433 – 504MyocilinAdd BLAST472
ChainiPRO_000042874933 – 226Myocilin, N-terminal fragmentAdd BLAST194
ChainiPRO_0000428750227 – 504Myocilin, C-terminal fragmentAdd BLAST278

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...)1 Publication1
Disulfide bondi245 ↔ 433PROSITE-ProRule annotationCombined sources1 Publication

Post-translational modificationi

Different isoforms may arise by post-translational modifications.1 Publication
Glycosylated.4 Publications
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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei226 – 227Cleavage; by CAPN22

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

EPDiQ99972.
PaxDbiQ99972.
PeptideAtlasiQ99972.
PRIDEiQ99972.

PTM databases

iPTMnetiQ99972.
PhosphoSitePlusiQ99972.

Expressioni

Tissue specificityi

Detected in aqueous humor (PubMed:12697062). Detected in the eye (at protein level) (PubMed:11431441). Widely expressed. Highly expressed in various types of muscle, ciliary body, papillary sphincter, skeletal muscle, heart, and bone marrow-derived mesenchymal stem cells. 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 seems to be expressed at higher levels than in normal eyes, regardless of the type or clinical severity of glaucoma. The myocilin 35 kDa fragment is detected in aqueous humor and to a lesser extent in iris and ciliary body.3 Publications

Inductioni

Up-regulated by dexamethasone, a glucocorticoid.2 Publications

Gene expression databases

BgeeiENSG00000034971.
CleanExiHS_MYOC.
ExpressionAtlasiQ99972. baseline and differential.
GenevisibleiQ99972. HS.

Organism-specific databases

HPAiHPA027364.

Interactioni

Subunit structurei

Homodimer (via N-terminus). Can also form higher oligomers (PubMed:9497363). Interacts with OLFM3, FN1, NRCAM, GLDN and NFASC (PubMed:12019210, PubMed:11773026, PubMed:23897819). Interacts (via N-terminus) with MYL2 (PubMed:11773029). Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt signaling (PubMed:19188438). Interacts with SNTA1; regulates muscle hypertrophy. Interacts with ERBB2 and ERBB3; acivates ERBB2-ERBB3 signaling pathway. Interacts with SNCG; affects its secretion and its aggregation (By similarity).By similarity6 Publications

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi110736. 43 interactors.
STRINGi9606.ENSP00000037502.

Structurei

Secondary structure

1504
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi248 – 251Combined sources4
Beta strandi255 – 259Combined sources5
Helixi263 – 265Combined sources3
Beta strandi266 – 272Combined sources7
Beta strandi285 – 289Combined sources5
Beta strandi292 – 303Combined sources12
Helixi304 – 309Combined sources6
Beta strandi313 – 322Combined sources10
Beta strandi328 – 330Combined sources3
Beta strandi333 – 338Combined sources6
Beta strandi341 – 348Combined sources8
Turni349 – 352Combined sources4
Beta strandi353 – 359Combined sources7
Beta strandi366 – 369Combined sources4
Turni375 – 378Combined sources4
Beta strandi380 – 384Combined sources5
Beta strandi387 – 392Combined sources6
Turni395 – 399Combined sources5
Beta strandi400 – 406Combined sources7
Turni408 – 410Combined sources3
Beta strandi413 – 422Combined sources10
Helixi423 – 425Combined sources3
Beta strandi426 – 432Combined sources7
Beta strandi435 – 454Combined sources20
Turni455 – 457Combined sources3
Beta strandi460 – 468Combined sources9
Beta strandi474 – 480Combined sources7
Turni481 – 484Combined sources4
Beta strandi485 – 490Combined sources6
Beta strandi493 – 497Combined sources5
Beta strandi499 – 501Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini244 – 503Olfactomedin-likePROSITE-ProRule annotationAdd BLAST260

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili74 – 184Sequence analysisAdd BLAST111

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi502 – 504Microbody targeting signalSequence analysis3

Sequence similaritiesi

Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG410INPA. Eukaryota.
ENOG410YBJJ. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000059654.
HOVERGENiHBG105662.
InParanoidiQ99972.
OMAiRYKYSSM.
OrthoDBiEOG091G05HN.
PhylomeDBiQ99972.
TreeFamiTF315964.

Family and domain databases

InterProiIPR031213. Myocilin.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF33. PTHR23192:SF33. 1 hit.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0096654F → S.1
Natural variantiVAR_0096669C → S.1
Natural variantiVAR_00966712G → R.2 PublicationsCorresponds to variant rs199752860dbSNPEnsembl.1
Natural variantiVAR_05426916P → L.1 PublicationCorresponds to variant rs745439002dbSNPEnsembl.1
Natural variantiVAR_05427017A → S.1 Publication1
Natural variantiVAR_00966819Q → H.1 PublicationCorresponds to variant rs2234925dbSNPEnsembl.1
Natural variantiVAR_05427125C → R in GLC1A. 1 PublicationCorresponds to variant rs755246983dbSNPEnsembl.1
Natural variantiVAR_05427248Q → H in GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance. 2 PublicationsCorresponds to variant rs74315339dbSNPEnsembl.1
Natural variantiVAR_00896953V → A in GLC1A. 1 PublicationCorresponds to variant rs200208925dbSNPEnsembl.1
Natural variantiVAR_05427357N → D.1 Publication1
Natural variantiVAR_05427457N → S Loss of higher molecular weight isoform. 2 PublicationsCorresponds to variant rs561439247dbSNPEnsembl.1
Natural variantiVAR_00966973N → S.1
Natural variantiVAR_00967076R → K.9 PublicationsCorresponds to variant rs2234926dbSNPEnsembl.1
Natural variantiVAR_05427577D → E.1 Publication1
Natural variantiVAR_00967182R → C in GLC1A. Corresponds to variant rs764005392dbSNPEnsembl.1
Natural variantiVAR_00967282R → H.Corresponds to variant rs201552559dbSNPEnsembl.1
Natural variantiVAR_05427695L → P.1 Publication1
Natural variantiVAR_054277126R → W in GLC1A. 1 PublicationCorresponds to variant rs200120115dbSNPEnsembl.1
Natural variantiVAR_054278158R → Q in GLC1A. 1 PublicationCorresponds to variant rs199746824dbSNPEnsembl.1
Natural variantiVAR_009673189R → Q.Corresponds to variant rs144579767dbSNPEnsembl.1
Natural variantiVAR_009674203S → F.1
Natural variantiVAR_014943208D → E in GLC1A; unknown pathological significance. 3 PublicationsCorresponds to variant rs2234927dbSNPEnsembl.1
Natural variantiVAR_054279215L → P.1 PublicationCorresponds to variant rs531050114dbSNPEnsembl.1
Natural variantiVAR_054280244G → V in GLC1A; unknown pathological significance. 1 PublicationCorresponds to variant rs757769997dbSNPEnsembl.1
Natural variantiVAR_054281245C → Y in GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly. 1 PublicationCorresponds to variant rs74315340dbSNPEnsembl.1
Natural variantiVAR_005468246G → R in GLC1A. 1 Publication1
Natural variantiVAR_054282251V → A in GLC1A. 1 Publication1
Natural variantiVAR_054283252G → R in GLC1A. 4 PublicationsCorresponds to variant rs74315341dbSNPEnsembl.1
Natural variantiVAR_054284261E → K in GLC1A. 1 Publication1
Natural variantiVAR_054285272R → G in GLC1A; unknown pathological significance. 1 Publication1
Natural variantiVAR_054286274P → R in GLC1A. 1 Publication1
Natural variantiVAR_009675286W → R in GLC1A. 1
Natural variantiVAR_009676293T → K in GLC1A; no effect on protein stability. 3 PublicationsCorresponds to variant rs139122673dbSNPEnsembl.1
Natural variantiVAR_054287300E → K in GLC1A; unknown pathological significance. 1 PublicationCorresponds to variant rs748621461dbSNPEnsembl.1
Natural variantiVAR_054288323E → K in GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 2 Publications1
Natural variantiVAR_009677329V → M Slightly decreased protein stability. 2 PublicationsCorresponds to variant rs146391864dbSNPEnsembl.1
Natural variantiVAR_054289337Q → E in GLC1A. 1 Publication1
Natural variantiVAR_005469337Q → R in GLC1A. 1 PublicationCorresponds to variant rs74315335dbSNPEnsembl.1
Natural variantiVAR_054290341S → P in GLC1A. 1 Publication1
Natural variantiVAR_054291342R → K in GLC1A. 1 Publication1
Natural variantiVAR_054292345I → M in GLC1A. 1 Publication1
Natural variantiVAR_009678352E → K in GLC1A; unknown pathological significance. 2 PublicationsCorresponds to variant rs61745146dbSNPEnsembl.1
Natural variantiVAR_009679353T → I in GLC1A; unknown pathological significance; no significant effect on protein stability. 4 PublicationsCorresponds to variant rs137853277dbSNPEnsembl.1
Natural variantiVAR_054293360I → N in GLC1A. 2 Publications1
Natural variantiVAR_009680361P → S in GLC1A. 1
Natural variantiVAR_054294363A → T in GLC1A. 2 Publications1
Natural variantiVAR_005470364G → V in GLC1A. 1 PublicationCorresponds to variant rs121909193dbSNPEnsembl.1
Natural variantiVAR_005471367G → R in GLC1A. 7 PublicationsCorresponds to variant rs74315334dbSNPEnsembl.1
Natural variantiVAR_054295369F → L in GLC1A. 1 Publication1
Natural variantiVAR_005472370P → 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 PublicationsCorresponds to variant rs74315330dbSNPEnsembl.1
Natural variantiVAR_054296377T → K in GLC1A. 1 Publication1
Natural variantiVAR_009681377T → M in GLC1A. 2 PublicationsCorresponds to variant rs566289099dbSNPEnsembl.1
Natural variantiVAR_009682380D → A in GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum. 1 Publication1
Natural variantiVAR_009683380D → G in GLC1A. 1 Publication1
Natural variantiVAR_054297380D → H in GLC1A. 1 PublicationCorresponds to variant rs121909194dbSNPEnsembl.1
Natural variantiVAR_054298380D → N in GLC1A. 1 Publication1
Natural variantiVAR_054299393S → N in GLC1A. 1 Publication1
Natural variantiVAR_009684393S → R in GLC1A. 1
Natural variantiVAR_009685398K → R.5 PublicationsCorresponds to variant rs56314834dbSNPEnsembl.1
Natural variantiVAR_054300399G → V in GLC1A. 1 PublicationCorresponds to variant rs28936694dbSNPEnsembl.1
Natural variantiVAR_009686402V → I.1
Natural variantiVAR_054301414E → K.1 Publication1
Natural variantiVAR_009687422R → C No effect on protein stability. 1 PublicationCorresponds to variant rs751113505dbSNPEnsembl.1
Natural variantiVAR_009688422R → H in GLC1A. Corresponds to variant rs201573718dbSNPEnsembl.1
Natural variantiVAR_009689423K → E in GLC1A; heterozygote specific phenotype. 3 PublicationsCorresponds to variant rs74315336dbSNPEnsembl.1
Natural variantiVAR_009690425S → P Decreases protein stability. 1 Publication1
Natural variantiVAR_005473426V → F in GLC1A. 2 Publications1
Natural variantiVAR_054302427A → T in GLC1A. 1 PublicationCorresponds to variant rs754237376dbSNPEnsembl.1
Natural variantiVAR_008970433C → R in GLC1A; severe form. 1 PublicationCorresponds to variant rs74315338dbSNPEnsembl.1
Natural variantiVAR_054303434G → S in GLC1A. 1 Publication1
Natural variantiVAR_005474437Y → H in GLC1A. 2 PublicationsCorresponds to variant rs74315328dbSNPEnsembl.1
Natural variantiVAR_054304438T → I in GLC1A. 1 Publication1
Natural variantiVAR_009691445A → V in GLC1A; no effect on protein stability. 3 PublicationsCorresponds to variant rs140967767dbSNPEnsembl.1
Natural variantiVAR_054305448T → P in GLC1A. 2 Publications1
Natural variantiVAR_054306450N → D in GLC1A. 1 Publication1
Natural variantiVAR_009692465I → M in GLC1A. 1
Natural variantiVAR_009693470R → C in GLC1A. 1 PublicationCorresponds to variant rs771122834dbSNPEnsembl.1
Natural variantiVAR_054307470R → H.1 PublicationCorresponds to variant rs750791099dbSNPEnsembl.1
Natural variantiVAR_054308471Y → C in GLC1A; unknown pathological significance. 1 PublicationCorresponds to variant rs554235897dbSNPEnsembl.1
Natural variantiVAR_009694473Y → C No effect on protein stability. 1 Publication1
Natural variantiVAR_009695477I → N in GLC1A; induces stress fiber formation in only 5% of cells. 2 PublicationsCorresponds to variant rs74315331dbSNPEnsembl.1
Natural variantiVAR_005475477I → S in GLC1A. 1 PublicationCorresponds to variant rs74315331dbSNPEnsembl.1
Natural variantiVAR_005476480N → K in GLC1A. 2 PublicationsCorresponds to variant rs74315332dbSNPEnsembl.1
Natural variantiVAR_009696481P → L in GLC1A. 1 Publication1
Natural variantiVAR_009697481P → T in GLC1A. 1
Natural variantiVAR_009698495V → I.1
Natural variantiVAR_005477499I → F in GLC1A. 2 Publications1
Natural variantiVAR_054309499I → S in GLC1A. 1 Publication1
Natural variantiVAR_009699500K → R.Corresponds to variant rs145977437dbSNPEnsembl.1
Natural variantiVAR_009700502S → P in GLC1A. 1 Publication1

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.