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Q96CV9 (OPTN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Optineurin
Alternative name(s):
E3-14.7K-interacting protein
FIP-2
Huntingtin yeast partner L
Huntingtin-interacting protein 7
Short name=HIP-7
Huntingtin-interacting protein L
NEMO-related protein
Optic neuropathy-inducing protein
Transcription factor IIIA-interacting protein
Short name=TFIIIA-IntP
Gene names
Name:OPTN
Synonyms:FIP2, GLC1E, HIP7, HYPL, NRP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). May constitute a cellular target for adenovirus E3 14.7, an inhibitor of TNF-alpha functions, thereby affecting cell death. Ref.2 Ref.14 Ref.17

Subunit structure

Interacts with E3 14.7 kDa protein of group C human adenovirus. Interacts with HD. Interacts with Rab8 (RAB8A and/or RAB8B). Interacts with transcription factor IIIA (GTF3A). Interacts with TRAF3, TBK1 and MYO6. Binds to ubiquitin. Ref.1 Ref.8 Ref.9 Ref.11 Ref.14 Ref.17

Subcellular location

Cytoplasmperinuclear region. Golgi apparatus. Golgi apparatustrans-Golgi network. Note: Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Ref.1 Ref.2 Ref.10 Ref.14 Ref.17 Ref.29

Tissue specificity

Present in aqueous humor of the eye (at protein level). Highly expressed in trabecular meshwork. Expressed nonpigmented ciliary epithelium, retina, brain, adrenal cortex, fetus, lymphocyte, fibroblast, skeletal muscle, heart, liver, brain and placenta. Ref.1 Ref.2

Induction

Upon TNF and interferon treatments. Up-regulated in direct response to viral infection. Ref.1 Ref.10 Ref.12 Ref.13 Ref.17

Domain

Ubiquitin-binding motif (UBAN) is essential for its inhibitory function, subcellular localization and interaction with TBK1.

Post-translational modification

Phosphorylated by TBK1, leading to restrict bacterial proliferation in case of infection. Phosphorylation is induced by phorbol esters and decreases its half-time. Ref.10 Ref.30

Involvement in disease

Glaucoma 1, open angle, E (GLC1E) [MIM:137760]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27

Glaucoma, normal pressure (NPG) [MIM:606657]: A primary glaucoma characterized by intraocular pression consistently within the statistically normal population range.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.28

Amyotrophic lateral sclerosis 12 (ALS12) [MIM:613435]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29

Caution

According to some authors (Ref.12) its expression is regulated by intraocular pressure, suggesting a protective role in case of high pressure, while according to other authors (Ref.13), it is not up-regulated in response to pressure elevation.

Sequence caution

The sequence CAI16552.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
Golgi apparatus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Glaucoma
Neurodegeneration
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

Golgi organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

Golgi ribbon formation

Inferred from direct assay Ref.14. Source: UniProtKB

Golgi to plasma membrane protein transport

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cell death

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

protein targeting to Golgi

Inferred from mutant phenotype Ref.14. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.14. Source: UniProtKB

Golgi membrane

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functionprotein C-terminus binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 24705354. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96CV9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96CV9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     210-215: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96CV9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Optineurin
PRO_0000058066

Regions

Region58 – 209152Interaction with Rab8
Region411 – 577167Interaction with HD
Region412 – 520109Interaction with MYO6
Coiled coil38 – 170133 Potential
Coiled coil239 – 508270 Potential
Motif474 – 4796UBAN

Amino acid modifications

Modified residue1771Phosphoserine; by TBK1 Ref.30

Natural variations

Alternative sequence1 – 5757Missing in isoform 3.
VSP_013261
Alternative sequence210 – 2156Missing in isoform 2.
VSP_013262
Natural variant261H → D in GLC1E. Ref.26 Ref.27 Ref.28
VAR_021537
Natural variant501E → K in GLC1E. Ref.2
Corresponds to variant rs28939688 [ dbSNP | Ensembl ].
VAR_021538
Natural variant981M → K May modify intraocular pressure and increase risk of GLC1E and NPG; may be a common polymorphism. Ref.2 Ref.21 Ref.24 Ref.26
Corresponds to variant rs11258194 [ dbSNP | Ensembl ].
VAR_021539
Natural variant1031E → D in GLC1E. Ref.22
VAR_021540
Natural variant2011P → S. Ref.1 Ref.2 Ref.3
VAR_021541
Natural variant2131K → H Requires 2 nucleotide substitutions. Ref.1 Ref.2 Ref.3
VAR_021542
Natural variant2161S → R. Ref.1 Ref.2 Ref.3
VAR_021543
Natural variant3081S → P.
Corresponds to variant rs7068431 [ dbSNP | Ensembl ].
VAR_030769
Natural variant3221K → E. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs523747 [ dbSNP | Ensembl ].
VAR_021544
Natural variant3571T → P. Ref.1 Ref.2 Ref.3
VAR_021545
Natural variant4781E → G in ALS12. Ref.29
VAR_063597
Natural variant4861H → R in GLC1E; juvenile onset. Ref.22 Ref.25
VAR_021546
Natural variant5451R → Q in GLC1E; unknown pathological significance. Ref.2 Ref.23 Ref.26
Corresponds to variant rs28939689 [ dbSNP | Ensembl ].
VAR_021547

Experimental info

Mutagenesis4741D → N: Significant reduction in ubiquitin binding and interaction with TBK1. Loss of ability to inhibit the activation of the IFNB promoter in response to TLR3 or RIG-I signaling. Ref.17
Sequence conflict4361A → V in AAC26850. Ref.8

Secondary structure

....... 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: DB0F841E3315AAE1

FASTA57765,921
        10         20         30         40         50         60 
MSHQPLSCLT EKEDSPSEST GNGPPHLAHP NLDTFTPEEL LQQMKELLTE NHQLKEAMKL 

        70         80         90        100        110        120 
NNQAMKGRFE ELSAWTEKQK EERQFFEIQS KEAKERLMAL SHENEKLKEE LGKLKGKSER 

       130        140        150        160        170        180 
SSEDPTDDSR LPRAEAEQEK DQLRTQVVRL QAEKADLLGI VSELQLKLNS SGSSEDSFVE 

       190        200        210        220        230        240 
IRMAEGEAEG SVKEIKHSPG PTRTVSTGTA LSKYRSRSAD GAKNYFEHEE LTVSQLLLCL 

       250        260        270        280        290        300 
REGNQKVERL EVALKEAKER VSDFEKKTSN RSEIETQTEG STEKENDEEK GPETVGSEVE 

       310        320        330        340        350        360 
ALNLQVTSLF KELQEAHTKL SKAELMKKRL QEKCQALERK NSAIPSELNE KQELVYTNKK 

       370        380        390        400        410        420 
LELQVESMLS EIKMEQAKTE DEKSKLTVLQ MTHNKLLQEH NNALKTIEEL TRKESEKVDR 

       430        440        450        460        470        480 
AVLKELSEKL ELAEKALASK QLQMDEMKQT IAKQEEDLET MTILRAQMEV YCSDFHAERA 

       490        500        510        520        530        540 
AREKIHEEKE QLALQLAVLL KENDAFEDGG RQSLMEMQSR HGARTSDSDQ QAYLVQRGAE 

       550        560        570 
DRDWRQQRNI PIHSCPKCGE VLPDIDTLQI HVMDCII 

« Hide

Isoform 2 [UniParc].

Checksum: 8CB5F88A1DDB3AE9
Show »

FASTA57165,202
Isoform 3 [UniParc].

Checksum: AB876FF328DD5272
Show »

FASTA52059,559

References

« Hide 'large scale' references
[1]"Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains."
Li Y., Kang J., Horwitz M.S.
Mol. Cell. Biol. 18:1601-1610(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3), VARIANTS SER-201; HIS-213; ARG-216; GLU-322 AND PRO-357, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH ADENOVIRUS E3.
Tissue: Cervix carcinoma.
[2]"Adult-onset primary open-angle glaucoma caused by mutations in optineurin."
Rezaie T., Child A., Hitchings R., Brice G., Miller L., Coca-Prados M., Heon E., Krupin T., Ritch R., Kreutzer D., Crick R.P., Sarfarazi M.
Science 295:1077-1079(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS GLC1E LYS-50 AND GLN-545, VARIANTS LYS-98; SER-201; HIS-213; ARG-216; GLU-322 AND PRO-357.
Tissue: Trabecular meshwork.
[3]"Human FIP-2: genomic structure and mutational analysis in ARVD patients."
Li D., Roberts R.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-201; HIS-213; ARG-216; GLU-322 AND PRO-357.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-322.
Tissue: Brain.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-322.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 1 AND 2), VARIANT GLU-322.
Tissue: Cervix and Skin.
[8]"Huntingtin interacts with a family of WW domain proteins."
Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E.
Hum. Mol. Genet. 7:1463-1474(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 412-555, INTERACTION WITH HD.
Tissue: Testis.
[9]"FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis."
Hattula K., Peraenen J.
Curr. Biol. 10:1603-1606(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HD AND RAB8.
[10]"Phorbol esters and cytokines regulate the expression of the NEMO-related protein, a molecule involved in a NF-kappa B-independent pathway."
Schwamborn K., Weil R., Courtois G., Whiteside S.T., Israeel A.
J. Biol. Chem. 275:22780-22789(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION.
[11]"Identification of a transcription factor IIIA-interacting protein."
Moreland R.J., Dresser M.E., Rodgers J.S., Roe B.A., Conaway J.W., Conaway R.C., Hanas J.S.
Nucleic Acids Res. 28:1986-1993(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTF3A.
[12]"Expression of optineurin, a glaucoma-linked gene, is influenced by elevated intraocular pressure."
Vittitow J., Borras T.
Biochem. Biophys. Res. Commun. 298:67-74(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[13]"Optineurin gene expression level in human trabecular meshwork does not change in response to pressure elevation."
Kamphuis W., Schneemann A.
Ophthalmic Res. 35:93-96(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis."
Sahlender D.A., Roberts R.C., Arden S.D., Spudich G., Taylor M.J., Luzio J.P., Kendrick-Jones J., Buss F.
J. Cell Biol. 169:285-295(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYO6 AND RAB8.
[15]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Optineurin negatively regulates the induction of IFNbeta in response to RNA virus infection."
Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M., Kohl A., Elliott R.M., Macdonald A.
PLoS Pathog. 6:E1000778-E1000778(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH TBK1 AND TRAF3, UBIQUITIN-BINDING MOTIF, MUTAGENESIS OF ASP-474.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"The M98K variant of the OPTINEURIN (OPTN) gene modifies initial intraocular pressure in patients with primary open angle glaucoma."
Melki R., Belmouden A., Akhayat O., Brezin A., Garchon H.-J.
J. Med. Genet. 40:842-844(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-98.
[22]"Different optineurin mutation pattern in primary open-angle glaucoma."
Leung Y.F., Fan B.J., Lam D.S.C., Lee W.S., Tam P.O.S., Chua J.K.H., Tham C.C.Y., Lai J.S.M., Fan D.S.P., Pang C.P.
Invest. Ophthalmol. Vis. Sci. 44:3880-3884(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1E ASP-103 AND ARG-486.
[23]"Evaluation of optineurin sequence variations in 1,048 patients with open-angle glaucoma."
Alward W.L.M., Kwon Y.H., Kawase K., Craig J.E., Hayreh S.S., Johnson A.T., Khanna C.L., Yamamoto T., Mackey D.A., Roos B.R., Affatigato L.M., Sheffield V.C., Stone E.M.
Am. J. Ophthalmol. 136:904-910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1E GLN-545.
[24]"Analysis of optineurin (OPTN) gene mutations in subjects with and without glaucoma: the blue mountains eye study."
Baird P.N., Richardson A.J., Craig J.E., Mackey D.A., Rochtchina E., Mitchell P.
Clin. Exp. Ophthalmol. 32:518-522(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-98.
[25]"Defining the pathogenicity of optineurin in juvenile open-angle glaucoma."
Willoughby C.E., Chan L.L.Y., Herd S., Billingsley G., Noordeh N., Levin A.V., Buys Y., Trope G., Sarfarazi M., Heon E.
Invest. Ophthalmol. Vis. Sci. 45:3122-3130(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1E ARG-486.
[26]"Variants in optineurin gene and their association with tumor necrosis factor-alpha polymorphisms in Japanese patients with glaucoma."
Funayama T., Ishikawa K., Ohtake Y., Tanino T., Kurosaka D., Kimura I., Suzuki K., Ideta H., Nakamoto K., Yasuda N., Fujimaki T., Murakami A., Asaoka R., Hotta Y., Tanihara H., Kanamoto T., Mishima H., Fukuchi T. expand/collapse author list , Abe H., Iwata T., Shimada N., Kudoh J., Shimizu N., Mashima Y.
Invest. Ophthalmol. Vis. Sci. 45:4359-4367(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLC1E ASP-26 AND GLN-545, VARIANT LYS-98.
[27]"Molecular genetic analysis of optineurin gene for primary open-angle and normal tension glaucoma in the Japanese population."
Fuse N., Takahashi K., Akiyama H., Nakazawa T., Seimiya M., Kuwahara S., Tamai M.
J. Glaucoma 13:299-303(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLC1E ASP-26.
[28]"Clinical relevance of optineurin sequence alterations in Japanese glaucoma patients."
Umeda T., Matsuo T., Nagayama M., Tamura N., Tanabe Y., Ohtsuki H.
Ophthalmic Genet. 25:91-99(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NPG ASP-26.
[29]"Mutations of optineurin in amyotrophic lateral sclerosis."
Maruyama H., Morino H., Ito H., Izumi Y., Kato H., Watanabe Y., Kinoshita Y., Kamada M., Nodera H., Suzuki H., Komure O., Matsuura S., Kobatake K., Morimoto N., Abe K., Suzuki N., Aoki M., Kawata A. expand/collapse author list , Hirai T., Kato T., Ogasawara K., Hirano A., Takumi T., Kusaka H., Hagiwara K., Kaji R., Kawakami H.
Nature 465:223-226(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS12 GLY-478, SUBCELLULAR LOCATION.
[30]"Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth."
Wild P., Farhan H., McEwan D.G., Wagner S., Rogov V.V., Brady N.R., Richter B., Korac J., Waidmann O., Choudhary C., Dotsch V., Bumann D., Dikic I.
Science 333:228-233(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-177 BY TBK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061034 mRNA. Translation: AAC16046.1.
AF061034 mRNA. Translation: AAC16047.1.
AF420371 mRNA. Translation: AAL76327.1.
AF420372 mRNA. Translation: AAL76328.1.
AF420373 mRNA. Translation: AAL76329.1.
AF283527 expand/collapse EMBL AC list , AF283520, AF283521, AF283522, AF283523, AF283524, AF283525, AF283526 Genomic DNA. Translation: AAG00497.1.
AK055403 mRNA. Translation: BAG51512.1.
AL355355 Genomic DNA. Translation: CAI16549.1.
AL355355 Genomic DNA. Translation: CAI16550.1.
AL355355 Genomic DNA. Translation: CAI16551.1.
AL355355 Genomic DNA. Translation: CAI16552.1. Sequence problems.
CH471072 Genomic DNA. Translation: EAW86301.1.
CH471072 Genomic DNA. Translation: EAW86302.1.
CH471072 Genomic DNA. Translation: EAW86303.1.
CH471072 Genomic DNA. Translation: EAW86304.1.
CH471072 Genomic DNA. Translation: EAW86306.1.
CH471072 Genomic DNA. Translation: EAW86308.1.
CH471072 Genomic DNA. Translation: EAW86309.1.
BC013876 mRNA. Translation: AAH13876.1.
BC032762 mRNA. Translation: AAH32762.1.
AF049614 mRNA. Translation: AAC26850.1.
CCDSCCDS7094.1. [Q96CV9-1]
RefSeqNP_001008212.1. NM_001008211.1.
NP_001008213.1. NM_001008212.1.
NP_001008214.1. NM_001008213.1.
NP_068815.2. NM_021980.4.
XP_005252393.2. XM_005252336.2.
XP_005252394.2. XM_005252337.2.
UniGeneHs.332706.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LO4NMR-A550-577[»]
2LUENMR-B169-185[»]
3VTVX-ray1.70A170-181[»]
3VTWX-ray2.52A/B/C170-181[»]
ProteinModelPortalQ96CV9.
SMRQ96CV9. Positions 550-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115436. 52 interactions.
DIPDIP-42001N.
IntActQ96CV9. 60 interactions.
MINTMINT-155870.

PTM databases

PhosphoSiteQ96CV9.

Polymorphism databases

DMDM317373403.

Proteomic databases

MaxQBQ96CV9.
PaxDbQ96CV9.
PRIDEQ96CV9.

Protocols and materials databases

DNASU10133.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263036; ENSP00000263036; ENSG00000123240. [Q96CV9-1]
ENST00000378747; ENSP00000368021; ENSG00000123240. [Q96CV9-1]
ENST00000378748; ENSP00000368022; ENSG00000123240. [Q96CV9-1]
ENST00000378752; ENSP00000368027; ENSG00000123240. [Q96CV9-2]
ENST00000378757; ENSP00000368032; ENSG00000123240. [Q96CV9-1]
ENST00000378764; ENSP00000368040; ENSG00000123240. [Q96CV9-2]
GeneID10133.
KEGGhsa:10133.
UCSCuc001ilu.1. human. [Q96CV9-1]
uc001ily.1. human. [Q96CV9-2]

Organism-specific databases

CTD10133.
GeneCardsGC10P013055.
GeneReviewsOPTN.
HGNCHGNC:17142. OPTN.
HPACAB019303.
HPA003279.
HPA003360.
MIM137760. phenotype.
602432. gene.
606657. phenotype.
613435. phenotype.
neXtProtNX_Q96CV9.
Orphanet803. Amyotrophic lateral sclerosis.
353225. Primary adult open-angle glaucoma.
PharmGKBPA31948.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG138369.
HOVERGENHBG106481.
InParanoidQ96CV9.
OMAAHPNLDT.
OrthoDBEOG7D2FD7.
PhylomeDBQ96CV9.
TreeFamTF326608.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

BgeeQ96CV9.
GenevestigatorQ96CV9.

Family and domain databases

InterProIPR021063. NEMO_N.
[Graphical view]
PfamPF11577. NEMO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOPTN. human.
GeneWikiOptineurin.
GenomeRNAi10133.
NextBio38327.
PROQ96CV9.
SOURCESearch...

Entry information

Entry nameOPTN_HUMAN
AccessionPrimary (citable) accession number: Q96CV9
Secondary accession number(s): B3KP00 expand/collapse secondary AC list , D3DRS4, D3DRS8, Q5T672, Q5T673, Q5T674, Q5T675, Q7LDL9, Q8N562, Q9UET9, Q9UEV4, Q9Y218
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM