Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13432

- U119A_HUMAN

UniProt

Q13432 - U119A_HUMAN

Protein

Protein unc-119 homolog A

Gene

UNC119

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons. Probably plays a role in trafficking proteins in photoreceptor cells. Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei131 – 1311Lipid

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis, completion of separation Source: UniProtKB
    2. lipoprotein transport Source: UniProtKB
    3. negative regulation of caveolin-mediated endocytosis Source: UniProtKB
    4. negative regulation of clathrin-mediated endocytosis Source: UniProtKB
    5. phototransduction Source: ProtInc
    6. positive regulation of protein tyrosine kinase activity Source: UniProtKB
    7. synaptic transmission Source: ProtInc
    8. visual perception Source: ProtInc

    Keywords - Biological processi

    Endocytosis, Protein transport, Sensory transduction, Transport, Vision

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein unc-119 homolog A
    Alternative name(s):
    Retinal protein 4
    Short name:
    hRG4
    Gene namesi
    Name:UNC119
    Synonyms:RG4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12565. UNC119.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle pole. Cytoplasmcytoskeletonspindle
    Note: Localizes to the centrosome in interphase cells and begins to translocate from the spindle pole to the spindle midzone after the onset of mitosis; it then localizes to the intercellular bridge in telophase cells and to the midbody in cytokinetic cells.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytosol Source: ProtInc
    3. intercellular bridge Source: UniProtKB
    4. spindle midzone Source: UniProtKB
    5. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Defects in UNC119 may be a cause of cone-rod dystrophy. A mutation was found in a 57-year-old woman with late-onset cone-rod dystrophy: from 40 year old, the patient suffered from poor night vision, defective color vision and light-sensitivity. At 57 year old, she displayed reduced visual acuity, myopa, macular atrophy and pericentral ring scotomas. The disease was caused by a heterozygous mutation causing premature termination and truncated UNC119 protein with dominant-negative effect.
    Immunodeficiency 13 (IMD13) [MIM:615518]: A rare and heterogeneous syndrome defined by a reproducible reduction in the CD4 T-lymphocyte count (less than 300 cells per microliter or less than 20% of total T-cells) in the absence of HIV infection or other known causes of immunodeficiency. IMD13 predisposes to infections and malignancy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221G → V in IMD13; impairs interaction with LCK; impairs LCK activation; induces LCK mislocalization. 1 Publication
    VAR_071184

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 324PQPP → AQPA: Impairs interaction with LCK. 1 Publication

    Keywords - Diseasei

    Cone-rod dystrophy, Disease mutation

    Organism-specific databases

    MIMi615518. phenotype.
    Orphaneti1872. Cone rod dystrophy.
    228000. Idiopathic CD4 lymphocytopenia.
    PharmGKBiPA37202.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 240240Protein unc-119 homolog APRO_0000221212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13432.
    PaxDbiQ13432.
    PRIDEiQ13432.

    PTM databases

    PhosphoSiteiQ13432.

    Expressioni

    Tissue specificityi

    Abundantly expressed in retina, in photoreceptor synapses and inner segments. Expressed in a much lesser extent in several other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ13432.
    BgeeiQ13432.
    CleanExiHS_UNC119.
    GenevestigatoriQ13432.

    Organism-specific databases

    HPAiHPA041912.

    Interactioni

    Subunit structurei

    Interacts with CABP4; in the absence of calcium. May interact with ARL1, ARL2 and ARL3 GTP-bound forms. Found in a complex with ARL3, RP2 and UNC119; RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119. Interacts with NPHP3 (when myristoylated). Interacts with CYS1 (when myristoylated). Interacts with C5orf30; interaction only takes place when UNC119 is not liganded with myristoylated proteins. Interacts with LCK; this interaction plays a crucial role in activation of LCK. Interacts with FYN. Interacts with RAB11A; in a cell cycle-dependent manner. Interacts with LYN (via SH2 and SH3 domains); leading to LYN activation. Interacts with DNM1; leading to a decrease of DNM1 GTPase activity By similarity. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases. Interacts with CD44; leading to Shigella invasion.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARL2P364042EBI-711260,EBI-752365
    Arl2Q9D0J42EBI-711260,EBI-1033319From a different organism.
    ARL3P364055EBI-711260,EBI-712710
    Arl3Q9WUL73EBI-711260,EBI-6860857From a different organism.

    Protein-protein interaction databases

    BioGridi114548. 90 interactions.
    IntActiQ13432. 88 interactions.
    MINTiMINT-1372196.
    STRINGi9606.ENSP00000337040.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi62 – 643
    Turni65 – 673
    Helixi79 – 813
    Beta strandi87 – 959
    Turni96 – 983
    Beta strandi101 – 1066
    Beta strandi128 – 1325
    Helixi135 – 1395
    Beta strandi141 – 15010
    Beta strandi158 – 16710
    Beta strandi170 – 1789
    Beta strandi186 – 19510
    Helixi201 – 2099
    Beta strandi214 – 2229
    Beta strandi225 – 23511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GQQX-ray1.95A/B/C/D/E/F56-240[»]
    3RBQX-ray2.00A/B/C/D/E/F56-240[»]
    4GOJX-ray2.10C/D1-240[»]
    4GOKX-ray2.60C/G1-240[»]
    ProteinModelPortaliQ13432.
    SMRiQ13432. Positions 57-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13432.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 5959Required for midbody localizationAdd
    BLAST
    Regioni121 – 240120Required for centrosome localizationAdd
    BLAST

    Domaini

    Adopts an immunoglobulin-like beta-sandwich fold forming a hydrophobic cavity that capture N-terminally myristoylated target peptides (PubMed:21642972). Phe residues within the hydrophobic beta sandwich are required for myristate binding (PubMed:22085962).2 Publications

    Sequence similaritiesi

    Belongs to the PDE6D/unc-119 family.Curated

    Phylogenomic databases

    eggNOGiNOG305476.
    HOGENOMiHOG000258286.
    HOVERGENiHBG108625.
    InParanoidiQ13432.
    OMAiIHERRPQ.
    OrthoDBiEOG7288SP.
    PhylomeDBiQ13432.
    TreeFamiTF314474.

    Family and domain databases

    Gene3Di2.70.50.40. 1 hit.
    InterProiIPR008015. GMP_PDE_delta.
    IPR014756. Ig_E-set.
    [Graphical view]
    PfamiPF05351. GMP_PDE_delta. 1 hit.
    [Graphical view]
    SUPFAMiSSF81296. SSF81296. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q13432-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKVKKGGGGA GTATESAPGP SGQSVAPIPQ PPAESESGSE SEPDAGPGPR    50
    PGPLQRKQPI GPEDVLGLQR ITGDYLCSPE ENIYKIDFVR FKIRDMDSGT 100
    VLFEIKKPPV SERLPINRRD LDPNAGRFVR YQFTPAFLRL RQVGATVEFT 150
    VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG FCIPSSKNTC EHIYDFPPLS 200
    EELISEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP 240
    Length:240
    Mass (Da):26,962
    Last modified:November 1, 1996 - v1
    Checksum:i22FD19C3518A4446
    GO
    Isoform B (identifier: Q13432-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         204-240: ISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP → SARAGSSGSGEVGASRD

    Show »
    Length:220
    Mass (Da):24,112
    Checksum:i70146298DD2628C7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221G → V in IMD13; impairs interaction with LCK; impairs LCK activation; induces LCK mislocalization. 1 Publication
    VAR_071184

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei204 – 24037ISEMI…YSGTP → SARAGSSGSGEVGASRD in isoform B. 3 PublicationsVSP_004545Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40998 mRNA. Translation: AAC50360.1.
    AF028788 mRNA. Translation: AAD01875.1.
    AF028789 mRNA. Translation: AAD01876.1.
    AF125998, AF125997 Genomic DNA. Translation: AAD31422.1.
    AK292329 mRNA. Translation: BAF85018.1.
    AB593014 mRNA. Translation: BAJ83969.1.
    AC005726 Genomic DNA. No translation available.
    CH471159 Genomic DNA. Translation: EAW51095.1.
    BC027176 mRNA. Translation: AAH27176.1.
    CCDSiCCDS11233.1. [Q13432-1]
    CCDS11234.1. [Q13432-2]
    RefSeqiNP_005139.1. NM_005148.3. [Q13432-1]
    NP_473376.1. NM_054035.2. [Q13432-2]
    UniGeneiHs.410455.

    Genome annotation databases

    EnsembliENST00000301032; ENSP00000301032; ENSG00000109103. [Q13432-2]
    ENST00000335765; ENSP00000337040; ENSG00000109103. [Q13432-1]
    GeneIDi9094.
    KEGGihsa:9094.
    UCSCiuc002hbk.2. human. [Q13432-1]
    uc002hbm.2. human. [Q13432-2]

    Polymorphism databases

    DMDMi2498854.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40998 mRNA. Translation: AAC50360.1 .
    AF028788 mRNA. Translation: AAD01875.1 .
    AF028789 mRNA. Translation: AAD01876.1 .
    AF125998 , AF125997 Genomic DNA. Translation: AAD31422.1 .
    AK292329 mRNA. Translation: BAF85018.1 .
    AB593014 mRNA. Translation: BAJ83969.1 .
    AC005726 Genomic DNA. No translation available.
    CH471159 Genomic DNA. Translation: EAW51095.1 .
    BC027176 mRNA. Translation: AAH27176.1 .
    CCDSi CCDS11233.1. [Q13432-1 ]
    CCDS11234.1. [Q13432-2 ]
    RefSeqi NP_005139.1. NM_005148.3. [Q13432-1 ]
    NP_473376.1. NM_054035.2. [Q13432-2 ]
    UniGenei Hs.410455.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GQQ X-ray 1.95 A/B/C/D/E/F 56-240 [» ]
    3RBQ X-ray 2.00 A/B/C/D/E/F 56-240 [» ]
    4GOJ X-ray 2.10 C/D 1-240 [» ]
    4GOK X-ray 2.60 C/G 1-240 [» ]
    ProteinModelPortali Q13432.
    SMRi Q13432. Positions 57-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114548. 90 interactions.
    IntActi Q13432. 88 interactions.
    MINTi MINT-1372196.
    STRINGi 9606.ENSP00000337040.

    PTM databases

    PhosphoSitei Q13432.

    Polymorphism databases

    DMDMi 2498854.

    Proteomic databases

    MaxQBi Q13432.
    PaxDbi Q13432.
    PRIDEi Q13432.

    Protocols and materials databases

    DNASUi 9094.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301032 ; ENSP00000301032 ; ENSG00000109103 . [Q13432-2 ]
    ENST00000335765 ; ENSP00000337040 ; ENSG00000109103 . [Q13432-1 ]
    GeneIDi 9094.
    KEGGi hsa:9094.
    UCSCi uc002hbk.2. human. [Q13432-1 ]
    uc002hbm.2. human. [Q13432-2 ]

    Organism-specific databases

    CTDi 9094.
    GeneCardsi GC17M026873.
    HGNCi HGNC:12565. UNC119.
    HPAi HPA041912.
    MIMi 604011. gene.
    615518. phenotype.
    neXtProti NX_Q13432.
    Orphaneti 1872. Cone rod dystrophy.
    228000. Idiopathic CD4 lymphocytopenia.
    PharmGKBi PA37202.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305476.
    HOGENOMi HOG000258286.
    HOVERGENi HBG108625.
    InParanoidi Q13432.
    OMAi IHERRPQ.
    OrthoDBi EOG7288SP.
    PhylomeDBi Q13432.
    TreeFami TF314474.

    Miscellaneous databases

    ChiTaRSi UNC119. human.
    EvolutionaryTracei Q13432.
    GeneWikii Protein_unc-119_homolog.
    GenomeRNAii 9094.
    NextBioi 34075.
    PROi Q13432.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13432.
    Bgeei Q13432.
    CleanExi HS_UNC119.
    Genevestigatori Q13432.

    Family and domain databases

    Gene3Di 2.70.50.40. 1 hit.
    InterProi IPR008015. GMP_PDE_delta.
    IPR014756. Ig_E-set.
    [Graphical view ]
    Pfami PF05351. GMP_PDE_delta. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNA for a novel photoreceptor protein."
      Higashide T., Murakami A., McLaren M.J., Inana G.
      J. Biol. Chem. 271:1797-1804(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
      Tissue: Retina.
    2. "Mammalian orthologs of C. elegans unc-119 highly expressed in photoreceptors."
      Swanson D.A., Chang J.T., Campochiaro P.A., Zack D.J., Valle D.
      Invest. Ophthalmol. Vis. Sci. 39:2085-2094(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), TISSUE SPECIFICITY.
      Tissue: Retina.
    3. "Characterization of the gene for HRG4 (UNC119), a novel photoreceptor synaptic protein homologous to unc-119."
      Higashide T., Inana G.
      Genomics 57:446-450(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
    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.
      , 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 B).
      Tissue: Testis.
    5. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
      Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
      Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Tissue: Retinoblastoma.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM A).
      Tissue: Lymph.
    9. "HRG4 (UNC119) mutation found in cone-rod dystrophy causes retinal degeneration in a transgenic model."
      Kobayashi A., Higashide T., Hamasaki D., Kubota S., Sakuma H., An W., Fujimaki T., McLaren M.J., Weleber R.G., Inana G.
      Invest. Ophthalmol. Vis. Sci. 41:3268-3277(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CONE-ROD DYSTROPHY.
    10. "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins."
      Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.
      J. Biol. Chem. 276:22826-22837(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARL1; ARL2 AND ARL3.
    11. "Identification of UNC119 as a novel activator of SRC-type tyrosine kinases."
      Cen O., Gorska M.M., Stafford S.J., Sur S., Alam R.
      J. Biol. Chem. 278:8837-8845(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYN, FUNCTION IN LYN ACTIVATION.
    12. "Unc119, a novel activator of Lck/Fyn, is essential for T cell activation."
      Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.
      J. Exp. Med. 199:369-379(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LCK AND FYN, FUNCTION IN LCK AND FYN ACTIVATION, MUTAGENESIS OF 29-PRO--PRO-32.
    13. "Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex."
      Veltel S., Kravchenko A., Ismail S., Wittinghofer A.
      FEBS Lett. 582:2501-2507(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ARL3 AND RP2.
    14. "Unc119 protects from Shigella infection by inhibiting the Abl family kinases."
      Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.
      PLoS ONE 4:E5211-E5211(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD44, IDENTIFICATION IN A COMPLEX WITH ABL1; ABL2 AND CRK, FUNCTION IN SHIGELLA FLEXNERI UPTAKE.
    15. Cited for: FUNCTION, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH NPHP3; CYS1 AND C5ORF30.
    16. "UNC119a bridges the transmission of Fyn signals to Rab11, leading to the completion of cytokinesis."
      Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.
      Cell Cycle 12:1303-1315(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FYN AND RAB11A, FUNCTION IN ACTIVATION OF FYN.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 56-240 IN COMPLEX WITH LAURYLATED GNAT1, FUNCTION, INTERACTION WITH GNAT1.
    18. "A mutation in the human Uncoordinated 119 gene impairs TCR signaling and is associated with CD4 lymphopenia."
      Gorska M.M., Alam R.
      Blood 119:1399-1406(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IMD13 VAL-22, CHARACTERIZATION OF VARIANT IMD13 VAL-22.

    Entry informationi

    Entry nameiU119A_HUMAN
    AccessioniPrimary (citable) accession number: Q13432
    Secondary accession number(s): A8K8G4, F1T095, O95126
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    According to some authors, acts by extracting target proteins from membranes (PubMed:21642972). According to a another report, rather acts by targeting proteins to membranes (PubMed:22085962).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3