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Q13432

- U119A_HUMAN

UniProt

Q13432 - U119A_HUMAN

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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

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 Publications1 Publication

Sites

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

GO - Molecular functioni

  1. lipid binding Source: UniProtKB

GO - Biological processi

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

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 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication
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.1 Publication

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
Complete GO annotation...

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

BgeeiQ13432.
CleanExiHS_UNC119.
ExpressionAtlasiQ13432. baseline and differential.
GenevestigatoriQ13432.

Organism-specific databases

HPAiHPA041912.

Interactioni

Subunit structurei

Interacts with CABP4; in the absence of calcium (By similarity). Interacts with DNM1; leading to a decrease of DNM1 GTPase activity (By similarity). May interact with GTP-bound ARL1. Interacts with ARL2 and ARL3 (GTP-bound forms); this promotes the release of myyristoylated cargo proteins (PubMed:22960633). 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. 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 similarity9 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. 105 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 – 643Combined sources
Turni65 – 673Combined sources
Helixi79 – 813Combined sources
Beta strandi87 – 959Combined sources
Turni96 – 983Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi128 – 1325Combined sources
Helixi135 – 1395Combined sources
Beta strandi141 – 15010Combined sources
Beta strandi158 – 16710Combined sources
Beta strandi170 – 1789Combined sources
Beta strandi186 – 19510Combined sources
Helixi201 – 2099Combined sources
Beta strandi214 – 2229Combined sources
Beta strandi225 – 23511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 captures 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.
GeneTreeiENSGT00390000014595.
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

        10         20         30         40         50
MKVKKGGGGA GTATESAPGP SGQSVAPIPQ PPAESESGSE SEPDAGPGPR
60 70 80 90 100
PGPLQRKQPI GPEDVLGLQR ITGDYLCSPE ENIYKIDFVR FKIRDMDSGT
110 120 130 140 150
VLFEIKKPPV SERLPINRRD LDPNAGRFVR YQFTPAFLRL RQVGATVEFT
160 170 180 190 200
VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG FCIPSSKNTC EHIYDFPPLS
210 220 230 240
EELISEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 105 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.
GeneTreei ENSGT00390000014595.
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

Bgeei Q13432.
CleanExi HS_UNC119.
ExpressionAtlasi Q13432. baseline and differential.
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

« Hide 'large scale' publications
  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, 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. "Structural basis for Arl3-specific release of myristoylated ciliary cargo from UNC119."
    Ismail S.A., Chen Y.X., Miertzschke M., Vetter I.R., Koerner C., Wittinghofer A.
    EMBO J. 31:4085-4094(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ARL2 AND ARL3, INTERACTION WITH ARL2 AND ARL3.
  19. "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: November 26, 2014
This is version 118 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