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UV radiation resistance-associated gene protein (p63)

 UVRAG_HUMAN             Reviewed;         699 AA.
Q9P2Y5; B3KTC1; O00392;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 137.
RecName: Full=UV radiation resistance-associated gene protein;
AltName: Full=p63;
Name=UVRAG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9169138; DOI=10.1006/geno.1997.4623;
Perelman B., Dafni N., Naiman T., Eli D., Yaakov M., Feng T.L.Y.,
Sinha S., Weber G., Khodaei S., Sancar A., Dotan I., Canaani D.;
"Molecular cloning of a novel human gene encoding a 63-kDa protein and
its sublocalization within the 11q13 locus.";
Genomics 41:397-405(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
POSSIBLE INVOLVEMENT IN HETEROTAXY.
TISSUE=Heart;
PubMed=10798355; DOI=10.1007/s004390051038;
Iida A., Emi M., Matsuoka R., Hiratsuka E., Okui K., Ohashi H.,
Inazawa J., Fukushima Y., Imai T., Nakamura Y.;
"Identification of a gene disrupted by inv(11)(q13.5;q25) in a patient
with left-right axis malformation.";
Hum. Genet. 106:277-287(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
ASSOCIATION WITH THE PI3K COMPLEX, AND FUNCTION.
PubMed=16799551; DOI=10.1038/ncb1426;
Liang C., Feng P., Ku B., Dotan I., Canaani D., Oh B.H., Jung J.U.;
"Autophagic and tumour suppressor activity of a novel Beclin1-binding
protein UVRAG.";
Nat. Cell Biol. 8:688-699(2006).
[6]
INTERACTION WITH SH3GLB1.
PubMed=17891140; DOI=10.1038/ncb1634;
Takahashi Y., Coppola D., Matsushita N., Cualing H.D., Sun M.,
Sato Y., Liang C., Jung J.U., Cheng J.Q., Mule J.J., Pledger W.J.,
Wang H.G.;
"Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy
and tumorigenesis.";
Nat. Cell Biol. 9:1142-1151(2007).
[7]
INTERACTION WITH BECN1 AND PIK3C3, AND SUBCELLULAR LOCATION.
PubMed=18843052; DOI=10.1091/mbc.E08-01-0080;
Itakura E., Kishi C., Inoue K., Mizushima N.;
"Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes
with mammalian Atg14 and UVRAG.";
Mol. Biol. Cell 19:5360-5372(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
FUNCTION, INTERACTION WITH VPS16; VPS11; VPS18; VPS33 AND VPS39, AND
SUBCELLULAR LOCATION.
PubMed=18552835; DOI=10.1038/ncb1740;
Liang C., Lee J.S., Inn K.S., Gack M.U., Li Q., Roberts E.A.,
Vergne I., Deretic V., Feng P., Akazawa C., Jung J.U.;
"Beclin1-binding UVRAG targets the class C Vps complex to coordinate
autophagosome maturation and endocytic trafficking.";
Nat. Cell Biol. 10:776-787(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
INTERACTION WITH BECN1.
PubMed=19050071; DOI=10.1073/pnas.0810452105;
Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q.;
"Identification of Barkor as a mammalian autophagy-specific factor for
Beclin 1 and class III phosphatidylinositol 3-kinase.";
Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-571, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
INTERACTION WITH BECN1; RUBCN; PIK3C3 AND PIK3R4.
PubMed=19270696; DOI=10.1038/ncb1846;
Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N.,
Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S.,
Noda T., Yoshimori T.;
"Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally
regulate autophagy at different stages.";
Nat. Cell Biol. 11:385-396(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=20643123; DOI=10.1016/j.yexcr.2010.07.008;
Thoresen S.B., Pedersen N.M., Liestol K., Stenmark H.;
"A phosphatidylinositol 3-kinase class III sub-complex containing
VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and
degradative endocytic traffic.";
Exp. Cell Res. 316:3368-3378(2010).
[16]
INTERACTION WITH RAB7A.
PubMed=20974968; DOI=10.1073/pnas.1010554107;
Sun Q., Westphal W., Wong K.N., Tan I., Zhong Q.;
"Rubicon controls endosome maturation as a Rab7 effector.";
Proc. Natl. Acad. Sci. U.S.A. 107:19338-19343(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
FUNCTION, INTERACTION WITH PRKDC; XRCC6; XRCC5 AND CEP63, AND
SUBCELLULAR LOCATION.
PubMed=22542840; DOI=10.1016/j.devcel.2011.12.027;
Zhao Z., Oh S., Li D., Ni D., Pirooz S.D., Lee J.H., Yang S.,
Lee J.Y., Ghozalli I., Costanzo V., Stark J.M., Liang C.;
"A dual role for UVRAG in maintaining chromosomal stability
independent of autophagy.";
Dev. Cell 22:1001-1016(2012).
[19]
INTERACTION WITH SCOC AND FEZ1.
PubMed=22354037; DOI=10.1038/emboj.2012.36;
McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
Johansen T., Tooze S.A.;
"Genome-wide siRNA screen reveals amino acid starvation-induced
autophagy requires SCOC and WAC.";
EMBO J. 31:1931-1946(2012).
[20]
INTERACTION WITH SLAMF1.
PubMed=22493499; DOI=10.1074/jbc.M112.367060;
Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.;
"Receptor signaling lymphocyte-activation molecule family 1 (Slamf1)
regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by
recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-
associated gene (UVRAG) complex.";
J. Biol. Chem. 287:18359-18365(2012).
[21]
INTERACTION WITH BECN1P1/BECN2.
PubMed=23954414; DOI=10.1016/j.cell.2013.07.035;
He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N.,
Khan S., Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L.,
Scherer P.E., Whistler J.L., Levine B.;
"Beclin 2 functions in autophagy, degradation of G protein-coupled
receptors, and metabolism.";
Cell 154:1085-1099(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; THR-518; SER-550
AND SER-689, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
INTERACTION WITH BECN1.
PubMed=23878393; DOI=10.1128/MCB.00079-13;
Fogel A.I., Dlouhy B.J., Wang C., Ryu S.W., Neutzner A., Hasson S.A.,
Sideris D.P., Abeliovich H., Youle R.J.;
"Role of membrane association and Atg14-dependent phosphorylation in
beclin-1-mediated autophagy.";
Mol. Cell. Biol. 33:3675-3688(2013).
[24]
FUNCTION, INTERACTION WITH RINT1, SUBCELLULAR LOCATION, ASSOCIATION
WITH THE PI3K COMPLEX, AND ASSOCIATION WITH THE NRZ COMPLEX.
PubMed=24056303; DOI=10.1038/ncb2848;
He S., Ni D., Ma B., Lee J.H., Zhang T., Ghozalli I., Pirooz S.D.,
Zhao Z., Bharatham N., Li B., Oh S., Lee W.H., Takahashi Y.,
Wang H.G., Minassian A., Feng P., Deretic V., Pepperkok R., Tagaya M.,
Yoon H.S., Liang C.;
"PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9
transport by differential interactions with the ER tether and the
beclin 1 complex.";
Nat. Cell Biol. 15:1206-1219(2013).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
FUNCTION, AND INTERACTION WITH STX7; VTI1B AND STX8.
PubMed=24550300; DOI=10.1073/pnas.1320629111;
Pirooz S.D., He S., Zhang T., Zhang X., Zhao Z., Oh S., O'Connell D.,
Khalilzadeh P., Amini-Bavil-Olyaee S., Farzan M., Liang C.;
"UVRAG is required for virus entry through combinatorial interaction
with the class C-Vps complex and SNAREs.";
Proc. Natl. Acad. Sci. U.S.A. 111:2716-2721(2014).
[27]
PHOSPHORYLATION AT SER-493; SER-498; SER-508; SER-522; SER-549;
SER-550 AND SER-582, INTERACTION WITH RUBCN; VPS39; VPS16 AND RAB7A,
AND MUTAGENESIS OF SER-498.
PubMed=25533187; DOI=10.1016/j.molcel.2014.11.013;
Kim Y.M., Jung C.H., Seo M., Kim E.K., Park J.M., Bae S.S., Kim D.H.;
"mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and
endosome maturation.";
Mol. Cell 57:207-218(2015).
-!- FUNCTION: Versatile protein that is involved in regulation of
different cellular pathways implicated in membrane trafficking.
Involved in regulation of the COPI-dependent retrograde transport
from Golgi and the endoplasmic reticulum by associating with the
NRZ complex; the function is dependent on its binding to
phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:24056303).
During autophagy acts as regulatory subunit of the alternative
PI3K complex II (PI3KC3-C2) that mediates formation of
phosphatidylinositol 3-phosphate and is believed to be involved in
maturation of autophagosomes and endocytosis. Activates lipid
kinase activity of PIK3C3. Involved in the regulation of
degradative endocytic trafficking and cytokinesis, and in
regulation of ATG9A transport from the Golgi to the autophagosome;
the functions seems to implicate its association with PI3KC3-C2
(PubMed:16799551, PubMed:20643123, PubMed:24056303). Involved in
maturation of autophagosomes and degradative endocytic trafficking
independently of BECN1 but depending on its association with a
class C Vps complex (possibly the HOPS complex); the association
is also proposed to promote autophagosome recruitment and
activation of Rab7 and endosome-endosome fusion events
(PubMed:18552835). Enhances class C Vps complex (possibly HOPS
complex) association with a SNARE complex and promotes fusogenic
SNARE complex formation during late endocytic membrane fusion
(PubMed:24550300). In case of negative-strand RNA virus infection
is required for efficient virus entry, promotes endocytic
transport of virions and is implicated in a VAMP8-specific
fusogenic SNARE complex assembly (PubMed:24550300).
{ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:20643123,
ECO:0000269|PubMed:24056303, ECO:0000305}.
-!- FUNCTION: Involved in maintaining chromosomal stability. Promotes
DNA double-strand break (DSB) repair by association with DNA-
dependent protein kinase complex DNA-PK and activating it in non-
homologous end joining (NHEJ) (PubMed:22542840). Required for
centrosome stability and proper chromosome segregation
(PubMed:22542840). {ECO:0000269|PubMed:22542840}.
-!- SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III
phosphatidylinositol 3-kinase) complex II (PI3KC3-C2) in which the
core composed of the catalytic subunit PIK3C3, the regulatory
subunit PIK3R4 and BECN1 is associated with UVRAG; in the complex
interacts directly with BECN1. PI3KC3-C2 can associate with
further regulatory subunits such as RUBCN and probably
SH3GLB1/Bif-1 (PubMed:16799551, PubMed:18843052, PubMed:19050071,
PubMed:19270696, PubMed:20643123, PubMed:23878393,
PubMed:24056303). Interacts with SH3GLB1; UVRAG bridges the
interaction to BECN1 indicative for an association with the PI3K
complex PI3KC3-C2 (PubMed:17891140). Interacts with RINT1.
Associates with the NRZ complex under basal conditions and
dissociates from it under autophagy conditions to associate with
the PI3K complex; these complex associations seem to be mutually
exclusive (PubMed:24056303). Interacts with VPS16; VPS11; VPS18;
VPS33 (VPS33A or VPS33B) and VPS39; indicative for an association
with a class C Vps tethering complex (possibly the HOPS complex)
(PubMed:18552835, PubMed:25533187). Interacts with RAB7A; RAB7A
competes with UVRAG for RUBCN binding (PubMed:25533187,
PubMed:20974968). Interacts with STX7, VTI1B, STX8
(PubMed:24550300). Interacts with PRKDC, XRCC6 and XRCC5;
indicative for an association with the DNA-dependent protein
kinase complex DNA-PK. Interacts with CEP63 (PubMed:22542840).
Directly interacts with FEZ1 and SCOC; the interaction with SCOC
is reduced by amino acid starvation, but the complex is stabilized
in the presence of FEZ1 (PubMed:22354037). Interacts with
BECN1P1/BECN2 (PubMed:23954414). Interracts with SLAMF1(
PubMed:22493499). {ECO:0000269|PubMed:16799551,
ECO:0000269|PubMed:17891140, ECO:0000269|PubMed:18552835,
ECO:0000269|PubMed:18843052, ECO:0000269|PubMed:19050071,
ECO:0000269|PubMed:19270696, ECO:0000269|PubMed:20643123,
ECO:0000269|PubMed:20974968, ECO:0000269|PubMed:22354037,
ECO:0000269|PubMed:22493499, ECO:0000269|PubMed:22542840,
ECO:0000269|PubMed:23878393, ECO:0000269|PubMed:23954414,
ECO:0000269|PubMed:24056303, ECO:0000269|PubMed:24550300,
ECO:0000269|PubMed:25533187}.
-!- INTERACTION:
Q07812:BAX; NbExp=6; IntAct=EBI-2952704, EBI-516580;
Q14457:BECN1; NbExp=29; IntAct=EBI-2952704, EBI-949378;
Q8NEB9:PIK3C3; NbExp=16; IntAct=EBI-2952704, EBI-1056470;
Q6NUQ1:RINT1; NbExp=17; IntAct=EBI-2952704, EBI-726876;
Q92622:RUBCN; NbExp=7; IntAct=EBI-2952704, EBI-2952709;
Q9Y371:SH3GLB1; NbExp=6; IntAct=EBI-2952704, EBI-2623095;
Q9QUM4:Slamf1 (xeno); NbExp=6; IntAct=EBI-2952704, EBI-7910086;
Q96AX1:VPS33A; NbExp=4; IntAct=EBI-2952704, EBI-2527283;
-!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:18843052}.
Lysosome {ECO:0000269|PubMed:18843052}. Early endosome
{ECO:0000269|PubMed:18552835, ECO:0000269|PubMed:18843052}.
Endoplasmic reticulum {ECO:0000269|PubMed:24056303}. Midbody
{ECO:0000269|PubMed:20643123}. Chromosome, centromere
{ECO:0000269|PubMed:22542840}. Note=Colocalizes with RAB9-positive
compartments involved in retrograde transport from late endosomes
to trans-Golgi network. Colocalization with early endosomes is
only partial.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9P2Y5-1; Sequence=Displayed;
Name=2;
IsoId=Q9P2Y5-2; Sequence=VSP_056176;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney and
liver. {ECO:0000269|PubMed:10798355}.
-!- PTM: Phosphorylated at Ser-498 by MTOR under basal conditions;
increases the interaction with RUBCN implicated in inhibitory
effect of RUBCN on PI3KC3 and decreases interaction with RAB7,A
and VPS16 and VPS39 (indicative for a class C Vps complex,
possibly the HOPS complex) (PubMed:25533187).
{ECO:0000269|PubMed:25533187}.
-!- DISEASE: Note=A chromosomal aberration involving UVRAG has been
observed in a patient with heterotaxy (left-right axis
malformation). Inversion Inv(11)(q13.5;q25).
{ECO:0000269|PubMed:10798355}.
-!- SEQUENCE CAUTION:
Sequence=CAA67507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X99050; CAA67507.1; ALT_SEQ; Genomic_DNA.
EMBL; AB012958; BAA90829.1; -; mRNA.
EMBL; AK095352; BAG53033.1; -; mRNA.
EMBL; AK296871; BAG59434.1; -; mRNA.
EMBL; AK316133; BAH14504.1; -; mRNA.
EMBL; AP002340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS8241.1; -. [Q9P2Y5-1]
RefSeq; NP_003360.2; NM_003369.3. [Q9P2Y5-1]
UniGene; Hs.202470; -.
ProteinModelPortal; Q9P2Y5; -.
SMR; Q9P2Y5; -.
BioGrid; 113248; 24.
CORUM; Q9P2Y5; -.
DIP; DIP-48652N; -.
IntAct; Q9P2Y5; 53.
MINT; MINT-4658044; -.
STRING; 9606.ENSP00000348455; -.
iPTMnet; Q9P2Y5; -.
PhosphoSitePlus; Q9P2Y5; -.
BioMuta; UVRAG; -.
DMDM; 20140879; -.
EPD; Q9P2Y5; -.
MaxQB; Q9P2Y5; -.
PaxDb; Q9P2Y5; -.
PeptideAtlas; Q9P2Y5; -.
PRIDE; Q9P2Y5; -.
Ensembl; ENST00000356136; ENSP00000348455; ENSG00000198382. [Q9P2Y5-1]
Ensembl; ENST00000531818; ENSP00000434082; ENSG00000198382. [Q9P2Y5-2]
Ensembl; ENST00000532130; ENSP00000436270; ENSG00000198382. [Q9P2Y5-2]
Ensembl; ENST00000533454; ENSP00000431256; ENSG00000198382. [Q9P2Y5-2]
GeneID; 7405; -.
KEGG; hsa:7405; -.
UCSC; uc001oxc.4; human. [Q9P2Y5-1]
CTD; 7405; -.
DisGeNET; 7405; -.
EuPathDB; HostDB:ENSG00000198382.8; -.
GeneCards; UVRAG; -.
HGNC; HGNC:12640; UVRAG.
HPA; HPA016932; -.
MIM; 602493; gene.
neXtProt; NX_Q9P2Y5; -.
OpenTargets; ENSG00000198382; -.
PharmGKB; PA37264; -.
eggNOG; KOG2896; Eukaryota.
eggNOG; ENOG410YZ0H; LUCA.
GeneTree; ENSGT00390000012877; -.
HOGENOM; HOG000147825; -.
HOVERGEN; HBG059846; -.
InParanoid; Q9P2Y5; -.
KO; K21249; -.
OMA; LPGEFHP; -.
OrthoDB; EOG091G0HDH; -.
PhylomeDB; Q9P2Y5; -.
TreeFam; TF323546; -.
BRENDA; 2.7.1.137; 2681.
Reactome; R-HSA-1632852; Macroautophagy.
SIGNOR; Q9P2Y5; -.
ChiTaRS; UVRAG; human.
GeneWiki; UVRAG; -.
GenomeRNAi; 7405; -.
PRO; PR:Q9P2Y5; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000198382; -.
CleanEx; HS_UVRAG; -.
ExpressionAtlas; Q9P2Y5; baseline and differential.
Genevisible; Q9P2Y5; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0006914; P:autophagy; IMP:CACAO.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IDA:UniProtKB.
GO; GO:0051684; P:maintenance of Golgi location; IMP:CACAO.
GO; GO:0071985; P:multivesicular body sorting pathway; TAS:ParkinsonsUK-UCL.
GO; GO:1901098; P:positive regulation of autophagosome maturation; TAS:ParkinsonsUK-UCL.
GO; GO:0032801; P:receptor catabolic process; IMP:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:CACAO.
GO; GO:0035493; P:SNARE complex assembly; IBA:GO_Central.
GO; GO:0007051; P:spindle organization; IEA:Ensembl.
GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR018791; UV_resistance/autophagy_Atg14.
Pfam; PF10186; Atg14; 1.
SMART; SM00239; C2; 1.
SUPFAM; SSF49562; SSF49562; 1.
1: Evidence at protein level;
Alternative splicing; Centromere; Chromosome; Coiled coil;
Complete proteome; DNA damage; DNA repair; Endoplasmic reticulum;
Endosome; Lysosome; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 699 UV radiation resistance-associated gene
protein.
/FTId=PRO_0000065750.
DOMAIN 44 128 C2.
REGION 200 269 Sufficient for interaction with STX7;
VTI1B AND STX8.
{ECO:0000269|PubMed:24550300}.
REGION 270 442 Sufficient for interaction with VPS16,
required for interaction with CEP63.
{ECO:0000269|PubMed:18552835,
ECO:0000269|PubMed:22542840}.
REGION 443 699 Required for interaction with PRKDC,
XRCC6 and XRCC5.
{ECO:0000269|PubMed:22542840}.
COILED 224 305 {ECO:0000255}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000269|PubMed:25533187}.
MOD_RES 498 498 Phosphoserine; by MTOR.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25533187}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000269|PubMed:25533187}.
MOD_RES 518 518 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000269|PubMed:25533187}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000269|PubMed:25533187}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:25533187}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000269|PubMed:25533187}.
MOD_RES 689 689 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 372 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056176.
VARIANT 10 10 P -> H (in dbSNP:rs7118567).
/FTId=VAR_059737.
MUTAGEN 498 498 S->A: Abolishes phosphorylation by MTOR,
decreases interaction with RUBCN,
increases interaction with VPS16 and
VPS39, promotes autophagosome maturation
and endosome-lysosomal degradation of
EGFR. {ECO:0000269|PubMed:25533187}.
SEQUENCE 699 AA; 78151 MW; 23C4413B10F641BA CRC64;
MSASASVGGP VPQPPPGPAA ALPPGSAARA LHVELPSQQR RLRHLRNIAA RNIVNRNGHQ
LLDTYFTLHL CSTEKIYKEF YRSEVIKNSL NPTWRSLDFG IMPDRLDTSV SCFVVKIWGG
KENIYQLLIE WKVCLDGLKY LGQQIHARNQ NEIIFGLNDG YYGAPFEHKG YSNAQKTILL
QVDQNCVRNS YDVFSLLRLH RAQCAIKQTQ VTVQKIGKEI EEKLRLTSTS NELKKKSECL
QLKILVLQNE LERQKKALGR EVALLHKQQI ALQDKGSAFS AEHLKLQLQK ESLNELRKEC
TAKRELFLKT NAQLTIRCRQ LLSELSYIYP IDLNEHKDYF VCGVKLPNSE DFQAKDDGSI
AVALGYTAHL VSMISFFLQV PLRYPIIHKG SRSTIKDNIN DKLTEKEREF PLYPKGGEKL
QFDYGVYLLN KNIAQLRYQH GLGTPDLRQT LPNLKNFMEH GLMVRCDRHH TSSAIPVPKR
QSSIFGGADV GFSGGIPSPD KGHRKRASSE NERLQYKTPP PSYNSALAQP VTTVPSMGET
ERKITSLSSS LDTSLDFSKE NKKKGEDLVG SLNGGHANVH PSQEQGEALS GHRATVNGTL
LPSEQAGSAS VQLPGEFHPV SEAELCCTVE QAEEIIGLEA TGFASGDQLE AFNCIPVDSA
VAVECDEQVL GEFEEFSRRI YALNENVSSF RRPRRSSDK


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