Q9P2Y5 (UVRAG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UV radiation resistance-associated gene protein

Alternative name(s):
p63

Gene names

Name:

UVRAG

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Forms a complex with BECN1, PIK3C3 and PIK3R4. A subpopulation of these complexes also harbor KIAA0226/Rubicon. UVRAG-containing complexes never including ATG14, both forming mutually exclusive complexes with BECN1 through direct competition.
Subcellular location	Late endosome. Lysosome. Early endosome. Note: Colocalizes with RAB9-positive compartments involved in retrograde transport from late endosomes to trans-Golgi network. Colocalization with early endosomes is only partial. Ref.5
Tissue specificity	Highly expressed in brain, lung, kidney and liver. Ref.2
Involvement in 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).
Sequence similarities	Contains 1 C2 domain.
Sequence caution	The sequence CAA67507.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endosome Lysosome
Coding sequence diversity	Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Traceable author statement. Source: ProtInc positive regulation of autophagy Inferred from electronic annotation. Source: InterPro
Cellular component	early endosome Inferred from direct assay Ref.10. Source: UniProtKB late endosome Inferred from direct assay Ref.10. Source: UniProtKB lysosome Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 699	699	UV radiation resistance-associated gene protein		PRO_0000065750
Regions
	Domain	44 – 128	85	C2
	Coiled coil	224 – 305	82	Potential
Amino acid modifications
	Modified residue	83	1	Phosphoserine Ref.3
	Modified residue	482	1	Phosphoserine Ref.9
	Modified residue	493	1	Phosphoserine Ref.9
	Modified residue	498	1	Phosphoserine Ref.4 Ref.9
	Modified residue	508	1	Phosphoserine Ref.9
	Modified residue	516	1	Phosphotyrosine Ref.9
	Modified residue	518	1	Phosphothreonine Ref.4 Ref.6 Ref.9 Ref.11
	Modified residue	522	1	Phosphoserine Ref.9
	Modified residue	545	1	Phosphothreonine Ref.9
	Modified residue	549	1	Phosphoserine Ref.9
	Modified residue	550	1	Phosphoserine Ref.9
	Modified residue	571	1	Phosphoserine Ref.9
	Modified residue	689	1	Phosphoserine Ref.8 Ref.9
Natural variations
	Natural variant	10	1	P → H. Corresponds to variant rs7118567 [ dbSNP | Ensembl ].		VAR_059737

Sequences

	Sequence		Length	Mass (Da)
	Q9P2Y5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 23C4413B10F641BA	FASTA	699	78,151
	10 20 30 40 50 60 MSASASVGGP VPQPPPGPAA ALPPGSAARA LHVELPSQQR RLRHLRNIAA RNIVNRNGHQ 70 80 90 100 110 120 LLDTYFTLHL CSTEKIYKEF YRSEVIKNSL NPTWRSLDFG IMPDRLDTSV SCFVVKIWGG 130 140 150 160 170 180 KENIYQLLIE WKVCLDGLKY LGQQIHARNQ NEIIFGLNDG YYGAPFEHKG YSNAQKTILL 190 200 210 220 230 240 QVDQNCVRNS YDVFSLLRLH RAQCAIKQTQ VTVQKIGKEI EEKLRLTSTS NELKKKSECL 250 260 270 280 290 300 QLKILVLQNE LERQKKALGR EVALLHKQQI ALQDKGSAFS AEHLKLQLQK ESLNELRKEC 310 320 330 340 350 360 TAKRELFLKT NAQLTIRCRQ LLSELSYIYP IDLNEHKDYF VCGVKLPNSE DFQAKDDGSI 370 380 390 400 410 420 AVALGYTAHL VSMISFFLQV PLRYPIIHKG SRSTIKDNIN DKLTEKEREF PLYPKGGEKL 430 440 450 460 470 480 QFDYGVYLLN KNIAQLRYQH GLGTPDLRQT LPNLKNFMEH GLMVRCDRHH TSSAIPVPKR 490 500 510 520 530 540 QSSIFGGADV GFSGGIPSPD KGHRKRASSE NERLQYKTPP PSYNSALAQP VTTVPSMGET 550 560 570 580 590 600 ERKITSLSSS LDTSLDFSKE NKKKGEDLVG SLNGGHANVH PSQEQGEALS GHRATVNGTL 610 620 630 640 650 660 LPSEQAGSAS VQLPGEFHPV SEAELCCTVE QAEEIIGLEA TGFASGDQLE AFNCIPVDSA 670 680 690 VAVECDEQVL GEFEEFSRRI YALNENVSSF RRPRRSSDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a novel human gene encoding a 63-kDa protein and its sublocalization within the 11q13 locus." 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. Genomics 41:397-405(1997) [PubMed: 9169138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of a gene disrupted by inv(11)(q13.5;q25) in a patient with left-right axis malformation." Iida A., Emi M., Matsuoka R., Hiratsuka E., Okui K., Ohashi H., Inazawa J., Fukushima Y., Imai T., Nakamura Y. Hum. Genet. 106:277-287(2000) [PubMed: 10798355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Heart.
[3]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND THR-518, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG." Itakura E., Kishi C., Inoue K., Mizushima N. Mol. Biol. Cell 19:5360-5372(2008) [PubMed: 18843052] [Abstract] Cited for: INTERACTION WITH BECN1 AND PIK3C3, SUBCELLULAR LOCATION.
[6]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase." Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q. Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008) [PubMed: 19050071] [Abstract] Cited for: INTERACTION WITH BECN1.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-493; SER-498; SER-508; TYR-516; THR-518; SER-522; THR-545; SER-549; SER-550; SER-571 AND SER-689, MASS SPECTROMETRY.
[10]	"Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages." 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. Nat. Cell Biol. 11:385-396(2009) [PubMed: 19270696] [Abstract] Cited for: INTERACTION WITH BECN1; KIAA0226; PIK3C3 AND PIK3R4.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X99050 Genomic DNA. Translation: CAA67507.1. Sequence problems. AB012958 mRNA. Translation: BAA90829.1.
IPI	IPI00002614.
RefSeq	NP_003360.2. NM_003369.3.
UniGene	Hs.728868.
3D structure databases
ProteinModelPortal	Q9P2Y5.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48652N.
IntAct	Q9P2Y5. 40 interactions.
STRING	Q9P2Y5.
PTM databases
PhosphoSite	Q9P2Y5.
Polymorphism databases
DMDM	20140879.
Proteomic databases
PRIDE	Q9P2Y5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356136; ENSP00000348455; ENSG00000198382.
GeneID	7405.
KEGG	hsa:7405.
UCSC	uc001oxc.1. human.
Organism-specific databases
CTD	7405.
GeneCards	GC11P075526.
H-InvDB	HIX0009956.
HGNC	HGNC:12640. UVRAG.
HPA	HPA016932.
MIM	602493. gene.
neXtProt	NX_Q9P2Y5.
PharmGKB	PA37264.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05683.
GeneTree	ENSGT00390000012877.
HOGENOM	HBG443588.
HOVERGEN	HBG059846.
InParanoid	Q9P2Y5.
OMA	CCTVEQA.
OrthoDB	EOG4KD6KJ.
PhylomeDB	Q9P2Y5.
Gene expression databases
ArrayExpress	Q9P2Y5.
Bgee	Q9P2Y5.
CleanEx	HS_UVRAG.
Genevestigator	Q9P2Y5.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018791. UV_resistance/autophagy_Atg14. [Graphical view]
Pfam	PF10186. Atg14. 1 hit. PF00168. C2. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit.
PROSITE	PS50004. C2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	28992.
SOURCE	Search...

Entry information

Entry name

UVRAG_HUMAN

Accession

Primary (citable) accession number: Q9P2Y5
Secondary accession number(s): O00392

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.