UniProt Accession

 XRP2_HUMAN; O75695; Q86XJ7; Q9NU67 

Genbank Protein ID

 AJ007590; AL050307; AL627143; BC043348; BC053530 

Genbank Nucleotide ID

 CAA07577.1; CAB82030.2; CAB82030.2; AAH43348.1; AAH53530.1 

Protein Name

 Protein XRP2 

Protein Synonyms/Alias

  

Gene Name

 RP2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
25	ENEEERPKQYSWDQR	ubiquitination	[1]
38	QREKVDPKDYMFSGL	ubiquitination	[2, 3]
109	FRNCRDCKCTLACQQ	ubiquitination	[4]
252	YTIANARKLIDEMVG	ubiquitination	[4]
260	LIDEMVGKGFFLVQT	ubiquitination	[1, 2, 3, 4, 5, 6]
273	QTKEVSMKAEDAQRV	ubiquitination	[1, 4, 5, 7, 8]

Reference

 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. 

Sequence Annotation

 DOMAIN 24 179 C-CAP/cofactor C-like.
 NP_BIND 98 99 GTP.
 NP_BIND 115 118 GTP.
 LIPID 2 2 N-myristoyl glycine (Probable).
 LIPID 3 3 S-palmitoyl cysteine (Probable).  

Keyword

 3D-structure; Cell membrane; Cell projection; Cilium; Complete proteome; Disease mutation; GTP-binding; GTPase activation; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate; Polymorphism; Protein transport; Reference proteome; Retinitis pigmentosa; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 350 AA 

Protein Sequence

Gene Ontology

 GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
 GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0000902; P:cell morphogenesis; IEA:InterPro.
 GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
 GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
 GO:0006457; P:protein folding; TAS:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
 GO:0007601; P:visual perception; TAS:ProtInc. 

Interpro

 IPR017901; C-CAP_CF_C-like.
 IPR016098; CAP/MinC_C.
 IPR006599; CARP_motif.
 IPR001564; Nucleoside_diP_kinase.
 IPR017332; Protein_XRP2.
 IPR012945; Tubulin-bd_cofactor_C. 

Pfam

 PF07986; TBCC 

SMART

 SM00673; CARP 

PROSITE

 PS51329; C_CAP_COFACTOR_C 

PRINTS