CPLM-019428

Genbank Nucleotide ID

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
48	PRVVRIVKSESGYGF	ubiquitination	[1]
126	DLIRAGEKELILTVL	ubiquitination	[2]
222	TFPRLPGKWPFSLSE	ubiquitination	[1, 3, 4, 5, 6]
245	GLEEYLEKVCSIRVI	ubiquitination	[1]
404	EKSYQLQKLYEQRKM	ubiquitination	[1, 3, 5]
522	ERVFCELKWRKENIF	ubiquitination	[1, 4]

[1] 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]
[2] 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]
[3] 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]
[4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[5] 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]
[6] 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

Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ- binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes.

DOMAIN 43 136 PDZ.
DOMAIN 161 269 PX.
DOMAIN 273 362 Ras-associating.
REGION 273 362 FERM-like region F1.
REGION 373 421 FERM-like region F2.
REGION 425 525 FERM-like region F3.
MOD_RES 51 51 Phosphoserine (By similarity).
MOD_RES 62 62 Phosphoserine.

3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Endosome; Lipid-binding; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:HPA.
GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO:0008333; P:endosome to lysosome transport; IEA:Compara.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0007165; P:signal transduction; IEA:InterPro.

IPR001478; PDZ.
IPR001683; Phox.
IPR000159; Ras-assoc.

PF00595; PDZ
PF00787; PX
PF00788; RA

SM00228; PDZ
SM00312; PX

PS50106; PDZ
PS50195; PX
PS50200; RA