CPLM-001645

Genbank Nucleotide ID

Synaptosomal-associated protein 29

Protein Synonyms/Alias

SNAP-29; Soluble 29 kDa NSF attachment protein; Vesicle-membrane fusion protein SNAP-29

Homo sapiens (Human)

Position	Peptide	Type	References
6	**MSAYPKSYNPFDD	ubiquitination	[1]
103	DKMDQDLKISQKHIN	acetylation	[2]
107	QDLKISQKHINSIKS	ubiquitination	[1]
113	QKHINSIKSVFGGLV	ubiquitination	[3]
124	GGLVNYFKSKPVETP	acetylation	[4]
124	GGLVNYFKSKPVETP	ubiquitination	[1]
126	LVNYFKSKPVETPPE	ubiquitination	[1, 5, 6]
154	KEAISTSKEQEAKYQ	ubiquitination	[1]

[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] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[3] 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]
[4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[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] 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]

Functional Description

SNAREs, Soluble N-ethylmaleimide-sensitive factor- attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Probably involved in multiple membrane trafficking steps.

DOMAIN 196 258 t-SNARE coiled-coil homology.
MOD_RES 210 210 Phosphoserine (By similarity).

Autophagy; Cell junction; Coiled coil; Complete proteome; Cytoplasm; Ichthyosis; Membrane; Palmoplantar keratoderma; Phosphoprotein; Protein transport; Reference proteome; Synapse; Synaptosome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:HPA.
GO:0005886; C:plasma membrane; TAS:ProtInc.
GO:0031201; C:SNARE complex; IDA:UniProtKB.
GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO:0005484; F:SNAP receptor activity; TAS:ProtInc.
GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
GO:0006887; P:exocytosis; TAS:ProtInc.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0006903; P:vesicle targeting; TAS:ProtInc.

IPR000928; SNAP-25.
IPR000727; T_SNARE_dom.

PF00835; SNAP-25
PF05739; SNARE