VPS29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VPS29_HUMAN
• UniProt AC: Q9UBQ0
• Protein Name: Vacuolar protein sorting-associated protein 29
• Gene Name: VPS29
• Organism: Homo sapiens (Human).
• Sequence Length: 182
• Subcellular Localization: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane ; Peripheral membrane protein . Early endosome . Late endosome .
• Protein Description: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA) (Probable). Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with ANKRD27. [PubMed: 24856514]
• Protein Sequence: MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYKKP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	HIPHRCNSLPAKFKK CCCCCCCCCCHHHHH	39.08	27251275
21	Acetylation	RCNSLPAKFKKLLVP CCCCCCHHHHHHCCC	56.64	25953088
21	Ubiquitination	RCNSLPAKFKKLLVP CCCCCCHHHHHHCCC	56.64	-
24	Malonylation	SLPAKFKKLLVPGKI CCCHHHHHHCCCCCC	50.62	26320211
24	2-Hydroxyisobutyrylation	SLPAKFKKLLVPGKI CCCHHHHHHCCCCCC	50.62	-
24	Ubiquitination	SLPAKFKKLLVPGKI CCCHHHHHHCCCCCC	50.62	-
30	Ubiquitination	KKLLVPGKIQHILCT HHHCCCCCCCEEEEC	32.87	-
30	Acetylation	KKLLVPGKIQHILCT HHHCCCCCCCEEEEC	32.87	25953088
37	Phosphorylation	KIQHILCTGNLCTKE CCCEEEECCCCCCHH	26.17	25693802
42	Phosphorylation	LCTGNLCTKESYDYL EECCCCCCHHHHHHH	40.80	25693802
43	Acetylation	CTGNLCTKESYDYLK ECCCCCCHHHHHHHH	43.60	26051181
43	Ubiquitination	CTGNLCTKESYDYLK ECCCCCCHHHHHHHH	43.60	-
45	Phosphorylation	GNLCTKESYDYLKTL CCCCCHHHHHHHHHH	25.51	25693802
46	Phosphorylation	NLCTKESYDYLKTLA CCCCHHHHHHHHHHC	15.08	28102081
48	Phosphorylation	CTKESYDYLKTLAGD CCHHHHHHHHHHCCC	11.23	28102081
50 (in isoform 1)	Ubiquitination	-	34.95	21906983
50	Acetylation	KESYDYLKTLAGDVH HHHHHHHHHHCCCEE	34.95	19608861
50	Ubiquitination	KESYDYLKTLAGDVH HHHHHHHHHHCCCEE	34.95	21906983
50	2-Hydroxyisobutyrylation	KESYDYLKTLAGDVH HHHHHHHHHHCCCEE	34.95	-
54 (in isoform 2)	Ubiquitination	-	40.35	21906983
54	Ubiquitination	DYLKTLAGDVHIVRG HHHHHHCCCEEEEEC	40.35	19608861
54	Acetylation	DYLKTLAGDVHIVRG HHHHHHCCCEEEEEC	40.35	19608861
69	Phosphorylation	DFDENLNYPEQKVVT CCCCCCCCCCCEEEE	16.00	28152594
73	Acetylation	NLNYPEQKVVTVGQF CCCCCCCEEEEEEEE	36.69	23954790
73	Ubiquitination	NLNYPEQKVVTVGQF CCCCCCCEEEEEEEE	36.69	2190698
73	Sumoylation	NLNYPEQKVVTVGQF CCCCCCCEEEEEEEE	36.69	-
73 (in isoform 1)	Ubiquitination	-	36.69	21906983
77 (in isoform 2)	Ubiquitination	-	3.71	21906983
96	Sulfoxidation	QVIPWGDMASLALLQ EEEECHHHHHHHHHH	2.11	30846556
173	Ubiquitination	QLIGDDVKVERIEYK HHHCCCCEEEEEEEC	45.43	-
173	Sumoylation	QLIGDDVKVERIEYK HHHCCCCEEEEEEEC	45.43	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of VPS29_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VPS29_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of VPS29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBCD5_HUMAN	TBC1D5	physical	20923837
TBCD5_HUMAN	TBC1D5	physical	19531583
TBCD5_HUMAN	TBC1D5	physical	22354992
A4_HUMAN	APP	physical	21832049
VPS35_HUMAN	VPS35	physical	22939629
YRDC_HUMAN	YRDC	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
VPS36_HUMAN	VPS36	physical	22939629
ZNHI2_HUMAN	ZNHIT2	physical	22939629
UBP7_HUMAN	USP7	physical	23452853
NIBL1_HUMAN	FAM129B	physical	22863883
T2FA_HUMAN	GTF2F1	physical	22863883
H33_HUMAN	H3F3A	physical	22863883
JMJD6_HUMAN	JMJD6	physical	22863883
NAA10_HUMAN	NAA10	physical	22863883
NUDC_HUMAN	NUDC	physical	22863883
PPM1G_HUMAN	PPM1G	physical	22863883
SAP_HUMAN	PSAP	physical	22863883
PUF60_HUMAN	PUF60	physical	22863883
SC24D_HUMAN	SEC24D	physical	22863883
SNX2_HUMAN	SNX2	physical	22863883
SNX6_HUMAN	SNX6	physical	22863883
STAT1_HUMAN	STAT1	physical	22863883
TOLIP_HUMAN	TOLLIP	physical	22863883
VPS35_HUMAN	VPS35	physical	22863883
WDR12_HUMAN	WDR12	physical	22863883
VPS35_HUMAN	VPS35	physical	25416956
GRHPR_HUMAN	GRHPR	physical	26344197
HAT1_HUMAN	HAT1	physical	26344197
SHOT1_HUMAN	KIAA1598	physical	26344197
OTUB1_HUMAN	OTUB1	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
TBCD5_HUMAN	TBC1D5	physical	28514442
ANR27_HUMAN	ANKRD27	physical	28514442
CP062_HUMAN	C16orf62	physical	28514442
VPS35_HUMAN	VPS35	physical	28514442
DSCR3_HUMAN	DSCR3	physical	28514442
COMD9_HUMAN	COMMD9	physical	28514442
CCD93_HUMAN	CCDC93	physical	28514442
COMD5_HUMAN	COMMD5	physical	28514442
COMD7_HUMAN	COMMD7	physical	28514442
FA45A_HUMAN	FAM45A	physical	28514442
CCD22_HUMAN	CCDC22	physical	28514442
COMD3_HUMAN	COMMD3	physical	28514442
COMD8_HUMAN	COMMD8	physical	28514442
COMD4_HUMAN	COMMD4	physical	28514442
WAC2C_HUMAN	FAM21C	physical	24819384
WASC5_HUMAN	KIAA0196	physical	24819384
FKB15_HUMAN	FKBP15	physical	24819384
VP26A_HUMAN	VPS26A	physical	24819384
VPS35_MOUSE	Vps35	physical	24819384

Drug and Disease Associations

• Kegg Disease
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND MASS SPECTROMETRY.
PubMed: 19608861