YKT6_HUMAN - dbPTM
YKT6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YKT6_HUMAN
UniProt AC O15498
Protein Name Synaptobrevin homolog YKT6
Gene Name YKT6
Organism Homo sapiens (Human).
Sequence Length 198
Subcellular Localization Cytoplasm, cytosol. Cytoplasmic vesicle membrane
Lipid-anchor
Cytoplasmic side. Golgi apparatus membrane
Lipid-anchor
Cytoplasmic side. Probably cycles through vesicles between Golgi and endosomes.
Protein Description Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity..
Protein Sequence MKLYSLSVLYKGEAKVVLLKAAYDVSSFSFFQRSSVQEFMTFTSQLIVERSSKGTRASVKEQDYLCHVYVRNDSLAGVVIADNEYPSRVAFTLLEKVLDEFSKQVDRIDWPVGSPATIHYPALDGHLSRYQNPREADPMTKVQAELDETKIILHNTMESLLERGEKLDDLVSKSEVLGTQSKAFYKTARKQNSCCAIM
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 Orthologous
Protein Cluster
4Phosphorylation----MKLYSLSVLYK
----CCEEEEEEEEC		11.3121406692
5Phosphorylation---MKLYSLSVLYKG
---CCEEEEEEEECC		25.3021406692
15AcetylationVLYKGEAKVVLLKAA
EEECCCEEEEEEEEE		28.68-
15AcetylationVLYKGEAKVVLLKAA
EEECCCEEEEEEEEE		28.6823236377
51PhosphorylationSQLIVERSSKGTRAS
HHHHHHHCCCCCCCC		23.93-
58PhosphorylationSSKGTRASVKEQDYL
CCCCCCCCHHHCCEE		30.3624719451
64PhosphorylationASVKEQDYLCHVYVR
CCHHHCCEEEEEEEC		15.7824719451
71DimethylationYLCHVYVRNDSLAGV
EEEEEEECCCCEEEE		24.45-
71MethylationYLCHVYVRNDSLAGV
EEEEEEECCCCEEEE		24.45115390027
88DimethylationADNEYPSRVAFTLLE
ECCCCCHHHHHHHHH		21.19-
88MethylationADNEYPSRVAFTLLE
ECCCCCHHHHHHHHH		21.19115390033
96UbiquitinationVAFTLLEKVLDEFSK
HHHHHHHHHHHHHHH		48.33-
103UbiquitinationKVLDEFSKQVDRIDW
HHHHHHHHCCCCCCC		60.7121890473
103AcetylationKVLDEFSKQVDRIDW
HHHHHHHHCCCCCCC		60.71-
103UbiquitinationKVLDEFSKQVDRIDW
HHHHHHHHCCCCCCC		60.7121890473
103AcetylationKVLDEFSKQVDRIDW
HHHHHHHHCCCCCCC		60.7123236377
103MethylationKVLDEFSKQVDRIDW
HHHHHHHHCCCCCCC		60.7142377385
107MethylationEFSKQVDRIDWPVGS
HHHHCCCCCCCCCCC		29.88115920221
114PhosphorylationRIDWPVGSPATIHYP
CCCCCCCCCCEEECC		16.1725159151
117PhosphorylationWPVGSPATIHYPALD
CCCCCCCEEECCCCC		16.2122199227
120PhosphorylationGSPATIHYPALDGHL
CCCCEEECCCCCCCH		6.0727080861
128PhosphorylationPALDGHLSRYQNPRE
CCCCCCHHCCCCHHH		24.2227080861
141UbiquitinationREADPMTKVQAELDE
HHCCCCCHHHHHHCC		26.54-
141UbiquitinationREADPMTKVQAELDE
HHCCCCCHHHHHHCC		26.5421890473
150UbiquitinationQAELDETKIILHNTM
HHHHCCCEEHHHHHH		26.2121890473
156PhosphorylationTKIILHNTMESLLER
CEEHHHHHHHHHHHH		16.1523186163
159PhosphorylationILHNTMESLLERGEK
HHHHHHHHHHHHCCC		27.6827050516
166AcetylationSLLERGEKLDDLVSK
HHHHHCCCHHHHHHH		61.1023236377
166UbiquitinationSLLERGEKLDDLVSK
HHHHHCCCHHHHHHH		61.10-
172PhosphorylationEKLDDLVSKSEVLGT
CCHHHHHHHHHHHCH		37.4525850435
173UbiquitinationKLDDLVSKSEVLGTQ
CHHHHHHHHHHHCHH		43.0621890473
174PhosphorylationLDDLVSKSEVLGTQS
HHHHHHHHHHHCHHH		25.9823401153
179PhosphorylationSKSEVLGTQSKAFYK
HHHHHHCHHHHHHHH		26.0526699800
181PhosphorylationSEVLGTQSKAFYKTA
HHHHCHHHHHHHHHH		26.2826699800
182UbiquitinationEVLGTQSKAFYKTAR
HHHCHHHHHHHHHHH		32.4721890473
182AcetylationEVLGTQSKAFYKTAR
HHHCHHHHHHHHHHH		32.4727452117
186UbiquitinationTQSKAFYKTARKQNS
HHHHHHHHHHHHHCC		29.29-
186AcetylationTQSKAFYKTARKQNS
HHHHHHHHHHHHHCC		29.2927452117
194S-palmitoylationTARKQNSCCAIM---
HHHHHCCCEECC---		2.0815479160
195MethylationARKQNSCCAIM----
HHHHCCCEECC----		2.63-
195FarnesylationARKQNSCCAIM----
HHHHCCCEECC----		2.6315044687
195S-palmitoylationARKQNSCCAIM----
HHHHCCCEECC----		2.6315479160
195FarnesylationARKQNSCCAIM----
HHHHCCCEECC----		2.6315044687
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of YKT6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YKT6_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of YKT6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNN3_HUMANCNN3physical
26344197
CRIP1_HUMANCRIP1physical
26344197
QOR_HUMANCRYZphysical
26344197
ACBP_HUMANDBIphysical
26344197
ETFA_HUMANETFAphysical
26344197
FKB1A_HUMANFKBP1Aphysical
26344197
AATC_HUMANGOT1physical
26344197
MDHM_HUMANMDH2physical
26344197
MEMO1_HUMANMEMO1physical
26344197
MIF_HUMANMIFphysical
26344197
PEBP1_HUMANPEBP1physical
26344197
RIFK_HUMANRFKphysical
26344197
TAGL_HUMANTAGLNphysical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TAGL3_HUMANTAGLN3physical
26344197
TKT_HUMANTKTphysical
26344197
UB2V1_HUMANUBE2V1physical
26344197
UFC1_HUMANUFC1physical
26344197
PTAR1_HUMANPTAR1physical
28514442
AASD1_HUMANAARSD1physical
28514442
C1QRF_HUMANC1QL1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YKT6_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Localization and activity of the SNARE Ykt6 determined by itsregulatory domain and palmitoylation.";
Fukasawa M., Varlamov O., Eng W.S., Soellner T.H., Rothman J.E.;
Proc. Natl. Acad. Sci. U.S.A. 101:4815-4820(2004).
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195,ISOPRENYLATION AT CYS-195, AND PALMITOYLATION.
"The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues.";
Veit M.;
Biochem. J. 384:233-237(2004).
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195, ANDPALMITOYLATION AT CYS-194.
Prenylation
ReferencePubMed
"Localization and activity of the SNARE Ykt6 determined by itsregulatory domain and palmitoylation.";
Fukasawa M., Varlamov O., Eng W.S., Soellner T.H., Rothman J.E.;
Proc. Natl. Acad. Sci. U.S.A. 101:4815-4820(2004).
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-42; CYS-194 AND CYS-195,ISOPRENYLATION AT CYS-195, AND PALMITOYLATION.

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