STX12_HUMAN - dbPTM
STX12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STX12_HUMAN
UniProt AC Q86Y82
Protein Name Syntaxin-12
Gene Name STX12
Organism Homo sapiens (Human).
Sequence Length 276
Subcellular Localization Endosome membrane
Single-pass type IV membrane protein . Golgi apparatus membrane
Single-pass type IV membrane protein . Endomembrane system
Single-pass type IV membrane protein
Cytoplasmic side . Early endosome membrane
Single-pass type IV membra
Protein Description SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network. The SNARE complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By similarity). Through complex formation with GRIP1, GRIA2 and NSG1 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity)..
Protein Sequence MSYGPLDMYRNPGPSGPQLRDFSSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQLQHSTNQLAKETNELLKELGSLPLPLSTSEQRQQRLQKERLMNDFSAALNNFQAVQRRVSEKEKESIARARAGSRLSAEERQREEQLVSFDSHEEWNQMQSQEDEVAITEQDLELIKERETAIRQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERATEQLQRAAYYQKKSRKKMCILVLVLSVIILILGLIIWLVYKTK
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
2Phosphorylation------MSYGPLDMY
------CCCCCCCCC
38.5030108239
2Acetylation------MSYGPLDMY
------CCCCCCCCC
38.5022223895
3Phosphorylation-----MSYGPLDMYR
-----CCCCCCCCCC
22.8225106551
9PhosphorylationSYGPLDMYRNPGPSG
CCCCCCCCCCCCCCC
13.6027259358
15PhosphorylationMYRNPGPSGPQLRDF
CCCCCCCCCHHHHCH
69.8527251275
44UbiquitinationSQATAQIKNLMSQLG
HHHHHHHHHHHHHHC
31.7621906983
44UbiquitinationSQATAQIKNLMSQLG
HHHHHHHHHHHHHHC
31.7621890473
53UbiquitinationLMSQLGTKQDSSKLQ
HHHHHCCCCCHHHHH
50.7621906983
58UbiquitinationGTKQDSSKLQENLQQ
CCCCCHHHHHHHHHH
59.1321890473
58UbiquitinationGTKQDSSKLQENLQQ
CCCCCHHHHHHHHHH
59.1322053931
75UbiquitinationHSTNQLAKETNELLK
HHHHHHHHHHHHHHH
73.9125015289
82UbiquitinationKETNELLKELGSLPL
HHHHHHHHHHCCCCC
64.6121906983
92PhosphorylationGSLPLPLSTSEQRQQ
CCCCCCCCCHHHHHH
28.1325850435
93PhosphorylationSLPLPLSTSEQRQQR
CCCCCCCCHHHHHHH
43.9225850435
94PhosphorylationLPLPLSTSEQRQQRL
CCCCCCCHHHHHHHH
28.4925850435
127UbiquitinationVQRRVSEKEKESIAR
HHHHCCHHHHHHHHH
67.5824816145
129UbiquitinationRRVSEKEKESIARAR
HHCCHHHHHHHHHHH
68.76-
139PhosphorylationIARARAGSRLSAEER
HHHHHHHCCCCHHHH
29.1229255136
142PhosphorylationARAGSRLSAEERQRE
HHHHCCCCHHHHHHH
32.3129255136
218PhosphorylationDQGDLIDSIEANVES
CCCCHHHHHHHHCCC
18.4826657352
225PhosphorylationSIEANVESSEVHVER
HHHHHCCCCCHHHHH
27.7626471730
226PhosphorylationIEANVESSEVHVERA
HHHHCCCCCHHHHHH
30.0827251275
234PhosphorylationEVHVERATEQLQRAA
CHHHHHHHHHHHHHH
30.4121949786
242PhosphorylationEQLQRAAYYQKKSRK
HHHHHHHHHHHHCHH
12.8721949786
245UbiquitinationQRAAYYQKKSRKKMC
HHHHHHHHHCHHHHH
36.2733845483
2452-HydroxyisobutyrylationQRAAYYQKKSRKKMC
HHHHHHHHHCHHHHH
36.27-
246UbiquitinationRAAYYQKKSRKKMCI
HHHHHHHHCHHHHHH
39.7123503661
247PhosphorylationAAYYQKKSRKKMCIL
HHHHHHHCHHHHHHH
57.2629083192
249UbiquitinationYYQKKSRKKMCILVL
HHHHHCHHHHHHHHH
52.5323503661
250UbiquitinationYQKKSRKKMCILVLV
HHHHCHHHHHHHHHH
37.5823503661

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 STX12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STX12_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 STX12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNP29_HUMANSNAP29physical
9852078
ABCA1_HUMANABCA1physical
15469992
DTX2_HUMANDTX2physical
25416956
EI2BE_HUMANEIF2B5physical
26186194
RNF13_HUMANRNF13physical
26186194
F234B_HUMANKIAA1467physical
26186194
YKT6_HUMANYKT6physical
26186194
EI2BA_HUMANEIF2B1physical
26186194
SEC20_HUMANBNIP1physical
26186194
EI2BD_HUMANEIF2B4physical
26186194
GOGA2_HUMANGOLGA2physical
26186194
BZW2_HUMANBZW2physical
26186194
ZKSC1_HUMANZKSCAN1physical
26186194
VPS45_HUMANVPS45physical
26186194
SNAB_HUMANNAPBphysical
26186194
SNAA_HUMANNAPAphysical
26186194
STX4_HUMANSTX4physical
26186194
USE1_HUMANUSE1physical
26186194
STX18_HUMANSTX18physical
26186194
SCFD2_HUMANSCFD2physical
26186194
NOP14_HUMANNOP14physical
26186194
GORS1_HUMANGORASP1physical
26186194
SNAG_HUMANNAPGphysical
26186194
STX5_HUMANSTX5physical
26186194
STXB5_HUMANSTXBP5physical
26186194
NBAS_HUMANNBASphysical
26186194
STX10_HUMANSTX10physical
26186194
F234A_HUMANITFG3physical
26186194
TXLNA_HUMANTXLNAphysical
26186194
SNP23_HUMANSNAP23physical
26186194
TBC15_HUMANTBC1D15physical
26186194
SNP47_HUMANSNAP47physical
26186194
MSPD2_HUMANMOSPD2physical
26186194
TBK1_HUMANTBK1physical
26186194
NOC4L_HUMANNOC4Lphysical
26186194
VTI1A_HUMANVTI1Aphysical
26186194
OPTN_HUMANOPTNphysical
26186194
ADPGK_HUMANADPGKphysical
26186194
EI2BG_HUMANEIF2B3physical
26186194
TBC17_HUMANTBC1D17physical
26186194
VAMP4_HUMANVAMP4physical
26186194
SNP29_HUMANSNAP29physical
26186194
STX8_HUMANSTX8physical
26186194
GOSR2_HUMANGOSR2physical
26186194
VAMP2_HUMANVAMP2physical
26186194
VAMP3_HUMANVAMP3physical
26186194
EI2BB_HUMANEIF2B2physical
26186194
GOSR1_HUMANGOSR1physical
26186194
VAMP8_HUMANVAMP8physical
26186194
ANM9_HUMANPRMT9physical
26186194
FRMD5_HUMANFRMD5physical
26186194
VAMP7_HUMANVAMP7physical
26186194
ZN219_HUMANZNF219physical
26186194
PPAL_HUMANACP2physical
26186194
CC138_HUMANCCDC138physical
26186194
BET1_HUMANBET1physical
26344197
EHD1_HUMANEHD1physical
26344197
OPTN_HUMANOPTNphysical
28514442
STXB5_HUMANSTXBP5physical
28514442
SNAG_HUMANNAPGphysical
28514442
VTI1A_HUMANVTI1Aphysical
28514442
GOSR1_HUMANGOSR1physical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
SNAB_HUMANNAPBphysical
28514442
VAMP8_HUMANVAMP8physical
28514442
GOGA2_HUMANGOLGA2physical
28514442
TBC17_HUMANTBC1D17physical
28514442
TBK1_HUMANTBK1physical
28514442
STX10_HUMANSTX10physical
28514442
GOSR2_HUMANGOSR2physical
28514442
ZN219_HUMANZNF219physical
28514442
USE1_HUMANUSE1physical
28514442
SNP47_HUMANSNAP47physical
28514442
STX8_HUMANSTX8physical
28514442
SNAA_HUMANNAPAphysical
28514442
YKT6_HUMANYKT6physical
28514442
MSPD2_HUMANMOSPD2physical
28514442
VAMP3_HUMANVAMP3physical
28514442
NOP14_HUMANNOP14physical
28514442
NBAS_HUMANNBASphysical
28514442
EI2BG_HUMANEIF2B3physical
28514442
NOC4L_HUMANNOC4Lphysical
28514442
FRMD5_HUMANFRMD5physical
28514442
SCFD2_HUMANSCFD2physical
28514442
CC138_HUMANCCDC138physical
28514442
TBC15_HUMANTBC1D15physical
28514442
VAMP7_HUMANVAMP7physical
28514442
RNF13_HUMANRNF13physical
28514442
VAMP2_HUMANVAMP2physical
28514442
STX5_HUMANSTX5physical
28514442
EI2BE_HUMANEIF2B5physical
28514442
CTR1_HUMANSLC7A1physical
28514442
STX4_HUMANSTX4physical
28514442
STX18_HUMANSTX18physical
28514442
SNP29_HUMANSNAP29physical
28514442
SNP23_HUMANSNAP23physical
28514442
EI2BD_HUMANEIF2B4physical
28514442
SEC20_HUMANBNIP1physical
28514442
EI2BB_HUMANEIF2B2physical
28514442
EI2BA_HUMANEIF2B1physical
28514442
ADPGK_HUMANADPGKphysical
28514442
PPAL_HUMANACP2physical
28514442
F234A_HUMANITFG3physical
28514442
F234B_HUMANKIAA1467physical
28514442
TXLNA_HUMANTXLNAphysical
28514442
BZW2_HUMANBZW2physical
28514442
COG6_HUMANCOG6physical
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 STX12_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-142, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASSSPECTROMETRY.

TOP