STX4_HUMAN - dbPTM
STX4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STX4_HUMAN
UniProt AC Q12846
Protein Name Syntaxin-4
Gene Name STX4
Organism Homo sapiens (Human).
Sequence Length 297
Subcellular Localization Cell membrane
Single-pass type IV membrane protein .
Protein Description Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes (By similarity). May also play a role in docking of synaptic vesicles at presynaptic active zones..
Protein Sequence MRDRTHELRQGDDSSDEEDKERVALVVHPGTARLGSPDEEFFHKVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMRKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQVTRQALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKVLIAICVSITVVLLAVIIGVTVVG
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
5Phosphorylation---MRDRTHELRQGD
---CCCCCCCCCCCC		24.8020363803
14PhosphorylationELRQGDDSSDEEDKE
CCCCCCCCCCHHHHH		44.4129255136
15PhosphorylationLRQGDDSSDEEDKER
CCCCCCCCCHHHHHC		56.9129255136
31PhosphorylationALVVHPGTARLGSPD
EEEECCCCCCCCCCC		17.0428857561
36PhosphorylationPGTARLGSPDEEFFH
CCCCCCCCCCHHHHH		33.5030266825
44UbiquitinationPDEEFFHKVRTIRQT
CCHHHHHHHHHHHHH		28.40-
51PhosphorylationKVRTIRQTIVKLGNK
HHHHHHHHHHHHCHH		20.21-
54UbiquitinationTIRQTIVKLGNKVQE
HHHHHHHHHCHHHHH		46.99-
56UbiquitinationRQTIVKLGNKVQELE
HHHHHHHCHHHHHHH		26.62-
58UbiquitinationTIVKLGNKVQELEKQ
HHHHHCHHHHHHHHH		43.42-
64UbiquitinationNKVQELEKQQVTILA
HHHHHHHHHCCEEEE		59.67-
68PhosphorylationELEKQQVTILATPLP
HHHHHCCEEEECCCC		13.1124043423
72PhosphorylationQQVTILATPLPEESM
HCCEEEECCCCHHHH		23.1624043423
78PhosphorylationATPLPEESMKQELQN
ECCCCHHHHHHHHHH		29.6224043423
80UbiquitinationPLPEESMKQELQNLR
CCCHHHHHHHHHHHH		50.31-
89UbiquitinationELQNLRDEIKQLGRE
HHHHHHHHHHHHHHH		45.7321890473
91UbiquitinationQNLRDEIKQLGREIR
HHHHHHHHHHHHHHH		37.1121890473
100UbiquitinationLGREIRLQLKAIEPQ
HHHHHHHHHHHHCCC		30.94-
102UbiquitinationREIRLQLKAIEPQKE
HHHHHHHHHHCCCHH		34.06-
106UbiquitinationLQLKAIEPQKEEADE
HHHHHHCCCHHHCCC		44.4221890473
108UbiquitinationLKAIEPQKEEADENY
HHHHCCCHHHCCCCC		69.1421906983
115PhosphorylationKEEADENYNSVNTRM
HHHCCCCCHHHHHHH		13.5325159151
117PhosphorylationEADENYNSVNTRMRK
HCCCCCHHHHHHHHH		13.3429255136
120PhosphorylationENYNSVNTRMRKTQH
CCCHHHHHHHHHHHC		24.5630266825
124UbiquitinationSVNTRMRKTQHGVLS
HHHHHHHHHHCCHHH		43.10-
125PhosphorylationVNTRMRKTQHGVLSQ
HHHHHHHHHCCHHHH		18.5529978859
131PhosphorylationKTQHGVLSQQFVELI
HHHCCHHHHHHHHHH		21.3825690035
140UbiquitinationQFVELINKCNSMQSE
HHHHHHHHHHHHCHH		28.00-
143PhosphorylationELINKCNSMQSEYRE
HHHHHHHHHCHHHHH		27.8929978859
146PhosphorylationNKCNSMQSEYREKNV
HHHHHHCHHHHHHHH		28.1429978859
148PhosphorylationCNSMQSEYREKNVER
HHHHCHHHHHHHHHH		29.3529978859
169PhosphorylationITNAGMVSDEELEQM
HCCCCCCCHHHHHHH		30.3428348404
179PhosphorylationELEQMLDSGQSEVFV
HHHHHHHCCCCHHHH		34.4728348404
204PhosphorylationRQALNEISARHSEIQ
HHHHHHHHHHHHHHH		17.0521406692
208PhosphorylationNEISARHSEIQQLER
HHHHHHHHHHHHHHH		30.7327794612
241UbiquitinationQGEMINRIEKNILSS
HHHHHHHHHHHHHCC		8.3721890473
243UbiquitinationEMINRIEKNILSSAD
HHHHHHHHHHHCCHH		47.0921890473
247PhosphorylationRIEKNILSSADYVER
HHHHHHHCCHHHHHH		21.4928152594
248PhosphorylationIEKNILSSADYVERG
HHHHHHCCHHHHHHH		23.0128152594
251PhosphorylationNILSSADYVERGQEH
HHHCCHHHHHHHHHH		12.1518707149
260UbiquitinationERGQEHVKTALENQK
HHHHHHHHHHHHHHH		29.95-
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 STX4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STX4_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 STX4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAMP4_HUMANVAMP4physical
16189514
VAMP3_HUMANVAMP3physical
16189514
SNAA_HUMANNAPAphysical
16189514
TXLNB_HUMANTXLNBphysical
15184072
STXB5_HUMANSTXBP5physical
12832401
STXB3_HUMANSTXBP3physical
12832401
SNP23_HUMANSNAP23physical
12828989
VAMP3_HUMANVAMP3physical
12828989
STXB3_HUMANSTXBP3physical
12773094
SNP23_HUMANSNAP23physical
12651853
VAPB_HUMANVAPBphysical
12651853
SNP23_HUMANSNAP23physical
9168999
SNP23_MOUSESnap23physical
9168999
SNP25_RATSnap25physical
9168999
SNP23_HUMANSNAP23physical
10820264
VAMP2_HUMANVAMP2physical
10820264
VAMP3_HUMANVAMP3physical
10820264
VAMP8_HUMANVAMP8physical
10820264
RAB5A_HUMANRAB5Aphysical
11884531
RAB4A_HUMANRAB4Aphysical
11063739
SYT1_HUMANSYT1physical
10397765
SNP23_HUMANSNAP23physical
8663154
SNP25_HUMANSNAP25physical
8663154
SNP23_HUMANSNAP23physical
10713150
TXLNA_HUMANTXLNAphysical
12558796
SNP25_HUMANSNAP25physical
10194441
VAMP2_HUMANVAMP2physical
10194441
SNP23_HUMANSNAP23physical
9852078
SNP25_HUMANSNAP25physical
9852078
SNP29_HUMANSNAP29physical
9852078
VAMP3_HUMANVAMP3physical
12130530
VAMP8_HUMANVAMP8physical
12130530
STX4_HUMANSTX4physical
25416956
STX5_HUMANSTX5physical
25416956
VAMP1_HUMANVAMP1physical
25416956
VAMP2_HUMANVAMP2physical
25416956
STX7_HUMANSTX7physical
25416956
VAMP4_HUMANVAMP4physical
25416956
STX16_HUMANSTX16physical
25416956
VAMP3_HUMANVAMP3physical
25416956
STX8_HUMANSTX8physical
25416956
GOSR2_HUMANGOSR2physical
25416956
STX6_HUMANSTX6physical
25416956
BET1_HUMANBET1physical
25416956
VTI1B_HUMANVTI1Bphysical
25416956
VAMP5_HUMANVAMP5physical
25416956
STX12_HUMANSTX12physical
25416956
SC22A_HUMANSEC22Aphysical
25416956
GIMA5_HUMANGIMAP5physical
25416956
SNAB_HUMANNAPBphysical
25416956
CYBR1_HUMANCYBRD1physical
25416956
SNP47_HUMANSNAP47physical
25416956
CYBR1_HUMANCYBRD1physical
21516116
STX7_HUMANSTX7physical
21516116
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.
Regulatory Network of STX4_HUMAN

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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-14; SER-15 AND SER-117,AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-251, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-115 AND TYR-251, ANDMASS SPECTROMETRY.

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