STX7_HUMAN - dbPTM
STX7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STX7_HUMAN
UniProt AC O15400
Protein Name Syntaxin-7
Gene Name STX7
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Early endosome membrane
Single-pass type IV membrane protein.
Protein Description May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes..
Protein Sequence MSYTPGVGGDPAQLAQRISSNIQKITQCSVEIQRTLNQLGTPQDSPELRQQLQQKQQYTNQLAKETDKYIKEFGSLPTTPSEQRQRKIQKDRLVAEFTTSLTNFQKVQRQAAEREKEFVARVRASSRVSGSFPEDSSKERNLVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDVIDSIEANVENAEVHVQQANQQLSRAADYQRKSRKTLCIIILILVIGVAIISLIIWGLNH
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------MSYTPGVGG
------CCCCCCCCC
37.4027155012
2Acetylation------MSYTPGVGG
------CCCCCCCCC
37.4022223895
3Phosphorylation-----MSYTPGVGGD
-----CCCCCCCCCC
18.6925159151
4Phosphorylation----MSYTPGVGGDP
----CCCCCCCCCCH
13.2725159151
24UbiquitinationRISSNIQKITQCSVE
HHHHHHHHHHHCHHH
43.8823000965
24MalonylationRISSNIQKITQCSVE
HHHHHHHHHHHCHHH
43.8826320211
28S-nitrosocysteineNIQKITQCSVEIQRT
HHHHHHHCHHHHHHH
3.54-
28S-nitrosylationNIQKITQCSVEIQRT
HHHHHHHCHHHHHHH
3.5419483679
35PhosphorylationCSVEIQRTLNQLGTP
CHHHHHHHHHHCCCC
17.4323403867
41PhosphorylationRTLNQLGTPQDSPEL
HHHHHCCCCCCCHHH
26.7725159151
45PhosphorylationQLGTPQDSPELRQQL
HCCCCCCCHHHHHHH
18.2825159151
55UbiquitinationLRQQLQQKQQYTNQL
HHHHHHHHHHHHHHH
26.8032015554
66PhosphorylationTNQLAKETDKYIKEF
HHHHHHHHHHHHHHH
36.7630624053
68UbiquitinationQLAKETDKYIKEFGS
HHHHHHHHHHHHHCC
57.1923000965
69PhosphorylationLAKETDKYIKEFGSL
HHHHHHHHHHHHCCC
21.7523312004
71UbiquitinationKETDKYIKEFGSLPT
HHHHHHHHHHCCCCC
43.8523000965
71 (in isoform 1)Ubiquitination-43.8521890473
71 (in isoform 2)Ubiquitination-43.8521890473
75PhosphorylationKYIKEFGSLPTTPSE
HHHHHHCCCCCCHHH
36.1723401153
78PhosphorylationKEFGSLPTTPSEQRQ
HHHCCCCCCHHHHHH
57.5430266825
79PhosphorylationEFGSLPTTPSEQRQR
HHCCCCCCHHHHHHH
23.9119664994
81PhosphorylationGSLPTTPSEQRQRKI
CCCCCCHHHHHHHHH
44.2430266825
87AcetylationPSEQRQRKIQKDRLV
HHHHHHHHHHHHHHH
40.947977159
90AcetylationQRQRKIQKDRLVAEF
HHHHHHHHHHHHHHH
48.577977171
98PhosphorylationDRLVAEFTTSLTNFQ
HHHHHHHHHHCHHHH
13.6426270265
99PhosphorylationRLVAEFTTSLTNFQK
HHHHHHHHHCHHHHH
27.3626270265
100PhosphorylationLVAEFTTSLTNFQKV
HHHHHHHHCHHHHHH
30.0926270265
102PhosphorylationAEFTTSLTNFQKVQR
HHHHHHCHHHHHHHH
33.4826270265
106UbiquitinationTSLTNFQKVQRQAAE
HHCHHHHHHHHHHHH
35.8833845483
125PhosphorylationFVARVRASSRVSGSF
HHHHHHHHHCCCCCC
14.2330266825
126PhosphorylationVARVRASSRVSGSFP
HHHHHHHHCCCCCCC
35.4029255136
129PhosphorylationVRASSRVSGSFPEDS
HHHHHCCCCCCCCCC
27.8429255136
131PhosphorylationASSRVSGSFPEDSSK
HHHCCCCCCCCCCCC
30.0729255136
136PhosphorylationSGSFPEDSSKERNLV
CCCCCCCCCCCCCCC
41.4723927012
137PhosphorylationGSFPEDSSKERNLVS
CCCCCCCCCCCCCCC
51.3523927012
138UbiquitinationSFPEDSSKERNLVSW
CCCCCCCCCCCCCCH
65.7233845483
144PhosphorylationSKERNLVSWESQTQP
CCCCCCCCHHCCCCC
28.4327251789
147PhosphorylationRNLVSWESQTQPQVQ
CCCCCHHCCCCCCEE
32.0628857561
149PhosphorylationLVSWESQTQPQVQVQ
CCCHHCCCCCCEEEC
52.0422817900
161PhosphorylationQVQDEEITEDDLRLI
EECCCCCCHHHHHHH
36.32-
173PhosphorylationRLIHERESSIRQLEA
HHHHHHHHHHHHHHH
36.9728450419
174PhosphorylationLIHERESSIRQLEAD
HHHHHHHHHHHHHHH
19.6228450419
205PhosphorylationEQGDVIDSIEANVEN
CCCCHHHHHHHHHHH
15.9425850435
225PhosphorylationQQANQQLSRAADYQR
HHHHHHHHHHHHHHH
18.6127080861
239S-palmitoylationRKSRKTLCIIILILV
HHHHHHHHHHHHHHH
2.2518980942

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 STX7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STX7_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 STX7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAMP8_HUMANVAMP8physical
11101518
VTI1A_HUMANVTI1Aphysical
11101518
STX8_HUMANSTX8physical
11101518
VTI1B_HUMANVTI1Bphysical
12114520
VPS11_HUMANVPS11physical
11382755
VPS18_HUMANVPS18physical
11382755
SNP29_HUMANSNAP29physical
9852078
GTF2I_HUMANGTF2Iphysical
11278762
STX6_HUMANSTX6physical
11278762
VAMP8_HUMANVAMP8physical
11278762
T10B_HUMANTIMM10Bphysical
22939629
YKT6_HUMANYKT6physical
26186194
GOGA2_HUMANGOLGA2physical
26186194
ZN101_HUMANZNF101physical
26186194
ZKSC1_HUMANZKSCAN1physical
26186194
VPS45_HUMANVPS45physical
26186194
SNAA_HUMANNAPAphysical
26186194
STX4_HUMANSTX4physical
26186194
USE1_HUMANUSE1physical
26186194
STX18_HUMANSTX18physical
26186194
GOSR1_HUMANGOSR1physical
26186194
NOP14_HUMANNOP14physical
26186194
GORS1_HUMANGORASP1physical
26186194
SNAG_HUMANNAPGphysical
26186194
STX5_HUMANSTX5physical
26186194
STXB5_HUMANSTXBP5physical
26186194
STX10_HUMANSTX10physical
26186194
SNP23_HUMANSNAP23physical
26186194
SNP47_HUMANSNAP47physical
26186194
PTTG_HUMANPTTG1IPphysical
26186194
STX12_HUMANSTX12physical
26186194
VTI1A_HUMANVTI1Aphysical
26186194
ADPGK_HUMANADPGKphysical
26186194
TYW5_HUMANTYW5physical
26186194
STX3_HUMANSTX3physical
26186194
VAMP4_HUMANVAMP4physical
26186194
SNP29_HUMANSNAP29physical
26186194
STX8_HUMANSTX8physical
26186194
GOSR2_HUMANGOSR2physical
26186194
VAMP3_HUMANVAMP3physical
26186194
VAMP2_HUMANVAMP2physical
26186194
NOC4L_HUMANNOC4Lphysical
26186194
CLDN1_HUMANCLDND1physical
26186194
VAMP8_HUMANVAMP8physical
26186194
VAMP7_HUMANVAMP7physical
26186194
ADCY9_HUMANADCY9physical
26186194
COPT1_HUMANSLC31A1physical
26186194
BET1_HUMANBET1physical
26344197
EHD1_HUMANEHD1physical
26344197
EHD3_HUMANEHD3physical
26344197
EHD4_HUMANEHD4physical
26344197
SNAG_HUMANNAPGphysical
28514442
STXB5_HUMANSTXBP5physical
28514442
GOSR1_HUMANGOSR1physical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
VTI1A_HUMANVTI1Aphysical
28514442
GOSR2_HUMANGOSR2physical
28514442
STX8_HUMANSTX8physical
28514442
STX3_HUMANSTX3physical
28514442
VAMP8_HUMANVAMP8physical
28514442
SNP47_HUMANSNAP47physical
28514442
GOGA2_HUMANGOLGA2physical
28514442
ZN101_HUMANZNF101physical
28514442
CLDN1_HUMANCLDND1physical
28514442
VAMP3_HUMANVAMP3physical
28514442
STX10_HUMANSTX10physical
28514442
ADCY9_HUMANADCY9physical
28514442
TYW5_HUMANTYW5physical
28514442
STX5_HUMANSTX5physical
28514442
STX4_HUMANSTX4physical
28514442
YKT6_HUMANYKT6physical
28514442
STX16_HUMANSTX16physical
28514442
VAMP2_HUMANVAMP2physical
28514442
USE1_HUMANUSE1physical
28514442
SNP23_HUMANSNAP23physical
28514442
NOP14_HUMANNOP14physical
28514442
STX12_HUMANSTX12physical
28514442
COPT1_HUMANSLC31A1physical
28514442
ADPGK_HUMANADPGKphysical
28514442
SNAA_HUMANNAPAphysical
28514442
PTTG_HUMANPTTG1IPphysical
28514442
NOC4L_HUMANNOC4Lphysical
28514442
STX18_HUMANSTX18physical
28514442
GORS1_HUMANGORASP1physical
28514442
VAMP7_HUMANVAMP7physical
28514442
SNP29_HUMANSNAP29physical
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 STX7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT SER-2.
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-129, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3, AND MASSSPECTROMETRY.

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