STXB3_HUMAN - dbPTM
STXB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STXB3_HUMAN
UniProt AC O00186
Protein Name Syntaxin-binding protein 3
Gene Name STXBP3
Organism Homo sapiens (Human).
Sequence Length 592
Subcellular Localization Cytoplasm, cytosol . Cell membrane . In platelets, predominantly cytosolic. Low amounts membrane-associated.
Protein Description Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes..
Protein Sequence MAPPVAERGLKSVVWQKIKATVFDDCKKEGEWKIMLLDEFTTKLLASCCKMTDLLEEGITVVENIYKNREPVRQMKALYFITPTSKSVDCFLHDFASKSENKYKAAYIYFTDFCPDNLFNKIKASCSKSIRRCKEINISFIPHESQVYTLDVPDAFYYCYSPDPGNAKGKDAIMETMADQIVTVCATLDENPGVRYKSKPLDNASKLAQLVEKKLEDYYKIDEKSLIKGKTHSQLLIIDRGFDPVSTVLHELTFQAMAYDLLPIENDTYKYKTDGKEKEAILEEEDDLWVRIRHRHIAVVLEEIPKLMKEISSTKKATEGKTSLSALTQLMKKMPHFRKQITKQVVHLNLAEDCMNKFKLNIEKLCKTEQDLALGTDAEGQKVKDSMRVLLPVLLNKNHDNCDKIRAILLYIFSINGTTEENLDRLIQNVKIENESDMIRNWSYLGVPIVPQSQQGKPLRKDRSAEETFQLSRWTPFIKDIMEDAIDNRLDSKEWPYCSQCPAVWNGSGAVSARQKPRANYLEDRKNGSKLIVFVIGGITYSEVRCAYEVSQAHKSCEVIIGSTHVLTPKKLLDDIKMLNKPKDKVSLIKDE
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
8MethylationMAPPVAERGLKSVVW
CCCCHHHHCHHHHHH
46.11115917997
11UbiquitinationPVAERGLKSVVWQKI
CHHHHCHHHHHHHHH
43.9929967540
11MethylationPVAERGLKSVVWQKI
CHHHHCHHHHHHHHH
43.99115980377
17UbiquitinationLKSVVWQKIKATVFD
HHHHHHHHHHEEEEH
30.3829967540
19UbiquitinationSVVWQKIKATVFDDC
HHHHHHHHEEEEHHH
45.0729967540
27UbiquitinationATVFDDCKKEGEWKI
EEEEHHHHHCCCEEE
61.9427667366
76MalonylationREPVRQMKALYFITP
CCCHHHCEEEEEECC
27.2326320211
79PhosphorylationVRQMKALYFITPTSK
HHHCEEEEEECCCCC
9.5921406692
82PhosphorylationMKALYFITPTSKSVD
CEEEEEECCCCCCHH
15.6021406692
84PhosphorylationALYFITPTSKSVDCF
EEEEECCCCCCHHHH
39.8921406692
85PhosphorylationLYFITPTSKSVDCFL
EEEECCCCCCHHHHH
24.9221406692
86UbiquitinationYFITPTSKSVDCFLH
EEECCCCCCHHHHHH
57.9121963094
98MalonylationFLHDFASKSENKYKA
HHHHHHCCCCCCCEE
59.3626320211
98UbiquitinationFLHDFASKSENKYKA
HHHHHHCCCCCCCEE
59.3632015554
103PhosphorylationASKSENKYKAAYIYF
HCCCCCCCEEEEEEE
19.90-
104AcetylationSKSENKYKAAYIYFT
CCCCCCCEEEEEEEE
28.317712229
128AcetylationKIKASCSKSIRRCKE
HHHHHHHHHHHHCCC
54.9825953088
170AcetylationDPGNAKGKDAIMETM
CCCCCCCHHHHHHHH
43.1919816639
197UbiquitinationENPGVRYKSKPLDNA
CCCCCCCCCCCCCCH
41.2529967540
197AcetylationENPGVRYKSKPLDNA
CCCCCCCCCCCCCCH
41.2519816647
198PhosphorylationNPGVRYKSKPLDNAS
CCCCCCCCCCCCCHH
30.4824719451
206UbiquitinationKPLDNASKLAQLVEK
CCCCCHHHHHHHHHH
45.4929967540
213UbiquitinationKLAQLVEKKLEDYYK
HHHHHHHHHHHHHHC
56.0029967540
214UbiquitinationLAQLVEKKLEDYYKI
HHHHHHHHHHHHHCC
43.5327667366
218PhosphorylationVEKKLEDYYKIDEKS
HHHHHHHHHCCCHHH
9.4022817900
219PhosphorylationEKKLEDYYKIDEKSL
HHHHHHHHCCCHHHH
17.5022817900
220UbiquitinationKKLEDYYKIDEKSLI
HHHHHHHCCCHHHHC
37.1422817900
224UbiquitinationDYYKIDEKSLIKGKT
HHHCCCHHHHCCCCC
46.9821906983
225PhosphorylationYYKIDEKSLIKGKTH
HHCCCHHHHCCCCCC
33.0224719451
228UbiquitinationIDEKSLIKGKTHSQL
CCHHHHCCCCCCCEE
60.7022817900
230UbiquitinationEKSLIKGKTHSQLLI
HHHHCCCCCCCEEEE
37.7530230243
309UbiquitinationEEIPKLMKEISSTKK
HHHHHHHHHHHCCCC
63.4329967540
312PhosphorylationPKLMKEISSTKKATE
HHHHHHHHCCCCCCC
32.8022817900
313PhosphorylationKLMKEISSTKKATEG
HHHHHHHCCCCCCCC
50.3222817900
314PhosphorylationLMKEISSTKKATEGK
HHHHHHCCCCCCCCC
29.7622817900
315UbiquitinationMKEISSTKKATEGKT
HHHHHCCCCCCCCCC
42.2123000965
316UbiquitinationKEISSTKKATEGKTS
HHHHCCCCCCCCCCH
61.7123000965
318PhosphorylationISSTKKATEGKTSLS
HHCCCCCCCCCCHHH
54.9028450419
321UbiquitinationTKKATEGKTSLSALT
CCCCCCCCCHHHHHH
28.8023000965
322PhosphorylationKKATEGKTSLSALTQ
CCCCCCCCHHHHHHH
45.8425159151
323PhosphorylationKATEGKTSLSALTQL
CCCCCCCHHHHHHHH
24.6625159151
325PhosphorylationTEGKTSLSALTQLMK
CCCCCHHHHHHHHHH
22.4728450419
328PhosphorylationKTSLSALTQLMKKMP
CCHHHHHHHHHHHCH
21.2630108239
332MalonylationSALTQLMKKMPHFRK
HHHHHHHHHCHHHHH
55.2926320211
332UbiquitinationSALTQLMKKMPHFRK
HHHHHHHHHCHHHHH
55.2921890473
333UbiquitinationALTQLMKKMPHFRKQ
HHHHHHHHCHHHHHH
43.64-
343UbiquitinationHFRKQITKQVVHLNL
HHHHHHHHHHHHHHH
42.6032015554
357UbiquitinationLAEDCMNKFKLNIEK
HHHHHHHHHCCCHHH
19.5929967540
357AcetylationLAEDCMNKFKLNIEK
HHHHHHHHHCCCHHH
19.5926051181
359UbiquitinationEDCMNKFKLNIEKLC
HHHHHHHCCCHHHHH
42.0823000965
364UbiquitinationKFKLNIEKLCKTEQD
HHCCCHHHHHCCHHH
56.2223000965
364MalonylationKFKLNIEKLCKTEQD
HHCCCHHHHHCCHHH
56.2226320211
367UbiquitinationLNIEKLCKTEQDLAL
CCHHHHHCCHHHHCC
66.5823000965
376PhosphorylationEQDLALGTDAEGQKV
HHHHCCCCCCCCCCH
32.6523401153
382UbiquitinationGTDAEGQKVKDSMRV
CCCCCCCCHHHHHHH
63.2121906983
384UbiquitinationDAEGQKVKDSMRVLL
CCCCCCHHHHHHHHH
51.6322817900
397UbiquitinationLLPVLLNKNHDNCDK
HHHHHHCCCCCCHHH
56.4832015554
404UbiquitinationKNHDNCDKIRAILLY
CCCCCHHHHHHHHHH
35.97-
431UbiquitinationDRLIQNVKIENESDM
HHHHHHCCCCCHHHH
52.4221963094
438SulfoxidationKIENESDMIRNWSYL
CCCCHHHHCCCCEEC
4.2821406390
457UbiquitinationVPQSQQGKPLRKDRS
CCHHHCCCCCCCCCC
36.2221890473
464PhosphorylationKPLRKDRSAEETFQL
CCCCCCCCHHHHHHH
50.6026471730
468PhosphorylationKDRSAEETFQLSRWT
CCCCHHHHHHHHCCC
14.2628857561
479UbiquitinationSRWTPFIKDIMEDAI
HCCCHHHHHHHHHHH
41.4021963094
493UbiquitinationIDNRLDSKEWPYCSQ
HHCCCCCCCCCCCCC
64.5621963094
508PhosphorylationCPAVWNGSGAVSARQ
CCCEECCCCCCCCCC
21.9925159151
512PhosphorylationWNGSGAVSARQKPRA
ECCCCCCCCCCCCCC
19.7326434776
521PhosphorylationRQKPRANYLEDRKNG
CCCCCCCCHHHCCCC
15.5221945579
542PhosphorylationVIGGITYSEVRCAYE
EECCCCHHHHHHHHH
22.44-
556PhosphorylationEVSQAHKSCEVIIGS
HHHHHHHCCEEEECC
12.97-
570AcetylationSTHVLTPKKLLDDIK
CCCCCCHHHHHHHHH
51.3125953088
571AcetylationTHVLTPKKLLDDIKM
CCCCCHHHHHHHHHH
56.337668015
571UbiquitinationTHVLTPKKLLDDIKM
CCCCCHHHHHHHHHH
56.33-
577AcetylationKKLLDDIKMLNKPKD
HHHHHHHHHHCCCHH
44.3120167786
577UbiquitinationKKLLDDIKMLNKPKD
HHHHHHHHHHCCCHH
44.3129967540
581AcetylationDDIKMLNKPKDKVSL
HHHHHHCCCHHHCCC
49.8620167786
583AcetylationIKMLNKPKDKVSLIK
HHHHCCCHHHCCCCC
72.3220167786
585UbiquitinationMLNKPKDKVSLIKDE
HHCCCHHHCCCCCCC
39.5929967540
587PhosphorylationNKPKDKVSLIKDE--
CCCHHHCCCCCCC--
30.0728355574
590UbiquitinationKDKVSLIKDE-----
HHHCCCCCCC-----
62.18-

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 STXB3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STXB3_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 STXB3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STX4_HUMANSTX4physical
12773094
STX2_HUMANSTX2physical
12773094
SNP23_HUMANSNAP23physical
12773094
STX4_HUMANSTX4physical
28514442
TBA3C_HUMANTUBA3Cphysical
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 STXB3_HUMAN

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Related Literatures of Post-Translational Modification

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