dbPTM

STXB4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STXB4_HUMAN
UniProt AC	Q6ZWJ1
Protein Name	Syntaxin-binding protein 4
Gene Name	STXBP4
Organism	Homo sapiens (Human).
Sequence Length	553
Subcellular Localization	Cytoplasm.
Protein Description	Plays a role in the translocation of transport vesicles from the cytoplasm to the plasma membrane. Inhibits the translocation of SLC2A4 from intracellular vesicles to the plasma membrane by STX4A binding and preventing the interaction between STX4A and VAMP2. Stimulation with insulin disrupts the interaction with STX4A, leading to increased levels of SLC2A4 at the plasma membrane. May also play a role in the regulation of insulin release by pancreatic beta cells after stimulation by glucose (By similarity)..
Protein Sequence	MNKNTSTVVSPSLLEKDPAFQMITIAKETGLGLKVLGGINRNEGPLVYIQEIIPGGDCYKDGRLKPGDQLVSVNKESMIGVSFEEAKSIITGAKLRLESAWEIAFIRQKSDNIQPENLSCTSLIEASGEYGPQASTLSLFSSPPEILIPKTSSTPKTNNDILSSCEIKTGYNKTVQIPITSENSTVGLSNTDVASAWTENYGLQEKISLNPSVRFKAEKLEMALNYLGIQPTKEQHQALRQQVQADSKGTVSFGDFVQVARNLFCLQLDEVNVGAHEISNILDSQLLPCDSSEADEMERLKCERDDALKEVNTLKEKLLESDKQRKQLTEELQNVKQEAKAVVEETRALRSRIHLAEAAQRQAHGMEMDYEEVIRLLEAKITELKAQLADYSDQNKESVQDLKKRIMVLDCQLRKSEMARKTFEASTEKLLHFVEAIQEVFSDNSTPLSNLSERRAVLASQTSLTPLGRNGRSIPATLALESKELVKSVRALLDMDCLPYGWEEAYTADGIKYFINHVTQTTSWIHPVMSVLNLSRSEENEEDCSRELPNQKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MNKNTSTVVSPS ---CCCCCCCCCCHH	27.64	21712546
6	Phosphorylation	--MNKNTSTVVSPSL --CCCCCCCCCCHHH	28.70	25159151
7	Phosphorylation	-MNKNTSTVVSPSLL -CCCCCCCCCCHHHH	23.92	25159151
10	Phosphorylation	KNTSTVVSPSLLEKD CCCCCCCCHHHHCCC	12.39	25159151
12	Phosphorylation	TSTVVSPSLLEKDPA CCCCCCHHHHCCCCC	37.77	21712546
16	Ubiquitination	VSPSLLEKDPAFQMI CCHHHHCCCCCCCEE	69.82	21906983
16 (in isoform 1)	Ubiquitination	-	69.82	21906983
27	Ubiquitination	FQMITIAKETGLGLK CCEEEEHHHHCCCEE	52.54	21906983
27 (in isoform 1)	Ubiquitination	-	52.54	21906983
60	Ubiquitination	IPGGDCYKDGRLKPG ECCCCCCCCCCCCCC	61.10	-
65	Ubiquitination	CYKDGRLKPGDQLVS CCCCCCCCCCCEEEE	45.66	-
82	Phosphorylation	KESMIGVSFEEAKSI CHHHCCCCHHHHHHH	23.02	25159151
99	Phosphorylation	GAKLRLESAWEIAFI CCEEEHHHHHHHEEE	43.18	-
151	Phosphorylation	PEILIPKTSSTPKTN CCEEECCCCCCCCCC	23.66	21712546
156	Ubiquitination	PKTSSTPKTNNDILS CCCCCCCCCCCCHHH	65.06	-
157	Phosphorylation	KTSSTPKTNNDILSS CCCCCCCCCCCHHHC	40.22	-
163	Phosphorylation	KTNNDILSSCEIKTG CCCCCHHHCCEEECC	33.02	25159151
164	Phosphorylation	TNNDILSSCEIKTGY CCCCHHHCCEEECCC	16.60	21815630
168	Ubiquitination	ILSSCEIKTGYNKTV HHHCCEEECCCCCEE	17.38	-
208	Phosphorylation	YGLQEKISLNPSVRF CCCCCCCCCCHHHCH	32.91	28555341
212	Phosphorylation	EKISLNPSVRFKAEK CCCCCCHHHCHHHHH	25.50	28857561
233	Ubiquitination	YLGIQPTKEQHQALR HCCCCCCHHHHHHHH	63.16	-
248	Ubiquitination	QQVQADSKGTVSFGD HHHHHCCCCCCCHHH	60.18	-
250	Phosphorylation	VQADSKGTVSFGDFV HHHCCCCCCCHHHHH	19.40	29214152
252	Phosphorylation	ADSKGTVSFGDFVQV HCCCCCCCHHHHHHH	24.29	22199227
323	Ubiquitination	EKLLESDKQRKQLTE HHHHHCHHHHHHHHH	62.37	-
326	Ubiquitination	LESDKQRKQLTEELQ HHCHHHHHHHHHHHH	47.36	-
346	Phosphorylation	AKAVVEETRALRSRI HHHHHHHHHHHHHHH	14.03	29978859
380	Ubiquitination	VIRLLEAKITELKAQ HHHHHHHHHHHHHHH	40.56	-
382	Phosphorylation	RLLEAKITELKAQLA HHHHHHHHHHHHHHC	34.26	23403867
385 (in isoform 1)	Ubiquitination	-	28.05	21906983
385	Ubiquitination	EAKITELKAQLADYS HHHHHHHHHHHCCCC	28.05	21906983
391	Phosphorylation	LKAQLADYSDQNKES HHHHHCCCCCCCHHH	14.45	29496907
392	Phosphorylation	KAQLADYSDQNKESV HHHHCCCCCCCHHHH	33.01	29496907
396	Ubiquitination	ADYSDQNKESVQDLK CCCCCCCHHHHHHHH	45.81	2190698
396 (in isoform 1)	Ubiquitination	-	45.81	21906983
421	Ubiquitination	RKSEMARKTFEASTE CHHHHHHHHHHHHHH	48.29	-
445	Phosphorylation	QEVFSDNSTPLSNLS HHHHCCCCCCCCCHH	36.07	-
446	Phosphorylation	EVFSDNSTPLSNLSE HHHCCCCCCCCCHHH	34.21	-
460	Phosphorylation	ERRAVLASQTSLTPL HHHHHHHCCCCCCCC	29.81	17525332
462	Phosphorylation	RAVLASQTSLTPLGR HHHHHCCCCCCCCCC	24.17	21082442
463	Phosphorylation	AVLASQTSLTPLGRN HHHHCCCCCCCCCCC	23.70	17525332
465	Phosphorylation	LASQTSLTPLGRNGR HHCCCCCCCCCCCCC	19.08	28122231
483	Ubiquitination	ATLALESKELVKSVR CCHHHCCHHHHHHHH	45.77	-
487	Ubiquitination	LESKELVKSVRALLD HCCHHHHHHHHHHHC	56.72	-
519	Phosphorylation	KYFINHVTQTTSWIH HHHHHHHHCCCCCHH	16.79	27251275
521	Phosphorylation	FINHVTQTTSWIHPV HHHHHHCCCCCHHHH	17.27	27251275
522	Phosphorylation	INHVTQTTSWIHPVM HHHHHCCCCCHHHHH	16.55	27251275
523	Phosphorylation	NHVTQTTSWIHPVMS HHHHCCCCCHHHHHH	27.67	27251275
545	Phosphorylation	EENEEDCSRELPNQK CCCHHHHHHCCCCCC	40.90	28985074

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 STXB4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
99	S	Phosphorylation	-
Phosphorylated on Ser-99 by PKB/AKT2 after insulin treatment.
99	S	Phosphorylation	-
Phosphorylation on Ser-99 abolishes the interaction with STX4A (By similarity).

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 STXB4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of STXB4_HUMAN !!

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 STXB4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-6 AND SER-10, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-10, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-10 AND THR-465,AND MASS SPECTROMETRY.	18691976 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-463, ANDMASS SPECTROMETRY.	17525332 [Abstract]

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