dbPTM

SC22B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SC22B_HUMAN
UniProt AC	O75396
Protein Name	Vesicle-trafficking protein SEC22b
Gene Name	SEC22B
Organism	Homo sapiens (Human).
Sequence Length	215
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type IV membrane protein . Endoplasmic reticulum-Golgi intermediate compartment membrane . Golgi apparatus, cis-Golgi network membrane . Golgi apparatus, trans-Golgi network membrane . Melanosome . Concent
Protein Description	SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER..
Protein Sequence	MVLLTMIARVADGLPLAASMQEDEQSGRDLQQYQSQAKQLFRKLNEQSPTRCTLEAGAMTFHYIIEQGVCDLVLCEAAFPKTLAFAYLEDLHSEFDEQHGKKVPTVSRPYSFIEFDTFIQKTKKLYIDSCARRNLGSINTELQDVQRIMVANIEEVLQRGEALSALDSKANNLSSLSKKYRQDAKYLNMHSTYAKLAAVAVFFIMLIVYVRFWWL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MVLLTMIARVAD ---CCHHHHHHHHHC	11.45	28857561
6	Sulfoxidation	--MVLLTMIARVADG --CCHHHHHHHHHCC	1.97	21406390
19	Phosphorylation	DGLPLAASMQEDEQS CCCCHHHHHCHHHHC	18.52	24043423
20	Sulfoxidation	GLPLAASMQEDEQSG CCCHHHHHCHHHHCC	4.30	21406390
24	Ubiquitination	AASMQEDEQSGRDLQ HHHHCHHHHCCHHHH	45.99	21963094
26	Phosphorylation	SMQEDEQSGRDLQQY HHCHHHHCCHHHHHH	33.47	20873877
33	Phosphorylation	SGRDLQQYQSQAKQL CCHHHHHHHHHHHHH	9.36	20873877
33	Nitration	SGRDLQQYQSQAKQL CCHHHHHHHHHHHHH	9.36	-
35	Phosphorylation	RDLQQYQSQAKQLFR HHHHHHHHHHHHHHH	27.46	17525332
38	Malonylation	QQYQSQAKQLFRKLN HHHHHHHHHHHHHHH	39.64	26320211
38	Ubiquitination	QQYQSQAKQLFRKLN HHHHHHHHHHHHHHH	39.64	23000965
38	Acetylation	QQYQSQAKQLFRKLN HHHHHHHHHHHHHHH	39.64	19608861
43	Ubiquitination	QAKQLFRKLNEQSPT HHHHHHHHHHHCCCC	48.61	23000965
48	Phosphorylation	FRKLNEQSPTRCTLE HHHHHHCCCCCCEEC	23.28	17192257
50	Phosphorylation	KLNEQSPTRCTLEAG HHHHCCCCCCEECCC	43.56	20071362
63	Ubiquitination	AGAMTFHYIIEQGVC CCCHHHHHHHHCCCC	10.21	21890473
81	Ubiquitination	LCEAAFPKTLAFAYL EECCCCCHHHHHHHH	50.12	-
81	Sumoylation	LCEAAFPKTLAFAYL EECCCCCHHHHHHHH	50.12	-
82	Ubiquitination	CEAAFPKTLAFAYLE ECCCCCHHHHHHHHH	24.45	21906983
93	Phosphorylation	AYLEDLHSEFDEQHG HHHHHHHHHHHHHCC	47.45	-
101	Ubiquitination	EFDEQHGKKVPTVSR HHHHHCCCCCCCCCC	48.77	32015554
102	Ubiquitination	FDEQHGKKVPTVSRP HHHHCCCCCCCCCCC	59.02	29967540
105	Phosphorylation	QHGKKVPTVSRPYSF HCCCCCCCCCCCCCE	33.82	29214152
107	Phosphorylation	GKKVPTVSRPYSFIE CCCCCCCCCCCCEEC	29.98	29214152
110	Phosphorylation	VPTVSRPYSFIEFDT CCCCCCCCCEECHHH	18.33	25884760
111	Ubiquitination	PTVSRPYSFIEFDTF CCCCCCCCEECHHHH	23.56	21890473
111	Phosphorylation	PTVSRPYSFIEFDTF CCCCCCCCEECHHHH	23.56	25884760
117	Phosphorylation	YSFIEFDTFIQKTKK CCEECHHHHHHHHCH	28.14	27251275
120	Ubiquitination	IEFDTFIQKTKKLYI ECHHHHHHHHCHHHH	43.08	21890473
121	Ubiquitination	EFDTFIQKTKKLYID CHHHHHHHHCHHHHH	58.45	21906983
127	Ubiquitination	QKTKKLYIDSCARRN HHHCHHHHHHHHHCC	4.56	21890473
137	Phosphorylation	CARRNLGSINTELQD HHHCCCCCCCHHHHH	18.81	19664994
140	Phosphorylation	RNLGSINTELQDVQR CCCCCCCHHHHHHHH	36.08	22167270
149	Sulfoxidation	LQDVQRIMVANIEEV HHHHHHHHHCCHHHH	2.25	28465586
164	Phosphorylation	LQRGEALSALDSKAN HHHCHHHHHHHHHHH	33.56	29255136
168	Phosphorylation	EALSALDSKANNLSS HHHHHHHHHHHCHHH	34.22	28355574
169	2-Hydroxyisobutyrylation	ALSALDSKANNLSSL HHHHHHHHHHCHHHH	55.59	-
169	Malonylation	ALSALDSKANNLSSL HHHHHHHHHHCHHHH	55.59	26320211
169	Ubiquitination	ALSALDSKANNLSSL HHHHHHHHHHCHHHH	55.59	23000965
174	Phosphorylation	DSKANNLSSLSKKYR HHHHHCHHHHCHHHH	31.21	23401153
175	Phosphorylation	SKANNLSSLSKKYRQ HHHHCHHHHCHHHHH	39.57	29255136
177	Phosphorylation	ANNLSSLSKKYRQDA HHCHHHHCHHHHHHH	29.11	29255136
178	Ubiquitination	NNLSSLSKKYRQDAK HCHHHHCHHHHHHHH	60.15	27667366
178	Malonylation	NNLSSLSKKYRQDAK HCHHHHCHHHHHHHH	60.15	26320211
178	2-Hydroxyisobutyrylation	NNLSSLSKKYRQDAK HCHHHHCHHHHHHHH	60.15	-
179	Ubiquitination	NLSSLSKKYRQDAKY CHHHHCHHHHHHHHH	42.14	23503661
185	Ubiquitination	KKYRQDAKYLNMHST HHHHHHHHHHCCHHH	59.57	21890473
192	Phosphorylation	KYLNMHSTYAKLAAV HHHCCHHHHHHHHHH	16.90	-
193	Phosphorylation	YLNMHSTYAKLAAVA HHCCHHHHHHHHHHH	12.54	-

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 SC22B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SC22B_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 SC22B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TMEDA_HUMAN	TMED10	physical	22939629
SEP11_HUMAN	SEPT11	physical	22939629
THTR_HUMAN	TST	physical	22939629
TCOF_HUMAN	TCOF1	physical	22939629
UBC12_HUMAN	UBE2M	physical	22939629
STIM1_HUMAN	STIM1	physical	22939629
TMED9_HUMAN	TMED9	physical	22939629
SUCB1_HUMAN	SUCLA2	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
SMCA2_HUMAN	SMARCA2	physical	22939629
SEPT9_HUMAN	SEPT9	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
UBXN1_HUMAN	UBXN1	physical	22939629
THTM_HUMAN	MPST	physical	22939629
SERPH_HUMAN	SERPINH1	physical	22939629
TM189_HUMAN	TMEM189	physical	22939629
XRCC1_HUMAN	XRCC1	physical	22939629
VAPB_HUMAN	VAPB	physical	22939629
TMEM9_HUMAN	TMEM9	physical	22939629
SUCB2_HUMAN	SUCLG2	physical	22939629
SIN3A_HUMAN	SIN3A	physical	22939629
TACO1_HUMAN	TACO1	physical	22939629
VPS29_HUMAN	VPS29	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
STX5_HUMAN	STX5	physical	24705552
STX1A_HUMAN	STX1A	physical	24705552
USE1_HUMAN	USE1	physical	28514442
SCFD2_HUMAN	SCFD2	physical	28514442
NBAS_HUMAN	NBAS	physical	28514442
STX18_HUMAN	STX18	physical	28514442
SEC20_HUMAN	BNIP1	physical	28514442
BET1_HUMAN	BET1	physical	28514442
STX5_HUMAN	STX5	physical	28514442
GOSR1_HUMAN	GOSR1	physical	28514442
GOSR2_HUMAN	GOSR2	physical	28514442
WASC4_HUMAN	KIAA1033	physical	28514442
STX8_HUMAN	STX8	physical	28514442
SNAA_HUMAN	NAPA	physical	28514442
CGT_HUMAN	UGT8	physical	28514442
SNP47_HUMAN	SNAP47	physical	28514442
VTI1B_HUMAN	VTI1B	physical	28514442
SNAG_HUMAN	NAPG	physical	28514442
CS025_HUMAN	C19orf25	physical	28514442
ZW10_HUMAN	ZW10	physical	28514442
STX7_HUMAN	STX7	physical	28514442
STX6_HUMAN	STX6	physical	28514442
F234B_HUMAN	KIAA1467	physical	28514442
SCFD1_HUMAN	SCFD1	physical	28514442
STX10_HUMAN	STX10	physical	28514442
STX12_HUMAN	STX12	physical	28514442
S39A3_HUMAN	SLC39A3	physical	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 SC22B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-137 AND SER-168, ANDMASS SPECTROMETRY.	19690332 [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-137, 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-48 AND SER-137, AND MASSSPECTROMETRY.	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-35, AND MASSSPECTROMETRY.	17525332 [Abstract]