dbPTM

SMAP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SMAP2_HUMAN
UniProt AC	Q8WU79
Protein Name	Stromal membrane-associated protein 2
Gene Name	SMAP2
Organism	Homo sapiens (Human).
Sequence Length	429
Subcellular Localization	Cytoplasm. Detected in multiple foci throughout the cytoplasm and in juxtanuclear structures..
Protein Description	GTPase activating protein that acts on ARF1. Can also activate ARF6 (in vitro). May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity)..
Protein Sequence	MTGKSVKDVDRYQAVLANLLLEEDNKFCADCQSKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQEQIQCMQEMGNGKANRLYEAYLPETFRRPQIDPAVEGFIRDKYEKKKYMDRSLDINAFRKEKDDKWKRGSEPVPEKKLEPVVFEKVKMPQKKEDPQLPRKSSPKSTAPVMDLLGLDAPVACSIANSKTSNTLEKDLDLLASVPSPSSSGSRKVVGSMPTAGSAGSVPENLNLFPEPGSKSEEIGKKQLSKDSILSLYGSQTPQMPTQAMFMAPAQMAYPTAYPSFPGVTPPNSIMGSMMPPPVGMVAQPGASGMVAPMAMPAGYMGGMQASMMGVPNGMMTTQQAGYMAGMAAMPQTVYGVQPAQQLQWNLTQMTQQMAGMNFYGANGMMNYGQSMSGGNGQAANQTLSPQMWK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MTGKSVKDVDRYQA -CCCCCHHHHHHHHH	60.16	-
26	Ubiquitination	LLLEEDNKFCADCQS HHCCCCCCCCHHHHC	54.89	-
63	Phosphorylation	RNLGVHISRVKSVNL HHCCEEHHHEEECCH	19.02	20873877
67	Phosphorylation	VHISRVKSVNLDQWT EEHHHEEECCHHHHH	17.24	27251275
88	Ubiquitination	MQEMGNGKANRLYEA HHHHCCCHHHHHHHH	46.63	-
93	Phosphorylation	NGKANRLYEAYLPET CCHHHHHHHHHCCHH	8.69	23532336
96	Phosphorylation	ANRLYEAYLPETFRR HHHHHHHHCCHHHCC	15.73	28796482
127	Phosphorylation	KKKYMDRSLDINAFR HHHHHCCCCCHHHHH	26.57	30108239
135	Ubiquitination	LDINAFRKEKDDKWK CCHHHHHCCCCCCCC	63.76	-
145	Phosphorylation	DDKWKRGSEPVPEKK CCCCCCCCCCCCHHH	42.64	27251275
151	Acetylation	GSEPVPEKKLEPVVF CCCCCCHHHCCCCEE	57.50	23749302
152	Ubiquitination	SEPVPEKKLEPVVFE CCCCCHHHCCCCEEE	57.32	-
176	Phosphorylation	DPQLPRKSSPKSTAP CCCCCCCCCCCCCCC	53.83	28464451
177	Phosphorylation	PQLPRKSSPKSTAPV CCCCCCCCCCCCCCH	39.11	28464451
180	Phosphorylation	PRKSSPKSTAPVMDL CCCCCCCCCCCHHHH	32.93	28464451
181	Phosphorylation	RKSSPKSTAPVMDLL CCCCCCCCCCHHHHH	40.90	28464451
196	Glutathionylation	GLDAPVACSIANSKT CCCCCCHHHHHCCCC	2.85	22555962
197	O-linked_Glycosylation	LDAPVACSIANSKTS CCCCCHHHHHCCCCC	18.26	31492838
203	Phosphorylation	CSIANSKTSNTLEKD HHHHCCCCCCCHHHH	27.34	-
204	Phosphorylation	SIANSKTSNTLEKDL HHHCCCCCCCHHHHH	31.39	26657352
206	Phosphorylation	ANSKTSNTLEKDLDL HCCCCCCCHHHHHHH	35.74	28464451
209	Ubiquitination	KTSNTLEKDLDLLAS CCCCCHHHHHHHHHC	67.70	-
216	Phosphorylation	KDLDLLASVPSPSSS HHHHHHHCCCCCCCC	34.23	30266825
219	Phosphorylation	DLLASVPSPSSSGSR HHHHCCCCCCCCCCC	34.95	29255136
221	Phosphorylation	LASVPSPSSSGSRKV HHCCCCCCCCCCCCE	41.28	29255136
222	Phosphorylation	ASVPSPSSSGSRKVV HCCCCCCCCCCCCEE	41.94	29255136
223	Phosphorylation	SVPSPSSSGSRKVVG CCCCCCCCCCCCEEE	45.16	30266825
225	Phosphorylation	PSPSSSGSRKVVGSM CCCCCCCCCCEEECC	30.76	29255136
231	Phosphorylation	GSRKVVGSMPTAGSA CCCCEEECCCCCCCC	15.24	23401153
234	Phosphorylation	KVVGSMPTAGSAGSV CEEECCCCCCCCCCC	34.70	29255136
237	Phosphorylation	GSMPTAGSAGSVPEN ECCCCCCCCCCCCCC	27.30	29255136
240	Phosphorylation	PTAGSAGSVPENLNL CCCCCCCCCCCCCCC	33.93	23401153
253	Phosphorylation	NLFPEPGSKSEEIGK CCCCCCCCCHHHHHC	43.66	26074081
255	Phosphorylation	FPEPGSKSEEIGKKQ CCCCCCCHHHHHCHH	42.00	23312004

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 SMAP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SMAP2_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 SMAP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CA094_HUMAN	C1orf94	physical	25416956
DAZP2_HUMAN	DAZAP2	physical	21516116
RBMS1_HUMAN	RBMS1	physical	27173435
ZN143_HUMAN	ZNF143	physical	27173435

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 SMAP2_HUMAN

Related Literatures of Post-Translational Modification

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-225, AND MASSSPECTROMETRY.	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-219, 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-219, AND MASSSPECTROMETRY.	18691976 [Abstract]