dbPTM

S35G2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	S35G2_HUMAN
UniProt AC	Q8TBE7
Protein Name	Solute carrier family 35 member G2 {ECO:0000312\|HGNC:HGNC:28480}
Gene Name	SLC35G2 {ECO:0000312\|HGNC:HGNC:28480}
Organism	Homo sapiens (Human).
Sequence Length	412
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	May play a role in cell proliferation..
Protein Sequence	MDTSPSRKYPVKKRVKIHPNTVMVKYTSHYPQPGDDGYEEINEGYGNFMEENPKKGLLSEMKKKGRAFFGTMDTLPPPTEDPMINEIGQFQSFAEKNIFQSRKMWIVLFGSALAHGCVALITRLVSDRSKVPSLELIFIRSVFQVLSVLVVCYYQEAPFGPSGYRLRLFFYGVCNVISITCAYTSFSIVPPSNGTTMWRATTTVFSAILAFLLVDEKMAYVDMATVVCSILGVCLVMIPNIVDEDNSLLNAWKEAFGYTMTVMAGLTTALSMIVYRSIKEKISMWTALFTFGWTGTIWGISTMFILQEPIIPLDGETWSYLIAICVCSTAAFLGVYYALDKFHPALVSTVQHLEIVVAMVLQLLVLHIFPSIYDVFGGVIIMISVFVLAGYKLYWRNLRKQDYQEILDSPIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MDTSPSRKYP -----CCCCCCCCCC	41.04	28355574
4	Phosphorylation	----MDTSPSRKYPV ----CCCCCCCCCCC	19.33	22199227
6	Phosphorylation	--MDTSPSRKYPVKK --CCCCCCCCCCCCC	40.97	22199227
9	Phosphorylation	DTSPSRKYPVKKRVK CCCCCCCCCCCCCEE	16.49	24260401
26	Phosphorylation	PNTVMVKYTSHYPQP CCEEEEEEECCCCCC	11.32	28796482
27	Phosphorylation	NTVMVKYTSHYPQPG CEEEEEEECCCCCCC	11.87	28796482
28	Phosphorylation	TVMVKYTSHYPQPGD EEEEEEECCCCCCCC	20.24	28796482
30	Phosphorylation	MVKYTSHYPQPGDDG EEEEECCCCCCCCCC	11.88	25884760
38	Phosphorylation	PQPGDDGYEEINEGY CCCCCCCHHHHHHCC	19.86	28796482
45	Phosphorylation	YEEINEGYGNFMEEN HHHHHHCCCCCCHHC	11.61	28796482
54	Ubiquitination	NFMEENPKKGLLSEM CCCHHCCCCCHHHHH	71.68	23503661
55	Ubiquitination	FMEENPKKGLLSEMK CCHHCCCCCHHHHHH	56.92	32142685
55	Acetylation	FMEENPKKGLLSEMK CCHHCCCCCHHHHHH	56.92	30593005
59	Phosphorylation	NPKKGLLSEMKKKGR CCCCCHHHHHHHHCC	40.46	25159151
62	Acetylation	KGLLSEMKKKGRAFF CCHHHHHHHHCCCCC	47.48	30593011
63	Acetylation	GLLSEMKKKGRAFFG CHHHHHHHHCCCCCC	60.18	30592999
92	Phosphorylation	NEIGQFQSFAEKNIF CCHHHHHHHHHHCHH	27.93	24719451
96	Ubiquitination	QFQSFAEKNIFQSRK HHHHHHHHCHHCCCC	52.49	23503661
147	Phosphorylation	RSVFQVLSVLVVCYY HHHHHHHHHHHHHHH	17.97	24719451
258	Phosphorylation	AWKEAFGYTMTVMAG HHHHHHCCHHHHHHH	6.20	22210691
259	Phosphorylation	WKEAFGYTMTVMAGL HHHHHCCHHHHHHHH	13.52	22210691
277	Phosphorylation	LSMIVYRSIKEKISM HHHHHHHHHHHHHHH	21.96	22210691
403	Phosphorylation	RNLRKQDYQEILDSP HHHCHHHHHHHHCCC	12.92	28796482
409	Phosphorylation	DYQEILDSPIK---- HHHHHHCCCCC----	25.69	30266825

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 S35G2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of S35G2_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 S35G2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGFB1_HUMAN	TGFB1	physical	26186194
DCC1_HUMAN	DSCC1	physical	26186194
CHRC1_HUMAN	CHRAC1	physical	28514442
DCC1_HUMAN	DSCC1	physical	28514442
DDX23_HUMAN	DDX23	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 S35G2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-409, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASSSPECTROMETRY.	17081983 [Abstract]