dbPTM

S35F2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	S35F2_HUMAN
UniProt AC	Q8IXU6
Protein Name	Solute carrier family 35 member F2
Gene Name	SLC35F2
Organism	Homo sapiens (Human).
Sequence Length	374
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description	Putative solute transporter..
Protein Sequence	MEADSPAGPGAPEPLAEGAAAEFSSLLRRIKGKLFTWNILKTIALGQMLSLCICGTAITSQYLAERYKVNTPMLQSFINYCLLFLIYTVMLAFRSGSDNLLVILKRKWWKYILLGLADVEANYVIVRAYQYTTLTSVQLLDCFGIPVLMALSWFILHARYRVIHFIAVAVCLLGVGTMVGADILAGREDNSGSDVLIGDILVLLGASLYAISNVCEEYIVKKLSRQEFLGMVGLFGTIISGIQLLIVEYKDIASIHWDWKIALLFVAFALCMFCLYSFMPLVIKVTSATSVNLGILTADLYSLFVGLFLFGYKFSGLYILSFTVIMVGFILYCSTPTRTAEPAESSVPPVTSIGIDNLGLKLEENLQETHSAVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEADSPAG -------CCCCCCCC	9.63	22814378
5	Phosphorylation	---MEADSPAGPGAP ---CCCCCCCCCCCC	24.57	25159151
24	Phosphorylation	EGAAAEFSSLLRRIK HCHHHHHHHHHHHHH	16.16	24043423
25	Phosphorylation	GAAAEFSSLLRRIKG CHHHHHHHHHHHHHC	36.42	24719451
31	Ubiquitination	SSLLRRIKGKLFTWN HHHHHHHHCCHHHHH	48.45	23000965
33	Ubiquitination	LLRRIKGKLFTWNIL HHHHHHCCHHHHHHH	35.11	23000965
33 (in isoform 2)	Ubiquitination	-	35.11	21890473
33 (in isoform 1)	Ubiquitination	-	35.11	21890473
58 (in isoform 3)	Ubiquitination	-	3.70	21906983
105	Ubiquitination	DNLLVILKRKWWKYI CCEEEEECHHHHHHH	40.59	2190698
105 (in isoform 2)	Ubiquitination	-	40.59	21890473
105 (in isoform 1)	Ubiquitination	-	40.59	21890473
129	Phosphorylation	NYVIVRAYQYTTLTS CEEEEEEEEECCCCC	7.47	21406692
131	Phosphorylation	VIVRAYQYTTLTSVQ EEEEEEEECCCCCHH	6.76	21406692
132	Phosphorylation	IVRAYQYTTLTSVQL EEEEEEECCCCCHHH	10.37	21406692
133	Phosphorylation	VRAYQYTTLTSVQLL EEEEEECCCCCHHHH	24.09	21406692
135	Phosphorylation	AYQYTTLTSVQLLDC EEEECCCCCHHHHHH	25.43	21406692
136	Phosphorylation	YQYTTLTSVQLLDCF EEECCCCCHHHHHHH	15.81	21406692
152	Phosphorylation	IPVLMALSWFILHAR HHHHHHHHHHHHHHH	15.48	21406692
339	Phosphorylation	YCSTPTRTAEPAESS HCCCCCCCCCCCCCC	37.54	25850435
345	Phosphorylation	RTAEPAESSVPPVTS CCCCCCCCCCCCCCE	38.45	28122231
346	Phosphorylation	TAEPAESSVPPVTSI CCCCCCCCCCCCCEE	30.10	25850435
351	Phosphorylation	ESSVPPVTSIGIDNL CCCCCCCCEEEECCC	22.02	28122231
352	Phosphorylation	SSVPPVTSIGIDNLG CCCCCCCEEEECCCC	21.03	25850435
361	Ubiquitination	GIDNLGLKLEENLQE EECCCCCCHHHHHHH	52.64	33845483
369	Phosphorylation	LEENLQETHSAVL-- HHHHHHHHHHHCC--	14.26	30266825
371	Phosphorylation	ENLQETHSAVL---- HHHHHHHHHCC----	27.74	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 S35F2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of S35F2_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 S35F2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of S35F2_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 S35F2_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-5, AND MASSSPECTROMETRY.	19690332 [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-5, AND MASSSPECTROMETRY.	18691976 [Abstract]