S22A2_HUMAN - dbPTM
S22A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S22A2_HUMAN
UniProt AC O15244
Protein Name Solute carrier family 22 member 2
Gene Name SLC22A2
Organism Homo sapiens (Human).
Sequence Length 555
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Mediates tubular uptake of organic compounds from circulation. Mediates the influx of agmatine, dopamine, noradrenaline (norepinephrine), serotonin, choline, famotidine, ranitidine, histamin, creatinine, amantadine, memantine, acriflavine, 4-[4-(dimethylamino)-styryl]-N-methylpyridinium ASP, amiloride, metformin, N-1-methylnicotinamide (NMN), tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP), cimetidine, cisplatin and oxaliplatin. Cisplatin may develop a nephrotoxic action. Transport of creatinine is inhibited by fluoroquinolones such as DX-619 and LVFX. This transporter is a major determinant of the anticancer activity of oxaliplatin and may contribute to antitumor specificity..
Protein Sequence MPTTVDDVLEHGGEFHFFQKQMFFLLALLSATFAPIYVGIVFLGFTPDHRCRSPGVAELSLRCGWSPAEELNYTVPGPGPAGEASPRQCRRYEVDWNQSTFDCVDPLASLDTNRSRLPLGPCRDGWVYETPGSSIVTEFNLVCANSWMLDLFQSSVNVGFFIGSMSIGYIADRFGRKLCLLTTVLINAAAGVLMAISPTYTWMLIFRLIQGLVSKAGWLIGYILITEFVGRRYRRTVGIFYQVAYTVGLLVLAGVAYALPHWRWLQFTVSLPNFFFLLYYWCIPESPRWLISQNKNAEAMRIIKHIAKKNGKSLPASLQRLRLEEETGKKLNPSFLDLVRTPQIRKHTMILMYNWFTSSVLYQGLIMHMGLAGDNIYLDFFYSALVEFPAAFMIILTIDRIGRRYPWAASNMVAGAACLASVFIPGDLQWLKIIISCLGRMGITMAYEIVCLVNAELYPTFIRNLGVHICSSMCDIGGIITPFLVYRLTNIWLELPLMVFGVLGLVAGGLVLLLPETKGKALPETIEEAENMQRPRKNKEKMIYLQVQKLDIPLN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
60PhosphorylationSPGVAELSLRCGWSP
CCCCEEEEEECCCCC
12.7924719451
72N-linked_GlycosylationWSPAEELNYTVPGPG
CCCHHHCCCCCCCCC
33.44UniProtKB CARBOHYD
236PhosphorylationVGRRYRRTVGIFYQV
HCHHHHHHHHHHHHH
17.68-
241PhosphorylationRRTVGIFYQVAYTVG
HHHHHHHHHHHHHHH
10.52-
313PhosphorylationIAKKNGKSLPASLQR
HHHHCCCCCCHHHHH
40.7727174698
317PhosphorylationNGKSLPASLQRLRLE
CCCCCCHHHHHHHHH
24.0927174698
471PhosphorylationNLGVHICSSMCDIGG
HHCHHHHHHCCCCCC
22.09-
489PhosphorylationPFLVYRLTNIWLELP
HHHHHHHHCHHHHHH
18.69-
517PhosphorylationLVLLLPETKGKALPE
EEHCCCCCCCCCCCH
43.06-
544PhosphorylationKNKEKMIYLQVQKLD
CCHHCEEEEEEEECC
6.3829759185

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 S22A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S22A2_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 S22A2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO2_HUMANSUMO2physical
21988832

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S22A2_HUMAN

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Related Literatures of Post-Translational Modification

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