S38A3_HUMAN - dbPTM
S38A3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S38A3_HUMAN
UniProt AC Q99624
Protein Name Sodium-coupled neutral amino acid transporter 3
Gene Name SLC38A3 {ECO:0000312|EMBL:AAH42875.1}
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission..
Protein Sequence MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFTDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKSSGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEEKTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPCPLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCHPEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVDPFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINLLVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFLLMTMSLSFIIIDWASGTSRHGGNH
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
19PhosphorylationLVPNGKHSEGLLPVI
ECCCCCCCCCCCCEE
36.5222798277
46UbiquitinationARSCMEGKSFLQKSP
HHHHHCCHHHHHCCC
25.4029967540
47PhosphorylationRSCMEGKSFLQKSPS
HHHHCCHHHHHCCCC
41.8820166139
51UbiquitinationEGKSFLQKSPSKEPH
CCHHHHHCCCCCCCC
67.4929967540
52PhosphorylationGKSFLQKSPSKEPHF
CHHHHHCCCCCCCCC
22.8030266825
54PhosphorylationSFLQKSPSKEPHFTD
HHHHCCCCCCCCCCC
57.6630266825
55UbiquitinationFLQKSPSKEPHFTDF
HHHCCCCCCCCCCCC
77.8629967540
60PhosphorylationPSKEPHFTDFEGKTS
CCCCCCCCCCCCCCC
36.4230266825
74N-linked_GlycosylationSFGMSVFNLSNAIMG
CCCCHHHCCCHHHHH
40.16UniProtKB CARBOHYD
120PhosphorylationSIHLLLKSSGVVGIR
HHHHHHHCCCCEEEE
32.0928111955
121PhosphorylationIHLLLKSSGVVGIRA
HHHHHHCCCCEEEEE
33.7428111955
129PhosphorylationGVVGIRAYEQLGYRA
CCEEEEEEHHHCCCH
8.3828111955
150PhosphorylationLAAALAITLQNIGAM
HHHHHHHHHHHHHCC
19.38-
159PhosphorylationQNIGAMSSYLYIIKS
HHHHCCHHHHHHHHC
13.18-
160PhosphorylationNIGAMSSYLYIIKSE
HHHCCHHHHHHHHCC
9.02-
247N-linked_GlycosylationCPLPPNFNNTTGNFS
CCCCCCCCCCCCCCC
52.13UniProtKB CARBOHYD
248N-linked_GlycosylationPLPPNFNNTTGNFSH
CCCCCCCCCCCCCCE
34.57UniProtKB CARBOHYD
252N-linked_GlycosylationNFNNTTGNFSHVEIV
CCCCCCCCCCEEEEE
32.91UniProtKB CARBOHYD
323N-linked_GlycosylationKKMQHISNLSIAVMY
HHHHHHHHHHHHHHH
36.89UniProtKB CARBOHYD
330PhosphorylationNLSIAVMYIMYFLAA
HHHHHHHHHHHHHHH
3.96-

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 S38A3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S38A3_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 S38A3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETB1_HUMANSETDB1physical
16169070
NEDD4_HUMANNEDD4physical
20737472

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
DB00174L-Asparagine
DB00130L-Glutamine
DB00117L-Histidine
Regulatory Network of S38A3_HUMAN

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Related Literatures of Post-Translational Modification

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