UniProt ID | YLAT2_HUMAN | |
---|---|---|
UniProt AC | Q92536 | |
Protein Name | Y+L amino acid transporter 2 | |
Gene Name | SLC7A6 {ECO:0000312|HGNC:HGNC:11064} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 515 | |
Subcellular Localization |
Basolateral cell membrane Multi-pass membrane protein . |
|
Protein Description | Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Also acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Involved in the transport of L-arginine in monocytes. Reduces uptake of ornithine in retinal pigment epithelial (RPE) cells.. | |
Protein Sequence | MEAREPGRPTPTYHLVPNTSQSQVEEDVSSPPQRSSETMQLKKEISLLNGVSLVVGNMIGSGIFVSPKGVLVHTASYGMSLIVWAIGGLFSVVGALCYAELGTTITKSGASYAYILEAFGGFIAFIRLWVSLLVVEPTGQAIIAITFANYIIQPSFPSCDPPYLACRLLAAACICLLTFVNCAYVKWGTRVQDTFTYAKVVALIAIIVMGLVKLCQGHSEHFQDAFEGSSWDMGNLSLALYSALFSYSGWDTLNFVTEEIKNPERNLPLAIGISMPIVTLIYILTNVAYYTVLNISDVLSSDAVAVTFADQTFGMFSWTIPIAVALSCFGGLNASIFASSRLFFVGSREGHLPDLLSMIHIERFTPIPALLFNCTMALIYLIVEDVFQLINYFSFSYWFFVGLSVVGQLYLRWKEPKRPRPLKLSVFFPIVFCICSVFLVIVPLFTDTINSLIGIGIALSGVPFYFMGVYLPESRRPLFIRNVLAAITRGTQQLCFCVLTELDVAEEKKDERKTD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
10 | Phosphorylation | AREPGRPTPTYHLVP CCCCCCCCCCEEECC | 27.23 | 21945579 | |
12 | Phosphorylation | EPGRPTPTYHLVPNT CCCCCCCCEEECCCC | 26.50 | 21945579 | |
13 | Phosphorylation | PGRPTPTYHLVPNTS CCCCCCCEEECCCCC | 8.38 | 21945579 | |
19 | Phosphorylation | TYHLVPNTSQSQVEE CEEECCCCCHHHCCC | 23.29 | 21945579 | |
20 | Phosphorylation | YHLVPNTSQSQVEED EEECCCCCHHHCCCC | 34.18 | 21945579 | |
22 | Phosphorylation | LVPNTSQSQVEEDVS ECCCCCHHHCCCCCC | 35.64 | 21945579 | |
29 | Phosphorylation | SQVEEDVSSPPQRSS HHCCCCCCCCCCCCH | 49.83 | 21945579 | |
30 | Phosphorylation | QVEEDVSSPPQRSSE HCCCCCCCCCCCCHH | 40.21 | 21945579 | |
35 | Phosphorylation | VSSPPQRSSETMQLK CCCCCCCCHHHHHHH | 27.55 | 29978859 | |
36 | Phosphorylation | SSPPQRSSETMQLKK CCCCCCCHHHHHHHH | 39.00 | 23312004 | |
38 | Phosphorylation | PPQRSSETMQLKKEI CCCCCHHHHHHHHHH | 16.50 | 29978859 | |
42 | Ubiquitination | SSETMQLKKEISLLN CHHHHHHHHHHHHHC | 31.31 | - | |
131 | Phosphorylation | AFIRLWVSLLVVEPT HHHHHHHHHHCCCCC | 12.38 | - | |
347 | Phosphorylation | SRLFFVGSREGHLPD CCEEECCCCCCCHHH | 23.12 | 21712546 | |
488 | Phosphorylation | RNVLAAITRGTQQLC HHHHHHHHHHHHHHH | 20.51 | - |
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 YLAT2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YLAT2_HUMAN !! |
* 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 YLAT2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of YLAT2_HUMAN !! |
Kegg Disease | ||||||
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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. |
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