S6A15_HUMAN - dbPTM
S6A15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S6A15_HUMAN
UniProt AC Q9H2J7
Protein Name Sodium-dependent neutral amino acid transporter B(0)AT2
Gene Name SLC6A15
Organism Homo sapiens (Human).
Sequence Length 730
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for the branched-chain amino acids, particularly leucine, valine and isoleucine and methionine. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent..
Protein Sequence MPKNSKVVKRELDDDVTESVKDLLSNEDAADDAFKTSELIVDGQEEKDTDVEEGSEVEDERPAWNSKLQYILAQVGFSVGLGNVWRFPYLCQKNGGGAYLLPYLILLMVIGIPLFFLELSVGQRIRRGSIGVWNYISPKLGGIGFASCVVCYFVALYYNVIIGWSLFYFSQSFQQPLPWDQCPLVKNASHTFVEPECEQSSATTYYWYREALNISSSISESGGLNWKMTICLLAAWVMVCLAMIKGIQSSGKIIYFSSLFPYVVLICFLIRAFLLNGSIDGIRHMFTPKLEIMLEPKVWREAATQVFFALGLGFGGVIAFSSYNKRDNNCHFDAVLVSFINFFTSVLATLVVFAVLGFKANVINEKCITQNSETIMKFLKMGNISQDIIPHHINLSTVTAEDYHLVYDIIQKVKEEEFPALHLNSCKIEEELNKAVQGTGLAFIAFTEAMTHFPASPFWSVMFFLMLVNLGLGSMFGTIEGIVTPIVDTFKVRKEILTVICCLLAFCIGLIFVQRSGNYFVTMFDDYSATLPLLIVVILENIAVCFVYGIDKFMEDLKDMLGFAPSRYYYYMWKYISPLMLLSLLIASVVNMGLSPPGYNAWIEDKASEEFLSYPTWGLVVCVSLVVFAILPVPVVFIVRRFNLIDDSSGNLASVTYKRGRVLKEPVNLEGDDTSLIHGKIPSEMPSPNFGKNIYRKQSGSPTLDTAPNGRYGIGYLMADIMPDMPESDL
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
17PhosphorylationRELDDDVTESVKDLL
CCCCCCHHHHHHHHH		29.5423090842
19PhosphorylationLDDDVTESVKDLLSN
CCCCHHHHHHHHHCC		25.7125159151
21UbiquitinationDDVTESVKDLLSNED
CCHHHHHHHHHCCCC		52.5221890473
25PhosphorylationESVKDLLSNEDAADD
HHHHHHHCCCCHHCC		45.5325159151
35UbiquitinationDAADDAFKTSELIVD
CHHCCHHHHCEEEEC		53.5121890473
36PhosphorylationAADDAFKTSELIVDG
HHCCHHHHCEEEECC		22.4523927012
37PhosphorylationADDAFKTSELIVDGQ
HCCHHHHCEEEECCC		30.8821815630
49PhosphorylationDGQEEKDTDVEEGSE
CCCCCCCCCCCCCCC		53.6821815630
55PhosphorylationDTDVEEGSEVEDERP
CCCCCCCCCCCCCCH		41.5723927012
66PhosphorylationDERPAWNSKLQYILA
CCCHHHHHHHHHHHH		24.8423927012
129PhosphorylationGQRIRRGSIGVWNYI
CCHHHCCCCCCHHCC		17.8524961811
137PhosphorylationIGVWNYISPKLGGIG
CCCHHCCCHHHCCHH		12.9624719451
187N-linked_GlycosylationDQCPLVKNASHTFVE
HHCCCEECCCCEEEC		38.91UniProtKB CARBOHYD
213N-linked_GlycosylationYWYREALNISSSISE
HHHHHHHCCCCCCCC		38.86UniProtKB CARBOHYD
383N-linked_GlycosylationMKFLKMGNISQDIIP
HHHHHHCCCCCCCCC		27.52UniProtKB CARBOHYD
394N-linked_GlycosylationDIIPHHINLSTVTAE
CCCCCCCCCCCCCHH		24.47UniProtKB CARBOHYD
551UbiquitinationVCFVYGIDKFMEDLK
HHHHHCHHHHHHHHH		33.5021890473
648PhosphorylationRFNLIDDSSGNLASV
ECCCCCCCCCCEEEE		36.0825002506
649PhosphorylationFNLIDDSSGNLASVT
CCCCCCCCCCEEEEE		38.4029978859
654PhosphorylationDSSGNLASVTYKRGR
CCCCCEEEEEEECCC		20.4021815630
656PhosphorylationSGNLASVTYKRGRVL
CCCEEEEEEECCCEE		22.3422210691
657PhosphorylationGNLASVTYKRGRVLK
CCEEEEEEECCCEEC		9.1322210691
658UbiquitinationNLASVTYKRGRVLKE
CEEEEEEECCCEECC		38.7221890473
664UbiquitinationYKRGRVLKEPVNLEG
EECCCEECCCCCCCC		58.0521890473
674PhosphorylationVNLEGDDTSLIHGKI
CCCCCCCCCCCCCCC		30.1229255136
675PhosphorylationNLEGDDTSLIHGKIP
CCCCCCCCCCCCCCC		32.1129255136
680UbiquitinationDTSLIHGKIPSEMPS
CCCCCCCCCCCCCCC		36.96-
683PhosphorylationLIHGKIPSEMPSPNF
CCCCCCCCCCCCCCC		50.4223927012
687PhosphorylationKIPSEMPSPNFGKNI
CCCCCCCCCCCCCCC		31.0329255136
692UbiquitinationMPSPNFGKNIYRKQS
CCCCCCCCCCCCCCC		35.71-
697UbiquitinationFGKNIYRKQSGSPTL
CCCCCCCCCCCCCCC		31.66-
699PhosphorylationKNIYRKQSGSPTLDT
CCCCCCCCCCCCCCC		44.2523927012
701PhosphorylationIYRKQSGSPTLDTAP
CCCCCCCCCCCCCCC		21.6929255136
703PhosphorylationRKQSGSPTLDTAPNG
CCCCCCCCCCCCCCC		38.6723927012
706PhosphorylationSGSPTLDTAPNGRYG
CCCCCCCCCCCCCCC		47.3122199227
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 S6A15_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S6A15_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 S6A15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEX2_HUMANTEX2physical
28514442
KLH36_HUMANKLHL36physical
28514442
TLCD1_HUMANTLCD1physical
28514442
TMTC4_HUMANTMTC4physical
28514442
GOGA5_HUMANGOLGA5physical
28514442
PLCC_HUMANAGPAT3physical
28514442
GPAT3_HUMANAGPAT9physical
28514442
CAV1_HUMANCAV1physical
28514442
TMPPE_HUMANTMPPEphysical
28514442
HACD2_HUMANPTPLBphysical
28514442
PLCB_HUMANAGPAT2physical
28514442
PTH2_HUMANPTRH2physical
28514442
ALG8_HUMANALG8physical
28514442
SPPL3_HUMANSPPL3physical
28514442
PXMP2_HUMANPXMP2physical
28514442
ACSL4_HUMANACSL4physical
28514442
EBP_HUMANEBPphysical
28514442
AT8B2_HUMANATP8B2physical
28514442
PIGU_HUMANPIGUphysical
28514442
PRAF3_HUMANARL6IP5physical
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 S6A15_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-699 ANDSER-701, AND MASS SPECTROMETRY.
"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-55 AND SER-687, AND MASSSPECTROMETRY.

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