EAA3_HUMAN - dbPTM
EAA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EAA3_HUMAN
UniProt AC P43005
Protein Name Excitatory amino acid transporter 3
Gene Name SLC1A1
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Cell membrane
Multi-pass membrane protein . Apical cell membrane
Multi-pass membrane protein .
Protein Description Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. [PubMed: 7914198]
Protein Sequence MGKPARKGCEWKRFLKNNWVLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILMRMLKLIILPLIISSMITGVAALDSNVSGKIGLRAVVYYFCTTLIAVILGIVLVVSIKPGVTQKVGEIARTGSTPEVSTVDAMLDLIRNMFPENLVQACFQQYKTKREEVKPPSDPEMNMTEESFTAVMTTAISKNKTKEYKIVGMYSDGINVLGLIVFCLVFGLVIGKMGEKGQILVDFFNALSDATMKIVQIIMCYMPLGILFLIAGKIIEVEDWEIFRKLGLYMATVLTGLAIHSIVILPLIYFIVVRKNPFRFAMGMAQALLTALMISSSSATLPVTFRCAEENNQVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITISITATSASIGAAGVPQAGLVTMVIVLSAVGLPAEDVTLIIAVDWLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSEVNIVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF
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
43N-linked_GlycosylationVLVREHSNLSTLEKF
HHHCCCCCCHHHHHH		39.66UniProtKB CARBOHYD
51PhosphorylationLSTLEKFYFAFPGEI
CHHHHHHHHHCCHHH		12.69-
130PhosphorylationKVGEIARTGSTPEVS
HHHHHHCCCCCCCCH		26.8523403867
133PhosphorylationEIARTGSTPEVSTVD
HHHCCCCCCCCHHHH		25.4723403867
137PhosphorylationTGSTPEVSTVDAMLD
CCCCCCCHHHHHHHH		22.5023403867
138PhosphorylationGSTPEVSTVDAMLDL
CCCCCCHHHHHHHHH		27.8123403867
178N-linked_GlycosylationPPSDPEMNMTEESFT
CCCCCCCCCCHHHHH		32.34UniProtKB CARBOHYD
185O-linked_GlycosylationNMTEESFTAVMTTAI
CCCHHHHHHHHHHHH		27.85OGP
193PhosphorylationAVMTTAISKNKTKEY
HHHHHHHHCCCCCCE		27.93-
195N-linked_GlycosylationMTTAISKNKTKEYKI
HHHHHHCCCCCCEEE		50.90UniProtKB CARBOHYD
201UbiquitinationKNKTKEYKIVGMYSD
CCCCCCEEEEEEECC		31.82-
476PhosphorylationELEQMDVSSEVNIVN
HHHHCCCCCCCEECC		19.2728857561
477PhosphorylationLEQMDVSSEVNIVNP
HHHCCCCCCCEECCH		45.4728857561
489PhosphorylationVNPFALESTILDNED
CCHHHCEEEECCCCC		22.9230108239
490PhosphorylationNPFALESTILDNEDS
CHHHCEEEECCCCCC		19.0430108239
497PhosphorylationTILDNEDSDTKKSYV
EECCCCCCCCCCCEE		40.7929759185
501UbiquitinationNEDSDTKKSYVNGGF
CCCCCCCCCEECCCE		49.4629967540
502PhosphorylationEDSDTKKSYVNGGFA
CCCCCCCCEECCCEE		35.5521945579
503PhosphorylationDSDTKKSYVNGGFAV
CCCCCCCEECCCEEE		13.5521945579
513PhosphorylationGGFAVDKSDTISFTQ
CCEEECCCCEEEEEE		35.2130266825
515PhosphorylationFAVDKSDTISFTQTS
EEECCCCEEEEEECC		26.1330266825
517PhosphorylationVDKSDTISFTQTSQF
ECCCCEEEEEECCCC		25.0830266825
519PhosphorylationKSDTISFTQTSQF--
CCCEEEEEECCCC--		24.9330266825
521PhosphorylationDTISFTQTSQF----
CEEEEEECCCC----		22.8023403867
522PhosphorylationTISFTQTSQF-----
EEEEEECCCC-----		21.5517525332
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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:18539596
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EAA3_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 EAA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPCA_HUMANPRKCAphysical
12843260
PRAF3_HUMANARL6IP5physical
11242046
A4_HUMANAPPphysical
21832049
LRAD1_HUMANLDLRAD1physical
25416956
NUMBL_HUMANNUMBLphysical
28514442
C2D1A_HUMANCC2D1Aphysical
28514442
FMC1_HUMANC7orf55physical
28514442
SNX3_HUMANSNX3physical
28514442
SHIP2_HUMANINPPL1physical
28514442
GOGA7_HUMANGOLGA7physical
28514442
ORML3_HUMANORMDL3physical
28514442
NFIP1_HUMANNDFIP1physical
28514442
PXMP2_HUMANPXMP2physical
28514442
SNX17_HUMANSNX17physical
28514442
HACD2_HUMANPTPLBphysical
28514442
CD320_HUMANCD320physical
28514442
CYTM_HUMANCST6physical
28514442
MPC2_HUMANMPC2physical
28514442
CHPT1_HUMANCHPT1physical
28514442
MICU2_HUMANMICU2physical
28514442
TIM14_HUMANDNAJC19physical
28514442
FGFR1_HUMANFGFR1physical
28514442
RAB8A_HUMANRAB8Aphysical
28514442
MIC27_HUMANAPOOLphysical
28514442
SBSN_HUMANSBSNphysical
28514442
PM34_HUMANSLC25A17physical
28514442
TR10B_HUMANTNFRSF10Bphysical
28514442
EPHA4_HUMANEPHA4physical
28514442
CXCR4_HUMANCXCR4physical
27173435
Drug and Disease Associations
Kegg Disease
H00911 Dicarboxylic aminoaciduria
OMIM Disease
222730Dicarboxylic aminoaciduria (DCBXA)
615232Schizophrenia 18 (SCZD18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00128L-Aspartic Acid
DB00230Pregabalin
Regulatory Network of EAA3_HUMAN

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Related Literatures of Post-Translational Modification

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