AAAT_HUMAN - dbPTM
AAAT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAAT_HUMAN
UniProt AC Q15758
Protein Name Neutral amino acid transporter B(0)
Gene Name SLC1A5
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Cell membrane
Multi-pass membrane protein . Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids. [PubMed: 8702519 Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development]
Protein Sequence MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGSRDQVRRCLRANLLVLLTVVAVVAGVALGLGVSGAGGALALGPERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLDPGALGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINASVGAAGSAENAPSKEVLDSFLDLARNIFPSNLVSAAFRSYSTTYEERNITGTRVKVPVGQEVEGMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNEATMVLVSWIMWYAPVGIMFLVAGKIVEMEDVGLLFARLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEENNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLSQQSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVNLPVDHISLILAVDWLVDRSCTVLNVEGDALGAGLLQNYVDRTESRSTEPELIQVKSELPLDPLPVPTEEGNPLLKHYRGPAGDATVASEKESVM
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
1Acetylation-------MVADPPRD
-------CCCCCCCC		5.1722814378
2 (in isoform 2)Phosphorylation-9.2226552605
3 (in isoform 2)Phosphorylation-23.4626552605
4 (in isoform 2)Phosphorylation-42.1826552605
5 (in isoform 2)Phosphorylation-18.9826552605
6 (in isoform 2)Phosphorylation-53.9426552605
9PhosphorylationVADPPRDSKGLAAAE
CCCCCCCCCCCCCCC		29.8729255136
10UbiquitinationADPPRDSKGLAAAEP
CCCCCCCCCCCCCCC		63.3321906983
18PhosphorylationGLAAAEPTANGGLAL
CCCCCCCCCCCCEEE		25.0229978859
27PhosphorylationNGGLALASIEDQGAA
CCCEEEEEHHHCCCC		27.6228188228
38PhosphorylationQGAAAGGYCGSRDQV
CCCCCCCCCCCHHHH		7.85-
39S-palmitoylationGAAAGGYCGSRDQVR
CCCCCCCCCCHHHHH		4.5129575903
163N-linked_GlycosylationGAASAAINASVGAAG
CHHHHHHHHCCCCCC		22.8019349973
163N-linked_GlycosylationGAASAAINASVGAAG
CHHHHHHHHCCCCCC		22.8019349973
178UbiquitinationSAENAPSKEVLDSFL
CCCCCCCHHHHHHHH		51.27-
183PhosphorylationPSKEVLDSFLDLARN
CCHHHHHHHHHHHHH		24.4521712546
194PhosphorylationLARNIFPSNLVSAAF
HHHHHCCHHHHHHHH		31.8521712546
198PhosphorylationIFPSNLVSAAFRSYS
HCCHHHHHHHHHHHC		19.6220068231
204PhosphorylationVSAAFRSYSTTYEER
HHHHHHHHCCCCCCC		13.0428985074
206PhosphorylationAAFRSYSTTYEERNI
HHHHHHCCCCCCCCC		25.7628985074
212N-linked_GlycosylationSTTYEERNITGTRVK
CCCCCCCCCCCCEEE		39.1819349973
212N-linked_GlycosylationSTTYEERNITGTRVK
CCCCCCCCCCCCEEE		39.1819349973
214PhosphorylationTYEERNITGTRVKVP
CCCCCCCCCCEEEEC		35.7328985074
247UbiquitinationVFGVALRKLGPEGEL
HHHHHHHHHCCCCHH		59.6621906983
2472-HydroxyisobutyrylationVFGVALRKLGPEGEL
HHHHHHHHHCCCCHH		59.66-
274 (in isoform 2)Ubiquitination-1.5020972266
274UbiquitinationMVLVSWIMWYAPVGI
HHHHHHHHHHHCCHH		1.5021890473
294UbiquitinationGKIVEMEDVGLLFAR
CCEEEHHHHHHHHHH		38.1721890473
300UbiquitinationEDVGLLFARLGKYIL
HHHHHHHHHHHHHHH		13.0321890473
320UbiquitinationHAIHGLLVLPLIYFL
HHHHHHHHHHHHHHH		6.6021890473
372UbiquitinationEENNGVAKHISRFIL
HHCCCHHHHHHHHHE		38.7821906983
467S-palmitoylationDWLVDRSCTVLNVEG
HHHHCCCCEEEEECC		2.9629575903
489PhosphorylationLQNYVDRTESRSTEP
HHHHHHCCCCCCCCC		33.5720873877
491PhosphorylationNYVDRTESRSTEPEL
HHHHCCCCCCCCCCC		30.8028176443
493PhosphorylationVDRTESRSTEPELIQ
HHCCCCCCCCCCCEE		46.5329255136
494PhosphorylationDRTESRSTEPELIQV
HCCCCCCCCCCCEEE		55.2229255136
502UbiquitinationEPELIQVKSELPLDP
CCCCEEECCCCCCCC		23.1021890473
502UbiquitinationEPELIQVKSELPLDP
CCCCEEECCCCCCCC		23.1021906983
503PhosphorylationPELIQVKSELPLDPL
CCCEEECCCCCCCCC		45.5729255136
514PhosphorylationLDPLPVPTEEGNPLL
CCCCCCCCCCCCCCH		47.0727050516
522SumoylationEEGNPLLKHYRGPAG
CCCCCCHHHCCCCCC		46.39-
522UbiquitinationEEGNPLLKHYRGPAG
CCCCCCHHHCCCCCC		46.3921890473
522AcetylationEEGNPLLKHYRGPAG
CCCCCCHHHCCCCCC		46.3927452117
522UbiquitinationEEGNPLLKHYRGPAG
CCCCCCHHHCCCCCC		46.3921890473
524PhosphorylationGNPLLKHYRGPAGDA
CCCCHHHCCCCCCCC		18.7121945579
525MethylationNPLLKHYRGPAGDAT
CCCHHHCCCCCCCCC		44.32115917057
532PhosphorylationRGPAGDATVASEKES
CCCCCCCCHHHHHHC		22.7321945579
535PhosphorylationAGDATVASEKESVM-
CCCCCHHHHHHCCC-		44.8829255136
537UbiquitinationDATVASEKESVM---
CCCHHHHHHCCC---		53.4421906983
537AcetylationDATVASEKESVM---
CCCHHHHHHCCC---		53.4425953088
5372-HydroxyisobutyrylationDATVASEKESVM---
CCCHHHHHHCCC---		53.44-
539PhosphorylationTVASEKESVM-----
CHHHHHHCCC-----		34.2523401153
541SulfoxidationASEKESVM-------
HHHHHCCC-------		6.7321406390
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 AAAT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAAT_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 AAAT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT35_HUMANMRPS35physical
22939629
NB5R3_HUMANCYB5R3physical
22939629
MCU_HUMANMCUphysical
22939629
SCMC1_HUMANSLC25A24physical
28514442
ATP9A_HUMANATP9Aphysical
28514442
S2546_HUMANSLC25A46physical
28514442
ZDH18_HUMANZDHHC18physical
28514442
CD47_HUMANCD47physical
28514442
HACD2_HUMANPTPLBphysical
28514442
SPPL3_HUMANSPPL3physical
28514442
ABCB8_HUMANABCB8physical
28514442
MTCH2_HUMANMTCH2physical
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
DB00174L-Asparagine
DB00130L-Glutamine
Regulatory Network of AAAT_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-532, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-535, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-532, AND MASS SPECTROMETRY.

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