UniProt Accession

 LAT1_HUMAN; Q01650; Q9UBN8; Q9UP15; Q9UQC0 

Genbank Protein ID

 AF077866; AF104032; AB018542; AB018009; AB017908; BC042600; M80244 

Genbank Nucleotide ID

 AAC61479.1; AAD20464.1; BAA33851.1; BAA84648.1; BAA75746.1; AAH42600.1; AAA35780.1 

Protein Name

 Large neutral amino acids transporter small subunit 1 

Protein Synonyms/Alias

 4F2 light chain; 4F2 LC; 4F2LC; CD98 light chain; Integral membrane protein E16; L-type amino acid transporter 1; hLAT1; Solute carrier family 7 member 5; y+ system cationic amino acid transporter 

Gene Name

 SLC7A5 

Gene Synonyms/Alias

 CD98LC; LAT1; MPE16 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
19	AAPAAEEKEEAREKM	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
25	EKEEAREKMLAAKSA	ubiquitination	[4, 5, 6, 8, 9]
30	REKMLAAKSADGSAP	ubiquitination	[1, 2, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14]
483	VWWKNKPKWLLQGIF	ubiquitination	[5]

Reference

 [1] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [2] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [13] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [14] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional Description

 Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood- brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L- nitrosocysteine (L-CNSO) across the transmembrane. May play an important role in high-grade gliomas. Mediates blood-to-retina L- leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts. 

Sequence Annotation

 MOD_RES 31 31 Phosphoserine.
 MOD_RES 45 45 Phosphothreonine.
 CARBOHYD 49 49 N-linked (GlcNAc...) (Potential).
 CARBOHYD 230 230 N-linked (GlcNAc...) (Potential).
 CARBOHYD 340 340 N-linked (GlcNAc...) (Potential).
 CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Amino-acid transport; Cell membrane; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein; Isopeptide bond; Membrane; Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Transport; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 507 AA 

Protein Sequence

Gene Ontology

 GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0015179; F:L-amino acid transmembrane transporter activity; IEA:Compara.
 GO:0015175; F:neutral amino acid transmembrane transporter activity; TAS:ProtInc.
 GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0007399; P:nervous system development; IEA:UniProtKB-KW. 

Interpro

 IPR002293; AA/rel_permease1.
 IPR004760; L_AA_transporter. 

Pfam

  

SMART

  

PROSITE

  

PRINTS