Q01650 (LAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Large neutral amino acids transporter small subunit 1

Alternative name(s):
4F2 light chain
Short name=4F2 LC
Short name=4F2LC
CD98 light chain
Integral membrane protein E16
L-type amino acid transporter 1
Short name=hLAT1
Solute carrier family 7 member 5
y+ system cationic amino acid transporter

Gene names

Name:	SLC7A5
Synonyms:	CD98LC, LAT1, MPE16

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.4 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.22
Subunit structure	Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. Ref.1 Ref.2 Ref.4 Ref.10 Ref.11 Ref.12 Ref.15 Ref.18
Subcellular location	Cytoplasm › cytosol. Apical cell membrane; Multi-pass membrane protein. Note: Located to the plasma membrane by SLC3A2/4F2hc. Localized to the apical membrane of placental syncytiophoblastic cells. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells By similarity. Ref.10 Ref.11 Ref.13 Ref.15 Ref.17 Ref.19
Tissue specificity	Expressed abundantly in adult lung, liver, brain, skeletal muscle, placenta, bone marrow, testis, resting lymphocytes and monocytes, and in fetal liver. Weaker expression in thymus, cornea, retina, peripheral leukocytes, spleen, kidney, colon and lymph node. During gestation, expression in the placenta was significantly stronger at full-term than at the mid-trimester stage. Also expressed in all human tumor cell lines tested and in the astrocytic process of primary astrocytic gliomas. Expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco-2. Ref.2 Ref.3 Ref.4 Ref.7 Ref.11 Ref.13 Ref.16 Ref.17 Ref.19
Induction	Expression induced in quiescent peripheral blood lymphocytes after treatment with phorbol myristate acetate (PMA) and phytohemagglutinin (PHA). Expression and the uptake of leucine is stimulated in mononuclear, cytotrophoblast-like choriocarcinoma cells by combined treatment with PMA and calcium ionophore. Ref.7 Ref.13
Miscellaneous	The uptake of leucine, tyrosine and tryptophan is inhibited by the different iodothyronines, in particular T3. Leucine transport is also inhibited by small zwitterionic amino acids (i.e. glycine, alanine, serine, threonine and cysteine) and by glutamine and asparginine. The uptake of T3 is almost completely blocked by coincubation with leucine, tryptophan, tyrosine, and phenylalanine, or 2-amino-bicyclo-(2,2,1)-heptane-2-carboxylate (BCH). Methionine uptake was inhibited by the L-system substrates L-leucine, BCH, L-cysteine and by the MeHg-L-cysteine complex and structurally related S-ethyl-L-cysteine. MeHg-L-cysteine uptake is inhibited by L-methionine, L-leucine, BCH and S-ethyl-L-cysteine. L-leucine uptake was inhibited by L-CNSO. Tyrosine uptake in fibroblasts was inhibited by D-methionine, and methyl-aminoisobutyric acid (MeAIB).
Sequence similarities	Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family. [View classification]
Biophysicochemical properties	Kinetic parameters: KM=7.9 µM for T4 (in the presence of choline chloride) Ref.9 Ref.12 Ref.14 Ref.15 Ref.22 KM=0.8 µM for T3 (in the presence of choline chloride) KM=12.5 µM for reverse triiodothyronine (rT3) (in the presence of choline chloride) KM=7.9 µM for 3,3'-diiodothyronine (in the presence of choline chloride) KM=46 µM for leucine (in the presence of choline chloride) KM=19 µM for tryptophan (in the presence of choline chloride) KM=32 µM for L-leucine KM=10 mM for L-alanine KM=2.2 mM for L-glutamine KM=35 µM for L-histidine KM=740 µM for L-phenylalanine KM=98 µM for MeHg-L-cysteine KM=99 µM for methionine KM=55.2 µM for phenylalanine (in T24 human bladder carcinoma cells) KM=60.4 µM for tyrosine (in T24 human bladder carcinoma cells) KM=16.4 µM for tyrosine (in human fibroblasts) KM=138 µM for Dopa (in T24 human bladder carcinoma cells) KM=96.5 µM for 3-O-methyldopa (in T24 human bladder carcinoma cells) KM=153 µM for alpha-methyltyrosine (in T24 human bladder carcinoma cells) KM=216 µM for alpha-methyldopa (in T24 human bladder carcinoma cells) KM=191 µM for gabapentin (in T24 human bladder carcinoma cells) KM=7.3 µM for triiodothyronine (in T24 human bladder carcinoma cells) KM=162 µM for thyroxine (in T24 human bladder carcinoma cells) KM=75.3 µM for melphanan (in T24 human bladder carcinoma cells) KM=156 µM for BCH (in T24 human bladder carcinoma cells)

Ontologies

Keywords
Biological process	Amino-acid transport Differentiation Neurogenesis Transport
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cellular amino acid metabolic process Traceable author statement Ref.1. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome nervous system development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	L-amino acid transmembrane transporter activity Inferred from electronic annotation. Source: Compara neutral amino acid transmembrane transporter activity Traceable author statement Ref.1. Source: ProtInc peptide antigen binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 507	507	Large neutral amino acids transporter small subunit 1		PRO_0000054270
Regions
	Transmembrane	50 – 70	21	Helical; Potential
	Transmembrane	84 – 104	21	Helical; Potential
	Transmembrane	120 – 140	21	Helical; Potential
	Transmembrane	146 – 166	21	Helical; Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Transmembrane	199 – 219	21	Helical; Potential
	Transmembrane	243 – 263	21	Helical; Potential
	Transmembrane	274 – 294	21	Helical; Potential
	Transmembrane	319 – 339	21	Helical; Potential
	Transmembrane	396 – 416	21	Helical; Potential
	Transmembrane	431 – 451	21	Helical; Potential
	Transmembrane	458 – 478	21	Helical; Potential
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.24 Ref.25 Ref.27
	Modified residue	45	1	Phosphothreonine Ref.25
	Glycosylation	49	1	N-linked (GlcNAc...) Potential
	Glycosylation	230	1	N-linked (GlcNAc...) Potential
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Cross-link	19		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
	Cross-link	30		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Natural variations
	Natural variant	230	1	N → K. Ref.1 Corresponds to variant rs1060250 [ dbSNP | Ensembl ].		VAR_048157
Experimental info
	Sequence conflict	15	1	A → V in BAA75746. Ref.5
	Sequence conflict	29 – 31	3	AKS → SKR in BAA75746. Ref.5
	Sequence conflict	35	1	S → A in BAA75746. Ref.5
	Sequence conflict	62	1	T → A in BAA75746. Ref.5
	Sequence conflict	88	1	V → M in BAA75746. Ref.5
	Sequence conflict	154	1	T → A in BAA75746. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q01650 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 767F3C60B62C0F02	FASTA	507	55,010
	10 20 30 40 50 60 MAGAGPKRRA LAAPAAEEKE EAREKMLAAK SADGSAPAGE GEGVTLQRNI TLLNGVAIIV 70 80 90 100 110 120 GTIIGSGIFV TPTGVLKEAG SPGLALVVWA ACGVFSIVGA LCYAELGTTI SKSGGDYAYM 130 140 150 160 170 180 LEVYGSLPAF LKLWIELLII RPSSQYIVAL VFATYLLKPL FPTCPVPEEA AKLVACLCVL 190 200 210 220 230 240 LLTAVNCYSV KAATRVQDAF AAAKLLALAL IILLGFVQIG KGDVSNLDPN FSFEGTKLDV 250 260 270 280 290 300 GNIVLALYSG LFAYGGWNYL NFVTEEMINP YRNLPLAIII SLPIVTLVYV LTNLAYFTTL 310 320 330 340 350 360 STEQMLSSEA VAVDFGNYHL GVMSWIIPVF VGLSCFGSVN GSLFTSSRLF FVGSREGHLP 370 380 390 400 410 420 SILSMIHPQL LTPVPSLVFT CVMTLLYAFS KDIFSVINFF SFFNWLCVAL AIIGMIWLRH 430 440 450 460 470 480 RKPELERPIK VNLALPVFFI LACLFLIAVS FWKTPVECGI GFTIILSGLP VYFFGVWWKN 490 500 KPKWLLQGIF STTVLCQKLM QVVPQET

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family." Mastroberardino L., Spindler B., Pfeiffer R., Skelly P.J., Loffing J., Shoemaker C.B., Verrey F. Nature 395:288-291(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, VARIANT LYS-230.
[2]	"Human LAT1, a subunit of system L amino acid transporter: molecular cloning and transport function." Prasad P.D., Wang H., Huang W., Kekuda R., Rajan D.P., Leibach F.H., Ganapathy V. Biochem. Biophys. Res. Commun. 255:283-288(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY. Tissue: Placenta.
[3]	"Primary structure of the light chain of fusion regulatory protein-1/CD98/4F2 predicts a protein with multiple transmembrane domains that is almost identical to the amino acid transporter E16." Tsurudome M., Ito M., Takebayashi S., Okumura K., Nishio M., Kawano M., Kusagawa S., Komada H., Ito Y. J. Immunol. 162:2462-2466(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
[4]	"Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines." Yanagida O., Kanai Y., Chairoungdua A., Kim D.K., Segawa H., Nii T., Cha S.H., Matsuo H., Fukushima J., Fukasawa Y., Tani Y., Taketani Y., Uchino H., Kim J.Y., Inatomi J., Okayasu I., Miyamoto K., Takeda E., Goya T., Endou H. Biochim. Biophys. Acta 1514:291-302(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY. Tissue: Ovary.
[5]	"Human 4F2 light chain: amino acid transporter." Minato N., Iwai K., Takizawa C., Nakamura E. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[7]	"A novel transiently expressed, integral membrane protein linked to cell activation. Molecular cloning via the rapid degradation signal AUUUA." Gaugitsch H.W., Prieschl E.E., Kalthoff F., Huber N.E., Baumruker T. J. Biol. Chem. 267:11267-11273(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-507, TISSUE SPECIFICITY, INDUCTION. Tissue: Peripheral blood lymphocyte.
[8]	"Identification of a membrane protein, LAT-2, that co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids." Pineda M., Fernandez E., Torrents D., Estevez R., Lopez C., Camps M., Lloberas J., Zorzano A., Palacin M. J. Biol. Chem. 274:19738-19744(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INHIBITION.
[9]	"LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine." Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F., Kuehn L.C. J. Biol. Chem. 274:34948-34954(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]	"Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains." Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V., Lang F., Broeer S. Biochem. J. 355:725-731(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[11]	"Role of the System L permease LAT1 in amino acid and iodothyronine transport in placenta." Ritchie J.W.A., Taylor P.M. Biochem. J. 356:719-725(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INHIBITION.
[12]	"Thyroid hormone transport by the heterodimeric human system L amino acid transporter." Friesema E.C.H., Docter R., Moerings E.P.C.M., Verrey F., Krenning E.P., Hennemann G., Visser T.J. Endocrinology 142:4339-4348(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INHIBITION.
[13]	"Expression and regulation of 4F2hc and hLAT1 in human trophoblasts." Okamoto Y., Sakata M., Ogura K., Yamamoto T., Yamaguchi M., Tasaka K., Kurachi H., Tsurudome M., Murata Y. Am. J. Physiol. 282:C196-C204(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[14]	"Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2." Simmons-Willis T.A., Koh A.S., Clarkson T.W., Ballatori N. Biochem. J. 367:239-246(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION.
[15]	"Characterization of the system L amino acid transporter in T24 human bladder carcinoma cells." Kim D.K., Kanai Y., Choi H.W., Tangtrongsup S., Chairoungdua A., Babu E., Tachampa K., Anzai N., Iribe Y., Endou H. Biochim. Biophys. Acta 1565:112-121(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INHIBITION.
[16]	"Identification and functional characterization of a Na+-independent large neutral amino acid transporter, LAT1, in human and rabbit cornea." Jain-Vakkalagadda B., Dey S., Pal D., Mitra A.K. Invest. Ophthalmol. Vis. Sci. 44:2919-2927(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[17]	"Expression of LAT1 and LAT2 amino acid transporters in human and rat intestinal epithelial cells." Fraga S., Pinho M.J., Soares-da-Silva P. Amino Acids 29:229-233(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[18]	"Identification of stereoselective transporters for S-nitroso-L-cysteine: role of LAT1 and LAT2 in biological activity of S-nitrosothiols." Li S., Whorton A.R. J. Biol. Chem. 280:20102-20110(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, INHIBITION.
[19]	"L-type amino acid transporter 1 as a potential molecular target in human astrocytic tumors." Nawashiro H., Otani N., Shinomiya N., Fukui S., Ooigawa H., Shima K., Matsuo H., Kanai Y., Endou H. Int. J. Cancer 119:484-492(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[20]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-30, MASS SPECTROMETRY.
[21]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[22]	"Functional characterization of tyrosine transport in fibroblast cells from healthy controls." Vumma R., Wiesel F.A., Flyckt L., Bjerkenstedt L., Venizelos N. Neurosci. Lett. 434:56-60(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION.
[23]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[24]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY.
[25]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND THR-45, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF077866 mRNA. Translation: AAC61479.1. AF104032 mRNA. Translation: AAD20464.1. AB018542 mRNA. Translation: BAA33851.1. AB018009 mRNA. Translation: BAA84648.1. AB017908 mRNA. Translation: BAA75746.1. BC042600 mRNA. Translation: AAH42600.1. M80244 mRNA. Translation: AAA35780.1.
IPI	IPI00008986.
PIR	JG0165.
RefSeq	NP_003477.4. NM_003486.5.
UniGene	Hs.513797.
3D structure databases
ProteinModelPortal	Q01650.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01650. 2 interactions.
STRING	9606.ENSP00000261622.
PTM databases
PhosphoSite	Q01650.
Polymorphism databases
DMDM	12643412.
Proteomic databases
PeptideAtlas	Q01650.
PRIDE	Q01650.
Protocols and materials databases
DNASU	8140.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261622; ENSP00000261622; ENSG00000103257. ENST00000565644; ENSP00000454323; ENSG00000103257.
GeneID	8140.
KEGG	hsa:8140.
UCSC	uc002fkm.3. human.
Organism-specific databases
CTD	8140.
GeneCards	GC16M087863.
HGNC	HGNC:11063. SLC7A5.
MIM	600182. gene.
neXtProt	NX_Q01650.
PharmGKB	PA35923.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000098892.
HOVERGEN	HBG000476.
InParanoid	Q01650.
KO	K13780.
OMA	PIVTAVY.
PhylomeDB	Q01650.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000103257-MONOMER.
Reactome	REACT_15518. Transmembrane transport of small molecules. REACT_19419. Amino acid and oligopeptide SLC transporters. REACT_604. Hemostasis.
SABIO-RK	Q01650.
Gene expression databases
Bgee	Q01650.
CleanEx	HS_SLC7A5.
Genevestigator	Q01650.
GermOnline	ENSG00000103257. Homo sapiens.
Family and domain databases
InterPro	IPR002293. AA/rel_permease1. IPR004760. L_AA_transporter. [Graphical view]
PANTHER	PTHR11785. PTHR11785. 1 hit.
PIRSF	PIRSF006060. AA_transporter. 1 hit.
TIGRFAMs	TIGR00911. 2A0308. 1 hit.
ProtoNet	Search...
Other
BindingDB	Q01650.
ChEMBL	CHEMBL4459.
ChiTaRS	SLC7A5. human.
GenomeRNAi	8140.
NextBio	30811.
SOURCE	Search...

Entry information

Entry name

LAT1_HUMAN

Accession

Primary (citable) accession number: Q01650
Secondary accession number(s): Q9UBN8, Q9UP15, Q9UQC0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 24, 2001
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.