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Q9UHI5

- LAT2_HUMAN

UniProt

Q9UHI5 - LAT2_HUMAN

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Protein

Large neutral amino acids transporter small subunit 2

Gene

SLC7A8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. 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. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney.8 Publications

Kineticsi

  1. KM=221 µM for L-leucine4 Publications
  2. KM=64 µM for MeHg-L-cysteine4 Publications
  3. KM=161 µM for methionine4 Publications
  4. KM=978 µM for L-alanine4 Publications
  5. KM=89.35 µM for L-phenylalanine4 Publications
  6. KM=57.3 µM for L-tryptophan4 Publications
  7. KM=48.8 µM for L-tyrosine4 Publications

GO - Molecular functioni

  1. amino acid transmembrane transporter activity Source: UniProtKB
  2. L-amino acid transmembrane transporter activity Source: Ensembl
  3. neutral amino acid transmembrane transporter activity Source: ProtInc
  4. organic cation transmembrane transporter activity Source: UniProtKB
  5. peptide antigen binding Source: UniProtKB
  6. toxin transporter activity Source: UniProtKB

GO - Biological processi

  1. amino acid transport Source: UniProtKB
  2. blood coagulation Source: Reactome
  3. cellular amino acid metabolic process Source: ProtInc
  4. ion transport Source: Reactome
  5. leukocyte migration Source: Reactome
  6. metal ion homeostasis Source: UniProtKB
  7. neutral amino acid transport Source: UniProtKB
  8. organic cation transport Source: GOC
  9. response to toxic substance Source: UniProtKB
  10. toxin transport Source: GOC
  11. transmembrane transport Source: Reactome
  12. transport Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000092068-MONOMER.
ReactomeiREACT_12560. Basigin interactions.
REACT_13796. Amino acid transport across the plasma membrane.
SABIO-RKQ9UHI5.

Protein family/group databases

TCDBi2.A.3.8.20. the amino acid-polyamine-organocation (apc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Large neutral amino acids transporter small subunit 2
Alternative name(s):
L-type amino acid transporter 2
Short name:
hLAT2
Solute carrier family 7 member 8
Gene namesi
Name:SLC7A8
Synonyms:LAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:11066. SLC7A8.

Subcellular locationi

Cytoplasm. Basolateral cell membrane; Multi-pass membrane protein
Note: Localized to the cytoplasm when expressed alone but when coexpressed with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal tubules and small intestine epithelia of the villi.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35926.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535Large neutral amino acids transporter small subunit 2PRO_0000054273Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9UHI5.
PRIDEiQ9UHI5.

PTM databases

PhosphoSiteiQ9UHI5.

Expressioni

Tissue specificityi

Strongest expression is observed in kidney and moderate expression in placenta and brain, followed by liver, prostate, testis, ovary, lymph node, thymus, spleen, skeletal muscle and heart. Also expressed in fetal liver as well as in the retinal pigment epithelial cell line ARPE-19 and the intestinal epithelial cell line Caco-2.4 Publications

Inductioni

Activity in polarized intestinal cells is regulated by the association between SLC3A2/4F2 (in the SLC3A2/4F2-LAT2 heterodimer) and ICAM1.1 Publication

Gene expression databases

BgeeiQ9UHI5.
CleanExiHS_LAT2.
HS_SLC7A8.
ExpressionAtlasiQ9UHI5. baseline and differential.
GenevestigatoriQ9UHI5.

Interactioni

Subunit structurei

Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc.6 Publications

Protein-protein interaction databases

BioGridi116996. 2 interactions.
STRINGi9606.ENSP00000320378.

Structurei

3D structure databases

ProteinModelPortaliQ9UHI5.
SMRiQ9UHI5. Positions 39-382.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei40 – 6021HelicalSequence AnalysisAdd
BLAST
Transmembranei72 – 9221HelicalSequence AnalysisAdd
BLAST
Transmembranei113 – 13321HelicalSequence AnalysisAdd
BLAST
Transmembranei155 – 17521HelicalSequence AnalysisAdd
BLAST
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST
Transmembranei231 – 25121HelicalSequence AnalysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence AnalysisAdd
BLAST
Transmembranei310 – 33021HelicalSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Transmembranei424 – 44421HelicalSequence AnalysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0531.
GeneTreeiENSGT00760000119037.
HOVERGENiHBG000476.
InParanoidiQ9UHI5.
KOiK13781.
OMAiAFEPFQD.
PhylomeDBiQ9UHI5.
TreeFamiTF313355.

Family and domain databases

InterProiIPR002293. AA/rel_permease1.
IPR004760. L_AA_transporter.
[Graphical view]
PANTHERiPTHR11785. PTHR11785. 1 hit.
PfamiPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsiTIGR00911. 2A0308. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UHI5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEEGARHRNN TEKKHPGGGE SDASPEAGSG GGGVALKKEI GLVSACGIIV
60 70 80 90 100
GNIIGSGIFV SPKGVLENAG SVGLALIVWI VTGFITVVGA LCYAELGVTI
110 120 130 140 150
PKSGGDYSYV KDIFGGLAGF LRLWIAVLVI YPTNQAVIAL TFSNYVLQPL
160 170 180 190 200
FPTCFPPESG LRLLAAICLL LLTWVNCSSV RWATRVQDIF TAGKLLALAL
210 220 230 240 250
IIIMGIVQIC KGEYFWLEPK NAFENFQEPD IGLVALAFLQ GSFAYGGWNF
260 270 280 290 300
LNYVTEELVD PYKNLPRAIF ISIPLVTFVY VFANVAYVTA MSPQELLASN
310 320 330 340 350
AVAVTFGEKL LGVMAWIMPI SVALSTFGGV NGSLFTSSRL FFAGAREGHL
360 370 380 390 400
PSVLAMIHVK RCTPIPALLF TCISTLLMLV TSDMYTLINY VGFINYLFYG
410 420 430 440 450
VTVAGQIVLR WKKPDIPRPI KINLLFPIIY LLFWAFLLVF SLWSEPVVCG
460 470 480 490 500
IGLAIMLTGV PVYFLGVYWQ HKPKCFSDFI ELLTLVSQKM CVVVYPEVER
510 520 530
GSGTEEANED MEEQQQPMYQ PTPTKDKDVA GQPQP
Length:535
Mass (Da):58,382
Last modified:May 1, 2000 - v1
Checksum:iAC129146353F1E47
GO
Isoform 2 (identifier: Q9UHI5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-203: Missing.

Note: No experimental confirmation available.

Show »
Length:332
Mass (Da):37,184
Checksum:iE6DD8F71252E064D
GO
Isoform 3 (identifier: Q9UHI5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: MEEGARHRNN...VTEELVDPYK → MGQLFQCAVG...HHGDCTDMQR

Note: No experimental confirmation available.

Show »
Length:311
Mass (Da):34,602
Checksum:i4CF5A20AD230155C
GO
Isoform 4 (identifier: Q9UHI5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: MEEGARHRNN...GLRLLAAICL → MGQYGQELSW...LEGVPRFLKR

Note: No experimental confirmation available.

Show »
Length:430
Mass (Da):48,283
Checksum:i4F7293A07EBFE696
GO

Sequence cautioni

The sequence CAD62616.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251N → D in CAB40137. (PubMed:10080183)Curated
Sequence conflicti401 – 4011V → G in CAB40137. (PubMed:10080183)Curated
Sequence conflicti503 – 5031G → R in AAF05696. (PubMed:10391915)Curated
Sequence conflicti503 – 5031G → R in AAF05697. (PubMed:10391915)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 263263MEEGA…VDPYK → MGQLFQCAVGHPGSRHLHSW EAPGLGPDYHHGDCTDMQR in isoform 3. 1 PublicationVSP_046945Add
BLAST
Alternative sequencei1 – 203203Missing in isoform 2. 1 PublicationVSP_046946Add
BLAST
Alternative sequencei1 – 169169MEEGA…AAICL → MGQYGQELSWKCLVKAVCLQ EHSQPSQLLCTLLLCWCVLG RERPFRKAQSTSSPLEGVPR FLKR in isoform 4. 1 PublicationVSP_046947Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135828 mRNA. Translation: AAF05695.1.
AF135829 mRNA. Translation: AAF05696.1.
AF135830 mRNA. Translation: AAF05697.1.
AF171669 mRNA. Translation: AAF20381.1.
Y18483 mRNA. Translation: CAB40137.1.
AB037669 mRNA. Translation: BAB21519.1.
BX248288 mRNA. Translation: CAD62616.1. Different initiation.
AK296702 mRNA. Translation: BAG59296.1.
AK300384 mRNA. Translation: BAG62118.1.
AK313465 mRNA. Translation: BAG36251.1.
AL117258 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66181.1.
CH471078 Genomic DNA. Translation: EAW66182.1.
BC052250 mRNA. Translation: AAH52250.1.
CCDSiCCDS41924.1. [Q9UHI5-2]
CCDS58304.1. [Q9UHI5-3]
CCDS58305.1. [Q9UHI5-4]
CCDS9590.1. [Q9UHI5-1]
RefSeqiNP_001253965.1. NM_001267036.1. [Q9UHI5-4]
NP_001253966.1. NM_001267037.1. [Q9UHI5-3]
NP_036376.2. NM_012244.3. [Q9UHI5-1]
NP_877392.1. NM_182728.2. [Q9UHI5-2]
UniGeneiHs.596643.

Genome annotation databases

EnsembliENST00000316902; ENSP00000320378; ENSG00000092068. [Q9UHI5-1]
ENST00000422941; ENSP00000416398; ENSG00000092068. [Q9UHI5-3]
ENST00000453702; ENSP00000391577; ENSG00000092068. [Q9UHI5-2]
ENST00000529705; ENSP00000434345; ENSG00000092068. [Q9UHI5-4]
GeneIDi23428.
KEGGihsa:23428.
UCSCiuc001wix.4. human. [Q9UHI5-1]

Polymorphism databases

DMDMi12643348.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135828 mRNA. Translation: AAF05695.1 .
AF135829 mRNA. Translation: AAF05696.1 .
AF135830 mRNA. Translation: AAF05697.1 .
AF171669 mRNA. Translation: AAF20381.1 .
Y18483 mRNA. Translation: CAB40137.1 .
AB037669 mRNA. Translation: BAB21519.1 .
BX248288 mRNA. Translation: CAD62616.1 . Different initiation.
AK296702 mRNA. Translation: BAG59296.1 .
AK300384 mRNA. Translation: BAG62118.1 .
AK313465 mRNA. Translation: BAG36251.1 .
AL117258 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66181.1 .
CH471078 Genomic DNA. Translation: EAW66182.1 .
BC052250 mRNA. Translation: AAH52250.1 .
CCDSi CCDS41924.1. [Q9UHI5-2 ]
CCDS58304.1. [Q9UHI5-3 ]
CCDS58305.1. [Q9UHI5-4 ]
CCDS9590.1. [Q9UHI5-1 ]
RefSeqi NP_001253965.1. NM_001267036.1. [Q9UHI5-4 ]
NP_001253966.1. NM_001267037.1. [Q9UHI5-3 ]
NP_036376.2. NM_012244.3. [Q9UHI5-1 ]
NP_877392.1. NM_182728.2. [Q9UHI5-2 ]
UniGenei Hs.596643.

3D structure databases

ProteinModelPortali Q9UHI5.
SMRi Q9UHI5. Positions 39-382.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116996. 2 interactions.
STRINGi 9606.ENSP00000320378.

Chemistry

BindingDBi Q9UHI5.
DrugBanki DB00160. L-Alanine.
DB01235. L-DOPA.
DB00130. L-Glutamine.
DB00120. L-Phenylalanine.

Protein family/group databases

TCDBi 2.A.3.8.20. the amino acid-polyamine-organocation (apc) family.

PTM databases

PhosphoSitei Q9UHI5.

Polymorphism databases

DMDMi 12643348.

Proteomic databases

PaxDbi Q9UHI5.
PRIDEi Q9UHI5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316902 ; ENSP00000320378 ; ENSG00000092068 . [Q9UHI5-1 ]
ENST00000422941 ; ENSP00000416398 ; ENSG00000092068 . [Q9UHI5-3 ]
ENST00000453702 ; ENSP00000391577 ; ENSG00000092068 . [Q9UHI5-2 ]
ENST00000529705 ; ENSP00000434345 ; ENSG00000092068 . [Q9UHI5-4 ]
GeneIDi 23428.
KEGGi hsa:23428.
UCSCi uc001wix.4. human. [Q9UHI5-1 ]

Organism-specific databases

CTDi 23428.
GeneCardsi GC14M023594.
HGNCi HGNC:11066. SLC7A8.
MIMi 604235. gene.
neXtProti NX_Q9UHI5.
PharmGKBi PA35926.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0531.
GeneTreei ENSGT00760000119037.
HOVERGENi HBG000476.
InParanoidi Q9UHI5.
KOi K13781.
OMAi AFEPFQD.
PhylomeDBi Q9UHI5.
TreeFami TF313355.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000092068-MONOMER.
Reactomei REACT_12560. Basigin interactions.
REACT_13796. Amino acid transport across the plasma membrane.
SABIO-RK Q9UHI5.

Miscellaneous databases

GeneWikii SLC7A8.
GenomeRNAii 23428.
NextBioi 45663.
PROi Q9UHI5.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHI5.
CleanExi HS_LAT2.
HS_SLC7A8.
ExpressionAtlasi Q9UHI5. baseline and differential.
Genevestigatori Q9UHI5.

Family and domain databases

InterProi IPR002293. AA/rel_permease1.
IPR004760. L_AA_transporter.
[Graphical view ]
PANTHERi PTHR11785. PTHR11785. 1 hit.
Pfami PF13520. AA_permease_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006060. AA_transporter. 1 hit.
TIGRFAMsi TIGR00911. 2A0308. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INHIBITION.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT.
    Tissue: Melanocyte.
  3. "SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance."
    Borsani G., Bassi M.T., Sperandeo M.P., De Grandi A., Buoninconti A., Riboni M., Manzoni M., Incerti B., Pepe A., Andria G., Ballabio A., Sebastio G.
    Nat. Genet. 21:297-301(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  4. "Reabsorption of neutral amino acids mediated by amino acid transporter LAT2 and TAT1 in the basolateral membrane of proximal tubule."
    Park S.Y., Kim J.-K., Kim I.J., Choi B.K., Jung K.Y., Lee S., Park K.J., Chairoungdua A., Kanai Y., Endou H., Kim D.K.
    Arch. Pharm. Res. 28:421-432(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INHIBITION.
    Tissue: Kidney.
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Hippocampus, Placenta and Tongue.
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Skin.
  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.
  11. "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.
  12. "CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia."
    Liu X., Charrier L., Gewirtz A., Sitaraman S., Merlin D.
    J. Biol. Chem. 278:23672-23677(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INDUCTION.
  13. "Identification and functional characterization of a Na(+)-independent large neutral amino acid transporter (LAT2) on ARPE-19 cells."
    Gandhi M.D., Pal D., Mitra A.K.
    Int. J. Pharm. 275:189-200(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INHIBITION.
  14. "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.
  15. "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.

Entry informationi

Entry nameiLAT2_HUMAN
AccessioniPrimary (citable) accession number: Q9UHI5
Secondary accession number(s): B2R8Q4
, B4DKT4, B4DTV6, D3DS46, F2Z2J4, Q86U05, Q9UKQ6, Q9UKQ7, Q9UKQ8, Q9Y445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

L-leucine transport activity inhibited by small zwitterionic amino acids (i.e. glycine, alanine, serine, threonine asparginine, glutamine, methionine, leucine, isoleucine, valine, phenylalanine, tyrosine, tryptophan, histidine and cysteine) and by glutamine and asparginine. Methionine uptake was inhibited by the L-system substrates L-leucine, 2-amino-bicyclo-(2,2,1)-heptane-2-carboxylate (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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3