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Q9UHI5 (LAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SLC7A8
Synonyms:LAT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.4 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Subunit structure

Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc. Ref.1 Ref.2 Ref.4 Ref.10 Ref.12 Ref.15

Subcellular location

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. Ref.1 Ref.4 Ref.14

Tissue specificity

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. Ref.1 Ref.4 Ref.13 Ref.14

Induction

Activity in polarized intestinal cells is regulated by the association between SLC3A2/4F2 (in the SLC3A2/4F2-LAT2 heterodimer) and ICAM1. Ref.12

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.

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=221 µM for L-leucine Ref.1 Ref.4 Ref.11 Ref.13

KM=64 µM for MeHg-L-cysteine

KM=161 µM for methionine

KM=978 µM for L-alanine

KM=89.35 µM for L-phenylalanine

KM=57.3 µM for L-tryptophan

KM=48.8 µM for L-tyrosine

Sequence caution

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

Ontologies

Keywords
   Biological processAmino-acid transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamino acid transport

Inferred from direct assay Ref.1Ref.2Ref.4. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cellular amino acid metabolic process

Traceable author statement Ref.1. Source: ProtInc

ion transport

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

metal ion homeostasis

Non-traceable author statement Ref.10. Source: UniProtKB

neutral amino acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

organic cation transport

Inferred from direct assay Ref.11. Source: GOC

response to toxic substance

Non-traceable author statement Ref.10. Source: UniProtKB

toxin transport

Inferred from direct assay Ref.11. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionL-amino acid transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

amino acid transmembrane transporter activity

Inferred from direct assay Ref.1Ref.2Ref.4. Source: UniProtKB

neutral amino acid transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

organic cation transmembrane transporter activity

Inferred from direct assay Ref.11. Source: UniProtKB

peptide antigen binding

Inferred from sequence or structural similarity. Source: UniProtKB

toxin transporter activity

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UHI5-1)

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.
Isoform 2 (identifier: Q9UHI5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-203: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UHI5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-263: MEEGARHRNN...VTEELVDPYK → MGQLFQCAVG...HHGDCTDMQR
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9UHI5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: MEEGARHRNN...GLRLLAAICL → MGQYGQELSW...LEGVPRFLKR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535Large neutral amino acids transporter small subunit 2
PRO_0000054273

Regions

Transmembrane40 – 6021Helical; Potential
Transmembrane72 – 9221Helical; Potential
Transmembrane113 – 13321Helical; Potential
Transmembrane155 – 17521Helical; Potential
Transmembrane189 – 20921Helical; Potential
Transmembrane231 – 25121Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane362 – 38221Helical; Potential
Transmembrane388 – 40821Helical; Potential
Transmembrane424 – 44421Helical; Potential
Transmembrane447 – 46721Helical; Potential

Natural variations

Alternative sequence1 – 263263MEEGA…VDPYK → MGQLFQCAVGHPGSRHLHSW EAPGLGPDYHHGDCTDMQR in isoform 3.
VSP_046945
Alternative sequence1 – 203203Missing in isoform 2.
VSP_046946
Alternative sequence1 – 169169MEEGA…AAICL → MGQYGQELSWKCLVKAVCLQ EHSQPSQLLCTLLLCWCVLG RERPFRKAQSTSSPLEGVPR FLKR in isoform 4.
VSP_046947

Experimental info

Sequence conflict2251N → D in CAB40137. Ref.3
Sequence conflict4011V → G in CAB40137. Ref.3
Sequence conflict5031G → R in AAF05696. Ref.1
Sequence conflict5031G → R in AAF05697. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AC129146353F1E47

FASTA53558,382
        10         20         30         40         50         60 
MEEGARHRNN TEKKHPGGGE SDASPEAGSG GGGVALKKEI GLVSACGIIV GNIIGSGIFV 

        70         80         90        100        110        120 
SPKGVLENAG SVGLALIVWI VTGFITVVGA LCYAELGVTI PKSGGDYSYV KDIFGGLAGF 

       130        140        150        160        170        180 
LRLWIAVLVI YPTNQAVIAL TFSNYVLQPL FPTCFPPESG LRLLAAICLL LLTWVNCSSV 

       190        200        210        220        230        240 
RWATRVQDIF TAGKLLALAL IIIMGIVQIC KGEYFWLEPK NAFENFQEPD IGLVALAFLQ 

       250        260        270        280        290        300 
GSFAYGGWNF LNYVTEELVD PYKNLPRAIF ISIPLVTFVY VFANVAYVTA MSPQELLASN 

       310        320        330        340        350        360 
AVAVTFGEKL LGVMAWIMPI SVALSTFGGV NGSLFTSSRL FFAGAREGHL PSVLAMIHVK 

       370        380        390        400        410        420 
RCTPIPALLF TCISTLLMLV TSDMYTLINY VGFINYLFYG VTVAGQIVLR WKKPDIPRPI 

       430        440        450        460        470        480 
KINLLFPIIY LLFWAFLLVF SLWSEPVVCG IGLAIMLTGV PVYFLGVYWQ HKPKCFSDFI 

       490        500        510        520        530 
ELLTLVSQKM CVVVYPEVER GSGTEEANED MEEQQQPMYQ PTPTKDKDVA GQPQP 

« Hide

Isoform 2 [UniParc].

Checksum: E6DD8F71252E064D
Show »

FASTA33237,184
Isoform 3 [UniParc].

Checksum: 4CF5A20AD230155C
Show »

FASTA31134,602
Isoform 4 [UniParc].

Checksum: 4F7293A07EBFE696
Show »

FASTA43048,283

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001253965.1. NM_001267036.1.
NP_001253966.1. NM_001267037.1.
NP_036376.2. NM_012244.3.
NP_877392.1. NM_182728.2.
UniGeneHs.596643.

3D structure databases

ProteinModelPortalQ9UHI5.
SMRQ9UHI5. Positions 39-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116996. 2 interactions.
STRING9606.ENSP00000320378.

Chemistry

BindingDBQ9UHI5.
DrugBankDB00160. L-Alanine.
DB00130. L-Glutamine.
DB00120. L-Phenylalanine.

Protein family/group databases

TCDB2.A.3.8.20. the amino acid-polyamine-organocation (apc) family.

PTM databases

PhosphoSiteQ9UHI5.

Polymorphism databases

DMDM12643348.

Proteomic databases

PaxDbQ9UHI5.
PRIDEQ9UHI5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316902; ENSP00000320378; ENSG00000092068. [Q9UHI5-1]
ENST00000422941; ENSP00000416398; ENSG00000092068. [Q9UHI5-3]
ENST00000453702; ENSP00000391577; ENSG00000092068. [Q9UHI5-2]
ENST00000529705; ENSP00000434345; ENSG00000092068. [Q9UHI5-4]
GeneID23428.
KEGGhsa:23428.
UCSCuc001wix.4. human. [Q9UHI5-1]

Organism-specific databases

CTD23428.
GeneCardsGC14M023594.
HGNCHGNC:11066. SLC7A8.
MIM604235. gene.
neXtProtNX_Q9UHI5.
PharmGKBPA35926.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0531.
HOVERGENHBG000476.
InParanoidQ9UHI5.
KOK13781.
OMALIVWIIT.
PhylomeDBQ9UHI5.
TreeFamTF313355.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000092068-MONOMER.
ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_19419. Amino acid and oligopeptide SLC transporters.
REACT_604. Hemostasis.
SABIO-RKQ9UHI5.

Gene expression databases

ArrayExpressQ9UHI5.
BgeeQ9UHI5.
CleanExHS_LAT2.
HS_SLC7A8.
GenevestigatorQ9UHI5.

Family and domain databases

InterProIPR002293. AA/rel_permease1.
IPR004760. L_AA_transporter.
[Graphical view]
PANTHERPTHR11785. PTHR11785. 1 hit.
PfamPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsTIGR00911. 2A0308. 1 hit.
ProtoNetSearch...

Other

GeneWikiSLC7A8.
GenomeRNAi23428.
NextBio45663.
PROQ9UHI5.
SOURCESearch...

Entry information

Entry nameLAT2_HUMAN
AccessionPrimary (citable) accession number: Q9UHI5
Secondary accession number(s): B2R8Q4 expand/collapse secondary AC list , B4DKT4, B4DTV6, D3DS46, F2Z2J4, Q86U05, Q9UKQ6, Q9UKQ7, Q9UKQ8, Q9Y445
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM