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Q01650 (LAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Protein existenceEvidence 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.21

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

Cytoplasmcytosol. 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.21

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 processAmino-acid transport
Differentiation
Neurogenesis
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processamino acid transport

Traceable author statement. Source: Reactome

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

ion transport

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

neutral amino acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionL-amino acid transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

amino acid transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Large neutral amino acids transporter small subunit 1
PRO_0000054270

Regions

Transmembrane50 – 7021Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane120 – 14021Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane199 – 21921Helical; Potential
Transmembrane243 – 26321Helical; Potential
Transmembrane274 – 29421Helical; Potential
Transmembrane319 – 33921Helical; Potential
Transmembrane396 – 41621Helical; Potential
Transmembrane431 – 45121Helical; Potential
Transmembrane458 – 47821Helical; Potential

Amino acid modifications

Modified residue311Phosphoserine Ref.23 Ref.24 Ref.26
Modified residue451Phosphothreonine Ref.24
Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Cross-link19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Natural variant2231D → V. Ref.6
Corresponds to variant rs17853937 [ dbSNP | Ensembl ].
VAR_070119
Natural variant2301N → K. Ref.1
Corresponds to variant rs1060250 [ dbSNP | Ensembl ].
VAR_048157

Experimental info

Sequence conflict151A → V in BAA75746. Ref.5
Sequence conflict29 – 313AKS → SKR in BAA75746. Ref.5
Sequence conflict351S → A in BAA75746. Ref.5
Sequence conflict621T → A in BAA75746. Ref.5
Sequence conflict881V → M in BAA75746. Ref.5
Sequence conflict1541T → A in BAA75746. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q01650 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 767F3C60B62C0F02

FASTA50755,010
        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 

« Hide

References

« Hide '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], VARIANT VAL-223.
Tissue: Liver and Lymph.
[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]"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.
[21]"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.
[22]"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.
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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].
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
BC039692 mRNA. Translation: AAH39692.1.
BC042600 mRNA. Translation: AAH42600.1.
M80244 mRNA. Translation: AAA35780.1.
CCDSCCDS10964.1.
PIRJG0165.
RefSeqNP_003477.4. NM_003486.5.
XP_006721350.1. XM_006721287.1.
UniGeneHs.513797.

3D structure databases

ProteinModelPortalQ01650.
SMRQ01650. Positions 48-414.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113801. 5 interactions.
IntActQ01650. 3 interactions.
MINTMINT-5000558.
STRING9606.ENSP00000261622.

Chemistry

BindingDBQ01650.
ChEMBLCHEMBL4459.

Protein family/group databases

TCDB2.A.3.8.25. the amino acid-polyamine-organocation (apc) family.

PTM databases

PhosphoSiteQ01650.

Polymorphism databases

DMDM12643412.

Proteomic databases

MaxQBQ01650.
PeptideAtlasQ01650.
PRIDEQ01650.

Protocols and materials databases

DNASU8140.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261622; ENSP00000261622; ENSG00000103257.
ENST00000565644; ENSP00000454323; ENSG00000103257.
GeneID8140.
KEGGhsa:8140.
UCSCuc002fkm.3. human.

Organism-specific databases

CTD8140.
GeneCardsGC16M087863.
HGNCHGNC:11063. SLC7A5.
HPAHPA052673.
MIM600182. gene.
neXtProtNX_Q01650.
PharmGKBPA35923.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000098892.
HOVERGENHBG000476.
InParanoidQ01650.
KOK13780.
OMAVFTCIMT.
OrthoDBEOG73BVCR.
PhylomeDBQ01650.
TreeFamTF313355.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000103257-MONOMER.
ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_19419. Amino acid and oligopeptide SLC transporters.
REACT_604. Hemostasis.
SABIO-RKQ01650.

Gene expression databases

BgeeQ01650.
CleanExHS_SLC7A5.
GenevestigatorQ01650.

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

ChiTaRSSLC7A5. human.
GeneWikiSLC7A5.
GenomeRNAi8140.
NextBio30811.
PROQ01650.
SOURCESearch...

Entry information

Entry nameLAT1_HUMAN
AccessionPrimary (citable) accession number: Q01650
Secondary accession number(s): Q8IV97 expand/collapse secondary AC list , Q9UBN8, Q9UP15, Q9UQC0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 147 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM