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Q9UM01 (YLAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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:
Y+L amino acid transporter 1
Alternative name(s):
Monocyte amino acid permease 2
Short name=MOP-2
Solute carrier family 7 member 7
y(+)L-type amino acid transporter 1
Short name=Y+LAT1
Short name=y+LAT-1
Gene names
Name:SLC7A7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the sodium-independent uptake of dibasic amino acids and sodium-dependent uptake of some neutral amino acids. Requires coexpression with SLC3A2/4F2hc to mediate the uptake of arginine, leucine and glutamine. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Involved in the transport of L-arginine in monocytes. Ref.1 Ref.2 Ref.13 Ref.14 Ref.15

Enzyme regulation

Arginine transport is inhibited by protein kinase C (PKC) and treatment with phorbol-12-myristate-13-acetate (PMA).

Subunit structure

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

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein Ref.21.

Tissue specificity

Highest expression in kidney and peripheral blood leukocytes. Weaker expression is observed in lung, heart, placenta, spleen, testis and small intestine. Expressed in normal fibroblasts and those from LPI patients. Also expressed in HUVECs, monocytes, retinal pigment epithelial cells, and various carcinoma cell lines, with highest expression in a colon-carcinoma cell line. Ref.1 Ref.3 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16

Induction

Expression is stimulated and enhanced by IFNG/IFN-gamma. Ref.14

Involvement in disease

Lysinuric protein intolerance (LPI) [MIM:222700]: A metabolic disorder characterized by increased renal excretion of cationic amino acid (CAA), reduced CAA absorption from intestine, and orotic aciduria. On a normal diet, LPI patients present poor feeding, vomiting, diarrhea, episodes of hyperammoniaemic coma and growth retardation. Hepatosplenomegaly, osteoporosis and a life-threatening pulmonary involvement (alveolar proteinosis) are also seen. Biochemically LPI is characterized by defective transport of dibasic amino acids at the basolateral membrane of epithelial cells in kidney and intestine.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24

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=31.7 µM for L-leucine (in the presence of 0.1 M NaCl) Ref.2

KM=16.2 µM for L-leucine (in the presence of 0.1 M LiCl)

Sequence caution

The sequence BAA95120.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAD62619.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Y+L amino acid transporter 1
PRO_0000054281

Regions

Transmembrane37 – 5721Helical; Potential
Transmembrane69 – 8921Helical; Potential
Transmembrane107 – 12721Helical; Potential
Transmembrane133 – 15321Helical; Potential
Transmembrane160 – 18021Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane222 – 24221Helical; Potential
Transmembrane259 – 27921Helical; Potential
Transmembrane304 – 32421Helical; Potential
Transmembrane383 – 40321Helical; Potential
Transmembrane416 – 43621Helical; Potential
Transmembrane441 – 46121Helical; Potential

Amino acid modifications

Modified residue181Phosphoserine By similarity
Glycosylation3251N-linked (GlcNAc...) Potential

Natural variations

Natural variant51T → I in LPI. Ref.24
VAR_039092
Natural variant361Missing in LPI; failed to induce cationic amino acid transport activity. Ref.24
VAR_039093
Natural variant501M → K in LPI; failed to induce cationic amino acid transport activity. Ref.22 Ref.24
VAR_030595
Natural variant531S → L in LPI. Ref.24
VAR_039094
Natural variant541G → V in LPI; failed to induce cationic amino acid transport activity. Ref.19 Ref.24
VAR_010261
Natural variant911A → V. Ref.6
Corresponds to variant rs11568438 [ dbSNP | Ensembl ].
VAR_039095
Natural variant1241L → P in LPI. Ref.24
VAR_039096
Natural variant1401A → P in LPI. Ref.24
VAR_039097
Natural variant1521F → L in LPI; moderately reduced cationic amino acid transport activity. Ref.21 Ref.24
VAR_039098
Natural variant1591R → C.
Corresponds to variant rs11568437 [ dbSNP | Ensembl ].
VAR_039099
Natural variant1881T → I in LPI; failed to induce cationic amino acid transport activity. Ref.22 Ref.24
VAR_030596
Natural variant1911K → E in LPI. Ref.24
VAR_039100
Natural variant2381S → F in LPI. Ref.20 Ref.24
VAR_030597
Natural variant2511E → D in LPI. Ref.24
VAR_039101
Natural variant2611L → P in LPI. Ref.24
VAR_039102
Natural variant3331R → M in LPI. Ref.22 Ref.24
VAR_030598
Natural variant3341L → R in LPI; failed to induce cationic amino acid transport activity. Ref.1 Ref.17 Ref.19 Ref.24
VAR_010262
Natural variant3381G → D in LPI. Ref.19 Ref.24
VAR_010999
Natural variant3651N → Y in LPI. Ref.24
VAR_039103
Natural variant3861S → R in LPI; failed to induce cationic amino acid transport activity. Ref.18 Ref.22 Ref.24
VAR_011000
Natural variant4131P → S in a breast cancer sample; somatic mutation. Ref.23
VAR_036609
Natural variant4891S → P in LPI. Ref.20 Ref.24
VAR_030599

Sequences

Sequence LengthMass (Da)Tools
Q9UM01 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: A71D677B6B075894

FASTA51155,991
        10         20         30         40         50         60 
MVDSTEYEVA SQPEVETSPL GDGASPGPEQ VKLKKEISLL NGVCLIVGNM IGSGIFVSPK 

        70         80         90        100        110        120 
GVLIYSASFG LSLVIWAVGG LFSVFGALCY AELGTTIKKS GASYAYILEA FGGFLAFIRL 

       130        140        150        160        170        180 
WTSLLIIEPT SQAIIAITFA NYMVQPLFPS CFAPYAASRL LAAACICLLT FINCAYVKWG 

       190        200        210        220        230        240 
TLVQDIFTYA KVLALIAVIV AGIVRLGQGA STHFENSFEG SSFAVGDIAL ALYSALFSYS 

       250        260        270        280        290        300 
GWDTLNYVTE EIKNPERNLP LSIGISMPIV TIIYILTNVA YYTVLDMRDI LASDAVAVTF 

       310        320        330        340        350        360 
ADQIFGIFNW IIPLSVALSC FGGLNASIVA ASRLFFVGSR EGHLPDAICM IHVERFTPVP 

       370        380        390        400        410        420 
SLLFNGIMAL IYLCVEDIFQ LINYYSFSYW FFVGLSIVGQ LYLRWKEPDR PRPLKLSVFF 

       430        440        450        460        470        480 
PIVFCLCTIF LVAVPLYSDT INSLIGIAIA LSGLPFYFLI IRVPEHKRPL YLRRIVGSAT 

       490        500        510 
RYLQVLCMSV AAEMDLEDGG EMPKQRDPKS N 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a membrane protein (y+L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y+L. A candidate gene for lysinuric protein intolerance."
Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J., Shi Y.-B., Zorzano A., Palacin M.
J. Biol. Chem. 273:32437-32445(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, VARIANT LPI ARG-334.
[2]"Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family."
Pfeiffer R., Rossier G., Spindler B., Meier C., Kuehn L.C., Verrey F.
EMBO J. 18:49-57(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Tissue: Testis.
[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], TISSUE SPECIFICITY.
Tissue: Placenta.
[4]"SLC7A7 genomic structure and novel variants in three Japanese lysinuric protein intolerance families."
Noguchi A., Shoji Y., Koizumi A., Takahashi T., Shoji Y., Matsumori M., Kayo T., Ohata T., Wada Y., Yoshimura I., Maisawa S., Konishi M., Takasago Y., Takada G.
Hum. Mutat. 15:367-372(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Molecular and biological characterization of a novel monocyte amino acid permease, MOP-2."
Takayama K., Yoshimoto M.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Characterization of a human system y+L amino acid transporter."
Fukasawa Y., Segawa H., Endou H., Kanai Y.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-91.
Tissue: Kidney.
[7]"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 [MRNA].
Tissue: B-cell and Placenta.
[8]"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].
Tissue: Umbilical cord blood.
[9]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].
[10]"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: Placenta.
[11]"Arginine transport through system y(+)L in cultured human fibroblasts: normal phenotype of cells from LPI subjects."
Dall'Asta V., Bussolati O., Sala R., Rotoli B.M., Sebastio G., Sperandeo M.P., Andria G., Gazzola G.C.
Am. J. Physiol. 279:C1829-C1837(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Two-way arginine transport in human endothelial cells: TNF-alpha stimulation is restricted to system y(+)."
Sala R., Rotoli B.M., Colla E., Visigalli R., Parolari A., Bussolati O., Gazzola G.C., Dall'Asta V.
Am. J. Physiol. 282:C134-C143(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"Nitric oxide synthesis requires activity of the cationic and neutral amino acid transport system y+L in human umbilical vein endothelium."
Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.
Exp. Physiol. 88:699-710(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"INFgamma stimulates arginine transport through system y+L in human monocytes."
Rotoli B.M., Bussolati O., Sala R., Barilli A., Talarico E., Gazzola G.C., Dall'Asta V.
FEBS Lett. 571:177-181(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[15]"Activation of classical protein kinase C decreases transport via systems y+ and y+L."
Rotmann A., Simon A., Martine U., Habermeier A., Closs E.I.
Am. J. Physiol. 292:C2259-C2268(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INHIBITION.
[16]"Ornithine transport via cationic amino acid transporter-1 is involved in ornithine cytotoxicity in retinal pigment epithelial cells."
Kaneko S., Ando A., Okuda-Ashitaka E., Maeda M., Furuta K., Suzuki M., Matsumura M., Ito S.
Invest. Ophthalmol. Vis. Sci. 48:464-471(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[17]"Identification of SLC7A7, encoding y+LAT-1, as the lysinuric protein intolerance gene."
Torrents D., Mykkaenen J., Pineda M., Feliubadalo L., Estevez R., de Cid R., Sanjurjo P., Zorzano A., Nunes V., Huoponen K., Reinikainen A., Simell O., Savontaus M.-L., Aula P., Palacin M.
Nat. Genet. 21:293-296(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LPI ARG-334, CHARACTERIZATION OF VARIANT LPI ARG-334.
[18]"Structure of the SLC7A7 gene and mutational analysis of patients affected by lysinuric protein intolerance."
Sperandeo M.P., Bassi M.T., Riboni M., Parenti G., Buoninconti A., Manzoni M., Incerti B., Larocca M.R., Di Rocco M., Strisciuglio P., Dianzani I., Parini R., Candito M., Endo F., Ballabio A., Andria G., Sebastio G., Borsani G.
Am. J. Hum. Genet. 66:92-99(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LPI ARG-386.
[19]"Functional analysis of novel mutations in y+LAT-1 amino acid transporter gene causing lysinuric protein intolerance (LPI)."
Mykkaenen J., Torrents D., Pineda M., Camps M., Yoldi M.E., Horelli-Kuitunen N., Huoponen K., Heinonen M., Oksanen J., Simell O., Savontaus M.-L., Zorzano A., Palacin M., Aula P.
Hum. Mol. Genet. 9:431-438(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LPI VAL-54 AND ASP-338, CHARACTERIZATION OF VARIANTS LPI VAL-54 AND ARG-334.
[20]"Five novel SLC7A7 variants and y+L gene-expression pattern in cultured lymphoblasts from Japanese patients with lysinuric protein intolerance."
Shoji Y., Noguchi A., Shoji Y., Matsumori M., Takasago Y., Takayanagi M., Yoshida Y., Ihara K., Hara T., Yamaguchi S., Yoshino M., Kaji M., Yamamoto S., Nakai A., Koizumi A., Hokezu Y., Nagamatsu K., Mikami H., Kitajima I., Takada G.
Hum. Mutat. 20:375-381(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LPI PHE-238 AND PRO-489.
[21]"A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity: implications for the molecular pathogenesis of lysinuric protein intolerance."
Sperandeo M.P., Paladino S., Maiuri L., Maroupulos G.D., Zurzolo C., Taglialatela M., Andria G., Sebastio G.
Eur. J. Hum. Genet. 13:628-634(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS LPI LEU-36 DEL AND LEU-152, SUBCELLULAR LOCATION.
[22]"Lysinuric protein intolerance: identification and functional analysis of mutations of the SLC7A7 gene."
Sperandeo M.P., Annunziata P., Ammendola V., Fiorito V., Pepe A., Soldovieri M.V., Taglialatela M., Andria G., Sebastio G.
Hum. Mutat. 25:410-410(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LPI LYS-50; ILE-188 AND MET-333, CHARACTERIZATION OF VARIANTS LPI LYS-50; ILE-188 AND ARG-386.
[23]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-413.
[24]"Lysinuric protein intolerance: update and extended mutation analysis of the SLC7A7 gene."
Sperandeo M.P., Andria G., Sebastio G.
Hum. Mutat. 29:14-21(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LPI ILE-5; GLU-36 DEL; LYS-50; LEU-53; VAL-54; PRO-124; PRO-140; LEU-152; ILE-188; GLU-191; PHE-238; ASP-251; PRO-261; MET-333; ARG-334; ASP-338; TYR-365; ARG-386 AND PRO-489.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF092032 mRNA. Translation: AAC83706.1.
AJ130718 mRNA. Translation: CAA10198.1.
Y18474 mRNA. Translation: CAB40136.1.
AB031537 Genomic DNA. Translation: BAA95120.1. Sequence problems.
AB011263 mRNA. Translation: BAB11849.1.
AB020532 mRNA. Translation: BAA87623.1.
BX161519 mRNA. Translation: CAD61952.1.
BX248291 mRNA. Translation: CAD62619.1. Different initiation.
AK314351 mRNA. Translation: BAG36987.1.
CH471078 Genomic DNA. Translation: EAW66245.1.
CH471078 Genomic DNA. Translation: EAW66246.1.
CH471078 Genomic DNA. Translation: EAW66247.1.
CH471078 Genomic DNA. Translation: EAW66248.1.
BC003062 mRNA. Translation: AAH03062.1.
BC010107 mRNA. Translation: AAH10107.1.
CCDSCCDS9574.1.
RefSeqNP_001119577.1. NM_001126105.2.
NP_001119578.1. NM_001126106.2.
XP_006720365.1. XM_006720302.1.
UniGeneHs.513147.
Hs.732349.

3D structure databases

ProteinModelPortalQ9UM01.
SMRQ9UM01. Positions 37-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114518. 2 interactions.
IntActQ9UM01. 1 interaction.
STRING9606.ENSP00000285850.

Protein family/group databases

TCDB2.A.3.8.22. the amino acid-polyamine-organocation (apc) family.

PTM databases

PhosphoSiteQ9UM01.

Polymorphism databases

DMDM12643378.

Proteomic databases

MaxQBQ9UM01.
PaxDbQ9UM01.
PRIDEQ9UM01.

Protocols and materials databases

DNASU9056.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285850; ENSP00000285850; ENSG00000155465.
ENST00000397528; ENSP00000380662; ENSG00000155465.
ENST00000397529; ENSP00000380663; ENSG00000155465.
ENST00000397532; ENSP00000380666; ENSG00000155465.
ENST00000555702; ENSP00000451881; ENSG00000155465.
GeneID9056.
KEGGhsa:9056.
UCSCuc001wgr.4. human.

Organism-specific databases

CTD9056.
GeneCardsGC14M023242.
GeneReviewsSLC7A7.
HGNCHGNC:11065. SLC7A7.
HPAHPA036227.
MIM222700. phenotype.
603593. gene.
neXtProtNX_Q9UM01.
Orphanet470. Lysinuric protein intolerance.
PharmGKBPA35925.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0531.
HOVERGENHBG000476.
InParanoidQ9UM01.
KOK13867.
OMACLAPYAA.
OrthoDBEOG73BVCR.
PhylomeDBQ9UM01.
TreeFamTF313355.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_19419. Amino acid and oligopeptide SLC transporters.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9UM01.
BgeeQ9UM01.
CleanExHS_SLC7A7.
GenevestigatorQ9UM01.

Family and domain databases

InterProIPR002293. AA/rel_permease1.
[Graphical view]
PANTHERPTHR11785. PTHR11785. 1 hit.
PfamPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFPIRSF006060. AA_transporter. 1 hit.
ProtoNetSearch...

Other

GeneWikiSLC7A7.
GenomeRNAi9056.
NextBio33935.
PROQ9UM01.
SOURCESearch...

Entry information

Entry nameYLAT1_HUMAN
AccessionPrimary (citable) accession number: Q9UM01
Secondary accession number(s): B2RAU0 expand/collapse secondary AC list , D3DS26, O95984, Q53XC1, Q86U07, Q9P2V5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: July 9, 2014
This is version 135 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 14

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