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Q07837

- SLC31_HUMAN

UniProt

Q07837 - SLC31_HUMAN

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Protein

Neutral and basic amino acid transport protein rBAT

Gene
SLC3A1, RBAT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney tubule.4 Publications

GO - Molecular functioni

  1. amino acid transmembrane transporter activity Source: ProtInc
  2. basic amino acid transmembrane transporter activity Source: ProtInc
  3. catalytic activity Source: InterPro
  4. cation binding Source: InterPro
  5. L-cystine transmembrane transporter activity Source: ProtInc
  6. protein binding Source: UniProtKB

GO - Biological processi

  1. amino acid transmembrane transport Source: GOC
  2. amino acid transport Source: Reactome
  3. basic amino acid transport Source: ProtInc
  4. carbohydrate metabolic process Source: InterPro
  5. cellular amino acid metabolic process Source: ProtInc
  6. ion transport Source: Reactome
  7. L-cystine transport Source: ProtInc
  8. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

ReactomeiREACT_13796. Amino acid transport across the plasma membrane.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.
TCDBi8.A.9.1.2. the rbat transport accessory protein (rbat) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral and basic amino acid transport protein rBAT
Short name:
NBAT
Alternative name(s):
D2h
Solute carrier family 3 member 1
b(0,+)-type amino acid transport protein
Gene namesi
Name:SLC3A1
Synonyms:RBAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11025. SLC3A1.

Subcellular locationi

Membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8787Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei88 – 10821Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini109 – 685577Extracellular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. brush border membrane Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of plasma membrane Source: ProtInc
  4. membrane Source: ProtInc
  5. mitochondrial inner membrane Source: Ensembl
  6. plasma membrane Source: Reactome
  7. vacuolar membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Cystinuria (CSNU) [MIM:220100]: An autosomal disorder characterized by impaired epithelial cell transport of cystine and dibasic amino acids (lysine, ornithine, and arginine) in the proximal renal tubule and gastrointestinal tract. The impaired renal reabsorption of cystine and its low solubility causes the formation of calculi in the urinary tract, resulting in obstructive uropathy, pyelonephritis, and, rarely, renal failure.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221P → S in CSNU. 1 Publication
VAR_064040
Natural varianti128 – 1281P → Q in CSNU. 1 Publication
VAR_011420
Natural varianti151 – 1511Y → C in CSNU. 1 Publication
VAR_038200
Natural varianti181 – 1811R → Q in CSNU. 1 Publication
VAR_011421
Natural varianti216 – 2161T → M in CSNU. 1 Publication
VAR_022600
Natural varianti253 – 2531N → K in CSNU. 1 Publication
VAR_038201
Natural varianti268 – 2681E → K in CSNU; reduction in amino acid transport activity. 1 Publication
VAR_011422
Natural varianti341 – 3411T → A in CSNU; reduction in amino acid transport activity. 1 Publication
VAR_011423
Natural varianti362 – 3621R → C in CSNU. 1 Publication
VAR_022601
Natural varianti362 – 3621R → H in CSNU. 1 Publication
VAR_038202
Natural varianti365 – 3651R → W in CSNU. 2 Publications
VAR_011424
Natural varianti398 – 3981G → R in CSNU. 1 Publication
VAR_038203
Natural varianti452 – 4521R → W in CSNU. 1 Publication
VAR_011425
Natural varianti461 – 4611Y → H in CSNU. 2 Publications
Corresponds to variant rs144162964 [ dbSNP | Ensembl ].
VAR_011426
Natural varianti467 – 4671M → K in CSNU. 1 Publication
VAR_011428
Natural varianti467 – 4671M → T in CSNU; loss of 80% of amino acid transport activity. 4 Publications
VAR_011427
Natural varianti481 – 4811G → V in CSNU. 1 Publication
VAR_038204
Natural varianti482 – 4821E → K in CSNU. 1 Publication
VAR_038205
Natural varianti508 – 5081P → A in CSNU. 1 Publication
VAR_022602
Natural varianti510 – 5101Q → R in CSNU. 1 Publication
VAR_038206
Natural varianti582 – 5821Y → H in CSNU. 1 Publication
VAR_011429
Natural varianti584 – 5841R → T in CSNU. 1 Publication
VAR_038207
Natural varianti599 – 5991F → S in CSNU. 1 Publication
VAR_038208
Natural varianti600 – 6001G → E in CSNU. 1 Publication
VAR_038209
Natural varianti615 – 6151P → T in CSNU. 1 Publication
VAR_011430
Natural varianti648 – 6481F → S in CSNU. 1 Publication
VAR_011432
Natural varianti652 – 6521T → R in CSNU. 1 Publication
VAR_011433
Natural varianti678 – 6781L → P in CSNU. 1 Publication
VAR_011434
Hypotonia-cystinuria syndrome (HCS) [MIM:606407]: Characterized generalized hypotonia at birth, nephrolithiasis, growth hormone deficiency, minor facial dysmorphism, failure to thrive, followed by hyperphagia and rapid weight gain in late childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications

Keywords - Diseasei

Cystinuria, Disease mutation

Organism-specific databases

MIMi220100. phenotype.
606407. phenotype.
Orphaneti163693. 2p21 microdeletion syndrome.
238523. Atypical hypotonia - cystinuria syndrome.
93612. Cystinuria type A.
163690. Hypotonia - cystinuria syndrome.
PharmGKBiPA35893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 685685Neutral and basic amino acid transport protein rBATPRO_0000071950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi214 – 2141N-linked (GlcNAc...) Reviewed prediction
Glycosylationi261 – 2611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi332 – 3321N-linked (GlcNAc...) Reviewed prediction
Glycosylationi495 – 4951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi513 – 5131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi575 – 5751N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ07837.
PRIDEiQ07837.

PTM databases

PhosphoSiteiQ07837.

Expressioni

Tissue specificityi

Expressed in the brush border membrane in the kidney (at protein level). Predominantly expressed in the kidney, small intestine and pancreas. Weakly expressed in liver.3 Publications

Gene expression databases

ArrayExpressiQ07837.
BgeeiQ07837.
CleanExiHS_SLC3A1.
GenevestigatoriQ07837.

Organism-specific databases

HPAiHPA038360.

Interactioni

Subunit structurei

Disulfide-linked heterodimer with the amino acid transport protein SLC7A9.2 Publications

Protein-protein interaction databases

BioGridi112410. 1 interaction.
STRINGi9606.ENSP00000260649.

Structurei

3D structure databases

ProteinModelPortaliQ07837.
SMRiQ07837. Positions 115-650.

Family & Domainsi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000220640.
HOVERGENiHBG053002.
InParanoidiQ07837.
KOiK14210.
OMAiTMYYGDE.
PhylomeDBiQ07837.
TreeFamiTF314498.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q07837-1) [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

MAEDKSKRDS IEMSMKGCQT NNGFVHNEDI LEQTPDPGSS TDNLKHSTRG    50
ILGSQEPDFK GVQPYAGMPK EVLFQFSGQA RYRIPREILF WLTVASVLVL 100
IAATIAIIAL SPKCLDWWQE GPMYQIYPRS FKDSNKDGNG DLKGIQDKLD 150
YITALNIKTV WITSFYKSSL KDFRYGVEDF REVDPIFGTM EDFENLVAAI 200
HDKGLKLIID FIPNHTSDKH IWFQLSRTRT GKYTDYYIWH DCTHENGKTI 250
PPNNWLSVYG NSSWHFDEVR NQCYFHQFMK EQPDLNFRNP DVQEEIKEIL 300
RFWLTKGVDG FSLDAVKFLL EAKHLRDEIQ VNKTQIPDTV TQYSELYHDF 350
TTTQVGMHDI VRSFRQTMDQ YSTEPGRYRF MGTEAYAESI DRTVMYYGLP 400
FIQEADFPFN NYLSMLDTVS GNSVYEVITS WMENMPEGKW PNWMIGGPDS 450
SRLTSRLGNQ YVNVMNMLLF TLPGTPITYY GEEIGMGNIV AANLNESYDI 500
NTLRSKSPMQ WDNSSNAGFS EASNTWLPTN SDYHTVNVDV QKTQPRSALK 550
LYQDLSLLHA NELLLNRGWF CHLRNDSHYV VYTRELDGID RIFIVVLNFG 600
ESTLLNLHNM ISGLPAKMRI RLSTNSADKG SKVDTSGIFL DKGEGLIFEH 650
NTKNLLHRQT AFRDRCFVSN RACYSSVLNI LYTSC 685
Length:685
Mass (Da):78,852
Last modified:May 10, 2005 - v2
Checksum:iF9D6DFD548283899
GO
Isoform B (identifier: Q07837-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-278: Missing.

Show »
Length:407
Mass (Da):46,728
Checksum:i073D5E14EF8FEC59
GO
Isoform C (identifier: Q07837-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-391: FMGTEAYAESID → LTTAYALISSQA
     392-685: Missing.

Show »
Length:391
Mass (Da):45,370
Checksum:iBD09E3E0DAD64C0B
GO
Isoform D (identifier: Q07837-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MAEDKSKR → MTLNLVNS
     9-377: Missing.

Show »
Length:316
Mass (Da):35,913
Checksum:i34F115707CF076E1
GO
Isoform E (identifier: Q07837-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     501-502: NT → VS
     503-685: Missing.

Show »
Length:502
Mass (Da):57,998
Checksum:i8EC96914C99BD5D7
GO
Isoform F (identifier: Q07837-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     541-564: QKTQPRSALKLYQDLSLLHANELL → SISENFMLILETKKWVSTESTHSP
     565-685: Missing.

Show »
Length:564
Mass (Da):65,013
Checksum:i00F102753414E97B
GO
Isoform G (identifier: Q07837-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     541-551: QKTQPRSALKL → LLRHPCSSAVA
     552-685: Missing.

Show »
Length:551
Mass (Da):63,401
Checksum:iB92CDFE941512647
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti122 – 1221P → S in CSNU. 1 Publication
VAR_064040
Natural varianti128 – 1281P → Q in CSNU. 1 Publication
VAR_011420
Natural varianti151 – 1511Y → C in CSNU. 1 Publication
VAR_038200
Natural varianti181 – 1811R → Q in CSNU. 1 Publication
VAR_011421
Natural varianti216 – 2161T → M in CSNU. 1 Publication
VAR_022600
Natural varianti253 – 2531N → K in CSNU. 1 Publication
VAR_038201
Natural varianti268 – 2681E → K in CSNU; reduction in amino acid transport activity. 1 Publication
VAR_011422
Natural varianti341 – 3411T → A in CSNU; reduction in amino acid transport activity. 1 Publication
VAR_011423
Natural varianti362 – 3621R → C in CSNU. 1 Publication
VAR_022601
Natural varianti362 – 3621R → H in CSNU. 1 Publication
VAR_038202
Natural varianti365 – 3651R → W in CSNU. 2 Publications
VAR_011424
Natural varianti398 – 3981G → R in CSNU. 1 Publication
VAR_038203
Natural varianti452 – 4521R → W in CSNU. 1 Publication
VAR_011425
Natural varianti461 – 4611Y → H in CSNU. 2 Publications
Corresponds to variant rs144162964 [ dbSNP | Ensembl ].
VAR_011426
Natural varianti467 – 4671M → K in CSNU. 1 Publication
VAR_011428
Natural varianti467 – 4671M → T in CSNU; loss of 80% of amino acid transport activity. 4 Publications
VAR_011427
Natural varianti481 – 4811G → V in CSNU. 1 Publication
VAR_038204
Natural varianti482 – 4821E → K in CSNU. 1 Publication
VAR_038205
Natural varianti508 – 5081P → A in CSNU. 1 Publication
VAR_022602
Natural varianti510 – 5101Q → R in CSNU. 1 Publication
VAR_038206
Natural varianti582 – 5821Y → H in CSNU. 1 Publication
VAR_011429
Natural varianti584 – 5841R → T in CSNU. 1 Publication
VAR_038207
Natural varianti599 – 5991F → S in CSNU. 1 Publication
VAR_038208
Natural varianti600 – 6001G → E in CSNU. 1 Publication
VAR_038209
Natural varianti615 – 6151P → T in CSNU. 1 Publication
VAR_011430
Natural varianti618 – 6181M → I.8 Publications
Corresponds to variant rs698761 [ dbSNP | Ensembl ].
VAR_011431
Natural varianti648 – 6481F → S in CSNU. 1 Publication
VAR_011432
Natural varianti652 – 6521T → R in CSNU. 1 Publication
VAR_011433
Natural varianti678 – 6781L → P in CSNU. 1 Publication
VAR_011434

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 278278Missing in isoform B. VSP_054339Add
BLAST
Alternative sequencei1 – 88MAEDKSKR → MTLNLVNS in isoform D. VSP_054340
Alternative sequencei9 – 377369Missing in isoform D. VSP_054341Add
BLAST
Alternative sequencei380 – 39112FMGTE…AESID → LTTAYALISSQA in isoform C. VSP_054342Add
BLAST
Alternative sequencei392 – 685294Missing in isoform C. VSP_054343Add
BLAST
Alternative sequencei501 – 5022NT → VS in isoform E. VSP_054344
Alternative sequencei503 – 685183Missing in isoform E. VSP_054345Add
BLAST
Alternative sequencei541 – 56424QKTQP…ANELL → SISENFMLILETKKWVSTES THSP in isoform F. VSP_054346Add
BLAST
Alternative sequencei541 – 55111QKTQPRSALKL → LLRHPCSSAVA in isoform G. VSP_054347Add
BLAST
Alternative sequencei552 – 685134Missing in isoform G. VSP_054348Add
BLAST
Alternative sequencei565 – 685121Missing in isoform F. VSP_054349Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95548 mRNA. Translation: AAA35500.1.
L11696 mRNA. Translation: AAA81778.1.
D82326 mRNA. Translation: BAA11541.1.
U60819
, U60810, U60811, U60812, U60813, U60816, U60818, U60814, U60815 Genomic DNA. Translation: AAB39829.1.
AB033549 mRNA. Translation: BAB16841.1.
DQ023512 mRNA. Translation: AAY89643.1.
DQ023513 mRNA. Translation: AAY89644.1.
DQ023514 mRNA. Translation: AAY89645.1.
DQ023515 mRNA. Translation: AAY89646.1.
DQ023516 mRNA. Translation: AAY89647.1.
DQ023517 mRNA. Translation: AAY89648.1.
AK223146 mRNA. Translation: BAD96866.1.
AK289636 mRNA. Translation: BAF82325.1.
AC013717 Genomic DNA. Translation: AAX88955.1.
BC022386 mRNA. Translation: AAH22386.1.
BC093624 mRNA. Translation: AAH93624.1.
BC093626 mRNA. Translation: AAH93626.1.
CCDSiCCDS1819.1. [Q07837-1]
PIRiA47102.
RefSeqiNP_000332.2. NM_000341.3. [Q07837-1]
UniGeneiHs.112916.

Genome annotation databases

EnsembliENST00000260649; ENSP00000260649; ENSG00000138079.
ENST00000409229; ENSP00000386620; ENSG00000138079.
ENST00000409741; ENSP00000386954; ENSG00000138079.
ENST00000410056; ENSP00000387337; ENSG00000138079.
GeneIDi6519.
KEGGihsa:6519.
UCSCiuc002ruc.4. human. [Q07837-1]

Polymorphism databases

DMDMi67472674.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Cysdb

Cystinuria database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M95548 mRNA. Translation: AAA35500.1 .
L11696 mRNA. Translation: AAA81778.1 .
D82326 mRNA. Translation: BAA11541.1 .
U60819
, U60810 , U60811 , U60812 , U60813 , U60816 , U60818 , U60814 , U60815 Genomic DNA. Translation: AAB39829.1 .
AB033549 mRNA. Translation: BAB16841.1 .
DQ023512 mRNA. Translation: AAY89643.1 .
DQ023513 mRNA. Translation: AAY89644.1 .
DQ023514 mRNA. Translation: AAY89645.1 .
DQ023515 mRNA. Translation: AAY89646.1 .
DQ023516 mRNA. Translation: AAY89647.1 .
DQ023517 mRNA. Translation: AAY89648.1 .
AK223146 mRNA. Translation: BAD96866.1 .
AK289636 mRNA. Translation: BAF82325.1 .
AC013717 Genomic DNA. Translation: AAX88955.1 .
BC022386 mRNA. Translation: AAH22386.1 .
BC093624 mRNA. Translation: AAH93624.1 .
BC093626 mRNA. Translation: AAH93626.1 .
CCDSi CCDS1819.1. [Q07837-1 ]
PIRi A47102.
RefSeqi NP_000332.2. NM_000341.3. [Q07837-1 ]
UniGenei Hs.112916.

3D structure databases

ProteinModelPortali Q07837.
SMRi Q07837. Positions 115-650.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112410. 1 interaction.
STRINGi 9606.ENSP00000260649.

Chemistry

DrugBanki DB00138. L-Cystine.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.
TCDBi 8.A.9.1.2. the rbat transport accessory protein (rbat) family.

PTM databases

PhosphoSitei Q07837.

Polymorphism databases

DMDMi 67472674.

Proteomic databases

PaxDbi Q07837.
PRIDEi Q07837.

Protocols and materials databases

DNASUi 6519.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260649 ; ENSP00000260649 ; ENSG00000138079 .
ENST00000409229 ; ENSP00000386620 ; ENSG00000138079 .
ENST00000409741 ; ENSP00000386954 ; ENSG00000138079 .
ENST00000410056 ; ENSP00000387337 ; ENSG00000138079 .
GeneIDi 6519.
KEGGi hsa:6519.
UCSCi uc002ruc.4. human. [Q07837-1 ]

Organism-specific databases

CTDi 6519.
GeneCardsi GC02P044414.
HGNCi HGNC:11025. SLC3A1.
HPAi HPA038360.
MIMi 104614. gene.
220100. phenotype.
606407. phenotype.
neXtProti NX_Q07837.
Orphaneti 163693. 2p21 microdeletion syndrome.
238523. Atypical hypotonia - cystinuria syndrome.
93612. Cystinuria type A.
163690. Hypotonia - cystinuria syndrome.
PharmGKBi PA35893.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0366.
HOGENOMi HOG000220640.
HOVERGENi HBG053002.
InParanoidi Q07837.
KOi K14210.
OMAi TMYYGDE.
PhylomeDBi Q07837.
TreeFami TF314498.

Enzyme and pathway databases

Reactomei REACT_13796. Amino acid transport across the plasma membrane.

Miscellaneous databases

ChiTaRSi SLC3A1. human.
GeneWikii SLC3A1.
GenomeRNAii 6519.
NextBioi 25349.
PROi Q07837.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q07837.
Bgeei Q07837.
CleanExi HS_SLC3A1.
Genevestigatori Q07837.

Family and domain databases

Gene3Di 3.20.20.80. 2 hits.
InterProi IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport."
    Lee W.-S., Wells R.G., Sabbag R.V., Mohandas T.K., Hediger M.A.
    J. Clin. Invest. 91:1959-1963(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, VARIANT ILE-618.
    Tissue: Kidney.
  2. Lee W.-S., Wells R.G., Sabbag R.V., Mohandas T.K., Hediger M.A.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Expression cloning of a human renal cDNA that induces high affinity transport of L-cystine shared with dibasic amino acids in Xenopus oocytes."
    Bertran J., Werner A., Chillaron J., Nunes V., Biber J., Testar X., Zorzano A., Estivill X., Murer H., Palacin M.
    J. Biol. Chem. 268:14842-14849(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Kidney cortex.
  4. "Effects of truncation of the COOH-terminal region of a Na+-independent neutral and basic amino acid transporter on amino acid transport in Xenopus oocytes."
    Miyamoto K., Segawa H., Tatsumi S., Katai K., Yamamoto H., Taketani Y., Haga H., Morita K., Takeda E.
    J. Biol. Chem. 271:16758-16763(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ILE-618, FUNCTION.
    Tissue: Kidney cortex.
  5. "Genomic organization of a human cystine transporter gene (SLC3A1) and identification of novel mutations causing cystinuria."
    Endsley J.K., Phillips J.A. III, Hruska K.A., Denneberg T., Carlson J., George A.L. Jr.
    Kidney Int. 51:1893-1899(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-618, VARIANTS CSNU TRP-452; HIS-461 AND THR-467.
  6. "Human cystinuria-related transporter: localization and functional characterization."
    Mizoguchi K., Cha S.H., Chairoungdua A., Kim J.Y., Shigeta Y., Matsuo H., Fukushima J., Awa Y., Akakura K., Goya T., Ito H., Endou H., Kanai Y.
    Kidney Int. 59:1821-1833(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, VARIANT ILE-618.
    Tissue: Kidney.
  7. "The 2p21 deletion syndrome: characterization of the transcription content."
    Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K., Hershkovitz E.
    Genomics 86:195-211(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C; D; E; F AND G), ALTERNATIVE SPLICING, VARIANT ILE-618.
  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.
    , 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] (ISOFORM A).
    Tissue: Amygdala.
  9. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Tissue: Kidney.
  10. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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 A), VARIANT ILE-618.
    Tissue: Brain and Kidney.
  12. Cited for: SUBUNIT.
  13. "Genetic heterogeneity in cystinuria: the SLC3A1 gene is linked to type I but not to type III cystinuria."
    Calonge M.J., Volpini V., Bisceglia L., Rousaud F., de Sanctis L., Beccia E., Zelante L., Testar X., Zorzano A., Estivill X., Gasparini P., Nunes V., Palacin M.
    Proc. Natl. Acad. Sci. U.S.A. 92:9667-9671(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  14. "rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for cystine in the kidney."
    Fernandez E., Carrascal M., Rousaud F., Abian J., Zorzano A., Palacin M., Chillaron J.
    Am. J. Physiol. 283:F540-F548(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  15. "Deletion of PREPL, a gene encoding a putative serine oligopeptidase, in patients with hypotonia-cystinuria syndrome."
    Jaeken J., Martens K., Francois I., Eyskens F., Lecointre C., Derua R., Meulemans S., Slootstra J.W., Waelkens E., de Zegher F., Creemers J.W.M., Matthijs G.
    Am. J. Hum. Genet. 78:38-51(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HCS.
  16. Cited for: VARIANTS CSNU GLN-181; LYS-467; THR-467; THR-615; ARG-652 AND PRO-678, CHARACTERIZATION OF VARIANT THR-467.
  17. "Mutations in the SLC3A1 transporter gene in cystinuria."
    Pras E., Raben N., Golomb E., Arber N., Aksentijevich I., Schapiro J.M., Harel D., Katz G., Liberman U., Pras M., Kastner D.L.
    Am. J. Hum. Genet. 56:1297-1303(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSNU GLN-128.
  18. "Molecular genetics of cystinuria: identification of four new mutations and seven polymorphisms, and evidence for genetic heterogeneity."
    Gasparini P., Calonge M.J., Bisceglia L., Purroy J., Dianzani I., Notarangelo A., Rousaud F., Gallucci M., Testar X., Ponzone A., Estivill X., Zorzano A., Palacin M., Nunes V., Zelante L.
    Am. J. Hum. Genet. 57:781-788(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CSNU TRP-365; HIS-582 AND SER-648, VARIANT ILE-618.
  19. "Mutations of the basic amino acid transporter gene associated with cystinuria."
    Miyamoto K., Katai K., Tatsumi S., Sone K., Segawa H., Yamamoto H., Taketani Y., Takada K., Morita K., Kanayama H., Kagawa S., Takeda E.
    Biochem. J. 310:951-955(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CSNU LYS-268 AND ALA-341, CHARACTERIZATION OF VARIANTS CSNU LYS-268 AND ALA-341.
  20. "Identification of two novel mutations [P122S (364C>T) and 1601delAC] in the SLC3A1 gene in type I cystinurics."
    Gitomer W.L., Reed B.Y., Pak C.Y.C.
    Hum. Mutat. 15:390-390(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSNU SER-122.
  21. "Identification of 12 novel mutations in the SLC3A1 gene in Swedish cystinuria patients."
    Harnevik L., Fjellstedt E., Molbaek A., Tiselius H.-G., Denneberg T., Soederkvist P.
    Hum. Mutat. 18:516-525(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CSNU CYS-151; LYS-253; HIS-362; ARG-398; HIS-461; THR-467; VAL-481; LYS-482; ARG-510; THR-584; SER-599 AND GLU-600, VARIANT ILE-618.
  22. "Cystinuria in children: distribution and frequencies of mutations in the SLC3A1 and SLC7A9 genes."
    Botzenhart E., Vester U., Schmidt C., Hesse A., Halber M., Wagner C., Lang F., Hoyer P., Zerres K., Eggermann T.
    Kidney Int. 62:1136-1142(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CSNU MET-216; CYS-362; TRP-365; THR-467 AND ALA-508.

Entry informationi

Entry nameiSLC31_HUMAN
AccessioniPrimary (citable) accession number: Q07837
Secondary accession number(s): A8K0S1
, O00658, Q15295, Q4J6B4, Q4J6B5, Q4J6B6, Q4J6B7, Q4J6B8, Q4J6B9, Q52M92, Q52M94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 10, 2005
Last modified: September 3, 2014
This is version 154 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

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