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Q07837 (SLC31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SLC3A1
Synonyms:RBAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.4 Ref.6

Subunit structure

Disulfide-linked heterodimer with the amino acid transport protein SLC7A9. Ref.12 Ref.14

Subcellular location

Membrane; Single-pass type II membrane protein Ref.14.

Tissue specificity

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. Ref.1 Ref.3 Ref.14

Involvement in disease

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. Ref.5 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

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. Ref.13 Ref.15

Ontologies

Keywords
   Biological processAmino-acid transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCystinuria
Disease mutation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-cystine transport

Traceable author statement Ref.16. Source: ProtInc

amino acid transmembrane transport

Traceable author statement PubMed 10799513. Source: GOC

amino acid transport

Traceable author statement. Source: Reactome

basic amino acid transport

Traceable author statement Ref.16. Source: ProtInc

carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cellular amino acid metabolic process

Traceable author statement Ref.16. Source: ProtInc

ion transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentbrush border membrane

Inferred from direct assay Ref.14. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.16. Source: ProtInc

membrane

Traceable author statement Ref.16. Source: ProtInc

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

vacuolar membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionL-cystine transmembrane transporter activity

Traceable author statement Ref.16. Source: ProtInc

amino acid transmembrane transporter activity

Traceable author statement PubMed 10799513. Source: ProtInc

basic amino acid transmembrane transporter activity

Traceable author statement Ref.16. Source: ProtInc

catalytic activity

Inferred from electronic annotation. Source: InterPro

cation binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q07837-1)

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 B (identifier: Q07837-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-278: Missing.
Isoform C (identifier: Q07837-3)

The sequence of this isoform differs from the canonical sequence as follows:
     380-391: FMGTEAYAESID → LTTAYALISSQA
     392-685: Missing.
Isoform D (identifier: Q07837-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MAEDKSKR → MTLNLVNS
     9-377: Missing.
Isoform E (identifier: Q07837-5)

The sequence of this isoform differs from the canonical sequence as follows:
     501-502: NT → VS
     503-685: Missing.
Isoform F (identifier: Q07837-6)

The sequence of this isoform differs from the canonical sequence as follows:
     541-564: QKTQPRSALKLYQDLSLLHANELL → SISENFMLILETKKWVSTESTHSP
     565-685: Missing.
Isoform G (identifier: Q07837-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 685685Neutral and basic amino acid transport protein rBAT
PRO_0000071950

Regions

Topological domain1 – 8787Cytoplasmic Potential
Transmembrane88 – 10821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain109 – 685577Extracellular Potential

Amino acid modifications

Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation4951N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation5751N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 278278Missing in isoform B.
VSP_054339
Alternative sequence1 – 88MAEDKSKR → MTLNLVNS in isoform D.
VSP_054340
Alternative sequence9 – 377369Missing in isoform D.
VSP_054341
Alternative sequence380 – 39112FMGTE…AESID → LTTAYALISSQA in isoform C.
VSP_054342
Alternative sequence392 – 685294Missing in isoform C.
VSP_054343
Alternative sequence501 – 5022NT → VS in isoform E.
VSP_054344
Alternative sequence503 – 685183Missing in isoform E.
VSP_054345
Alternative sequence541 – 56424QKTQP…ANELL → SISENFMLILETKKWVSTES THSP in isoform F.
VSP_054346
Alternative sequence541 – 55111QKTQPRSALKL → LLRHPCSSAVA in isoform G.
VSP_054347
Alternative sequence552 – 685134Missing in isoform G.
VSP_054348
Alternative sequence565 – 685121Missing in isoform F.
VSP_054349
Natural variant1221P → S in CSNU. Ref.20
VAR_064040
Natural variant1281P → Q in CSNU. Ref.17
VAR_011420
Natural variant1511Y → C in CSNU. Ref.21
VAR_038200
Natural variant1811R → Q in CSNU. Ref.16
VAR_011421
Natural variant2161T → M in CSNU. Ref.22
VAR_022600
Natural variant2531N → K in CSNU. Ref.21
VAR_038201
Natural variant2681E → K in CSNU; reduction in amino acid transport activity. Ref.19
VAR_011422
Natural variant3411T → A in CSNU; reduction in amino acid transport activity. Ref.19
VAR_011423
Natural variant3621R → C in CSNU. Ref.22
VAR_022601
Natural variant3621R → H in CSNU. Ref.21
VAR_038202
Natural variant3651R → W in CSNU. Ref.18 Ref.22
VAR_011424
Natural variant3981G → R in CSNU. Ref.21
VAR_038203
Natural variant4521R → W in CSNU. Ref.5
VAR_011425
Natural variant4611Y → H in CSNU. Ref.5 Ref.21
Corresponds to variant rs144162964 [ dbSNP | Ensembl ].
VAR_011426
Natural variant4671M → K in CSNU. Ref.16
VAR_011428
Natural variant4671M → T in CSNU; loss of 80% of amino acid transport activity. Ref.5 Ref.16 Ref.21 Ref.22
VAR_011427
Natural variant4811G → V in CSNU. Ref.21
VAR_038204
Natural variant4821E → K in CSNU. Ref.21
VAR_038205
Natural variant5081P → A in CSNU. Ref.22
VAR_022602
Natural variant5101Q → R in CSNU. Ref.21
VAR_038206
Natural variant5821Y → H in CSNU. Ref.18
VAR_011429
Natural variant5841R → T in CSNU. Ref.21
VAR_038207
Natural variant5991F → S in CSNU. Ref.21
VAR_038208
Natural variant6001G → E in CSNU. Ref.21
VAR_038209
Natural variant6151P → T in CSNU. Ref.16
VAR_011430
Natural variant6181M → I. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.11 Ref.18 Ref.21
Corresponds to variant rs698761 [ dbSNP | Ensembl ].
VAR_011431
Natural variant6481F → S in CSNU. Ref.18
VAR_011432
Natural variant6521T → R in CSNU. Ref.16
VAR_011433
Natural variant6781L → P in CSNU. Ref.16
VAR_011434

Sequences

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

Last modified May 10, 2005. Version 2.
Checksum: F9D6DFD548283899

FASTA68578,852
        10         20         30         40         50         60 
MAEDKSKRDS IEMSMKGCQT NNGFVHNEDI LEQTPDPGSS TDNLKHSTRG ILGSQEPDFK 

        70         80         90        100        110        120 
GVQPYAGMPK EVLFQFSGQA RYRIPREILF WLTVASVLVL IAATIAIIAL SPKCLDWWQE 

       130        140        150        160        170        180 
GPMYQIYPRS FKDSNKDGNG DLKGIQDKLD YITALNIKTV WITSFYKSSL KDFRYGVEDF 

       190        200        210        220        230        240 
REVDPIFGTM EDFENLVAAI HDKGLKLIID FIPNHTSDKH IWFQLSRTRT GKYTDYYIWH 

       250        260        270        280        290        300 
DCTHENGKTI PPNNWLSVYG NSSWHFDEVR NQCYFHQFMK EQPDLNFRNP DVQEEIKEIL 

       310        320        330        340        350        360 
RFWLTKGVDG FSLDAVKFLL EAKHLRDEIQ VNKTQIPDTV TQYSELYHDF TTTQVGMHDI 

       370        380        390        400        410        420 
VRSFRQTMDQ YSTEPGRYRF MGTEAYAESI DRTVMYYGLP FIQEADFPFN NYLSMLDTVS 

       430        440        450        460        470        480 
GNSVYEVITS WMENMPEGKW PNWMIGGPDS SRLTSRLGNQ YVNVMNMLLF TLPGTPITYY 

       490        500        510        520        530        540 
GEEIGMGNIV AANLNESYDI NTLRSKSPMQ WDNSSNAGFS EASNTWLPTN SDYHTVNVDV 

       550        560        570        580        590        600 
QKTQPRSALK LYQDLSLLHA NELLLNRGWF CHLRNDSHYV VYTRELDGID RIFIVVLNFG 

       610        620        630        640        650        660 
ESTLLNLHNM ISGLPAKMRI RLSTNSADKG SKVDTSGIFL DKGEGLIFEH NTKNLLHRQT 

       670        680 
AFRDRCFVSN RACYSSVLNI LYTSC 

« Hide

Isoform B [UniParc].

Checksum: 073D5E14EF8FEC59
Show »

FASTA40746,728
Isoform C [UniParc].

Checksum: BD09E3E0DAD64C0B
Show »

FASTA39145,370
Isoform D [UniParc].

Checksum: 34F115707CF076E1
Show »

FASTA31635,913
Isoform E [UniParc].

Checksum: 8EC96914C99BD5D7
Show »

FASTA50257,998
Isoform F [UniParc].

Checksum: 00F102753414E97B
Show »

FASTA56465,013
Isoform G [UniParc].

Checksum: B92CDFE941512647
Show »

FASTA55163,401

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]"Luminal heterodimeric amino acid transporter defective in cystinuria."
Pfeiffer R., Loffing J., Rossier G., Bauch C., Meier C., Eggermann T., Loffing-Cueni D., Kuehn L.C., Verrey F.
Mol. Biol. Cell 10:4135-4147(1999) [PubMed] [Europe PMC] [Abstract]
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]"Cystinuria caused by mutations in rBAT, a gene involved in the transport of cystine."
Calonge M.J., Gasparini P., Chillaron J., Chillon M., Gallucci M., Rousaud F., Zelante L., Testar X., Dallapiccola B., Di Silverio F., Barcelo P., Estivill X., Zorzano A., Nunes V., Palacin M.
Nat. Genet. 6:420-425(1994) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cysdb

Cystinuria database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95548 mRNA. Translation: AAA35500.1.
L11696 mRNA. Translation: AAA81778.1.
D82326 mRNA. Translation: BAA11541.1.
U60819 expand/collapse EMBL AC list , 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.
CCDSCCDS1819.1.
PIRA47102.
RefSeqNP_000332.2. NM_000341.3. [Q07837-1]
UniGeneHs.112916.

3D structure databases

ProteinModelPortalQ07837.
SMRQ07837. Positions 115-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112410. 1 interaction.
STRING9606.ENSP00000260649.

Chemistry

DrugBankDB00138. L-Cystine.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.
TCDB8.A.9.1.2. the rbat transport accessory protein (rbat) family.

PTM databases

PhosphoSiteQ07837.

Polymorphism databases

DMDM67472674.

Proteomic databases

PaxDbQ07837.
PRIDEQ07837.

Protocols and materials databases

DNASU6519.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260649; ENSP00000260649; ENSG00000138079.
ENST00000409229; ENSP00000386620; ENSG00000138079.
ENST00000409741; ENSP00000386954; ENSG00000138079.
ENST00000410056; ENSP00000387337; ENSG00000138079.
GeneID6519.
KEGGhsa:6519.
UCSCuc002ruc.4. human. [Q07837-1]

Organism-specific databases

CTD6519.
GeneCardsGC02P044414.
HGNCHGNC:11025. SLC3A1.
HPAHPA038360.
MIM104614. gene.
220100. phenotype.
606407. phenotype.
neXtProtNX_Q07837.
Orphanet163693. 2p21 microdeletion syndrome.
238523. Atypical hypotonia - cystinuria syndrome.
93612. Cystinuria type A.
163690. Hypotonia - cystinuria syndrome.
PharmGKBPA35893.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000220640.
HOVERGENHBG053002.
InParanoidQ07837.
KOK14210.
OMATMYYGDE.
PhylomeDBQ07837.
TreeFamTF314498.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ07837.
BgeeQ07837.
CleanExHS_SLC3A1.
GenevestigatorQ07837.

Family and domain databases

Gene3D3.20.20.80. 2 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSLC3A1. human.
GeneWikiSLC3A1.
GenomeRNAi6519.
NextBio25349.
PROQ07837.
SOURCESearch...

Entry information

Entry nameSLC31_HUMAN
AccessionPrimary (citable) accession number: Q07837
Secondary accession number(s): A8K0S1 expand/collapse secondary AC list , O00658, Q15295, Q4J6B4, Q4J6B5, Q4J6B6, Q4J6B7, Q4J6B8, Q4J6B9, Q52M92, Q52M94
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 10, 2005
Last modified: July 9, 2014
This is version 153 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM