Q07837 (SLC31_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neutral and basic amino acid transport protein rBAT
Short name=NBAT

Alternative name(s):
B(0,+)-type amino acid transport protein
D2h

Gene names

Name:	SLC3A1
Synonyms:	RBAT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
Subcellular location	Membrane; Single-pass type II membrane protein Potential.
Tissue specificity	Predominantly expressed in the kidney, small intestine and pancreas. Weakly expressed in liver. Ref.1 Ref.3
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.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 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.12 Ref.13

Ontologies

Keywords
Biological process	Amino-acid transport Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Cystinuria Disease mutation
Domain	Signal-anchor Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Traceable author statement Ref.14. Source: ProtInc
Cellular_component	integral to plasma membrane Traceable author statement Ref.14. Source: ProtInc mitochondrial inner membrane Inferred from electronic annotation. Source: Compara vacuolar membrane Inferred from electronic annotation. Source: Compara
Molecular_function	L-cystine transmembrane transporter activity Traceable author statement Ref.14. Source: ProtInc basic amino acid transmembrane transporter activity Traceable author statement Ref.14. Source: ProtInc catalytic activity Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 685	685	Neutral and basic amino acid transport protein rBAT		PRO_0000071950
Regions
	Topological domain	1 – 87	87	Cytoplasmic Potential
	Transmembrane	88 – 108	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	109 – 685	577	Extracellular Potential
Amino acid modifications
	Glycosylation	214	1	N-linked (GlcNAc...) Potential
	Glycosylation	261	1	N-linked (GlcNAc...) Potential
	Glycosylation	332	1	N-linked (GlcNAc...) Potential
	Glycosylation	495	1	N-linked (GlcNAc...) Potential
	Glycosylation	513	1	N-linked (GlcNAc...) Potential
	Glycosylation	575	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	122	1	P → S in CSNU. Ref.18		VAR_064040
	Natural variant	128	1	P → Q in CSNU. Ref.15		VAR_011420
	Natural variant	151	1	Y → C in CSNU. Ref.19		VAR_038200
	Natural variant	181	1	R → Q in CSNU. Ref.14		VAR_011421
	Natural variant	216	1	T → M in CSNU. Ref.20		VAR_022600
	Natural variant	253	1	N → K in CSNU. Ref.19		VAR_038201
	Natural variant	268	1	E → K in CSNU; reduction in amino acid transport activity. Ref.17		VAR_011422
	Natural variant	341	1	T → A in CSNU; reduction in amino acid transport activity. Ref.17		VAR_011423
	Natural variant	362	1	R → C in CSNU. Ref.20		VAR_022601
	Natural variant	362	1	R → H in CSNU. Ref.19		VAR_038202
	Natural variant	365	1	R → W in CSNU. Ref.16 Ref.20		VAR_011424
	Natural variant	398	1	G → R in CSNU. Ref.19		VAR_038203
	Natural variant	452	1	R → W in CSNU. Ref.5		VAR_011425
	Natural variant	461	1	Y → H in CSNU. Ref.5 Ref.19		VAR_011426
	Natural variant	467	1	M → K in CSNU. Ref.14		VAR_011428
	Natural variant	467	1	M → T in CSNU; loss of 80% of amino acid transport activity. Ref.5 Ref.14 Ref.19 Ref.20		VAR_011427
	Natural variant	481	1	G → V in CSNU. Ref.19		VAR_038204
	Natural variant	482	1	E → K in CSNU. Ref.19		VAR_038205
	Natural variant	508	1	P → A in CSNU. Ref.20		VAR_022602
	Natural variant	510	1	Q → R in CSNU. Ref.19		VAR_038206
	Natural variant	582	1	Y → H in CSNU. Ref.16		VAR_011429
	Natural variant	584	1	R → T in CSNU. Ref.19		VAR_038207
	Natural variant	599	1	F → S in CSNU. Ref.19		VAR_038208
	Natural variant	600	1	G → E in CSNU. Ref.19		VAR_038209
	Natural variant	615	1	P → T in CSNU. Ref.14		VAR_011430
	Natural variant	618	1	M → I. Ref.1 Ref.4 Ref.5 Ref.6 Ref.10 Ref.16 Ref.19 Corresponds to variant rs698761 [ dbSNP | Ensembl ].		VAR_011431
	Natural variant	648	1	F → S in CSNU. Ref.16		VAR_011432
	Natural variant	652	1	T → R in CSNU. Ref.14		VAR_011433
	Natural variant	678	1	L → P in CSNU. Ref.14		VAR_011434

Sequences

	Sequence		Length	Mass (Da)
	Q07837 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: F9D6DFD548283899	FASTA	685	78,852
	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

References

	« Hide 'large scale' referencesShow '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], 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], 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], 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], FUNCTION, VARIANT ILE-618. Tissue: Kidney.
[7]	"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]. Tissue: Amygdala.
[8]	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]. Tissue: Kidney.
[9]	"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].
[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], VARIANT ILE-618. Tissue: Brain and Kidney.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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

GeneReviews

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 , U60810, U60811, U60812, U60813, U60816, U60818, U60814, U60815 Genomic DNA. Translation: AAB39829.1. AB033549 mRNA. Translation: BAB16841.1. 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.
IPI	IPI00029268.
PIR	A47102.
RefSeq	NP_000332.2. NM_000341.3.
UniGene	Hs.112916.
3D structure databases
ProteinModelPortal	Q07837.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000260649.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
PTM databases
PhosphoSite	Q07837.
Polymorphism databases
DMDM	67472674.
Proteomic databases
PaxDb	Q07837.
PRIDE	Q07837.
Protocols and materials databases
DNASU	6519.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260649; ENSP00000260649; ENSG00000138079.
GeneID	6519.
KEGG	hsa:6519.
UCSC	uc002ruc.4. human.
Organism-specific databases
CTD	6519.
GeneCards	GC02P044414.
HGNC	HGNC:11025. SLC3A1.
HPA	HPA038360.
MIM	104614. gene. 220100. phenotype. 606407. phenotype.
neXtProt	NX_Q07837.
Orphanet	163693. 2p21 microdeletion syndrome. 238523. Atypical hypotonia - cystinuria syndrome. 93612. Cystinuria type A. 163690. Hypotonia - cystinuria syndrome.
PharmGKB	PA35893.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0366.
HOGENOM	HOG000220640.
HOVERGEN	HBG053002.
InParanoid	Q07837.
KO	K14210.
OMA	QWQGQTL.
OrthoDB	EOG47H5PM.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules. REACT_19419. Amino acid and oligopeptide SLC transporters.
Gene expression databases
ArrayExpress	Q07837.
Bgee	Q07837.
CleanEx	HS_SLC3A1.
Genevestigator	Q07837.
GermOnline	ENSG00000138079. Homo sapiens.
Family and domain databases
Gene3D	3.20.20.80. 2 hits.
InterPro	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]
PANTHER	PTHR10357. PTHR10357. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. [Graphical view]
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SLC3A1. human.
DrugBank	DB00138. L-Cystine.
GenomeRNAi	6519.
NextBio	25349.
SOURCE	Search...

Entry information

Entry name

SLC31_HUMAN

Accession

Primary (citable) accession number: Q07837
Secondary accession number(s): A8K0S1 , O00658, Q15295, Q52M92, Q52M94

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.