Q92581 (SL9A6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sodium/hydrogen exchanger 6

Alternative name(s):
Na(+)/H(+) exchanger 6
Short name=NHE-6
Solute carrier family 9 member 6

Gene names

Name:	SLC9A6
Synonyms:	KIAA0267, NHE6

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	669 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electroneutral exchange of protons for Na+ and K+ across the early and recycling endosome membranes. Contributes to calcium homeostasis.
Subcellular location	Endosome membrane; Multi-pass membrane protein. Note: Is present in the recycling compartments including early and recycling endosomes, and only appears transiently on the plasma membrane. Ref.6
Tissue specificity	Ubiquitous; but is most abundant in mitochondrion-rich tissues such as brain, skeletal muscle and heart.
Involvement in disease	Mental retardation, X-linked, syndromic, Christianson type (MRXSCH) [MIM:300243]: A syndrome characterized by profound mental retardation, epilepsy, ataxia, and microcephaly. It shows phenotypic overlap with Angelman syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8
Sequence similarities	Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. [View classification]
Caution	Was originally (Ref.1) identified as a mitochondrial inner membrane protein, but was later shown to be localized in early and recycling endosomes and not mitochondria (Ref.6).

Ontologies

Keywords
Biological process	Antiport Ion transport Sodium transport Transport
Cellular component	Endosome Membrane
Coding sequence diversity	Alternative splicing
Disease	Epilepsy Mental retardation
Domain	Transmembrane Transmembrane helix
Ligand	Sodium
PTM	Glycoprotein Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of pH Inferred from electronic annotation. Source: InterPro
Cellular_component	early endosome membrane Inferred from direct assay Ref.6. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay PubMed 11641397. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.6. Source: UniProtKB recycling endosome membrane Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	sodium:hydrogen antiporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92581-1)

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 2 (identifier: Q92581-2)

The sequence of this isoform differs from the canonical sequence as follows:
     144-144: V → VNVSGKFYEYMLKGEISSHELNNVQDNEMLRKV

Isoform 3 (identifier: Q92581-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     144-144: V → VNVSGKFYEYMLKGEISSHELNNVQDNEMLRKV

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 669	669	Sodium/hydrogen exchanger 6		PRO_0000052362
Regions
	Transmembrane	28 – 48	21	Helical; Potential
	Transmembrane	71 – 91	21	Helical; Potential
	Transmembrane	103 – 123	21	Helical; Potential
	Transmembrane	142 – 162	21	Helical; Potential
	Transmembrane	179 – 199	21	Helical; Potential
	Transmembrane	220 – 240	21	Helical; Potential
	Transmembrane	246 – 266	21	Helical; Potential
	Transmembrane	292 – 312	21	Helical; Potential
	Transmembrane	340 – 360	21	Helical; Potential
	Transmembrane	382 – 402	21	Helical; Potential
	Transmembrane	404 – 424	21	Helical; Potential
	Transmembrane	447 – 467	21	Helical; Potential
	Transmembrane	483 – 503	21	Helical; Potential
Amino acid modifications
	Glycosylation	128	1	N-linked (GlcNAc...) Ref.9
	Cross-link	443		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Natural variations
	Alternative sequence	1 – 52	52	Missing in isoform 3.		VSP_044868
	Alternative sequence	144	1	V → VNVSGKFYEYMLKGEISSHE LNNVQDNEMLRKV in isoform 2 and isoform 3.		VSP_042030
Experimental info
	Sequence conflict	20	1	R → G in AAH35029. Ref.4
	Sequence conflict	92	1	K → E in BAF82464. Ref.2
	Sequence conflict	144	1	V → I in BAH14626. Ref.2
	Sequence conflict	307	1	A → T in BAH14626. Ref.2
	Sequence conflict	372	1	T → M in BAF82464. Ref.2
	Sequence conflict	373	1	E → G in BAG62192. Ref.2
	Sequence conflict	634	1	A → S in BAF82464. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: F6416596229F2639	FASTA	669	74,162
	10 20 30 40 50 60 MARRGWRRAP LRRGVGSSPR ARRLMRPLWL LLAVGVFDWA GASDGGGGEA RAMDEEIVSE 70 80 90 100 110 120 KQAEESHRQD SANLLIFILL LTLTILTIWL FKHRRARFLH ETGLAMIYGL LVGLVLRYGI 130 140 150 160 170 180 HVPSDVNNVT LSCEVQSSPT TLLVTFDPEV FFNILLPPII FYAGYSLKRR HFFRNLGSIL 190 200 210 220 230 240 AYAFLGTAIS CFVIGSIMYG CVTLMKVTGQ LAGDFYFTDC LLFGAIVSAT DPVTVLAIFH 250 260 270 280 290 300 ELQVDVELYA LLFGESVLND AVAIVLSSSI VAYQPAGDNS HTFDVTAMFK SIGIFLGIFS 310 320 330 340 350 360 GSFAMGAATG VVTALVTKFT KLREFQLLET GLFFLMSWST FLLAEAWGFT GVVAVLFCGI 370 380 390 400 410 420 TQAHYTYNNL STESQHRTKQ LFELLNFLAE NFIFSYMGLT LFTFQNHVFN PTFVVGAFVA 430 440 450 460 470 480 IFLGRAANIY PLSLLLNLGR RSKIGSNFQH MMMFAGLRGA MAFALAIRDT ATYARQMMFS 490 500 510 520 530 540 TTLLIVFFTV WVFGGGTTAM LSCLHIRVGV DSDQEHLGVP ENERRTTKAE SAWLFRMWYN 550 560 570 580 590 600 FDHNYLKPLL THSGPPLTTT LPACCGPIAR CLTSPQAYEN QEQLKDDDSD LILNDGDISL 610 620 630 640 650 660 TYGDSTVNTE PATSSAPRRF MGNSSEDALD RELAFGDHEL VIRGTRLVLP MDDSEPPLNL LDNTRHGPA
	Isoform 2 [UniParc]. Checksum: A2BE0E4EF07A62EC	FASTA	701	77,917
	10 20 30 40 50 60 MARRGWRRAP LRRGVGSSPR ARRLMRPLWL LLAVGVFDWA GASDGGGGEA RAMDEEIVSE 70 80 90 100 110 120 KQAEESHRQD SANLLIFILL LTLTILTIWL FKHRRARFLH ETGLAMIYGL LVGLVLRYGI 130 140 150 160 170 180 HVPSDVNNVT LSCEVQSSPT TLLVNVSGKF YEYMLKGEIS SHELNNVQDN EMLRKVTFDP 190 200 210 220 230 240 EVFFNILLPP IIFYAGYSLK RRHFFRNLGS ILAYAFLGTA ISCFVIGSIM YGCVTLMKVT 250 260 270 280 290 300 GQLAGDFYFT DCLLFGAIVS ATDPVTVLAI FHELQVDVEL YALLFGESVL NDAVAIVLSS 310 320 330 340 350 360 SIVAYQPAGD NSHTFDVTAM FKSIGIFLGI FSGSFAMGAA TGVVTALVTK FTKLREFQLL 370 380 390 400 410 420 ETGLFFLMSW STFLLAEAWG FTGVVAVLFC GITQAHYTYN NLSTESQHRT KQLFELLNFL 430 440 450 460 470 480 AENFIFSYMG LTLFTFQNHV FNPTFVVGAF VAIFLGRAAN IYPLSLLLNL GRRSKIGSNF 490 500 510 520 530 540 QHMMMFAGLR GAMAFALAIR DTATYARQMM FSTTLLIVFF TVWVFGGGTT AMLSCLHIRV 550 560 570 580 590 600 GVDSDQEHLG VPENERRTTK AESAWLFRMW YNFDHNYLKP LLTHSGPPLT TTLPACCGPI 610 620 630 640 650 660 ARCLTSPQAY ENQEQLKDDD SDLILNDGDI SLTYGDSTVN TEPATSSAPR RFMGNSSEDA 670 680 690 700 LDRELAFGDH ELVIRGTRLV LPMDDSEPPL NLLDNTRHGP A
	Isoform 3 [UniParc]. Checksum: F875E7739A25438F	FASTA	649	72,260
	10 20 30 40 50 60 MDEEIVSEKQ AEESHRQDSA NLLIFILLLT LTILTIWLFK HRRARFLHET GLAMIYGLLV 70 80 90 100 110 120 GLVLRYGIHV PSDVNNVTLS CEVQSSPTTL LVNVSGKFYE YMLKGEISSH ELNNVQDNEM 130 140 150 160 170 180 LRKVTFDPEV FFNILLPPII FYAGYSLKRR HFFRNLGSIL AYAFLGTAIS CFVIGSIMYG 190 200 210 220 230 240 CVTLMKVTGQ LAGDFYFTDC LLFGAIVSAT DPVTVLAIFH ELQVDVELYA LLFGESVLND 250 260 270 280 290 300 AVAIVLSSSI VAYQPAGDNS HTFDVTAMFK SIGIFLGIFS GSFAMGAATG VVTALVTKFT 310 320 330 340 350 360 KLREFQLLET GLFFLMSWST FLLAEAWGFT GVVAVLFCGI TQAHYTYNNL STESQHRTKQ 370 380 390 400 410 420 LFELLNFLAE NFIFSYMGLT LFTFQNHVFN PTFVVGAFVA IFLGRAANIY PLSLLLNLGR 430 440 450 460 470 480 RSKIGSNFQH MMMFAGLRGA MAFALAIRDT ATYARQMMFS TTLLIVFFTV WVFGGGTTAM 490 500 510 520 530 540 LSCLHIRVGV DSDQEHLGVP ENERRTTKAE SAWLFRMWYN FDHNYLKPLL THSGPPLTTT 550 560 570 580 590 600 LPACCGPIAR CLTSPQAYEN QEQLKDDDSD LILNDGDISL TYGDSTVNTE PATSSAPRRF 610 620 630 640 MGNSSEDALD RELAFGDHEL VIRGTRLVLP MDDSEPPLNL LDNTRHGPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a mitochondrial Na+/H+ exchanger." Numata M., Petrecca K., Lake N., Orlowski J. J. Biol. Chem. 273:6951-6959(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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] (ISOFORMS 2 AND 3). Tissue: Brain and Placenta.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 2). Tissue: Brain.
[5]	"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-669 (ISOFORM 1). Tissue: Bone marrow.
[6]	"Human Na(+)/H(+) exchanger isoform 6 is found in recycling endosomes of cells, not in mitochondria." Brett C.L., Wei Y., Donowitz M., Rao R. Am. J. Physiol. 282:C1031-C1041(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-443, MASS SPECTROMETRY. Tissue: Mammary cancer.
[8]	"SLC9A6 mutations cause X-linked mental retardation, microcephaly, epilepsy, and ataxia, a phenotype mimicking Angelman syndrome." Gilfillan G.D., Selmer K.K., Roxrud I., Smith R., Kyllerman M., Eiklid K., Kroken M., Mattingsdal M., Egeland T., Stenmark H., Sjoholm H., Server A., Samuelsson L., Christianson A., Tarpey P., Whibley A., Stratton M.R., Futreal P.A. , Teague J., Edkins S., Gecz J., Turner G., Raymond F.L., Schwartz C., Stevenson R.E., Undlien D.E., Stromme P. Am. J. Hum. Genet. 82:1003-1010(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MRXSCH.
[9]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF030409 mRNA. Translation: AAC39643.1. AK289775 mRNA. Translation: BAF82464.1. AK300475 mRNA. Translation: BAG62192.1. AK316255 mRNA. Translation: BAH14626.1. AL732579 Genomic DNA. Translation: CAI39923.1. AL732579 Genomic DNA. Translation: CAI39924.1. AL732579 Genomic DNA. Translation: CAI39925.1. BC035029 mRNA. Translation: AAH35029.1. BC049169 mRNA. Translation: AAH49169.1. D87743 mRNA. Translation: BAA13449.1.
IPI	IPI00022061. IPI00647658.
RefSeq	NP_001036002.1. NM_001042537.1. NP_001171122.1. NM_001177651.1. NP_006350.1. NM_006359.2.
UniGene	Hs.62185.
3D structure databases
ProteinModelPortal	Q92581.
SMR	Q92581. Positions 218-246.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000359729.
PTM databases
PhosphoSite	Q92581.
Polymorphism databases
DMDM	6919937.
Proteomic databases
PaxDb	Q92581.
PRIDE	Q92581.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370695; ENSP00000359729; ENSG00000198689. ENST00000370698; ENSP00000359732; ENSG00000198689. ENST00000370701; ENSP00000359735; ENSG00000198689. ENST00000595850; ENSP00000470998; ENSG00000269036. ENST00000595964; ENSP00000471427; ENSG00000269036. ENST00000597470; ENSP00000470918; ENSG00000269036.
GeneID	10479.
KEGG	hsa:10479.
UCSC	uc004ezj.3. human.
Organism-specific databases
CTD	10479.
GeneCards	GC0XP135068.
HGNC	HGNC:11079. SLC9A6.
MIM	300231. gene. 300243. phenotype.
neXtProt	NX_Q92581.
Orphanet	85278. X-linked intellectual deficit, South African type.
PharmGKB	PA35935.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0025.
HOGENOM	HOG000172307.
HOVERGEN	HBG055575.
KO	K12041.
OMA	DQEHLGV.
PhylomeDB	Q92581.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q92581.
Bgee	Q92581.
CleanEx	HS_SLC9A6.
Genevestigator	Q92581.
GermOnline	ENSG00000198689. Homo sapiens.
Family and domain databases
InterPro	IPR006153. Cation/H_exchanger. IPR018422. Cation/H_exchanger_CPA1. IPR002090. Na/H_exchanger_6. IPR004709. NaH_exchanger. [Graphical view]
PANTHER	PTHR10110. PTHR10110. 1 hit.
Pfam	PF00999. Na_H_Exchanger. 1 hit. [Graphical view]
PRINTS	PR01084. NAHEXCHNGR. PR01088. NAHEXCHNGR6.
TIGRFAMs	TIGR00840. b_cpa1. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10479.
NextBio	35480885.
SOURCE	Search...

Entry information

Entry name

SL9A6_HUMAN

Accession

Primary (citable) accession number: Q92581
Secondary accession number(s): A6NIQ9 , A8K160, B4DU30, B7ZAE0, Q3ZCW7, Q5JPP8, Q5JPP9, Q86VS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 121 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.