Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sodium/hydrogen exchanger 6

Gene

SLC9A6

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

Functioni

Electroneutral exchange of protons for Na+ and K+ across the early and recycling endosome membranes. Contributes to calcium homeostasis.

GO - Molecular functioni

  • sodium:proton antiporter activity Source: ProtInc

GO - Biological processi

  • axon extension Source: MGI
  • brain-derived neurotrophic factor receptor signaling pathway Source: Ensembl
  • dendrite extension Source: MGI
  • dendritic spine development Source: Ensembl
  • ion transport Source: Reactome
  • neuron projection morphogenesis Source: MGI
  • regulation of neurotrophin TRK receptor signaling pathway Source: Ensembl
  • regulation of pH Source: InterPro
  • sodium ion transmembrane transport Source: GOC
  • synapse organization Source: Ensembl
  • transmembrane transport Source: Reactome
  • transport Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Enzyme and pathway databases

ReactomeiREACT_19314. Sodium/Proton exchangers.

Protein family/group databases

TCDBi2.A.36.1.14. the monovalent cation:proton antiporter-1 (cpa1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/hydrogen exchanger 6
Alternative name(s):
Na(+)/H(+) exchanger 6
Short name:
NHE-6
Solute carrier family 9 member 6
Gene namesi
Name:SLC9A6
Synonyms:KIAA0267, NHE6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11079. SLC9A6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei28 – 4821HelicalSequence AnalysisAdd
BLAST
Transmembranei71 – 9121HelicalSequence AnalysisAdd
BLAST
Transmembranei103 – 12321HelicalSequence AnalysisAdd
BLAST
Transmembranei142 – 16221HelicalSequence AnalysisAdd
BLAST
Transmembranei179 – 19921HelicalSequence AnalysisAdd
BLAST
Transmembranei220 – 24021HelicalSequence AnalysisAdd
BLAST
Transmembranei246 – 26621HelicalSequence AnalysisAdd
BLAST
Transmembranei292 – 31221HelicalSequence AnalysisAdd
BLAST
Transmembranei340 – 36021HelicalSequence AnalysisAdd
BLAST
Transmembranei382 – 40221HelicalSequence AnalysisAdd
BLAST
Transmembranei404 – 42421HelicalSequence AnalysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence AnalysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axonal spine Source: Ensembl
  • axon terminus Source: Ensembl
  • cytoplasmic vesicle Source: Ensembl
  • dendrite Source: Ensembl
  • early endosome membrane Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: HPA
  • late endosome Source: Ensembl
  • plasma membrane Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, Christianson type (MRXSCH)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by profound mental retardation, epilepsy, ataxia, and microcephaly. It shows phenotypic overlap with Angelman syndrome.

See also OMIM:300243

Keywords - Diseasei

Epilepsy, Mental retardation

Organism-specific databases

MIMi300243. phenotype.
Orphaneti85278. Christianson syndrome.
PharmGKBiPA35935.

Polymorphism and mutation databases

BioMutaiSLC9A6.
DMDMi6919937.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 669669Sodium/hydrogen exchanger 6PRO_0000052362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)1 Publication
Cross-linki443 – 443Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ92581.
PaxDbiQ92581.
PRIDEiQ92581.

PTM databases

PhosphoSiteiQ92581.

Expressioni

Tissue specificityi

Ubiquitous; but is most abundant in mitochondrion-rich tissues such as brain, skeletal muscle and heart.

Gene expression databases

BgeeiQ92581.
CleanExiHS_SLC9A6.
GenevisibleiQ92581. HS.

Organism-specific databases

HPAiHPA059445.
HPA059590.

Interactioni

Protein-protein interaction databases

BioGridi115742. 6 interactions.
STRINGi9606.ENSP00000359729.

Structurei

3D structure databases

ProteinModelPortaliQ92581.
SMRiQ92581. Positions 159-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0025.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000172307.
HOVERGENiHBG055575.
InParanoidiQ92581.
KOiK12041.
OMAiDQEHLGV.
OrthoDBiEOG7NW69D.
PhylomeDBiQ92581.
TreeFamiTF318755.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR002090. Na/H_exchanger_6.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01088. NAHEXCHNGR6.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92581-1) [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

        10         20         30         40         50
MARRGWRRAP LRRGVGSSPR ARRLMRPLWL LLAVGVFDWA GASDGGGGEA
60 70 80 90 100
RAMDEEIVSE KQAEESHRQD SANLLIFILL LTLTILTIWL FKHRRARFLH
110 120 130 140 150
ETGLAMIYGL LVGLVLRYGI HVPSDVNNVT LSCEVQSSPT TLLVTFDPEV
160 170 180 190 200
FFNILLPPII FYAGYSLKRR HFFRNLGSIL AYAFLGTAIS CFVIGSIMYG
210 220 230 240 250
CVTLMKVTGQ LAGDFYFTDC LLFGAIVSAT DPVTVLAIFH ELQVDVELYA
260 270 280 290 300
LLFGESVLND AVAIVLSSSI VAYQPAGDNS HTFDVTAMFK SIGIFLGIFS
310 320 330 340 350
GSFAMGAATG VVTALVTKFT KLREFQLLET GLFFLMSWST FLLAEAWGFT
360 370 380 390 400
GVVAVLFCGI TQAHYTYNNL STESQHRTKQ LFELLNFLAE NFIFSYMGLT
410 420 430 440 450
LFTFQNHVFN PTFVVGAFVA IFLGRAANIY PLSLLLNLGR RSKIGSNFQH
460 470 480 490 500
MMMFAGLRGA MAFALAIRDT ATYARQMMFS TTLLIVFFTV WVFGGGTTAM
510 520 530 540 550
LSCLHIRVGV DSDQEHLGVP ENERRTTKAE SAWLFRMWYN FDHNYLKPLL
560 570 580 590 600
THSGPPLTTT LPACCGPIAR CLTSPQAYEN QEQLKDDDSD LILNDGDISL
610 620 630 640 650
TYGDSTVNTE PATSSAPRRF MGNSSEDALD RELAFGDHEL VIRGTRLVLP
660
MDDSEPPLNL LDNTRHGPA
Length:669
Mass (Da):74,162
Last modified:May 1, 1999 - v2
Checksum:iF6416596229F2639
GO
Isoform 2 (identifier: Q92581-2) [UniParc]FASTAAdd to basket

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

Show »
Length:701
Mass (Da):77,917
Checksum:iA2BE0E4EF07A62EC
GO
Isoform 3 (identifier: Q92581-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:649
Mass (Da):72,260
Checksum:iF875E7739A25438F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201R → G in AAH35029 (PubMed:15489334).Curated
Sequence conflicti92 – 921K → E in BAF82464 (PubMed:14702039).Curated
Sequence conflicti144 – 1441V → I in BAH14626 (PubMed:14702039).Curated
Sequence conflicti307 – 3071A → T in BAH14626 (PubMed:14702039).Curated
Sequence conflicti372 – 3721T → M in BAF82464 (PubMed:14702039).Curated
Sequence conflicti373 – 3731E → G in BAG62192 (PubMed:14702039).Curated
Sequence conflicti634 – 6341A → S in BAF82464 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform 3. 1 PublicationVSP_044868Add
BLAST
Alternative sequencei144 – 1441V → VNVSGKFYEYMLKGEISSHE LNNVQDNEMLRKV in isoform 2 and isoform 3. 2 PublicationsVSP_042030

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14654.1. [Q92581-1]
CCDS44003.1. [Q92581-2]
CCDS55504.1. [Q92581-3]
RefSeqiNP_001036002.1. NM_001042537.1. [Q92581-2]
NP_001171122.1. NM_001177651.1. [Q92581-3]
NP_006350.1. NM_006359.2. [Q92581-1]
XP_006724789.1. XM_006724726.2. [Q92581-3]
UniGeneiHs.62185.

Genome annotation databases

EnsembliENST00000370695; ENSP00000359729; ENSG00000198689. [Q92581-2]
ENST00000370698; ENSP00000359732; ENSG00000198689.
ENST00000370701; ENSP00000359735; ENSG00000198689. [Q92581-3]
GeneIDi10479.
KEGGihsa:10479.
UCSCiuc004ezj.3. human. [Q92581-1]
uc004ezk.3. human. [Q92581-2]
uc011mvx.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14654.1. [Q92581-1]
CCDS44003.1. [Q92581-2]
CCDS55504.1. [Q92581-3]
RefSeqiNP_001036002.1. NM_001042537.1. [Q92581-2]
NP_001171122.1. NM_001177651.1. [Q92581-3]
NP_006350.1. NM_006359.2. [Q92581-1]
XP_006724789.1. XM_006724726.2. [Q92581-3]
UniGeneiHs.62185.

3D structure databases

ProteinModelPortaliQ92581.
SMRiQ92581. Positions 159-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115742. 6 interactions.
STRINGi9606.ENSP00000359729.

Protein family/group databases

TCDBi2.A.36.1.14. the monovalent cation:proton antiporter-1 (cpa1) family.

PTM databases

PhosphoSiteiQ92581.

Polymorphism and mutation databases

BioMutaiSLC9A6.
DMDMi6919937.

Proteomic databases

MaxQBiQ92581.
PaxDbiQ92581.
PRIDEiQ92581.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370695; ENSP00000359729; ENSG00000198689. [Q92581-2]
ENST00000370698; ENSP00000359732; ENSG00000198689.
ENST00000370701; ENSP00000359735; ENSG00000198689. [Q92581-3]
GeneIDi10479.
KEGGihsa:10479.
UCSCiuc004ezj.3. human. [Q92581-1]
uc004ezk.3. human. [Q92581-2]
uc011mvx.2. human.

Organism-specific databases

CTDi10479.
GeneCardsiGC0XP135068.
HGNCiHGNC:11079. SLC9A6.
HPAiHPA059445.
HPA059590.
MIMi300231. gene.
300243. phenotype.
neXtProtiNX_Q92581.
Orphaneti85278. Christianson syndrome.
PharmGKBiPA35935.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0025.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000172307.
HOVERGENiHBG055575.
InParanoidiQ92581.
KOiK12041.
OMAiDQEHLGV.
OrthoDBiEOG7NW69D.
PhylomeDBiQ92581.
TreeFamiTF318755.

Enzyme and pathway databases

ReactomeiREACT_19314. Sodium/Proton exchangers.

Miscellaneous databases

GeneWikiiSLC9A6.
GenomeRNAii10479.
NextBioi35480885.
PROiQ92581.
SOURCEiSearch...

Gene expression databases

BgeeiQ92581.
CleanExiHS_SLC9A6.
GenevisibleiQ92581. HS.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR002090. Na/H_exchanger_6.
IPR004709. NaH_exchanger.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01088. NAHEXCHNGR6.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Tissue: Mammary cancer.
  8. 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.
    Tissue: Liver.
  10. Cited for: INVOLVEMENT IN MRXSCH.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSL9A6_HUMAN
AccessioniPrimary (citable) accession number: Q92581
Secondary accession number(s): A6NIQ9
, A8K160, B4DU30, B7ZAE0, Q3ZCW7, Q5JPP8, Q5JPP9, Q86VS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 144 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

Caution

Was originally (PubMed:9507001) identified as a mitochondrial inner membrane protein, but was later shown to be localized in early and recycling endosomes and not mitochondria (PubMed:11940519).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.