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Q92581

- SL9A6_HUMAN

UniProt

Q92581 - SL9A6_HUMAN

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Protein

Sodium/hydrogen exchanger 6

Gene

SLC9A6

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. sodium:proton antiporter activity Source: ProtInc

GO - Biological processi

  1. axon extension Source: MGI
  2. brain-derived neurotrophic factor receptor signaling pathway Source: Ensembl
  3. dendrite extension Source: MGI
  4. dendritic spine development Source: Ensembl
  5. ion transport Source: Reactome
  6. neuron projection morphogenesis Source: MGI
  7. regulation of neurotrophin TRK receptor signaling pathway Source: Ensembl
  8. regulation of pH Source: InterPro
  9. sodium ion transmembrane transport Source: GOC
  10. synapse organization Source: Ensembl
  11. transmembrane transport Source: Reactome
  12. 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: Chromosome X

Organism-specific databases

HGNCiHGNC:11079. SLC9A6.

Subcellular locationi

Endosome membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Is present in the recycling compartments including early and recycling endosomes, and only appears transiently on the plasma membrane.

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

  1. axonal spine Source: Ensembl
  2. axon terminus Source: Ensembl
  3. cytoplasmic vesicle Source: Ensembl
  4. dendrite Source: Ensembl
  5. early endosome membrane Source: UniProtKB
  6. endoplasmic reticulum membrane Source: UniProtKB
  7. integral component of membrane Source: UniProtKB-KW
  8. late endosome Source: Ensembl
  9. plasma membrane Source: UniProtKB
  10. recycling endosome membrane Source: UniProtKB
  11. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Epilepsy, Mental retardation

Organism-specific databases

MIMi300243. phenotype.
Orphaneti85278. Christianson syndrome.
PharmGKBiPA35935.

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.
ExpressionAtlasiQ92581. baseline and differential.
GenevestigatoriQ92581.

Organism-specific databases

HPAiHPA059445.

Interactioni

Protein-protein interaction databases

BioGridi115742. 6 interactions.
STRINGi9606.ENSP00000359729.

Structurei

3D structure databases

ProteinModelPortaliQ92581.
SMRiQ92581. Positions 219-266.
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. Align

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_006724726.1. [Q92581-3]
UniGeneiHs.62185.

Genome annotation databases

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

Polymorphism databases

DMDMi6919937.

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 .
CCDSi CCDS14654.1. [Q92581-1 ]
CCDS44003.1. [Q92581-2 ]
CCDS55504.1. [Q92581-3 ]
RefSeqi NP_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_006724726.1. [Q92581-3 ]
UniGenei Hs.62185.

3D structure databases

ProteinModelPortali Q92581.
SMRi Q92581. Positions 219-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115742. 6 interactions.
STRINGi 9606.ENSP00000359729.

Protein family/group databases

TCDBi 2.A.36.1.14. the monovalent cation:proton antiporter-1 (cpa1) family.

PTM databases

PhosphoSitei Q92581.

Polymorphism databases

DMDMi 6919937.

Proteomic databases

MaxQBi Q92581.
PaxDbi Q92581.
PRIDEi Q92581.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370695 ; ENSP00000359729 ; ENSG00000198689 . [Q92581-2 ]
ENST00000370698 ; ENSP00000359732 ; ENSG00000198689 . [Q92581-1 ]
ENST00000370701 ; ENSP00000359735 ; ENSG00000198689 . [Q92581-3 ]
GeneIDi 10479.
KEGGi hsa:10479.
UCSCi uc004ezj.3. human. [Q92581-1 ]
uc004ezk.3. human. [Q92581-2 ]
uc011mvx.2. human.

Organism-specific databases

CTDi 10479.
GeneCardsi GC0XP135068.
HGNCi HGNC:11079. SLC9A6.
HPAi HPA059445.
MIMi 300231. gene.
300243. phenotype.
neXtProti NX_Q92581.
Orphaneti 85278. Christianson syndrome.
PharmGKBi PA35935.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0025.
GeneTreei ENSGT00760000119074.
HOGENOMi HOG000172307.
HOVERGENi HBG055575.
InParanoidi Q92581.
KOi K12041.
OMAi DQEHLGV.
OrthoDBi EOG7NW69D.
PhylomeDBi Q92581.
TreeFami TF318755.

Enzyme and pathway databases

Reactomei REACT_19314. Sodium/Proton exchangers.

Miscellaneous databases

GeneWikii SLC9A6.
GenomeRNAii 10479.
NextBioi 35480885.
PROi Q92581.
SOURCEi Search...

Gene expression databases

Bgeei Q92581.
CleanExi HS_SLC9A6.
ExpressionAtlasi Q92581. baseline and differential.
Genevestigatori Q92581.

Family and domain databases

InterProi IPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR002090. Na/H_exchanger_6.
IPR004709. NaH_exchanger.
[Graphical view ]
PANTHERi PTHR10110. PTHR10110. 1 hit.
Pfami PF00999. Na_H_Exchanger. 1 hit.
[Graphical view ]
PRINTSi PR01084. NAHEXCHNGR.
PR01088. NAHEXCHNGR6.
TIGRFAMsi TIGR00840. b_cpa1. 1 hit.
ProtoNeti Search...

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.

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: October 29, 2014
This is version 137 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 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