P05023 (AT1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sodium/potassium-transporting ATPase subunit alpha-1
Short name=Na(+)/K(+) ATPase alpha-1 subunit
EC=3.6.3.9

Alternative name(s):
Sodium pump subunit alpha-1

Gene names

Name:

ATP1A1

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	1023 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Catalytic activity	ATP + H2O + Na+(In) + K+(Out) = ADP + phosphate + Na+(Out) + K+(In).
Subunit structure	Interacts with SIK1 By similarity. Composed of three subunits: alpha (catalytic), beta and gamma. Binds the HLA class II histocompatibility antigen, DR1. Ref.11
Subcellular location	Cell membrane; Multi-pass membrane protein. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.14 Ref.16
Post-translational modification	Phosphorylation on Tyr-10 modulates pumping activity. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Sodium/potassium transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Sodium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro regulation of sodium ion transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: BHF-UCL endoplasmic reticulum Inferred from sequence or structural similarity. Source: BHF-UCL melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell sodium:potassium-exchanging ATPase complex Traceable author statement PubMed 1975705. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW chaperone binding Inferred from sequence or structural similarity. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sodium:potassium-exchanging ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: P05023-1)

Also known as: Long;

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: P05023-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     638-681: NETVEDIAAR...DMTSEQLDDI → SGPMSRGKSW...PGGIRSSSRG
     682-1023: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 3 (identifier: P05023-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 5	5			PRO_0000002483
	Chain	6 – 1023	1018	Sodium/potassium-transporting ATPase subunit alpha-1		PRO_0000002484
Regions
	Topological domain	6 – 87	82	Cytoplasmic Potential
	Transmembrane	88 – 108	21	Helical; Potential
	Topological domain	109 – 131	23	Extracellular Potential
	Transmembrane	132 – 152	21	Helical; Potential
	Topological domain	153 – 288	136	Cytoplasmic Potential
	Transmembrane	289 – 308	20	Helical; Potential
	Topological domain	309 – 320	12	Extracellular Potential
	Transmembrane	321 – 338	18	Helical; Potential
	Topological domain	339 – 772	434	Cytoplasmic Potential
	Transmembrane	773 – 792	20	Helical; Potential
	Topological domain	793 – 802	10	Extracellular Potential
	Transmembrane	803 – 823	21	Helical; Potential
	Topological domain	824 – 843	20	Cytoplasmic Potential
	Transmembrane	844 – 866	23	Helical; Potential
	Topological domain	867 – 918	52	Extracellular Potential
	Transmembrane	919 – 938	20	Helical; Potential
	Topological domain	939 – 951	13	Cytoplasmic Potential
	Transmembrane	952 – 970	19	Helical; Potential
	Topological domain	971 – 985	15	Extracellular Potential
	Transmembrane	986 – 1006	21	Helical; Potential
	Topological domain	1007 – 1023	17	Cytoplasmic Potential
	Region	82 – 84	3	Phosphoinositide-3 kinase binding By similarity
Sites
	Active site	376	1	4-aspartylphosphate intermediate By similarity
	Metal binding	717	1	Magnesium By similarity
	Metal binding	721	1	Magnesium By similarity
Amino acid modifications
	Modified residue	10	1	Phosphotyrosine By similarity
	Modified residue	16	1	Phosphoserine By similarity
	Modified residue	47	1	Phosphoserine By similarity
	Modified residue	217	1	Phosphoserine By similarity
	Modified residue	219	1	Phosphothreonine By similarity
	Modified residue	228	1	Phosphoserine By similarity
	Modified residue	260	1	Phosphotyrosine By similarity
	Modified residue	452	1	Phosphoserine By similarity
	Modified residue	542	1	Phosphotyrosine Ref.17
	Modified residue	943	1	Phosphoserine; by PKA By similarity
Natural variations
	Alternative sequence	1 – 31	31	Missing in isoform 3.		VSP_044242
	Alternative sequence	638 – 681	44	NETVE…QLDDI → SGPMSRGKSWSSPATQPSSS VSWWCSGPTWSSVRPGGIRS SSRG in isoform 2.		VSP_000415
	Alternative sequence	682 – 1023	342	Missing in isoform 2.		VSP_000416
	Natural variant	47	1	S → I. Corresponds to variant rs12564026 [ dbSNP | Ensembl ].		VAR_048374
Experimental info
	Sequence conflict	248	1	N → S in BAG37313. Ref.3
	Sequence conflict	475	1	A → T in CAA27390. Ref.13
	Sequence conflict	499	1	S → A in CAA27390. Ref.13
	Sequence conflict	502	1	Q → R in CAA27390. Ref.13
	Sequence conflict	523	1	L → I in CAA27390. Ref.13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified August 13, 1987. Version 1. Checksum: F3C6FDE04FB3F667	FASTA	1,023	112,896
	10 20 30 40 50 60 MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS 70 80 90 100 110 120 RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA 130 140 150 160 170 180 TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI 190 200 210 220 230 240 NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 250 260 270 280 290 300 NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV 310 320 330 340 350 360 FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 370 380 390 400 410 420 LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA 430 440 450 460 470 480 LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI 490 500 510 520 530 540 PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN 550 560 570 580 590 600 AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP 610 620 630 640 650 660 DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA 670 680 690 700 710 720 KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN 730 740 750 760 770 780 DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL 790 800 810 820 830 840 TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK 850 860 870 880 890 900 TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED 910 920 930 940 950 960 SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE 970 980 990 1000 1010 1020 ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE TYY
	Isoform 2 (Short) [UniParc]. Checksum: B74A8E7E31E975AD	FASTA	681	74,140
	10 20 30 40 50 60 MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS 70 80 90 100 110 120 RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA 130 140 150 160 170 180 TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI 190 200 210 220 230 240 NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR 250 260 270 280 290 300 NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV 310 320 330 340 350 360 FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN 370 380 390 400 410 420 LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA 430 440 450 460 470 480 LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI 490 500 510 520 530 540 PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN 550 560 570 580 590 600 AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP 610 620 630 640 650 660 DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGSGP MSRGKSWSSP ATQPSSSVSW 670 680 WCSGPTWSSV RPGGIRSSSR G
	Isoform 3 [UniParc]. Checksum: 6F607167FD03A23B	FASTA	992	109,550
	10 20 30 40 50 60 MDELKKEVSM DDHKLSLDEL HRKYGTDLSR GLTSARAAEI LARDGPNALT PPPTTPEWIK 70 80 90 100 110 120 FCRQLFGGFS MLLWIGAILC FLAYSIQAAT EEEPQNDNLY LGVVLSAVVI ITGCFSYYQE 130 140 150 160 170 180 AKSSKIMESF KNMVPQQALV IRNGEKMSIN AEEVVVGDLV EVKGGDRIPA DLRIISANGC 190 200 210 220 230 240 KVDNSSLTGE SEPQTRSPDF TNENPLETRN IAFFSTNCVE GTARGIVVYT GDRTVMGRIA 250 260 270 280 290 300 TLASGLEGGQ TPIAAEIEHF IHIITGVAVF LGVSFFILSL ILEYTWLEAV IFLIGIIVAN 310 320 330 340 350 360 VPEGLLATVT VCLTLTAKRM ARKNCLVKNL EAVETLGSTS TICSDKTGTL TQNRMTVAHM 370 380 390 400 410 420 WFDNQIHEAD TTENQSGVSF DKTSATWLAL SRIAGLCNRA VFQANQENLP ILKRAVAGDA 430 440 450 460 470 480 SESALLKCIE LCCGSVKEMR ERYAKIVEIP FNSTNKYQLS IHKNPNTSEP QHLLVMKGAP 490 500 510 520 530 540 ERILDRCSSI LLHGKEQPLD EELKDAFQNA YLELGGLGER VLGFCHLFLP DEQFPEGFQF 550 560 570 580 590 600 DTDDVNFPID NLCFVGLISM IDPPRAAVPD AVGKCRSAGI KVIMVTGDHP ITAKAIAKGV 610 620 630 640 650 660 GIISEGNETV EDIAARLNIP VSQVNPRDAK ACVVHGSDLK DMTSEQLDDI LKYHTEIVFA 670 680 690 700 710 720 RTSPQQKLII VEGCQRQGAI VAVTGDGVND SPALKKADIG VAMGIAGSDV SKQAADMILL 730 740 750 760 770 780 DDNFASIVTG VEEGRLIFDN LKKSIAYTLT SNIPEITPFL IFIIANIPLP LGTVTILCID 790 800 810 820 830 840 LGTDMVPAIS LAYEQAESDI MKRQPRNPKT DKLVNERLIS MAYGQIGMIQ ALGGFFTYFV 850 860 870 880 890 900 ILAENGFLPI HLLGLRVDWD DRWINDVEDS YGQQWTYEQR KIVEFTCHTA FFVSIVVVQW 910 920 930 940 950 960 ADLVICKTRR NSVFQQGMKN KILIFGLFEE TALAAFLSYC PGMGVALRMY PLKPTWWFCA 970 980 990 FPYSLLIFVY DEVRKLIIRR RPGGWVEKET YY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence." Kawakami K., Ohta T., Nojima H., Nagano K. J. Biochem. 100:389-397(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Characterization and quantification of full-length and truncated Na,K-ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal pigment epithelium." Ruiz A., Bhat S.P., Bok D. Gene 155:179-184(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Retinal pigment epithelium.
[3]	"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 1 AND 3). Tissue: Cerebellum.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 1). Tissue: Brain, Cervix and Skin.
[7]	"The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking region and identification of a restriction fragment length polymorphism." Shull M.M., Pugh D.G., Lingrel J.B. Genomics 6:451-460(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
[8]	Zhang J.-S., Yang J.X., Fang M.W., Lu S.D. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-148. Tissue: Placenta.
[9]	"Multiple genes encode the human Na+,K+-ATPase catalytic subunit." Shull M.M., Lingrel J.B. Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-189 AND 213-244.
[10]	"Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue expression, DNA polymorphism, and chromosomal localization." Chehab F.F., Kan Y.W., Law M.L., Hartz J., Kao F.T., Blostein R. Proc. Natl. Acad. Sci. U.S.A. 84:7901-7905(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-943 (ISOFORM 1). Tissue: Placenta.
[11]	"Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size." Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A.A., Strominger J.L. Nature 358:764-768(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 199-216, INTERACTION WITH HLA-DR1.
[12]	"The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit." Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., Petrukhin K.E., Gryshin A.V., Kiyatkin N.I., Kostina M.B., Sverdlov V.E., Modyanov N.N., Ovchinnikov Y.A. FEBS Lett. 217:275-278(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-341 AND 420-444.
[13]	"Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic region of the alpha-subunit of NA+,K+-ATPase." Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V., Modyanov N.N. Dokl. Biochem. 288:270-272(1986) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 471-619.
[14]	"Subcellular distribution and immunocytochemical localization of Na,K-ATPase subunit isoforms in human skeletal muscle." Hundal H.S., Maxwell D.L., Ahmed A., Darakhshan F., Mitsumoto Y., Klip A. Mol. Membr. Biol. 11:255-262(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[16]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-542, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00099 mRNA. Translation: BAA00061.1. X04297 mRNA. Translation: CAA27840.1. U16798 mRNA. Translation: AAC50131.1. AK296362 mRNA. Translation: BAH12332.1. AK314777 mRNA. Translation: BAG37313.1. AL136376 Genomic DNA. Translation: CAI22199.1. CH471122 Genomic DNA. Translation: EAW56644.1. BC003077 mRNA. Translation: AAH03077.1. BC001330 mRNA. Translation: AAH01330.1. BC050359 mRNA. Translation: AAH50359.1. M30310, M30309 Genomic DNA. Translation: AAA51801.1. L76938 Genomic DNA. Translation: AAA92713.1. M16793 mRNA. Translation: AAD56251.1. M16794 mRNA. Translation: AAD56252.1. J03007 mRNA. Translation: AAA51803.1. M27572 Genomic DNA. Translation: AAA35573.1. M27579 Genomic DNA. Translation: AAA35574.2. X03757 mRNA. Translation: CAA27390.1.
IPI	IPI00006482. IPI00414005.
PIR	A24414.
RefSeq	NP_000692.2. NM_000701.7. NP_001153705.1. NM_001160233.1. NP_001153706.1. NM_001160234.1.
UniGene	Hs.371889.
3D structure databases
ProteinModelPortal	P05023.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38196N.
IntAct	P05023. 15 interactions.
MINT	MINT-4998863.
STRING	9606.ENSP00000295598.
Protein family/group databases
TCDB	3.A.3.1.1. P-type ATPase (P-ATPase) superfamily.
PTM databases
PhosphoSite	P05023.
Polymorphism databases
DMDM	114374.
Proteomic databases
PaxDb	P05023.
PeptideAtlas	P05023.
PRIDE	P05023.
Protocols and materials databases
DNASU	476.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295598; ENSP00000295598; ENSG00000163399. ENST00000369496; ENSP00000358508; ENSG00000163399.
GeneID	476.
KEGG	hsa:476.
UCSC	uc001ege.3. human.
Organism-specific databases
CTD	476.
GeneCards	GC01P116915.
HGNC	HGNC:799. ATP1A1.
HPA	CAB018702.
MIM	182310. gene.
neXtProt	NX_P05023.
PharmGKB	PA62.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0474.
HOVERGEN	HBG004298.
InParanoid	P05023.
KO	K01539.
OMA	QFPEGFQ.
OrthoDB	EOG46MBHS.
PhylomeDB	P05023.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P05023.
Bgee	P05023.
CleanEx	HS_ATP1A1.
Genevestigator	P05023.
GermOnline	ENSG00000163399. Homo sapiens.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023299. ATPase_P-typ_cyto_domN. IPR005775. ATPase_P-typ_Na/K_IIC. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR008250. ATPase_P-typ_transduc_dom_A. IPR001757. Cation_transp_P_typ_ATPase. IPR023214. HAD-like_dom. [Graphical view]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P05023.
ChEMBL	CHEMBL1807.
ChiTaRS	ATP1A1. human.
DrugBank	DB00511. Acetyldigitoxin. DB01430. Almitrine. DB01370. Aluminium. DB01244. Bepridil. DB01158. Bretylium. DB01197. Captopril. DB01078. Deslanoside. DB01119. Diazoxide. DB01396. Digitoxin. DB00390. Digoxin. DB00736. Esomeprazole. DB00903. Ethacrynic acid. DB00695. Furosemide. DB00774. Hydroflumethiazide. DB00232. Methyclothiazide. DB01092. Ouabain. DB00213. Pantoprazole. DB01021. Trichlormethiazide.
GenomeRNAi	476.
NextBio	1971.
SOURCE	Search...

Entry information

Entry name

AT1A1_HUMAN

Accession

Primary (citable) accession number: P05023
Secondary accession number(s): B2RBR6 , B7Z3U6, Q16689, Q6LDM4, Q9UCN1, Q9UJ20, Q9UJ21

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 163 of the entry and version 1 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.