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Protein

Phospholipid-transporting ATPase IA

Gene

ATP8A1

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

Functioni

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Acts as aminophospholipid translocase at the plasma membrane in neuronal cells.

Catalytic activityi

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Enzyme regulationi

ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei409 – 40914-aspartylphosphate intermediateBy similarity
Metal bindingi801 – 8011MagnesiumBy similarity
Metal bindingi805 – 8051MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi741 – 7488ATPSequence analysis
Nucleotide bindingi1095 – 11028ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.1. 2681.
ReactomeiR-HSA-936837. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.8.13. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase IA (EC:3.6.3.1)
Alternative name(s):
ATPase class I type 8A member 1
Chromaffin granule ATPase II
P4-ATPase flippase complex alpha subunit ATP8A1
Gene namesi
Name:ATP8A1
Synonyms:ATPIA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:13531. ATP8A1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6565CytoplasmicSequence analysisAdd
BLAST
Transmembranei66 – 8621HelicalSequence analysisAdd
BLAST
Topological domaini87 – 926Exoplasmic loopSequence analysis
Transmembranei93 – 11523HelicalSequence analysisAdd
BLAST
Topological domaini116 – 297182CytoplasmicSequence analysisAdd
BLAST
Transmembranei298 – 31922HelicalSequence analysisAdd
BLAST
Topological domaini320 – 34425Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei345 – 36622HelicalSequence analysisAdd
BLAST
Topological domaini367 – 857491CytoplasmicSequence analysisAdd
BLAST
Transmembranei858 – 87821HelicalSequence analysisAdd
BLAST
Topological domaini879 – 89012Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei891 – 91020HelicalSequence analysisAdd
BLAST
Topological domaini911 – 94030CytoplasmicSequence analysisAdd
BLAST
Transmembranei941 – 96222HelicalSequence analysisAdd
BLAST
Topological domaini963 – 97614Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei977 – 99923HelicalSequence analysisAdd
BLAST
Topological domaini1000 – 10056CytoplasmicSequence analysis
Transmembranei1006 – 102621HelicalSequence analysisAdd
BLAST
Topological domaini1027 – 104418Exoplasmic loopSequence analysisAdd
BLAST
Transmembranei1045 – 107026HelicalSequence analysisAdd
BLAST
Topological domaini1071 – 116494CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • chromaffin granule membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: GOC
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • trans-Golgi network Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25165.

Chemistry

DrugBankiDB00144. Phosphatidylserine.

Polymorphism and mutation databases

BioMutaiATP8A1.
DMDMi8134331.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11641164Phospholipid-transporting ATPase IAPRO_0000046360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei28 – 281PhosphothreonineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei443 – 4431PhosphoserineBy similarity
Modified residuei1126 – 11261PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y2Q0.
MaxQBiQ9Y2Q0.
PaxDbiQ9Y2Q0.
PRIDEiQ9Y2Q0.

PTM databases

iPTMnetiQ9Y2Q0.
PhosphoSiteiQ9Y2Q0.

Expressioni

Tissue specificityi

Found in most adult tissues except liver, testis and placenta. Most abundant in heart, brain and skeletal muscle. Also detected in fetal tissues. Isoform 1 is only detected in brain, skeletal muscle and heart and is the most abundant form in skeletal muscle.

Gene expression databases

BgeeiQ9Y2Q0.
CleanExiHS_ATP8A1.
ExpressionAtlasiQ9Y2Q0. baseline and differential.
GenevisibleiQ9Y2Q0. HS.

Organism-specific databases

HPAiHPA049948.
HPA052935.

Interactioni

Subunit structurei

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex; the interaction with TMEM30B is reported conflictingly.3 Publications

Protein-protein interaction databases

BioGridi115668. 2 interactions.
IntActiQ9Y2Q0. 1 interaction.
STRINGi9606.ENSP00000371084.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2Q0.
SMRiQ9Y2Q0. Positions 389-867.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410ITKD. Eukaryota.
ENOG410XPYK. LUCA.
GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
HOVERGENiHBG050601.
InParanoidiQ9Y2Q0.
KOiK14802.
OMAiEKTFNDP.
OrthoDBiEOG7RRF68.
PhylomeDBiQ9Y2Q0.
TreeFamiTF300654.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR030342. ATP8A1.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PTHR24092:SF56. PTHR24092:SF56. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9Y2Q0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC
60 70 80 90 100
NNHVSTAKYN IITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT
110 120 130 140 150
TLVPLLFILA VAAIKEIIED IKRHKADNAV NKKQTQVLRN GAWEIVHWEK
160 170 180 190 200
VAVGEIVKVT NGEHLPADLI SLSSSEPQAM CYIETSNLDG ETNLKIRQGL
210 220 230 240 250
PATSDIKDVD SLMRISGRIE CESPNRHLYD FVGNIRLDGH GTVPLGADQI
260 270 280 290 300
LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI
310 320 330 340 350
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL NLNYGGASNF GLNFLTFIIL
360 370 380 390 400
FNNLIPISLL VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL
410 420 430 440 450
GQVKYIFSDK TGTLTCNVMQ FKKCTIAGVA YGHVPEPEDY GCSPDEWQNS
460 470 480 490 500
QFGDEKTFSD SSLLENLQNN HPTAPIICEF LTMMAVCHTA VPEREGDKII
510 520 530 540 550
YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER YELLNVLEFT
560 570 580 590 600
SARKRMSVIV RTPSGKLRLY CKGADTVIYD RLAETSKYKE ITLKHLEQFA
610 620 630 640 650
TEGLRTLCFA VAEISESDFQ EWRAVYQRAS TSVQNRLLKL EESYELIEKN
660 670 680 690 700
LQLLGATAIE DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCK
710 720 730 740 750
LLKKNMGMIV INEGSLDGTR ETLSRHCTTL GDALRKENDF ALIIDGKTLK
760 770 780 790 800
YALTFGVRQY FLDLALSCKA VICCRVSPLQ KSEVVEMVKK QVKVVTLAIG
810 820 830 840 850
DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL KNLLMIHGAW
860 870 880 890 900
NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF
910 920 930 940 950
TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF
960 970 980 990 1000
HSVILFWFPL KALQYGTAFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET
1010 1020 1030 1040 1050
SYWTWFSHIA IWGSIALWVV FFGIYSSLWP AIPMAPDMSG EAAMLFSSGV
1060 1070 1080 1090 1100
FWMGLLFIPV ASLLLDVVYK VIKRTAFKTL VDEVQELEAK SQDPGAVVLG
1110 1120 1130 1140 1150
KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD ENGIVSQSEV
1160
IRAYDTTKQR PDEW
Length:1,164
Mass (Da):131,369
Last modified:November 1, 1999 - v1
Checksum:iCE1EAF0206CD36F7
GO
Isoform 2 (identifier: Q9Y2Q0-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     433-447: Missing.

Show »
Length:1,149
Mass (Da):129,628
Checksum:iDC609CEA87E9F9B1
GO
Isoform 3 (identifier: Q9Y2Q0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-171: AVGEIVKVTNGEHLPADLIS → NVGDIVIIKGKEYIPADTVL
     433-447: Missing.

Show »
Length:1,149
Mass (Da):129,723
Checksum:i83D2F58984DDF966
GO

Sequence cautioni

The sequence AAI09318.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA77248.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti364 – 3641E → K in BAA77248 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti673 – 6731T → M.
Corresponds to variant rs3792687 [ dbSNP | Ensembl ].
VAR_022003

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 17120AVGEI…ADLIS → NVGDIVIIKGKEYIPADTVL in isoform 3. 1 PublicationVSP_040977Add
BLAST
Alternative sequencei433 – 44715Missing in isoform 2 and isoform 3. 2 PublicationsVSP_000431Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067820 mRNA. Translation: AAD34706.1.
AC084010 Genomic DNA. Translation: AAY40980.1.
AC096734 Genomic DNA. Translation: AAY40924.1.
AC110788 Genomic DNA. No translation available.
AC139717 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW93003.1.
BC109317 mRNA. Translation: AAI09318.1. Different initiation.
BC109318 mRNA. Translation: AAI09319.1.
AB013452 mRNA. Translation: BAA77248.1. Different initiation.
CCDSiCCDS3466.1. [Q9Y2Q0-1]
CCDS47049.1. [Q9Y2Q0-3]
RefSeqiNP_001098999.1. NM_001105529.1. [Q9Y2Q0-3]
NP_006086.1. NM_006095.2. [Q9Y2Q0-1]
UniGeneiHs.435052.

Genome annotation databases

EnsembliENST00000264449; ENSP00000264449; ENSG00000124406. [Q9Y2Q0-3]
ENST00000381668; ENSP00000371084; ENSG00000124406. [Q9Y2Q0-1]
GeneIDi10396.
KEGGihsa:10396.
UCSCiuc003gwr.3. human. [Q9Y2Q0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067820 mRNA. Translation: AAD34706.1.
AC084010 Genomic DNA. Translation: AAY40980.1.
AC096734 Genomic DNA. Translation: AAY40924.1.
AC110788 Genomic DNA. No translation available.
AC139717 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW93003.1.
BC109317 mRNA. Translation: AAI09318.1. Different initiation.
BC109318 mRNA. Translation: AAI09319.1.
AB013452 mRNA. Translation: BAA77248.1. Different initiation.
CCDSiCCDS3466.1. [Q9Y2Q0-1]
CCDS47049.1. [Q9Y2Q0-3]
RefSeqiNP_001098999.1. NM_001105529.1. [Q9Y2Q0-3]
NP_006086.1. NM_006095.2. [Q9Y2Q0-1]
UniGeneiHs.435052.

3D structure databases

ProteinModelPortaliQ9Y2Q0.
SMRiQ9Y2Q0. Positions 389-867.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115668. 2 interactions.
IntActiQ9Y2Q0. 1 interaction.
STRINGi9606.ENSP00000371084.

Chemistry

DrugBankiDB00144. Phosphatidylserine.

Protein family/group databases

TCDBi3.A.3.8.13. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiQ9Y2Q0.
PhosphoSiteiQ9Y2Q0.

Polymorphism and mutation databases

BioMutaiATP8A1.
DMDMi8134331.

Proteomic databases

EPDiQ9Y2Q0.
MaxQBiQ9Y2Q0.
PaxDbiQ9Y2Q0.
PRIDEiQ9Y2Q0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264449; ENSP00000264449; ENSG00000124406. [Q9Y2Q0-3]
ENST00000381668; ENSP00000371084; ENSG00000124406. [Q9Y2Q0-1]
GeneIDi10396.
KEGGihsa:10396.
UCSCiuc003gwr.3. human. [Q9Y2Q0-1]

Organism-specific databases

CTDi10396.
GeneCardsiATP8A1.
HGNCiHGNC:13531. ATP8A1.
HPAiHPA049948.
HPA052935.
MIMi609542. gene.
neXtProtiNX_Q9Y2Q0.
PharmGKBiPA25165.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITKD. Eukaryota.
ENOG410XPYK. LUCA.
GeneTreeiENSGT00770000120474.
HOGENOMiHOG000202528.
HOVERGENiHBG050601.
InParanoidiQ9Y2Q0.
KOiK14802.
OMAiEKTFNDP.
OrthoDBiEOG7RRF68.
PhylomeDBiQ9Y2Q0.
TreeFamiTF300654.

Enzyme and pathway databases

BRENDAi3.6.3.1. 2681.
ReactomeiR-HSA-936837. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSiATP8A1. human.
GenomeRNAii10396.
PROiQ9Y2Q0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2Q0.
CleanExiHS_ATP8A1.
ExpressionAtlasiQ9Y2Q0. baseline and differential.
GenevisibleiQ9Y2Q0. HS.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR030342. ATP8A1.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR006539. P-type_ATPase_IV.
IPR032631. P-type_ATPase_N.
IPR001757. P_typ_ATPase.
IPR032630. P_typ_ATPase_c.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PTHR24092:SF56. PTHR24092:SF56. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF16212. PhoLip_ATPase_C. 1 hit.
PF16209. PhoLip_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and chromosomal mapping of a human ATPase II gene, member of the third subfamily of P-type ATPases and orthologous to the presumed bovine and murine aminophospholipid translocase."
    Mouro I., Halleck M.S., Schlegel R.A., Mattei M.-G., Williamson P.L., Zachowski A., Devaux P., Cartron J.-P., Colin Y.
    Biochem. Biophys. Res. Commun. 257:333-339(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Skeletal muscle.
  2. "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].
  3. 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 3).
  5. "cDNA cloning of human ATPaseII."
    Osada S., Nakanishi Y.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-1164 (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases."
    van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.
    J. Biol. Chem. 285:40088-40096(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM30A, SUBCELLULAR LOCATION.
  9. "CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."
    Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G., Holthuis J.C.
    J. Biol. Chem. 285:40562-40572(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM30A AND TMEM30B.
  10. "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner."
    Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K., Shin H.W.
    J. Biol. Chem. 286:38159-38167(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM30A, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAT8A1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Q0
Secondary accession number(s): Q32M35
, Q32M36, Q4W5J7, Q4W5P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 153 of the entry and version 1 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.