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Q9NTI2

- AT8A2_HUMAN

UniProt

Q9NTI2 - AT8A2_HUMAN

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Protein

Phospholipid-transporting ATPase IB

Gene

ATP8A2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Involved in regulation of neurite outgrowth; acting in synergy with TMEM30A. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival.

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). ATPase activity is inhibited by N-ethylmaleimide (NEM) and vanadate. Flippase activity is inhibited by NEM and 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS) (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei388 – 38814-aspartylphosphate intermediateBy similarity
Metal bindingi781 – 7811MagnesiumBy similarity
Metal bindingi785 – 7851MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cation-transporting ATPase activity Source: InterPro
  3. magnesium ion binding Source: InterPro
  4. phospholipid-translocating ATPase activity Source: UniProtKB-EC

GO - Biological processi

  1. aging Source: Ensembl
  2. axonogenesis Source: Ensembl
  3. detection of light stimulus involved in visual perception Source: Ensembl
  4. eating behavior Source: Ensembl
  5. inner ear morphogenesis Source: Ensembl
  6. involuntary skeletal muscle contraction Source: Ensembl
  7. negative regulation of cell proliferation Source: ProtInc
  8. neurofilament cytoskeleton organization Source: Ensembl
  9. neuromuscular process controlling posture Source: Ensembl
  10. positive regulation of multicellular organism growth Source: Ensembl
  11. positive regulation of neuron projection development Source: Ensembl
  12. positive regulation of phospholipid translocation Source: Ensembl
  13. response to auditory stimulus Source: Ensembl
  14. retina layer formation Source: Ensembl
  15. skin development Source: Ensembl
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

ReactomeiREACT_25149. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid-transporting ATPase IB (EC:3.6.3.1)
Alternative name(s):
ATPase class I type 8A member 2
ML-1
P4-ATPase flippase complex alpha subunit ATP8A2
Gene namesi
Name:ATP8A2
Synonyms:ATPIB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:13533. ATP8A2.

Subcellular locationi

Membrane Curated; Multi-pass membrane protein Curated. Golgi apparatus 1 Publication. Endosome By similarity. Cell projectionciliumphotoreceptor outer segment By similarity. Cell membrane 1 Publication
Note: Localizes to the Golgi and endosomes in photoreceptor cells. Localizes to disk membranes of rod photoreceptor outer segments (ROS) (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei45 – 6622HelicalSequence AnalysisAdd
BLAST
Topological domaini67 – 715Exoplasmic loopSequence Analysis
Transmembranei72 – 9423HelicalSequence AnalysisAdd
BLAST
Topological domaini95 – 276182CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei277 – 29822HelicalSequence AnalysisAdd
BLAST
Topological domaini299 – 32325Exoplasmic loopSequence AnalysisAdd
BLAST
Transmembranei324 – 34522HelicalSequence AnalysisAdd
BLAST
Topological domaini346 – 837492CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei838 – 85821HelicalSequence AnalysisAdd
BLAST
Topological domaini859 – 87012Exoplasmic loopSequence AnalysisAdd
BLAST
Transmembranei871 – 89020HelicalSequence AnalysisAdd
BLAST
Topological domaini891 – 92030CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei921 – 94222HelicalSequence AnalysisAdd
BLAST
Topological domaini943 – 95614Exoplasmic loopSequence AnalysisAdd
BLAST
Transmembranei957 – 97923HelicalSequence AnalysisAdd
BLAST
Topological domaini980 – 9856CytoplasmicSequence Analysis
Transmembranei986 – 100621HelicalSequence AnalysisAdd
BLAST
Topological domaini1007 – 102418Exoplasmic loopSequence AnalysisAdd
BLAST
Transmembranei1025 – 104925HelicalSequence AnalysisAdd
BLAST
Topological domaini1050 – 114899CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. endosome Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 4 (CMARQ4) [MIM:615268]: A congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mental retardation.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361I → M in CMARQ4. 1 Publication
VAR_069928
A chromosomal aberration disrupting ATP8A2 has been found in a patient with severe mental retardation and major hypotonia. Translocation t(10;13)(p12.1;q12.13) (PubMed:20683487).1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi615268. phenotype.
Orphaneti1766. Dysequilibrium syndrome.
PharmGKBiPA25166.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11481148Phospholipid-transporting ATPase IBPRO_0000046362Add
BLAST

Proteomic databases

PaxDbiQ9NTI2.
PRIDEiQ9NTI2.

Expressioni

Tissue specificityi

Strongly expressed in the brain, cerebellum, retina and testis.2 Publications

Gene expression databases

BgeeiQ9NTI2.
CleanExiHS_ATP8A2.
ExpressionAtlasiQ9NTI2. baseline and differential.
GenevestigatoriQ9NTI2.

Organism-specific databases

HPAiHPA039926.

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.2 Publications

Protein-protein interaction databases

BioGridi119718. 2 interactions.
IntActiQ9NTI2. 1 interaction.
STRINGi9606.ENSP00000371070.

Structurei

3D structure databases

ProteinModelPortaliQ9NTI2.
SMRiQ9NTI2. Positions 95-847.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0474.
HOVERGENiHBG050601.
InParanoidiQ9NTI2.
KOiK14802.
PhylomeDBiQ9NTI2.
TreeFamiTF300654.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERiPTHR24092. PTHR24092. 1 hit.
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
SUPFAMiSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsiTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NTI2-1) [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
MSRATSVGDQ LEAPARTIYL NQPHLNKFRD NQISTAKYSV LTFLPRFLYE
60 70 80 90 100
QIRRAANAFF LFIALLQQIP DVSPTGRYTT LVPLIIILTI AGIKEIVEDF
110 120 130 140 150
KRHKADNAVN KKKTIVLRNG MWHTIMWKEV AVGDIVKVVN GQYLPADVVL
160 170 180 190 200
LSSSEPQAMC YVETANLDGE TNLKIRQGLS HTADMQTREV LMKLSGTIEC
210 220 230 240 250
EGPNRHLYDF TGNLNLDGKS LVALGPDQIL LRGTQLRNTQ WVFGIVVYTG
260 270 280 290 300
HDTKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSAGALYWNR
310 320 330 340 350
SHGEKNWYIK KMDTTSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA
360 370 380 390 400
LFINWDTDMY YIGNDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF
410 420 430 440 450
KKCSIAGVTY GHFPELAREP SSDDFCRMPP PCSDSCDFDD PRLLKNIEDR
460 470 480 490 500
HPTAPCIQEF LTLLAVCHTV VPEKDGDNII YQASSPDEAA LVKGAKKLGF
510 520 530 540 550
VFTARTPFSV IIEAMGQEQT FGILNVLEFS SDRKRMSVIV RTPSGRLRLY
560 570 580 590 600
CKGADNVIFE RLSKDSKYME ETLCHLEYFA TEGLRTLCVA YADLSENEYE
610 620 630 640 650
EWLKVYQEAS TILKDRAQRL EECYEIIEKN LLLLGATAIE DRLQAGVPET
660 670 680 690 700
IATLLKAEIK IWVLTGDKQE TAINIGYSCR LVSQNMALIL LKEDSLDATR
710 720 730 740 750
AAITQHCTDL GNLLGKENDV ALIIDGHTLK YALSFEVRRS FLDLALSCKA
760 770 780 790 800
VICCRVSPLQ KSEIVDVVKK RVKAITLAIG DGANDVGMIQ TAHVGVGISG
810 820 830 840 850
NEGMQATNNS DYAIAQFSYL EKLLLVHGAW SYNRVTKCIL YCFYKNVVLY
860 870 880 890 900
IIELWFAFVN GFSGQILFER WCIGLYNVIF TALPPFTLGI FERSCTQESM
910 920 930 940 950
LRFPQLYKIT QNGEGFNTKV FWGHCINALV HSLILFWFPM KALEHDTVLT
960 970 980 990 1000
SGHATDYLFV GNIVYTYVVV TVCLKAGLET TAWTKFSHLA VWGSMLTWLV
1010 1020 1030 1040 1050
FFGIYSTIWP TIPIAPDMRG QATMVLSSAH FWLGLFLVPT ACLIEDVAWR
1060 1070 1080 1090 1100
AAKHTCKKTL LEEVQELETK SRVLGKAVLR DSNGKRLNER DRLIKRLGRK
1110 1120 1130 1140
TPPTLFRGSS LQQGVPHGYA FSQEEHGAVS QEEVIRAYDT TKKKSRKK

Note: No experimental confirmation available.

Length:1,148
Mass (Da):129,242
Last modified:April 30, 2003 - v2
Checksum:iE9F363B568C7EE82
GO
Isoform 2 (identifier: Q9NTI2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     515-528: MGQEQTFGILNVLE → VSNMRVHISDHLLL
     529-1148: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:528
Mass (Da):59,296
Checksum:i1CAD4BDC7B38F391
GO

Sequence cautioni

Isoform 2 : The sequence AAF40215.2 differs from that shown. Reason: Frameshift at position 522. Curated
The sequence BAC04396.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361I → M in CMARQ4. 1 Publication
VAR_069928
Natural varianti1029 – 10291A → T.
Corresponds to variant rs2296242 [ dbSNP | Ensembl ].
VAR_055543

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei515 – 52814MGQEQ…LNVLE → VSNMRVHISDHLLL in isoform 2. 1 PublicationVSP_037646Add
BLAST
Alternative sequencei529 – 1148620Missing in isoform 2. 1 PublicationVSP_037647Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236871 mRNA. Translation: AAF40215.2. Frameshift.
AL138815
, AL136438, AL138958, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH70513.1.
AL138958
, AL136438, AL138815, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH71291.1.
AL157366
, AL136438, AL138815, AL138958, AL356316, AL669971 Genomic DNA. Translation: CAH74073.1.
AL356316
, AL136438, AL138815, AL138958, AL157366, AL669971 Genomic DNA. Translation: CAH70876.1.
AL669971
, AL136438, AL138815, AL138958, AL157366, AL356316 Genomic DNA. Translation: CAH73647.1.
AL136438
, AL138815, AL138958, AL157366, AL356316, AL669971 Genomic DNA. Translation: CAH70146.1.
AL137256 mRNA. Translation: CAB70658.1.
AL390129 mRNA. Translation: CAB99084.1.
BX537836 mRNA. Translation: CAD97848.1.
AK094653 mRNA. Translation: BAC04396.1. Different initiation.
PIRiT46328.
T51867.
RefSeqiNP_057613.4. NM_016529.4.
XP_005266476.1. XM_005266419.1. [Q9NTI2-1]
XP_006719897.1. XM_006719834.1. [Q9NTI2-1]
UniGeneiHs.444957.

Genome annotation databases

EnsembliENST00000381655; ENSP00000371070; ENSG00000132932.
GeneIDi51761.
KEGGihsa:51761.
UCSCiuc001uql.1. human. [Q9NTI2-3]

Polymorphism databases

DMDMi30316390.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236871 mRNA. Translation: AAF40215.2 . Frameshift.
AL138815
, AL136438 , AL138958 , AL157366 , AL356316 , AL669971 Genomic DNA. Translation: CAH70513.1 .
AL138958
, AL136438 , AL138815 , AL157366 , AL356316 , AL669971 Genomic DNA. Translation: CAH71291.1 .
AL157366
, AL136438 , AL138815 , AL138958 , AL356316 , AL669971 Genomic DNA. Translation: CAH74073.1 .
AL356316
, AL136438 , AL138815 , AL138958 , AL157366 , AL669971 Genomic DNA. Translation: CAH70876.1 .
AL669971
, AL136438 , AL138815 , AL138958 , AL157366 , AL356316 Genomic DNA. Translation: CAH73647.1 .
AL136438
, AL138815 , AL138958 , AL157366 , AL356316 , AL669971 Genomic DNA. Translation: CAH70146.1 .
AL137256 mRNA. Translation: CAB70658.1 .
AL390129 mRNA. Translation: CAB99084.1 .
BX537836 mRNA. Translation: CAD97848.1 .
AK094653 mRNA. Translation: BAC04396.1 . Different initiation.
PIRi T46328.
T51867.
RefSeqi NP_057613.4. NM_016529.4.
XP_005266476.1. XM_005266419.1. [Q9NTI2-1 ]
XP_006719897.1. XM_006719834.1. [Q9NTI2-1 ]
UniGenei Hs.444957.

3D structure databases

ProteinModelPortali Q9NTI2.
SMRi Q9NTI2. Positions 95-847.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119718. 2 interactions.
IntActi Q9NTI2. 1 interaction.
STRINGi 9606.ENSP00000371070.

Polymorphism databases

DMDMi 30316390.

Proteomic databases

PaxDbi Q9NTI2.
PRIDEi Q9NTI2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381655 ; ENSP00000371070 ; ENSG00000132932 .
GeneIDi 51761.
KEGGi hsa:51761.
UCSCi uc001uql.1. human. [Q9NTI2-3 ]

Organism-specific databases

CTDi 51761.
GeneCardsi GC13P025946.
HGNCi HGNC:13533. ATP8A2.
HPAi HPA039926.
MIMi 605870. gene.
615268. phenotype.
neXtProti NX_Q9NTI2.
Orphaneti 1766. Dysequilibrium syndrome.
PharmGKBi PA25166.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0474.
HOVERGENi HBG050601.
InParanoidi Q9NTI2.
KOi K14802.
PhylomeDBi Q9NTI2.
TreeFami TF300654.

Enzyme and pathway databases

Reactomei REACT_25149. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSi ATP8A2. human.
GenomeRNAii 51761.
NextBioi 55870.
PROi Q9NTI2.
SOURCEi Search...

Gene expression databases

Bgeei Q9NTI2.
CleanExi HS_ATP8A2.
ExpressionAtlasi Q9NTI2. baseline and differential.
Genevestigatori Q9NTI2.

Family and domain databases

Gene3Di 2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProi IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view ]
PANTHERi PTHR24092. PTHR24092. 1 hit.
Pfami PF00122. E1-E2_ATPase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
SUPFAMi SSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsi TIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Sun X.L., Milo G.E., Li D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes."
    Sun X.L., Li D., Fang J., Noyes I., Casto B., Theil K., Shuler C., Milo G.E.
    Gene Expr. 8:129-139(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-1148 (ISOFORM 1).
    Tissue: Amygdala and Testis.
  5. "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] OF 319-1148 (ISOFORM 1).
    Tissue: Amygdala.
  6. "Disruption of the ATP8A2 gene in a patient with a t(10;13) de novo balanced translocation and a severe neurological phenotype."
    Cacciagli P., Haddad M.R., Mignon-Ravix C., El-Waly B., Moncla A., Missirian C., Chabrol B., Villard L.
    Eur. J. Hum. Genet. 18:1360-1363(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION.
  7. "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.
  8. "Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2."
    Coleman J.A., Molday R.S.
    J. Biol. Chem. 286:17205-17216(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM30A.
  9. "Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion."
    Onat O.E., Gulsuner S., Bilguvar K., Nazli Basak A., Topaloglu H., Tan M., Tan U., Gunel M., Ozcelik T.
    Eur. J. Hum. Genet. 21:281-285(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, VARIANT CMARQ4 MET-336.

Entry informationi

Entry nameiAT8A2_HUMAN
AccessioniPrimary (citable) accession number: Q9NTI2
Secondary accession number(s): Q9H527
, Q9NPU6, Q9NTL2, Q9NYM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: April 30, 2003
Last modified: October 29, 2014
This is version 122 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 13
    Human chromosome 13: 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

External Data

Dasty 3