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Q9HD20 (AT131_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable cation-transporting ATPase 13A1

EC=3.6.3.-
Gene names
Name:ATP13A1
Synonyms:ATP13A, KIAA1825
ORF Names:CGI-152
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily. [View classification]

Ontologies

Alternative products

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

Note: Experimental confirmation may be lacking for some isoforms.
Isoform A (identifier: Q9HD20-1)

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 B (identifier: Q9HD20-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
     119-132: HWSVHAHCALTCTP → MEKWEELNSHQPGE
Isoform C (identifier: Q9HD20-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-860: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 12041203Probable cation-transporting ATPase 13A1
PRO_0000046421

Regions

Topological domain2 – 6665Cytoplasmic Potential
Transmembrane67 – 8721Helical; Potential
Topological domain88 – 958Extracellular Potential
Transmembrane96 – 11621Helical; Potential
Topological domain117 – 243127Cytoplasmic Potential
Transmembrane244 – 26421Helical; Potential
Topological domain265 – 443179Extracellular Potential
Transmembrane444 – 46421Helical; Potential
Topological domain465 – 989525Cytoplasmic Potential
Transmembrane990 – 101021Helical; Potential
Topological domain10111Extracellular Potential
Transmembrane1012 – 103221Helical; Potential
Topological domain1033 – 105119Cytoplasmic Potential
Transmembrane1052 – 107221Helical; Potential
Topological domain1073 – 109624Extracellular Potential
Transmembrane1097 – 111721Helical; Potential
Topological domain1118 – 113215Cytoplasmic Potential
Transmembrane1133 – 115321Helical; Potential
Topological domain1154 – 116613Extracellular Potential
Transmembrane1167 – 118721Helical; Potential
Topological domain1188 – 120417Cytoplasmic Potential
Compositional bias455 – 4606Poly-Ala
Compositional bias892 – 8976Poly-Arg

Sites

Active site53314-aspartylphosphate intermediate By similarity
Metal binding8641Magnesium By similarity
Metal binding8681Magnesium By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.11
Modified residue8991Phosphoserine Ref.7
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Ref.6

Natural variations

Alternative sequence1 – 860860Missing in isoform C.
VSP_000433
Alternative sequence1 – 118118Missing in isoform B.
VSP_000434
Alternative sequence119 – 13214HWSVH…LTCTP → MEKWEELNSHQPGE in isoform B.
VSP_000435

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 9DE335C025FBBA89

FASTA1,204132,955
        10         20         30         40         50         60 
MAAAAAVGNA VPCGARPCGV RPDGQPKPGP QPRALLAAGP ALIANGDELV AAVWPYRRLA 

        70         80         90        100        110        120 
LLRRLTVLPF AGLLYPAWLG AAAAGCWGWG SSWVQIPEAA LLVLATICLA HALTVLSGHW 

       130        140        150        160        170        180 
SVHAHCALTC TPEYDPSKAT FVKVVPTPNN GSTELVALHR NEGEDGLEVL SFEFQKIKYS 

       190        200        210        220        230        240 
YDALEKKQFL PVAFPVGNAF SYYQSNRGFQ EDSEIRAAEK KFGSNKAEMV VPDFSELFKE 

       250        260        270        280        290        300 
RATAPFFVFQ VFCVGLWCLD EYWYYSVFTL SMLVAFEASL VQQQMRNMSE IRKMGNKPHM 

       310        320        330        340        350        360 
IQVYRSRKWR PIASDEIVPG DIVSIGRSPQ ENLVPCDVLL LRGRCIVDEA MLTGESVPQM 

       370        380        390        400        410        420 
KEPIEDLSPD RVLDLQADSR LHVIFGGTKV VQHIPPQKAT TGLKPVDSGC VAYVLRTGFN 

       430        440        450        460        470        480 
TSQGKLLRTI LFGVKRVTAN NLETFIFILF LLVFAIAAAA YVWIEGTKDP SRNRYKLFLE 

       490        500        510        520        530        540 
CTLILTSVVP PELPIELSLA VNTSLIALAK LYMYCTEPFR IPFAGKVEVC CFDKTGTLTS 

       550        560        570        580        590        600 
DSLVVRGVAG LRDGKEVTPV SSIPVETHRA LASCHSLMQL DDGTLVGDPL EKAMLTAVDW 

       610        620        630        640        650        660 
TLTKDEKVFP RSIKTQGLKI HQRFHFASAL KRMSVLASYE KLGSTDLCYI AAVKGAPETL 

       670        680        690        700        710        720 
HSMFSQCPPD YHHIHTEISR EGARVLALGY KELGHLTHQQ AREVKREALE CSLKFVGFIV 

       730        740        750        760        770        780 
VSCPLKADSK AVIREIQNAS HRVVMITGDN PLTACHVAQE LHFIEKAHTL ILQPPSEKGR 

       790        800        810        820        830        840 
QCEWRSIDGS IVLPLARGSP KALALEYALC LTGDGLAHLQ ATDPQQLLRL IPHVQVFARV 

       850        860        870        880        890        900 
APKQKEFVIT SLKELGYVTL MCGDGTNDVG ALKHADVGVA LLANAPERVV ERRRRPRDSP 

       910        920        930        940        950        960 
TLSNSGIRAT SRTAKQRSGL PPSEEQPTSQ RDRLSQVLRD LEDESTPIVK LGDASIAAPF 

       970        980        990       1000       1010       1020 
TSKLSSIQCI CHVIKQGRCT LVTTLQMFKI LALNALILAY SQSVLYLEGV KFSDFQATLQ 

      1030       1040       1050       1060       1070       1080 
GLLLAGCFLF ISRSKPLKTL SRERPLPNIF NLYTILTVML QFFVHFLSLV YLYREAQARS 

      1090       1100       1110       1120       1130       1140 
PEKQEQFVDL YKEFEPSLVN STVYIMAMAM QMATFAINYK GPPFMESLPE NKPLVWSLAV 

      1150       1160       1170       1180       1190       1200 
SLLAIIGLLL GSSPDFNSQF GLVDIPVEFK LVIAQVLLLD FCLALLADRV LQFFLGTPKL 


KVPS 

« Hide

Isoform B [UniParc].

Checksum: 0D0D62BF402E68D0
Show »

FASTA1,086121,110
Isoform C [UniParc].

Checksum: E988B4A90EC2DE3D
Show »

FASTA34438,207

References

[1]"Identification of novel human genes by comparative proteomics."
Chou M.C.-H., Lin W.-C.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
[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. expand/collapse author list , 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 A AND C).
Tissue: Kidney epithelium.
[3]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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].
[4]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1204 (ISOFORM A).
Tissue: Brain.
[5]"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] OF 844-1204.
Tissue: Brain.
[6]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-420.
Tissue: Plasma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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].
[10]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF288687 mRNA. Translation: AAG01173.1.
AK026044 mRNA. Translation: BAB15334.1.
AK056420 mRNA. Translation: BAG51704.1.
AK095287 mRNA. Translation: BAG53019.1.
AB058728 mRNA. Translation: BAB47454.1.
CH471106 Genomic DNA. Translation: EAW84849.1.
CH471106 Genomic DNA. Translation: EAW84850.1.
BC009302 mRNA. Translation: AAH09302.2.
RefSeqNP_065143.2. NM_020410.2.
UniGeneHs.501794.

3D structure databases

ProteinModelPortalQ9HD20.
SMRQ9HD20. Positions 260-888.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121393. 3 interactions.
IntActQ9HD20. 1 interaction.
STRING9606.ENSP00000349877.

Protein family/group databases

TCDB3.A.3.10.19. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteQ9HD20.

Polymorphism databases

DMDM18202961.

Proteomic databases

PaxDbQ9HD20.
PeptideAtlasQ9HD20.
PRIDEQ9HD20.

Protocols and materials databases

DNASU57130.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291503; ENSP00000291503; ENSG00000105726. [Q9HD20-2]
ENST00000357324; ENSP00000349877; ENSG00000105726. [Q9HD20-1]
GeneID57130.
KEGGhsa:57130.
UCSCuc002nne.3. human. [Q9HD20-3]
uc002nnf.4. human. [Q9HD20-2]
uc002nnh.4. human. [Q9HD20-1]

Organism-specific databases

CTD57130.
GeneCardsGC19M019758.
HGNCHGNC:24215. ATP13A1.
HPAHPA031798.
HPA049717.
neXtProtNX_Q9HD20.
PharmGKBPA134988892.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000199432.
HOVERGENHBG050602.
InParanoidQ9HD20.
KOK14950.
OMAAGRIDVC.
OrthoDBEOG7T1R9G.
PhylomeDBQ9HD20.
TreeFamTF300725.

Gene expression databases

ArrayExpressQ9HD20.
BgeeQ9HD20.
CleanExHS_ATP13A1.
GenevestigatorQ9HD20.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR006544. ATPase_P-typ_Cation_typ_V.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24093:SF82. PTHR24093:SF82. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01494. ATPase_P-type. 2 hits.
TIGR01657. P-ATPase-V. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP13A1. human.
GenomeRNAi57130.
NextBio63043.
PROQ9HD20.

Entry information

Entry nameAT131_HUMAN
AccessionPrimary (citable) accession number: Q9HD20
Secondary accession number(s): B3KPJ2, B3KTA7, Q9H6C6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

Index of protein domains and families

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Human chromosome 19: entries, gene names and cross-references to MIM