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Q9HD20

- AT131_HUMAN

UniProt

Q9HD20 - AT131_HUMAN

Protein

Manganese-transporting ATPase 13A1

Gene

ATP13A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      Previous versions | rss
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    Functioni

    Mediates manganese transport into the endoplasmic reticulum. The ATPase activity is required for cellular manganese homeostasis.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei533 – 53314-aspartylphosphate intermediateBy similarity
    Metal bindingi864 – 8641MagnesiumBy similarity
    Metal bindingi868 – 8681MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cation-transporting ATPase activity Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

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

    Protein family/group databases

    TCDBi3.A.3.10.19. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Manganese-transporting ATPase 13A1 (EC:3.6.3.-)
    Gene namesi
    Name:ATP13A1
    Synonyms:ATP13A, KIAA1825
    ORF Names:CGI-152
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24215. ATP13A1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134988892.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 12041203Manganese-transporting ATPase 13A1PRO_0000046421Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi420 – 4201N-linked (GlcNAc...)1 Publication
    Modified residuei899 – 8991Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HD20.
    PaxDbiQ9HD20.
    PeptideAtlasiQ9HD20.
    PRIDEiQ9HD20.

    PTM databases

    PhosphoSiteiQ9HD20.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HD20.
    BgeeiQ9HD20.
    CleanExiHS_ATP13A1.
    GenevestigatoriQ9HD20.

    Organism-specific databases

    HPAiHPA031798.
    HPA049717.

    Interactioni

    Protein-protein interaction databases

    BioGridi121393. 3 interactions.
    IntActiQ9HD20. 1 interaction.
    STRINGi9606.ENSP00000349877.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HD20.
    SMRiQ9HD20. Positions 260-881.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 6665CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini88 – 958ExtracellularSequence Analysis
    Topological domaini117 – 243127CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini265 – 443179ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini465 – 989525CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1011 – 10111ExtracellularSequence Analysis
    Topological domaini1033 – 105119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1073 – 109624ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1118 – 113215CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1154 – 116613ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1188 – 120417CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei67 – 8721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei96 – 11621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei244 – 26421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei444 – 46421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei990 – 101021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1012 – 103221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1052 – 107221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1097 – 111721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1133 – 115321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1167 – 118721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi455 – 4606Poly-Ala
    Compositional biasi892 – 8976Poly-Arg

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0474.
    HOGENOMiHOG000199432.
    HOVERGENiHBG050602.
    InParanoidiQ9HD20.
    KOiK14950.
    OMAiIISCPLK.
    OrthoDBiEOG7T1R9G.
    PhylomeDBiQ9HD20.
    TreeFamiTF300725.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR006544. 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]
    PANTHERiPTHR24093:SF82. PTHR24093:SF82. 1 hit.
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsiTIGR01494. ATPase_P-type. 2 hits.
    TIGR01657. P-ATPase-V. 1 hit.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform A (identifier: Q9HD20-1) [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

    MAAAAAVGNA VPCGARPCGV RPDGQPKPGP QPRALLAAGP ALIANGDELV     50
    AAVWPYRRLA LLRRLTVLPF AGLLYPAWLG AAAAGCWGWG SSWVQIPEAA 100
    LLVLATICLA HALTVLSGHW SVHAHCALTC TPEYDPSKAT FVKVVPTPNN 150
    GSTELVALHR NEGEDGLEVL SFEFQKIKYS YDALEKKQFL PVAFPVGNAF 200
    SYYQSNRGFQ EDSEIRAAEK KFGSNKAEMV VPDFSELFKE RATAPFFVFQ 250
    VFCVGLWCLD EYWYYSVFTL SMLVAFEASL VQQQMRNMSE IRKMGNKPHM 300
    IQVYRSRKWR PIASDEIVPG DIVSIGRSPQ ENLVPCDVLL LRGRCIVDEA 350
    MLTGESVPQM KEPIEDLSPD RVLDLQADSR LHVIFGGTKV VQHIPPQKAT 400
    TGLKPVDSGC VAYVLRTGFN TSQGKLLRTI LFGVKRVTAN NLETFIFILF 450
    LLVFAIAAAA YVWIEGTKDP SRNRYKLFLE CTLILTSVVP PELPIELSLA 500
    VNTSLIALAK LYMYCTEPFR IPFAGKVEVC CFDKTGTLTS DSLVVRGVAG 550
    LRDGKEVTPV SSIPVETHRA LASCHSLMQL DDGTLVGDPL EKAMLTAVDW 600
    TLTKDEKVFP RSIKTQGLKI HQRFHFASAL KRMSVLASYE KLGSTDLCYI 650
    AAVKGAPETL HSMFSQCPPD YHHIHTEISR EGARVLALGY KELGHLTHQQ 700
    AREVKREALE CSLKFVGFIV VSCPLKADSK AVIREIQNAS HRVVMITGDN 750
    PLTACHVAQE LHFIEKAHTL ILQPPSEKGR QCEWRSIDGS IVLPLARGSP 800
    KALALEYALC LTGDGLAHLQ ATDPQQLLRL IPHVQVFARV APKQKEFVIT 850
    SLKELGYVTL MCGDGTNDVG ALKHADVGVA LLANAPERVV ERRRRPRDSP 900
    TLSNSGIRAT SRTAKQRSGL PPSEEQPTSQ RDRLSQVLRD LEDESTPIVK 950
    LGDASIAAPF TSKLSSIQCI CHVIKQGRCT LVTTLQMFKI LALNALILAY 1000
    SQSVLYLEGV KFSDFQATLQ GLLLAGCFLF ISRSKPLKTL SRERPLPNIF 1050
    NLYTILTVML QFFVHFLSLV YLYREAQARS PEKQEQFVDL YKEFEPSLVN 1100
    STVYIMAMAM QMATFAINYK GPPFMESLPE NKPLVWSLAV SLLAIIGLLL 1150
    GSSPDFNSQF GLVDIPVEFK LVIAQVLLLD FCLALLADRV LQFFLGTPKL 1200
    KVPS 1204
    Length:1,204
    Mass (Da):132,955
    Last modified:October 18, 2001 - v2
    Checksum:i9DE335C025FBBA89
    GO
    Isoform B (identifier: Q9HD20-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.
         119-132: HWSVHAHCALTCTP → MEKWEELNSHQPGE

    Show »
    Length:1,086
    Mass (Da):121,110
    Checksum:i0D0D62BF402E68D0
    GO
    Isoform C (identifier: Q9HD20-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:344
    Mass (Da):38,207
    Checksum:iE988B4A90EC2DE3D
    GO

    Sequence cautioni

    The sequence AAH69211.1 differs from that shown. Reason: Frameshift at position 846.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti364 – 3641I → T in BAD18759. (PubMed:14702039)Curated
    Sequence conflicti501 – 5011V → D in BAD18759. (PubMed:14702039)Curated
    Sequence conflicti1150 – 11501L → P in BAD18759. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 860860Missing in isoform C. 1 PublicationVSP_000433Add
    BLAST
    Alternative sequencei1 – 118118Missing in isoform B. 1 PublicationVSP_000434Add
    BLAST
    Alternative sequencei119 – 13214HWSVH…LTCTP → MEKWEELNSHQPGE in isoform B. 1 PublicationVSP_000435Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF288687 mRNA. Translation: AAG01173.1.
    AK026044 mRNA. Translation: BAB15334.1.
    AK056420 mRNA. Translation: BAG51704.1.
    AK095287 mRNA. Translation: BAG53019.1.
    AK172778 mRNA. Translation: BAD18759.1.
    AB058728 mRNA. Translation: BAB47454.1.
    CH471106 Genomic DNA. Translation: EAW84849.1.
    CH471106 Genomic DNA. Translation: EAW84850.1.
    BC009302 mRNA. Translation: AAH09302.2.
    BC069211 mRNA. Translation: AAH69211.1. Frameshift.
    CCDSiCCDS32970.2. [Q9HD20-1]
    RefSeqiNP_065143.2. NM_020410.2. [Q9HD20-1]
    UniGeneiHs.501794.

    Genome annotation databases

    EnsembliENST00000291503; ENSP00000291503; ENSG00000105726. [Q9HD20-2]
    ENST00000357324; ENSP00000349877; ENSG00000105726. [Q9HD20-1]
    GeneIDi57130.
    KEGGihsa:57130.
    UCSCiuc002nne.3. human. [Q9HD20-3]
    uc002nnf.4. human. [Q9HD20-2]
    uc002nnh.4. human. [Q9HD20-1]

    Polymorphism databases

    DMDMi18202961.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF288687 mRNA. Translation: AAG01173.1 .
    AK026044 mRNA. Translation: BAB15334.1 .
    AK056420 mRNA. Translation: BAG51704.1 .
    AK095287 mRNA. Translation: BAG53019.1 .
    AK172778 mRNA. Translation: BAD18759.1 .
    AB058728 mRNA. Translation: BAB47454.1 .
    CH471106 Genomic DNA. Translation: EAW84849.1 .
    CH471106 Genomic DNA. Translation: EAW84850.1 .
    BC009302 mRNA. Translation: AAH09302.2 .
    BC069211 mRNA. Translation: AAH69211.1 . Frameshift.
    CCDSi CCDS32970.2. [Q9HD20-1 ]
    RefSeqi NP_065143.2. NM_020410.2. [Q9HD20-1 ]
    UniGenei Hs.501794.

    3D structure databases

    ProteinModelPortali Q9HD20.
    SMRi Q9HD20. Positions 260-881.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121393. 3 interactions.
    IntActi Q9HD20. 1 interaction.
    STRINGi 9606.ENSP00000349877.

    Protein family/group databases

    TCDBi 3.A.3.10.19. the p-type atpase (p-atpase) superfamily.

    PTM databases

    PhosphoSitei Q9HD20.

    Polymorphism databases

    DMDMi 18202961.

    Proteomic databases

    MaxQBi Q9HD20.
    PaxDbi Q9HD20.
    PeptideAtlasi Q9HD20.
    PRIDEi Q9HD20.

    Protocols and materials databases

    DNASUi 57130.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000291503 ; ENSP00000291503 ; ENSG00000105726 . [Q9HD20-2 ]
    ENST00000357324 ; ENSP00000349877 ; ENSG00000105726 . [Q9HD20-1 ]
    GeneIDi 57130.
    KEGGi hsa:57130.
    UCSCi uc002nne.3. human. [Q9HD20-3 ]
    uc002nnf.4. human. [Q9HD20-2 ]
    uc002nnh.4. human. [Q9HD20-1 ]

    Organism-specific databases

    CTDi 57130.
    GeneCardsi GC19M019758.
    HGNCi HGNC:24215. ATP13A1.
    HPAi HPA031798.
    HPA049717.
    neXtProti NX_Q9HD20.
    PharmGKBi PA134988892.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0474.
    HOGENOMi HOG000199432.
    HOVERGENi HBG050602.
    InParanoidi Q9HD20.
    KOi K14950.
    OMAi IISCPLK.
    OrthoDBi EOG7T1R9G.
    PhylomeDBi Q9HD20.
    TreeFami TF300725.

    Miscellaneous databases

    ChiTaRSi ATP13A1. human.
    GenomeRNAii 57130.
    NextBioi 63043.
    PROi Q9HD20.

    Gene expression databases

    ArrayExpressi Q9HD20.
    Bgeei Q9HD20.
    CleanExi HS_ATP13A1.
    Genevestigatori Q9HD20.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR006544. 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 ]
    PANTHERi PTHR24093:SF82. PTHR24093:SF82. 1 hit.
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF56784. SSF56784. 3 hits.
    SSF81660. SSF81660. 1 hit.
    TIGRFAMsi TIGR01494. ATPase_P-type. 2 hits.
    TIGR01657. P-ATPase-V. 1 hit.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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: Hepatoma and Kidney epithelium.
    3. 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 and Kidney.
    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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: FUNCTION, SUBCELLULAR LOCATION, MISCELLANEOUS.

    Entry informationi

    Entry nameiAT131_HUMAN
    AccessioniPrimary (citable) accession number: Q9HD20
    Secondary accession number(s): B3KPJ2
    , B3KTA7, Q6NT90, Q6ZMG7, Q9H6C6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 131 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

    Miscellaneous

    Depletion of ATP13A1 with siRNAs leads to induction of the unfolded protein response (UPR) and increased activity of glucosylceramide synthase (GlcCer).

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3