Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NPH0

- PPA6_HUMAN

UniProt

Q9NPH0 - PPA6_HUMAN

Protein

Lysophosphatidic acid phosphatase type 6

Gene

ACP6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Hydrolyzes lysophosphatidic acid (LPA) containing a medium length fatty acid chain to the corresponding monoacylglycerol. Has highest activity with lysophosphatidic acid containing myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 and C6:0 lysophosphatidic acid.2 Publications

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei59 – 591Nucleophile1 Publication
    Active sitei335 – 3351Proton donor1 Publication

    GO - Molecular functioni

    1. acid phosphatase activity Source: UniProtKB-EC
    2. lysophosphatidic acid phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. lysobisphosphatidic acid metabolic process Source: UniProtKB
    3. phospholipid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Phospholipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysophosphatidic acid phosphatase type 6 (EC:3.1.3.2)
    Alternative name(s):
    Acid phosphatase 6, lysophosphatidic
    Acid phosphatase-like protein 1
    PACPL1
    Gene namesi
    Name:ACP6
    Synonyms:ACPL1, LPAP
    ORF Names:UNQ205/PRO231
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29609. ACP6.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 581R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi59 – 591H → A: Abolishes enzyme activity. 2 Publications
    Mutagenesisi62 – 621R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi106 – 1061Y → F: Decreases enzyme activity. 1 Publication
    Mutagenesisi110 – 1101Y → F: Decreases enzyme activity.
    Mutagenesisi168 – 1681R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi257 – 2571A → F or L: Decreases enzyme activity by interfering with water access to the active site cavity. 1 Publication
    Mutagenesisi257 – 2571A → W: Abolishes enzyme activity by interfering with water access to the active site cavity. 1 Publication
    Mutagenesisi285 – 2851S → W: Decreases activity toward substrates with medium and long aliphatic chains, but not toward substrates with short aliphatic chains. 1 Publication
    Mutagenesisi289 – 2891L → W: Decreases activity toward substrates with medium and long aliphatic chains, but not toward substrates with short aliphatic chains. 1 Publication
    Mutagenesisi334 – 3341H → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi335 – 3351D → A: Abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134930830.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232Mitochondrion1 PublicationAdd
    BLAST
    Chaini33 – 428396Lysophosphatidic acid phosphatase type 6PRO_0000023965Add
    BLAST

    Proteomic databases

    MaxQBiQ9NPH0.
    PaxDbiQ9NPH0.
    PRIDEiQ9NPH0.

    PTM databases

    PhosphoSiteiQ9NPH0.

    Expressioni

    Tissue specificityi

    Highly expressed in kidney, heart, small intestine, muscle, liver, prostate, testis, ovary and weakly expressed in thymus and colon.2 Publications

    Inductioni

    Induced with the differentiation from myoblast to myotube.1 Publication

    Gene expression databases

    BgeeiQ9NPH0.
    CleanExiHS_ACP6.
    GenevestigatoriQ9NPH0.

    Organism-specific databases

    HPAiHPA028560.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi119378. 9 interactions.
    IntActiQ9NPH0. 2 interactions.
    MINTiMINT-1387194.
    STRINGi9606.ENSP00000358241.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi45 – 473
    Beta strandi48 – 5811
    Beta strandi69 – 713
    Helixi78 – 814
    Helixi85 – 873
    Beta strandi92 – 1009
    Helixi105 – 1117
    Turni116 – 1183
    Helixi126 – 14318
    Turni144 – 1463
    Beta strandi152 – 1543
    Turni156 – 1583
    Beta strandi159 – 1635
    Helixi167 – 18115
    Beta strandi185 – 1873
    Beta strandi190 – 1934
    Turni196 – 1983
    Turni205 – 2073
    Helixi209 – 22113
    Helixi222 – 2243
    Helixi228 – 23811
    Helixi249 – 26113
    Helixi268 – 2725
    Helixi274 – 28815
    Helixi294 – 31421
    Beta strandi318 – 3203
    Turni322 – 3243
    Beta strandi327 – 3337
    Helixi335 – 34410
    Beta strandi358 – 3669
    Turni367 – 3693
    Beta strandi372 – 3787
    Beta strandi381 – 3833
    Beta strandi389 – 3946
    Helixi395 – 4028
    Turni403 – 4053
    Helixi409 – 4168

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JOBX-ray2.17A33-428[»]
    4JOCX-ray2.21A33-428[»]
    4JODX-ray2.21A33-428[»]
    ProteinModelPortaliQ9NPH0.
    SMRiQ9NPH0. Positions 42-419.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 168111Substrate bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG235758.
    HOGENOMiHOG000290692.
    HOVERGENiHBG079458.
    InParanoidiQ9NPH0.
    KOiK14395.
    OMAiHDVTLMP.
    OrthoDBiEOG747PJ2.
    PhylomeDBiQ9NPH0.
    TreeFamiTF318821.

    Family and domain databases

    Gene3Di3.40.50.1240. 2 hits.
    InterProiIPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view]
    PfamiPF00328. His_Phos_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 2 hits.
    PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NPH0-1) [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

    MITGVFSMRL WTPVGVLTSL AYCLHQRRVA LAELQEADGQ CPVDRSLLKL    50
    KMVQVVFRHG ARSPLKPLPL EEQVEWNPQL LEVPPQTQFD YTVTNLAGGP 100
    KPYSPYDSQY HETTLKGGMF AGQLTKVGMQ QMFALGERLR KNYVEDIPFL 150
    SPTFNPQEVF IRSTNIFRNL ESTRCLLAGL FQCQKEGPII IHTDEADSEV 200
    LYPNYQSCWS LRQRTRGRRQ TASLQPGISE DLKKVKDRMG IDSSDKVDFF 250
    ILLDNVAAEQ AHNLPSCPML KRFARMIEQR AVDTSLYILP KEDRESLQMA 300
    VGPFLHILES NLLKAVDSAT APDKIRKLYL YAAHDVTFIP LLMTLGIFDH 350
    KWPPFAVDLT MELYQHLESK EWFVQLYYHG KEQVPRGCPD GLCPLDMFLN 400
    AMSVYTLSPE KYHALCSQTQ VMEVGNEE 428
    Length:428
    Mass (Da):48,854
    Last modified:January 11, 2011 - v2
    Checksum:i37A09CFD1BB45BFA
    GO
    Isoform 2 (identifier: Q9NPH0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         261-271: AHNLPSCPMLK → EKMGSCRFHGS
         272-428: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:271
    Mass (Da):30,790
    Checksum:iFF6FF0AFF8D01144
    GO

    Sequence cautioni

    The sequence BAA89311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD92485.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti428 – 4281E → D in CAG33382. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti316 – 3161V → M.6 Publications
    Corresponds to variant rs6593795 [ dbSNP | Ensembl ].
    VAR_022678

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei261 – 27111AHNLPSCPMLK → EKMGSCRFHGS in isoform 2. 1 PublicationVSP_014121Add
    BLAST
    Alternative sequencei272 – 428157Missing in isoform 2. 1 PublicationVSP_014122Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031478 mRNA. Translation: BAA89311.1. Different initiation.
    AB030039 mRNA. Translation: BAA94309.2.
    AY358552 mRNA. Translation: AAQ88916.1.
    AK000657 mRNA. Translation: BAA91310.1.
    AB209248 mRNA. Translation: BAD92485.1. Different initiation.
    AL359207 Genomic DNA. Translation: CAI15199.1.
    BC009965 mRNA. Translation: AAH09965.1.
    BC034686 mRNA. Translation: AAH34686.1.
    CR457101 mRNA. Translation: CAG33382.1.
    CCDSiCCDS928.1. [Q9NPH0-1]
    RefSeqiNP_057445.4. NM_016361.4.
    UniGeneiHs.562154.

    Genome annotation databases

    EnsembliENST00000392988; ENSP00000376714; ENSG00000162836. [Q9NPH0-2]
    GeneIDi51205.
    KEGGihsa:51205.
    UCSCiuc001epr.2. human. [Q9NPH0-1]
    uc009wjj.1. human. [Q9NPH0-2]

    Polymorphism databases

    DMDMi317373268.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031478 mRNA. Translation: BAA89311.1 . Different initiation.
    AB030039 mRNA. Translation: BAA94309.2 .
    AY358552 mRNA. Translation: AAQ88916.1 .
    AK000657 mRNA. Translation: BAA91310.1 .
    AB209248 mRNA. Translation: BAD92485.1 . Different initiation.
    AL359207 Genomic DNA. Translation: CAI15199.1 .
    BC009965 mRNA. Translation: AAH09965.1 .
    BC034686 mRNA. Translation: AAH34686.1 .
    CR457101 mRNA. Translation: CAG33382.1 .
    CCDSi CCDS928.1. [Q9NPH0-1 ]
    RefSeqi NP_057445.4. NM_016361.4.
    UniGenei Hs.562154.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4JOB X-ray 2.17 A 33-428 [» ]
    4JOC X-ray 2.21 A 33-428 [» ]
    4JOD X-ray 2.21 A 33-428 [» ]
    ProteinModelPortali Q9NPH0.
    SMRi Q9NPH0. Positions 42-419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119378. 9 interactions.
    IntActi Q9NPH0. 2 interactions.
    MINTi MINT-1387194.
    STRINGi 9606.ENSP00000358241.

    PTM databases

    PhosphoSitei Q9NPH0.

    Polymorphism databases

    DMDMi 317373268.

    Proteomic databases

    MaxQBi Q9NPH0.
    PaxDbi Q9NPH0.
    PRIDEi Q9NPH0.

    Protocols and materials databases

    DNASUi 51205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392988 ; ENSP00000376714 ; ENSG00000162836 . [Q9NPH0-2 ]
    GeneIDi 51205.
    KEGGi hsa:51205.
    UCSCi uc001epr.2. human. [Q9NPH0-1 ]
    uc009wjj.1. human. [Q9NPH0-2 ]

    Organism-specific databases

    CTDi 51205.
    GeneCardsi GC01M147119.
    H-InvDB HIX0000989.
    HGNCi HGNC:29609. ACP6.
    HPAi HPA028560.
    MIMi 611471. gene.
    neXtProti NX_Q9NPH0.
    PharmGKBi PA134930830.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235758.
    HOGENOMi HOG000290692.
    HOVERGENi HBG079458.
    InParanoidi Q9NPH0.
    KOi K14395.
    OMAi HDVTLMP.
    OrthoDBi EOG747PJ2.
    PhylomeDBi Q9NPH0.
    TreeFami TF318821.

    Miscellaneous databases

    GeneWikii ACP6.
    GenomeRNAii 51205.
    NextBioi 54254.
    PROi Q9NPH0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NPH0.
    CleanExi HS_ACP6.
    Genevestigatori Q9NPH0.

    Family and domain databases

    Gene3Di 3.40.50.1240. 2 hits.
    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view ]
    Pfami PF00328. His_Phos_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 2 hits.
    PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis."
      Hiroyama M., Takenawa T.
      J. Biol. Chem. 274:29172-29180(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-59, INDUCTION, VARIANT MET-316.
      Tissue: Brain.
    2. "Novel human and mouse genes encoding an acid phosphatase family member and its downregulation in W/W(V) mouse jejunum."
      Takayama I., Daigo Y., Ward S.M., Sanders K.M., Walker R.L., Horowitz B., Yamanaka T., Fujino M.A.
      Gut 50:790-796(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT MET-316.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-316.
    4. "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] (ISOFORM 1), VARIANT MET-316.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. "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].
    7. "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), VARIANT MET-316.
      Tissue: Cervix and Pancreas.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-428 (ISOFORM 1), VARIANT MET-316.
    9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 33-47.
    10. "Crystal structures and biochemical studies of human lysophosphatidic acid phosphatase type 6."
      Li J., Dong Y., Lu X., Wang L., Peng W., Zhang X.C., Rao Z.
      Protein Cell 4:548-561(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 33-428 IN COMPLEXES WITH MALONATE AND TARTRATE, ACTIVE SITE, PROBABLE SUBSTRATE-BINDING SITES, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-58; HIS-59; ARG-62; TYR-106; ARG-168; ALA-257; SER-285; LEU-289; HIS-334 AND ASP-335.

    Entry informationi

    Entry nameiPPA6_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPH0
    Secondary accession number(s): Q59G61
    , Q5T490, Q6IAQ3, Q7LG81, Q9UIG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 115 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3