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P13686

- PPA5_HUMAN

UniProt

P13686 - PPA5_HUMAN

Protein

Tartrate-resistant acid phosphatase type 5

Gene

ACP5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias.

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.

    Cofactori

    Binds 2 iron ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi33 – 331Iron 1
    Metal bindingi71 – 711Iron 1
    Metal bindingi71 – 711Iron 2
    Metal bindingi74 – 741Iron 1
    Metal bindingi110 – 1101Iron 2
    Metal bindingi205 – 2051Iron 2
    Metal bindingi240 – 2401Iron 2
    Metal bindingi242 – 2421Iron 1

    GO - Molecular functioni

    1. acid phosphatase activity Source: Reactome
    2. ferric iron binding Source: UniProtKB
    3. ferrous iron binding Source: UniProtKB

    GO - Biological processi

    1. bone morphogenesis Source: Ensembl
    2. bone resorption Source: Ensembl
    3. defense response to Gram-positive bacterium Source: Ensembl
    4. negative regulation of inflammatory response Source: Ensembl
    5. negative regulation of interleukin-12 production Source: Ensembl
    6. negative regulation of interleukin-1 beta production Source: Ensembl
    7. negative regulation of nitric oxide biosynthetic process Source: Ensembl
    8. negative regulation of superoxide anion generation Source: Ensembl
    9. negative regulation of tumor necrosis factor production Source: Ensembl
    10. response to cytokine Source: Ensembl
    11. response to lipopolysaccharide Source: Ensembl
    12. riboflavin metabolic process Source: Reactome
    13. small molecule metabolic process Source: Reactome
    14. vitamin metabolic process Source: Reactome
    15. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_11070. Vitamin B2 (riboflavin) metabolism.
    SABIO-RKP13686.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tartrate-resistant acid phosphatase type 5 (EC:3.1.3.2)
    Short name:
    TR-AP
    Alternative name(s):
    Tartrate-resistant acid ATPase
    Short name:
    TrATPase
    Type 5 acid phosphatase
    Gene namesi
    Name:ACP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:124. ACP5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: ProtInc
    4. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Spondyloenchondrodysplasia with immune dysregulation (SPENCDI) [MIM:607944]: A disease characterized by vertebral and metaphyseal dysplasia, spasticity with cerebral calcifications, and strong predisposition to autoimmune diseases. The skeletal dysplasia is characterized by radiolucent and irregular spondylar and metaphyseal lesions that represent islands of chondroid tissue within bone.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. ACP5 inactivating mutations result in a functional excess of phosphorylated osteopontin causing deregulation of osteopontin signaling and consequential autoimmune disease.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521K → M in SPENCDI. 1 Publication
    VAR_065920
    Natural varianti89 – 891T → I in SPENCDI. 1 Publication
    VAR_065921
    Natural varianti109 – 1091G → R in SPENCDI. 1 Publication
    VAR_065922
    Natural varianti201 – 2011L → P in SPENCDI. 1 Publication
    VAR_065923
    Natural varianti215 – 2151G → R in SPENCDI. 2 Publications
    VAR_065924
    Natural varianti241 – 2411D → N in SPENCDI. 1 Publication
    VAR_065925
    Natural varianti262 – 2621N → H in SPENCDI. 1 Publication
    VAR_065926
    Natural varianti264 – 2641M → K in SPENCDI. 2 Publications
    VAR_065927
    Natural varianti278 – 2781Missing in SPENCDI. 1 Publication
    VAR_065928

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi607944. phenotype.
    Orphaneti1855. Spondyloenchondrodysplasia.
    PharmGKBiPA24448.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21214 PublicationsAdd
    BLAST
    Chaini22 – 325304Tartrate-resistant acid phosphatase type 5PRO_0000023981Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication
    Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi161 ↔ 219By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP13686.
    PRIDEiP13686.

    PTM databases

    PhosphoSiteiP13686.

    Miscellaneous databases

    PMAP-CutDBP13686.

    Expressioni

    Gene expression databases

    ArrayExpressiP13686.
    BgeeiP13686.
    CleanExiHS_ACP5.
    GenevestigatoriP13686.

    Organism-specific databases

    HPAiCAB002584.

    Interactioni

    Subunit structurei

    Exists either as monomer or, after proteolytic processing, as a dimer of two chains linked by disulfide bond(s).3 Publications

    Protein-protein interaction databases

    BioGridi106570. 8 interactions.
    IntActiP13686. 9 interactions.
    MINTiMINT-1387442.
    STRINGi9606.ENSP00000218758.

    Structurei

    Secondary structure

    1
    325
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 316
    Helixi45 – 6117
    Beta strandi64 – 685
    Turni74 – 763
    Helixi85 – 895
    Turni90 – 934
    Helixi97 – 1004
    Beta strandi104 – 1063
    Helixi110 – 1134
    Helixi117 – 1226
    Helixi123 – 1253
    Beta strandi128 – 1314
    Beta strandi134 – 1429
    Beta strandi149 – 1546
    Helixi157 – 1615
    Helixi164 – 1663
    Helixi178 – 19417
    Beta strandi198 – 2036
    Beta strandi211 – 2144
    Helixi218 – 2236
    Helixi225 – 2306
    Beta strandi235 – 2384
    Beta strandi240 – 2489
    Beta strandi254 – 2585
    Helixi271 – 2733
    Beta strandi279 – 2835
    Beta strandi291 – 2977
    Beta strandi299 – 30810
    Beta strandi313 – 3208

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WARX-ray2.22A22-325[»]
    2BQ8X-ray2.20X22-325[»]
    ProteinModelPortaliP13686.
    SMRiP13686. Positions 22-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13686.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1409.
    HOVERGENiHBG000433.
    InParanoidiP13686.
    KOiK14379.
    OMAiGEEMDIN.
    OrthoDBiEOG7WHH9R.
    PhylomeDBiP13686.
    TreeFamiTF313175.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR024927. Acid_Pase_5.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000898. Acid_Ptase_5. 1 hit.
    SUPFAMiSSF56300. SSF56300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P13686-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDMWTALLIL QALLLPSLAD GATPALRFVA VGDWGGVPNA PFHTAREMAN    50
    AKEIARTVQI LGADFILSLG DNFYFTGVQD INDKRFQETF EDVFSDRSLR 100
    KVPWYVLAGN HDHLGNVSAQ IAYSKISKRW NFPSPFYRLH FKIPQTNVSV 150
    AIFMLDTVTL CGNSDDFLSQ QPERPRDVKL ARTQLSWLKK QLAAAREDYV 200
    LVAGHYPVWS IAEHGPTHCL VKQLRPLLAT YGVTAYLCGH DHNLQYLQDE 250
    NGVGYVLSGA GNFMDPSKRH QRKVPNGYLR FHYGTEDSLG GFAYVEISSK 300
    EMTVTYIEAS GKSLFKTRLP RRARP 325
    Length:325
    Mass (Da):36,599
    Last modified:December 21, 2004 - v3
    Checksum:i079174A71A5BA264
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 462AR → GP in AAA76849. (PubMed:2909539)Curated
    Sequence conflicti47 – 471E → G AA sequence (PubMed:1477968)Curated
    Sequence conflicti47 – 471E → Q AA sequence (PubMed:2775236)Curated
    Sequence conflicti50 – 501N → W AA sequence (PubMed:2775236)Curated
    Sequence conflicti177 – 1804DVKL → LT in AAA76849. (PubMed:2909539)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521K → M in SPENCDI. 1 Publication
    VAR_065920
    Natural varianti89 – 891T → I in SPENCDI. 1 Publication
    VAR_065921
    Natural varianti109 – 1091G → R in SPENCDI. 1 Publication
    VAR_065922
    Natural varianti148 – 1481V → M.1 Publication
    Corresponds to variant rs2305799 [ dbSNP | Ensembl ].
    VAR_020602
    Natural varianti200 – 2001V → M.1 Publication
    Corresponds to variant rs2229531 [ dbSNP | Ensembl ].
    VAR_020603
    Natural varianti201 – 2011L → P in SPENCDI. 1 Publication
    VAR_065923
    Natural varianti215 – 2151G → R in SPENCDI. 2 Publications
    VAR_065924
    Natural varianti221 – 2211V → I.
    Corresponds to variant rs2229532 [ dbSNP | Ensembl ].
    VAR_029288
    Natural varianti241 – 2411D → N in SPENCDI. 1 Publication
    VAR_065925
    Natural varianti262 – 2621N → H in SPENCDI. 1 Publication
    VAR_065926
    Natural varianti264 – 2641M → K in SPENCDI. 2 Publications
    VAR_065927
    Natural varianti278 – 2781Missing in SPENCDI. 1 Publication
    VAR_065928

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04430 mRNA. Translation: AAA76849.1.
    X14618 mRNA. Translation: CAA32771.1.
    CR457078 mRNA. Translation: CAG33359.1.
    AK290717 mRNA. Translation: BAF83406.1.
    BC025414 mRNA. Translation: AAH25414.1.
    BC111014 mRNA. Translation: AAI11015.1.
    X67123 Genomic DNA. No translation available.
    CCDSiCCDS12265.1.
    PIRiS15752.
    RefSeqiNP_001104504.1. NM_001111034.1.
    NP_001104505.1. NM_001111035.1.
    NP_001104506.1. NM_001111036.1.
    NP_001602.1. NM_001611.3.
    XP_005259995.1. XM_005259938.1.
    XP_005259996.1. XM_005259939.2.
    UniGeneiHs.1211.

    Genome annotation databases

    EnsembliENST00000218758; ENSP00000218758; ENSG00000102575.
    ENST00000412435; ENSP00000392374; ENSG00000102575.
    ENST00000433365; ENSP00000413456; ENSG00000102575.
    ENST00000592828; ENSP00000468767; ENSG00000102575.
    GeneIDi54.
    KEGGihsa:54.
    UCSCiuc002msg.4. human.

    Polymorphism databases

    DMDMi56757583.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Tartrate-resistant acid phosphatase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04430 mRNA. Translation: AAA76849.1 .
    X14618 mRNA. Translation: CAA32771.1 .
    CR457078 mRNA. Translation: CAG33359.1 .
    AK290717 mRNA. Translation: BAF83406.1 .
    BC025414 mRNA. Translation: AAH25414.1 .
    BC111014 mRNA. Translation: AAI11015.1 .
    X67123 Genomic DNA. No translation available.
    CCDSi CCDS12265.1.
    PIRi S15752.
    RefSeqi NP_001104504.1. NM_001111034.1.
    NP_001104505.1. NM_001111035.1.
    NP_001104506.1. NM_001111036.1.
    NP_001602.1. NM_001611.3.
    XP_005259995.1. XM_005259938.1.
    XP_005259996.1. XM_005259939.2.
    UniGenei Hs.1211.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WAR X-ray 2.22 A 22-325 [» ]
    2BQ8 X-ray 2.20 X 22-325 [» ]
    ProteinModelPortali P13686.
    SMRi P13686. Positions 22-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106570. 8 interactions.
    IntActi P13686. 9 interactions.
    MINTi MINT-1387442.
    STRINGi 9606.ENSP00000218758.

    PTM databases

    PhosphoSitei P13686.

    Polymorphism databases

    DMDMi 56757583.

    Proteomic databases

    PaxDbi P13686.
    PRIDEi P13686.

    Protocols and materials databases

    DNASUi 54.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000218758 ; ENSP00000218758 ; ENSG00000102575 .
    ENST00000412435 ; ENSP00000392374 ; ENSG00000102575 .
    ENST00000433365 ; ENSP00000413456 ; ENSG00000102575 .
    ENST00000592828 ; ENSP00000468767 ; ENSG00000102575 .
    GeneIDi 54.
    KEGGi hsa:54.
    UCSCi uc002msg.4. human.

    Organism-specific databases

    CTDi 54.
    GeneCardsi GC19M011685.
    HGNCi HGNC:124. ACP5.
    HPAi CAB002584.
    MIMi 171640. gene.
    607944. phenotype.
    neXtProti NX_P13686.
    Orphaneti 1855. Spondyloenchondrodysplasia.
    PharmGKBi PA24448.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1409.
    HOVERGENi HBG000433.
    InParanoidi P13686.
    KOi K14379.
    OMAi GEEMDIN.
    OrthoDBi EOG7WHH9R.
    PhylomeDBi P13686.
    TreeFami TF313175.

    Enzyme and pathway databases

    Reactomei REACT_11070. Vitamin B2 (riboflavin) metabolism.
    SABIO-RK P13686.

    Miscellaneous databases

    ChiTaRSi ACP5. human.
    EvolutionaryTracei P13686.
    GeneWikii Tartrate-resistant_acid_phosphatase.
    GenomeRNAii 54.
    NextBioi 217.
    PMAP-CutDB P13686.
    PROi P13686.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13686.
    Bgeei P13686.
    CleanExi HS_ACP5.
    Genevestigatori P13686.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR024927. Acid_Pase_5.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000898. Acid_Ptase_5. 1 hit.
    SUPFAMi SSF56300. SSF56300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta."
      Ketcham C.M., Roberts R.M., Simmen R.C.M., Nick H.S.
      J. Biol. Chem. 264:557-563(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage."
      Lord D.K., Cross N.C.P., Bevilacqua M.A., Roder S.H., Gorman P.A., Groves A.V., Moss D.W., Sheer D., Cox T.M.
      Eur. J. Biochem. 189:287-293(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    3. "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], VARIANTS MET-148 AND MET-200.
    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].
      Tissue: Lung.
    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].
      Tissue: Brain and Skin.
    6. "Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase."
      Cassady A.I., King A.G., Cross N.C.P., Hume D.A.
      Gene 130:201-207(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245.
    7. "Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas."
      Hayman A.R., Warburton M.J., Pringle J.A.S., Coles B., Chambers T.J.
      Biochem. J. 261:601-609(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-64 AND 183-202.
      Tissue: Osteoclastoma.
    8. "Heterogeneity of hairy cell tartrate-resistant acid phosphatase."
      Janckila A.J., Latham M.D., Lam K.-W., Chow K.-C., Li C.-Y., Yam L.T.
      Clin. Biochem. 25:437-443(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-55 AND 183-203, SUBUNIT.
      Tissue: Spleen.
    9. "Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen."
      Stepan J.J., Lau K.H.W., Mohan S., Kraenzlin M., Baylink D.J.
      Biochem. Biophys. Res. Commun. 165:1027-1034(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-37.
      Tissue: Osteoclastoma.
    10. "Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure."
      Stepan J.J., Lau K.H.W., Mohan S., Singer F.R., Baylink D.J.
      Biochem. Biophys. Res. Commun. 168:792-800(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-31.
      Tissue: Osteoclastoma.
    11. "Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide."
      Hayman A.R., Dryden A.J., Chambers T.J., Warburton M.J.
      Biochem. J. 277:631-634(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    12. "Crystal structures of recombinant human purple acid phosphatase with and without an inhibitory conformation of the repression loop."
      Straeter N., Jasper B., Scholte M., Krebs B., Duff A.P., Langley D.B., Han R., Averill B.A., Freeman H.C., Guss J.M.
      J. Mol. Biol. 351:233-246(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 22-325 IN COMPLEX WITH IRON IONS, GLYCOSYLATION AT ASN-116.
    13. Cited for: VARIANTS SPENCDI ILE-89; ARG-215; ASN-241 AND LYS-264.
    14. "Genetic deficiency of tartrate-resistant acid phosphatase associated with skeletal dysplasia, cerebral calcifications and autoimmunity."
      Lausch E., Janecke A., Bros M., Trojandt S., Alanay Y., De Laet C., Hubner C.A., Meinecke P., Nishimura G., Matsuo M., Hirano Y., Tenoutasse S., Kiss A., Rosa R.F., Unger S.L., Renella R., Bonafe L., Spranger J.
      , Unger S., Zabel B., Superti-Furga A.
      Nat. Genet. 43:132-137(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPENCDI MET-52; ARG-109; PRO-201; ARG-215; HIS-262; LYS-264 AND TYR-278 DEL.

    Entry informationi

    Entry nameiPPA5_HUMAN
    AccessioniPrimary (citable) accession number: P13686
    Secondary accession number(s): A8K3V2
    , Q2TAB1, Q6IAS6, Q9UCJ5, Q9UCJ6, Q9UCJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 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 19
      Human chromosome 19: 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