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P13686

- PPA5_HUMAN

UniProt

P13686 - PPA5_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
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.2 Publications
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...) Reviewed prediction
Disulfide bondi161 ↔ 219 By 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).2 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.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462AR → GP in AAA76849. 1 Publication
Sequence conflicti47 – 471E → G AA sequence 1 Publication
Sequence conflicti47 – 471E → Q AA sequence 1 Publication
Sequence conflicti50 – 501N → W AA sequence 1 Publication
Sequence conflicti177 – 1804DVKL → LT in AAA76849. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 148 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

Similar proteinsi