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Q9NPH0

- PPA6_HUMAN

UniProt

Q9NPH0 - PPA6_HUMAN

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Protein
Lysophosphatidic acid phosphatase type 6
Gene
ACP6, ACPL1, LPAP, UNQ205/PRO231
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 donor Inferred

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

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 Publication
Add
BLAST
Chaini33 – 428396Lysophosphatidic acid phosphatase type 6
PRO_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

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 168111Substrate binding By similarity
Add
BLAST

Sequence similaritiesi

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.

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.
VSP_014121Add
BLAST
Alternative sequencei272 – 428157Missing in isoform 2.
VSP_014122Add
BLAST

Sequence conflict

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

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

EnsembliENST00000369238; ENSP00000358241; ENSG00000162836. [Q9NPH0-1]
ENST00000392988; 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...

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 ENST00000369238 ; ENSP00000358241 ; ENSG00000162836 . [Q9NPH0-1 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 114 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

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