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Protein

Lysosomal thioesterase PPT2

Gene

PPT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins.3 Publications

Kineticsi

  1. KM=67 µM for S-palmitoyl-CoA1 Publication
  2. KM=37 µM for S-palmitoyl-N-acetylcysteamine1 Publication
  3. KM=117 µM for 4-methylumbelliferyl-6-S-palmitoyl-beta-D-glucopyranoside1 Publication

Vmax=1.7 µmol/min/mg enzyme toward S-palmitoyl-CoA1 Publication

Vmax=3.3 µmol/min/mg enzyme toward S-palmitoyl-N-acetylcysteamine1 Publication

Vmax=0.43 µmol/min/mg enzyme toward 4-methylumbelliferyl-6-S-palmitoyl-beta-D-glucopyranoside1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111Nucleophile
Active sitei228 – 2281
Active sitei283 – 2831

GO - Molecular functioni

  1. palmitoyl-(protein) hydrolase activity Source: Ensembl
  2. palmitoyl hydrolase activity Source: UniProtKB
  3. thiolester hydrolase activity Source: UniProtKB

GO - Biological processi

  1. macromolecule depalmitoylation Source: GOC
  2. metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysosomal thioesterase PPT2 (EC:3.1.2.-)
Short name:
PPT-2
Alternative name(s):
S-thioesterase G14
Gene namesi
Name:PPT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:9326. PPT2.

Subcellular locationi

Lysosome 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111S → A: Abolishes enzymatic activity. 1 Publication
Mutagenesisi228 – 2281D → A: Abolishes enzymatic activity. 1 Publication
Mutagenesisi283 – 2831H → A: Abolishes enzymatic activity. 1 Publication
Mutagenesisi287 – 2871H → A: No effect on enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA33689.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 302275Lysosomal thioesterase PPT2PRO_0000025554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi109 ↔ 1171 Publication
Disulfide bondi165 ↔ 1761 Publication
Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi276 ↔ 2961 Publication
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9UMR5.
PaxDbiQ9UMR5.
PRIDEiQ9UMR5.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9UMR5.
ExpressionAtlasiQ9UMR5. baseline and differential.
GenevestigatoriQ9UMR5.

Organism-specific databases

HPAiHPA000414.

Interactioni

Protein-protein interaction databases

BioGridi114775. 28 interactions.
MINTiMINT-4721124.

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 424Combined sources
Helixi49 – 524Combined sources
Helixi53 – 6210Combined sources
Beta strandi68 – 703Combined sources
Helixi77 – 804Combined sources
Helixi83 – 10018Combined sources
Beta strandi105 – 1106Combined sources
Helixi112 – 12312Combined sources
Beta strandi129 – 1368Combined sources
Helixi147 – 1526Combined sources
Helixi158 – 1658Combined sources
Helixi170 – 1723Combined sources
Helixi175 – 1784Combined sources
Helixi185 – 1917Combined sources
Helixi195 – 1984Combined sources
Helixi207 – 2148Combined sources
Beta strandi218 – 2247Combined sources
Beta strandi229 – 2335Combined sources
Helixi234 – 2385Combined sources
Helixi251 – 2533Combined sources
Helixi255 – 2584Combined sources
Turni259 – 2624Combined sources
Helixi264 – 2696Combined sources
Beta strandi273 – 2775Combined sources
Turni283 – 2875Combined sources
Helixi290 – 2967Combined sources
Helixi298 – 3003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJAX-ray2.70A1-302[»]
ProteinModelPortaliQ9UMR5.
SMRiQ9UMR5. Positions 35-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UMR5.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1075.
GeneTreeiENSGT00530000063368.
HOVERGENiHBG019159.
InParanoidiQ9UMR5.
KOiK01074.
OMAiVPWISEL.
PhylomeDBiQ9UMR5.
TreeFamiTF323926.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
IPR030295. PPT2.
[Graphical view]
PANTHERiPTHR11247:SF22. PTHR11247:SF22. 1 hit.
PfamiPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSiPR00414. PPTHIESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

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. AlignAdd to basket

Isoform 1 (identifier: Q9UMR5-1) [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

        10         20         30         40         50
MLGLCGQRLP AAWVLLLLPF LPLLLLAAPA PHRASYKPVI VVHGLFDSSY
60 70 80 90 100
SFRHLLEYIN ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMAK
110 120 130 140 150
APQGVHLICY SQGGLVCRAL LSVMDDHNVD SFISLSSPQM GQYGDTDYLK
160 170 180 190 200
WLFPTSMRSN LYRICYSPWG QEFSICNYWH DPHHDDLYLN ASSFLALING
210 220 230 240 250
ERDHPNATVW RKNFLRVGHL VLIGGPDDGV ITPWQSSFFG FYDANETVLE
260 270 280 290 300
MEEQLVYLRD SFGLKTLLAR GAIVRCPMAG ISHTAWHSNR TLYETCIEPW

LS
Length:302
Mass (Da):34,225
Last modified:May 18, 2010 - v4
Checksum:iE242D677970B4BEA
GO
Isoform 2 (identifier: Q9UMR5-2) [UniParc]FASTAAdd to basket

Also known as: I

The sequence of this isoform differs from the canonical sequence as follows:
     256-300: VYLRDSFGLK...TLYETCIEPW → PARPTHQSEL...ESWGPGLSCA

Note: Catalytically inactive due to lack of His-283. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:301
Mass (Da):34,055
Checksum:i37EC25978B3FE96E
GO
Isoform 3 (identifier: Q9UMR5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKSCGSM

Note: No experimental confirmation available.

Show »
Length:308
Mass (Da):34,819
Checksum:iE83460052465B3A4
GO

Sequence cautioni

The sequence CAG38577.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891L → P in CAG38577 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51C → W.10 Publications
Corresponds to variant rs3134604 [ dbSNP | Ensembl ].
VAR_027107
Natural varianti34 – 341A → E.3 Publications
Corresponds to variant rs3096696 [ dbSNP | Ensembl ].
VAR_027108

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MKSCGSM in isoform 3. 1 PublicationVSP_054027
Alternative sequencei256 – 30045VYLRD…CIEPW → PARPTHQSELLLLRLVCLKP PRRKKPACRVQRQSESWGPG LSCA in isoform 2. 2 PublicationsVSP_005188Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020543 mRNA. Translation: AAB80730.1.
AF020544 mRNA. Translation: AAB80731.1.
Y17958 mRNA. Translation: CAB46981.1.
AL110128 mRNA. Translation: CAB53659.1.
CR533546 mRNA. Translation: CAG38577.1. Different initiation.
AK292729 mRNA. Translation: BAF85418.1.
U89336 Genomic DNA. Translation: AAB47495.1.
AL662828 Genomic DNA. Translation: CAI17424.1.
AL662828 Genomic DNA. Translation: CAI17426.2.
AL662828 Genomic DNA. Translation: CAM24823.1.
AL662828 Genomic DNA. Translation: CAM24825.1.
AL662884 Genomic DNA. Translation: CAI18342.1.
AL662884 Genomic DNA. Translation: CAI18344.1.
AL662884 Genomic DNA. Translation: CAI41763.1.
AL845464 Genomic DNA. Translation: CAI41797.1.
AL845464 Genomic DNA. Translation: CAI41798.1.
AL845464 Genomic DNA. Translation: CAI41799.1.
AL845464 Genomic DNA. Translation: CAM25714.1.
BX284686 Genomic DNA. Translation: CAM26213.1.
BX284686 Genomic DNA. Translation: CAM26215.1.
BX284686 Genomic DNA. Translation: CAM26216.1.
BX284686 Genomic DNA. Translation: CAM26218.1.
BX927239 Genomic DNA. Translation: CAQ06588.1.
BX927239 Genomic DNA. Translation: CAQ06590.1.
CR753803 Genomic DNA. Translation: CAQ09561.1.
CR933878 Genomic DNA. Translation: CAQ09617.1.
CR933878 Genomic DNA. Translation: CAQ09619.1.
CR812478 Genomic DNA. Translation: CAQ10692.1.
CR812478 Genomic DNA. Translation: CAQ10694.1.
CH471081 Genomic DNA. Translation: EAX03597.1.
CH471081 Genomic DNA. Translation: EAX03591.1.
BC001355 mRNA. Translation: AAH01355.1.
CCDSiCCDS4740.1. [Q9UMR5-3]
CCDS4742.1. [Q9UMR5-1]
RefSeqiNP_001191032.1. NM_001204103.1. [Q9UMR5-1]
NP_005146.4. NM_005155.6. [Q9UMR5-1]
NP_619731.2. NM_138717.2. [Q9UMR5-3]
UniGeneiHs.332138.
Hs.731888.

Genome annotation databases

EnsembliENST00000324816; ENSP00000320528; ENSG00000221988. [Q9UMR5-1]
ENST00000361568; ENSP00000354608; ENSG00000221988. [Q9UMR5-3]
ENST00000375137; ENSP00000364279; ENSG00000221988. [Q9UMR5-1]
ENST00000375143; ENSP00000364285; ENSG00000221988. [Q9UMR5-1]
ENST00000383301; ENSP00000372789; ENSG00000206329.
ENST00000395523; ENSP00000378894; ENSG00000221988. [Q9UMR5-1]
ENST00000412651; ENSP00000416505; ENSG00000236649.
ENST00000414356; ENSP00000398462; ENSG00000168452.
ENST00000415972; ENSP00000408333; ENSG00000228116.
ENST00000423347; ENSP00000406219; ENSG00000231618.
ENST00000433748; ENSP00000410001; ENSG00000206256.
ENST00000476214; ENSP00000432308; ENSG00000168452.
ENST00000480383; ENSP00000432502; ENSG00000236649.
ENST00000483565; ENSP00000431928; ENSG00000231618.
ENST00000488579; ENSP00000434992; ENSG00000236649.
ENST00000490624; ENSP00000433323; ENSG00000168452.
ENST00000493809; ENSP00000436963; ENSG00000227600.
ENST00000496937; ENSP00000432964; ENSG00000231618.
ENST00000527704; ENSP00000433061; ENSG00000227600.
GeneIDi9374.
KEGGihsa:9374.
UCSCiuc003nzx.3. human. [Q9UMR5-1]
uc010jtu.1. human. [Q9UMR5-2]

Polymorphism databases

DMDMi296453016.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020543 mRNA. Translation: AAB80730.1.
AF020544 mRNA. Translation: AAB80731.1.
Y17958 mRNA. Translation: CAB46981.1.
AL110128 mRNA. Translation: CAB53659.1.
CR533546 mRNA. Translation: CAG38577.1. Different initiation.
AK292729 mRNA. Translation: BAF85418.1.
U89336 Genomic DNA. Translation: AAB47495.1.
AL662828 Genomic DNA. Translation: CAI17424.1.
AL662828 Genomic DNA. Translation: CAI17426.2.
AL662828 Genomic DNA. Translation: CAM24823.1.
AL662828 Genomic DNA. Translation: CAM24825.1.
AL662884 Genomic DNA. Translation: CAI18342.1.
AL662884 Genomic DNA. Translation: CAI18344.1.
AL662884 Genomic DNA. Translation: CAI41763.1.
AL845464 Genomic DNA. Translation: CAI41797.1.
AL845464 Genomic DNA. Translation: CAI41798.1.
AL845464 Genomic DNA. Translation: CAI41799.1.
AL845464 Genomic DNA. Translation: CAM25714.1.
BX284686 Genomic DNA. Translation: CAM26213.1.
BX284686 Genomic DNA. Translation: CAM26215.1.
BX284686 Genomic DNA. Translation: CAM26216.1.
BX284686 Genomic DNA. Translation: CAM26218.1.
BX927239 Genomic DNA. Translation: CAQ06588.1.
BX927239 Genomic DNA. Translation: CAQ06590.1.
CR753803 Genomic DNA. Translation: CAQ09561.1.
CR933878 Genomic DNA. Translation: CAQ09617.1.
CR933878 Genomic DNA. Translation: CAQ09619.1.
CR812478 Genomic DNA. Translation: CAQ10692.1.
CR812478 Genomic DNA. Translation: CAQ10694.1.
CH471081 Genomic DNA. Translation: EAX03597.1.
CH471081 Genomic DNA. Translation: EAX03591.1.
BC001355 mRNA. Translation: AAH01355.1.
CCDSiCCDS4740.1. [Q9UMR5-3]
CCDS4742.1. [Q9UMR5-1]
RefSeqiNP_001191032.1. NM_001204103.1. [Q9UMR5-1]
NP_005146.4. NM_005155.6. [Q9UMR5-1]
NP_619731.2. NM_138717.2. [Q9UMR5-3]
UniGeneiHs.332138.
Hs.731888.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJAX-ray2.70A1-302[»]
ProteinModelPortaliQ9UMR5.
SMRiQ9UMR5. Positions 35-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114775. 28 interactions.
MINTiMINT-4721124.

Chemistry

ChEMBLiCHEMBL2189137.

Polymorphism databases

DMDMi296453016.

Proteomic databases

MaxQBiQ9UMR5.
PaxDbiQ9UMR5.
PRIDEiQ9UMR5.

Protocols and materials databases

DNASUi9374.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324816; ENSP00000320528; ENSG00000221988. [Q9UMR5-1]
ENST00000361568; ENSP00000354608; ENSG00000221988. [Q9UMR5-3]
ENST00000375137; ENSP00000364279; ENSG00000221988. [Q9UMR5-1]
ENST00000375143; ENSP00000364285; ENSG00000221988. [Q9UMR5-1]
ENST00000383301; ENSP00000372789; ENSG00000206329.
ENST00000395523; ENSP00000378894; ENSG00000221988. [Q9UMR5-1]
ENST00000412651; ENSP00000416505; ENSG00000236649.
ENST00000414356; ENSP00000398462; ENSG00000168452.
ENST00000415972; ENSP00000408333; ENSG00000228116.
ENST00000423347; ENSP00000406219; ENSG00000231618.
ENST00000433748; ENSP00000410001; ENSG00000206256.
ENST00000476214; ENSP00000432308; ENSG00000168452.
ENST00000480383; ENSP00000432502; ENSG00000236649.
ENST00000483565; ENSP00000431928; ENSG00000231618.
ENST00000488579; ENSP00000434992; ENSG00000236649.
ENST00000490624; ENSP00000433323; ENSG00000168452.
ENST00000493809; ENSP00000436963; ENSG00000227600.
ENST00000496937; ENSP00000432964; ENSG00000231618.
ENST00000527704; ENSP00000433061; ENSG00000227600.
GeneIDi9374.
KEGGihsa:9374.
UCSCiuc003nzx.3. human. [Q9UMR5-1]
uc010jtu.1. human. [Q9UMR5-2]

Organism-specific databases

CTDi9374.
GeneCardsiGC06P032122.
GC06Pi32132.
GC06Pj32069.
GC06Pk32096.
GC06Pl32160.
GC06Pm32197.
GC06Pn32078.
GC06Po32128.
HGNCiHGNC:9326. PPT2.
HPAiHPA000414.
MIMi603298. gene.
neXtProtiNX_Q9UMR5.
PharmGKBiPA33689.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1075.
GeneTreeiENSGT00530000063368.
HOVERGENiHBG019159.
InParanoidiQ9UMR5.
KOiK01074.
OMAiVPWISEL.
PhylomeDBiQ9UMR5.
TreeFamiTF323926.

Miscellaneous databases

ChiTaRSiPPT2. human.
EvolutionaryTraceiQ9UMR5.
GeneWikiiPPT2.
GenomeRNAii9374.
NextBioi35116.
PROiQ9UMR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UMR5.
ExpressionAtlasiQ9UMR5. baseline and differential.
GenevestigatoriQ9UMR5.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
IPR030295. PPT2.
[Graphical view]
PANTHERiPTHR11247:SF22. PTHR11247:SF22. 1 hit.
PfamiPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSiPR00414. PPTHIESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity."
    Soyombo A.A., Hofmann S.L.
    J. Biol. Chem. 272:27456-27463(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, PH DEPENDENCE, VARIANT TRP-5.
  2. "Characterization of a human MHC class III region gene product with S-thioesterase activity."
    Aguado B., Campbell R.D.
    Biochem. J. 341:679-689(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, FUNCTION, VARIANT TRP-5.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT TRP-5.
    Tissue: Brain.
  4. "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] (ISOFORM 1), VARIANT TRP-5.
  5. "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 2), VARIANT TRP-5.
    Tissue: Kidney.
  6. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS TRP-5 AND GLU-34.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS TRP-5 AND GLU-34.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-5.
  9. "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 TRP-5.
    Tissue: Skin.
  10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2."
    Calero G., Gupta P., Nonato M.C., Tandel S., Biehl E.R., Hofmann S.L., Clardy J.
    J. Biol. Chem. 278:37957-37964(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), FUNCTION, KINETIC PARAMETERS, MUTAGENESIS OF SER-111; ASP-228; HIS-283 AND HIS-287, GLYCOSYLATION AT ASN-190, DISULFIDE BONDS.
  13. "Structure of the human palmitoyl-protein thioesterase-2 gene (PPT2) in the major histocompatibility complex on chromosome 6p21.3."
    Soyombo A.A., Yi W., Hofmann S.L.
    Genomics 56:208-216(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TRP-5 AND GLU-34.

Entry informationi

Entry nameiPPT2_HUMAN
AccessioniPrimary (citable) accession number: Q9UMR5
Secondary accession number(s): A2ABC9
, A2ABD1, A2ARM7, A2BFH7, A2BFH9, A2BFI2, A8K9L4, B0S868, G8JLE1, O14799, Q0P6K0, Q5JP13, Q5JP14, Q5JQF0, Q5SSX4, Q5SSX5, Q5SSX6, Q5STJ4, Q5STJ5, Q5STJ6, Q6FI80, Q99945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: May 18, 2010
Last modified: March 4, 2015
This is version 129 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.