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Q9UMR5

- PPT2_HUMAN

UniProt

Q9UMR5 - PPT2_HUMAN

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Protein
Lysosomal thioesterase PPT2
Gene
PPT2
Organism
Homo sapiens (Human)
Status
Reviewed - 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-acetylcysteamine
  3. KM=117 µM for 4-methylumbelliferyl-6-S-palmitoyl-beta-D-glucopyranoside

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

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

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

pH dependencei

Optimum pH is 7.0.

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: UniProtKB
  2. thiolester hydrolase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: UniProtKB
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

Organism-specific databases

HGNCiHGNC:9326. PPT2.

Subcellular locationi

Lysosome 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  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 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 302275Lysosomal thioesterase PPT2
PRO_0000025554Add
BLAST

Amino acid modifications

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

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

ArrayExpressiQ9UMR5.
BgeeiQ9UMR5.
GenevestigatoriQ9UMR5.

Organism-specific databases

HPAiHPA000414.

Interactioni

Protein-protein interaction databases

BioGridi114775. 27 interactions.
MINTiMINT-4721124.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJAX-ray2.70A1-302[»]
ProteinModelPortaliQ9UMR5.
SMRiQ9UMR5. Positions 35-302.

Miscellaneous databases

EvolutionaryTraceiQ9UMR5.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
[Graphical view]
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. Align

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

MLGLCGQRLP AAWVLLLLPF LPLLLLAAPA PHRASYKPVI VVHGLFDSSY    50
SFRHLLEYIN ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMAK 100
APQGVHLICY SQGGLVCRAL LSVMDDHNVD SFISLSSPQM GQYGDTDYLK 150
WLFPTSMRSN LYRICYSPWG QEFSICNYWH DPHHDDLYLN ASSFLALING 200
ERDHPNATVW RKNFLRVGHL VLIGGPDDGV ITPWQSSFFG FYDANETVLE 250
MEEQLVYLRD SFGLKTLLAR GAIVRCPMAG ISHTAWHSNR TLYETCIEPW 300
LS 302
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.

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.
VSP_054027
Alternative sequencei256 – 30045VYLRD…CIEPW → PARPTHQSELLLLRLVCLKP PRRKKPACRVQRQSESWGPG LSCA in isoform 2.
VSP_005188Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891L → P in CAG38577. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000375137; ENSP00000364279; ENSG00000221988. [Q9UMR5-1]
ENST00000375143; ENSP00000364285; ENSG00000221988. [Q9UMR5-1]
ENST00000395523; ENSP00000378894; ENSG00000221988. [Q9UMR5-1]
ENST00000399856; ENSP00000382748; ENSG00000206329.
ENST00000399859; ENSP00000382749; ENSG00000206329.
ENST00000399860; ENSP00000382750; ENSG00000206329.
ENST00000415972; ENSP00000408333; ENSG00000228116.
ENST00000420778; ENSP00000412827; ENSG00000168452.
ENST00000422988; ENSP00000406566; ENSG00000227600.
ENST00000424353; ENSP00000411007; ENSG00000231618.
ENST00000427556; ENSP00000389930; ENSG00000168452.
ENST00000433748; ENSP00000410001; ENSG00000206256.
ENST00000438385; ENSP00000395242; ENSG00000227600.
ENST00000440507; ENSP00000392885; ENSG00000231618.
ENST00000440533; ENSP00000403820; ENSG00000236649.
ENST00000445462; ENSP00000399879; ENSG00000236649.
ENST00000445576; ENSP00000412381; ENSG00000221988. [Q9UMR5-2]
ENST00000452304; ENSP00000411625; ENSG00000231618.
ENST00000452562; ENSP00000408703; ENSG00000168452.
ENST00000456497; ENSP00000406496; ENSG00000227600.
ENST00000457509; ENSP00000388341; ENSG00000236649.
ENST00000476214; ENSP00000432308; ENSG00000168452.
ENST00000480383; ENSP00000432502; ENSG00000236649.
ENST00000483565; ENSP00000431928; ENSG00000231618.
ENST00000488579; ENSP00000434992; ENSG00000236649.
ENST00000490624; ENSP00000433323; ENSG00000168452.
ENST00000493809; ENSP00000436963; ENSG00000227600.
ENST00000496937; ENSP00000432964; ENSG00000231618.
ENST00000525601; ENSP00000433696; ENSG00000227600.
ENST00000527704; ENSP00000433061; ENSG00000227600.
ENST00000546871; ENSP00000448392; ENSG00000206329.
ENST00000547309; ENSP00000448877; ENSG00000227600.
ENST00000547565; ENSP00000448120; ENSG00000236649.
ENST00000548089; ENSP00000448456; ENSG00000231618.
ENST00000549544; ENSP00000447998; ENSG00000168452.
ENST00000550796; ENSP00000447926; ENSG00000236649.
ENST00000551222; ENSP00000447973; ENSG00000231618.
ENST00000552076; ENSP00000448072; ENSG00000227600.
ENST00000552922; ENSP00000447950; ENSG00000168452.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4740.1. [Q9UMR5-3 ]
CCDS4742.1. [Q9UMR5-1 ]
RefSeqi NP_001191032.1. NM_001204103.1. [Q9UMR5-1 ]
NP_005146.4. NM_005155.6. [Q9UMR5-1 ]
NP_619731.2. NM_138717.2. [Q9UMR5-3 ]
UniGenei Hs.332138.
Hs.731888.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PJA X-ray 2.70 A 1-302 [» ]
ProteinModelPortali Q9UMR5.
SMRi Q9UMR5. Positions 35-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114775. 27 interactions.
MINTi MINT-4721124.

Chemistry

ChEMBLi CHEMBL2189137.

Polymorphism databases

DMDMi 296453016.

Proteomic databases

MaxQBi Q9UMR5.
PaxDbi Q9UMR5.
PRIDEi Q9UMR5.

Protocols and materials databases

DNASUi 9374.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324816 ; ENSP00000320528 ; ENSG00000221988 . [Q9UMR5-1 ]
ENST00000361568 ; ENSP00000354608 ; ENSG00000221988 .
ENST00000375137 ; ENSP00000364279 ; ENSG00000221988 . [Q9UMR5-1 ]
ENST00000375143 ; ENSP00000364285 ; ENSG00000221988 . [Q9UMR5-1 ]
ENST00000395523 ; ENSP00000378894 ; ENSG00000221988 . [Q9UMR5-1 ]
ENST00000399856 ; ENSP00000382748 ; ENSG00000206329 .
ENST00000399859 ; ENSP00000382749 ; ENSG00000206329 .
ENST00000399860 ; ENSP00000382750 ; ENSG00000206329 .
ENST00000415972 ; ENSP00000408333 ; ENSG00000228116 .
ENST00000420778 ; ENSP00000412827 ; ENSG00000168452 .
ENST00000422988 ; ENSP00000406566 ; ENSG00000227600 .
ENST00000424353 ; ENSP00000411007 ; ENSG00000231618 .
ENST00000427556 ; ENSP00000389930 ; ENSG00000168452 .
ENST00000433748 ; ENSP00000410001 ; ENSG00000206256 .
ENST00000438385 ; ENSP00000395242 ; ENSG00000227600 .
ENST00000440507 ; ENSP00000392885 ; ENSG00000231618 .
ENST00000440533 ; ENSP00000403820 ; ENSG00000236649 .
ENST00000445462 ; ENSP00000399879 ; ENSG00000236649 .
ENST00000445576 ; ENSP00000412381 ; ENSG00000221988 . [Q9UMR5-2 ]
ENST00000452304 ; ENSP00000411625 ; ENSG00000231618 .
ENST00000452562 ; ENSP00000408703 ; ENSG00000168452 .
ENST00000456497 ; ENSP00000406496 ; ENSG00000227600 .
ENST00000457509 ; ENSP00000388341 ; ENSG00000236649 .
ENST00000476214 ; ENSP00000432308 ; ENSG00000168452 .
ENST00000480383 ; ENSP00000432502 ; ENSG00000236649 .
ENST00000483565 ; ENSP00000431928 ; ENSG00000231618 .
ENST00000488579 ; ENSP00000434992 ; ENSG00000236649 .
ENST00000490624 ; ENSP00000433323 ; ENSG00000168452 .
ENST00000493809 ; ENSP00000436963 ; ENSG00000227600 .
ENST00000496937 ; ENSP00000432964 ; ENSG00000231618 .
ENST00000525601 ; ENSP00000433696 ; ENSG00000227600 .
ENST00000527704 ; ENSP00000433061 ; ENSG00000227600 .
ENST00000546871 ; ENSP00000448392 ; ENSG00000206329 .
ENST00000547309 ; ENSP00000448877 ; ENSG00000227600 .
ENST00000547565 ; ENSP00000448120 ; ENSG00000236649 .
ENST00000548089 ; ENSP00000448456 ; ENSG00000231618 .
ENST00000549544 ; ENSP00000447998 ; ENSG00000168452 .
ENST00000550796 ; ENSP00000447926 ; ENSG00000236649 .
ENST00000551222 ; ENSP00000447973 ; ENSG00000231618 .
ENST00000552076 ; ENSP00000448072 ; ENSG00000227600 .
ENST00000552922 ; ENSP00000447950 ; ENSG00000168452 .
GeneIDi 9374.
KEGGi hsa:9374.
UCSCi uc003nzx.3. human. [Q9UMR5-1 ]
uc010jtu.1. human. [Q9UMR5-2 ]

Organism-specific databases

CTDi 9374.
GeneCardsi GC06P032122.
GC06Pi32132.
GC06Pj32069.
GC06Pk32096.
GC06Pl32160.
GC06Pm32197.
GC06Pn32078.
GC06Po32128.
HGNCi HGNC:9326. PPT2.
HPAi HPA000414.
MIMi 603298. gene.
neXtProti NX_Q9UMR5.
PharmGKBi PA33689.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1075.
HOVERGENi HBG019159.
InParanoidi Q9UMR5.
KOi K01074.
OMAi VPWISEL.
PhylomeDBi Q9UMR5.
TreeFami TF323926.

Miscellaneous databases

EvolutionaryTracei Q9UMR5.
GeneWikii PPT2.
GenomeRNAii 9374.
NextBioi 35116.
PROi Q9UMR5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UMR5.
Bgeei Q9UMR5.
Genevestigatori Q9UMR5.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
[Graphical view ]
Pfami PF02089. Palm_thioest. 1 hit.
[Graphical view ]
PRINTSi PR00414. PPTHIESTRASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 124 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

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