Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UMR5 (PPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal thioesterase PPT2

Short name=PPT-2
EC=3.1.2.-
Alternative name(s):
S-thioesterase G14
Gene names
Name:PPT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.12

Subcellular location

Lysosome Ref.1.

Tissue specificity

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

Sequence similarities

Belongs to the palmitoyl-protein thioesterase family.

Caution

Was originally (Ref.1) referred as a palmitoyl-protein thioesterase (palmitoyl-protein hydrolase).

Biophysicochemical properties

Kinetic parameters:

KM=67 µM for S-palmitoyl-CoA Ref.12

KM=37 µM for S-palmitoyl-N-acetylcysteamine

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 dependence:

Optimum pH is 7.0.

Sequence caution

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

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein modification process

Non-traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentlysosome

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionpalmitoyl-(protein) hydrolase activity

Non-traceable author statement Ref.2. Source: UniProtKB

thiolester hydrolase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UMR5-1)

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.
Isoform 2 (identifier: Q9UMR5-2)

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.
Isoform 3 (identifier: Q9UMR5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKSCGSM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 302275Lysosomal thioesterase PPT2
PRO_0000025554

Sites

Active site1111Nucleophile
Active site2281
Active site2831

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Ref.12
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Disulfide bond109 ↔ 117 Ref.12
Disulfide bond165 ↔ 176 Ref.12
Disulfide bond276 ↔ 296 Ref.12

Natural variations

Alternative sequence11M → MKSCGSM in isoform 3.
VSP_054027
Alternative sequence256 – 30045VYLRD…CIEPW → PARPTHQSELLLLRLVCLKP PRRKKPACRVQRQSESWGPG LSCA in isoform 2.
VSP_005188
Natural variant51C → W. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.13
Corresponds to variant rs3134604 [ dbSNP | Ensembl ].
VAR_027107
Natural variant341A → E. Ref.6 Ref.7 Ref.13
Corresponds to variant rs3096696 [ dbSNP | Ensembl ].
VAR_027108

Experimental info

Mutagenesis1111S → A: Abolishes enzymatic activity. Ref.12
Mutagenesis2281D → A: Abolishes enzymatic activity. Ref.12
Mutagenesis2831H → A: Abolishes enzymatic activity. Ref.12
Mutagenesis2871H → A: No effect on enzymatic activity. Ref.12
Sequence conflict1891L → P in CAG38577. Ref.4

Secondary structure

.................................................... 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: E242D677970B4BEA

FASTA30234,225
        10         20         30         40         50         60 
MLGLCGQRLP AAWVLLLLPF LPLLLLAAPA PHRASYKPVI VVHGLFDSSY SFRHLLEYIN 

        70         80         90        100        110        120 
ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMAK APQGVHLICY SQGGLVCRAL 

       130        140        150        160        170        180 
LSVMDDHNVD SFISLSSPQM GQYGDTDYLK WLFPTSMRSN LYRICYSPWG QEFSICNYWH 

       190        200        210        220        230        240 
DPHHDDLYLN ASSFLALING ERDHPNATVW RKNFLRVGHL VLIGGPDDGV ITPWQSSFFG 

       250        260        270        280        290        300 
FYDANETVLE MEEQLVYLRD SFGLKTLLAR GAIVRCPMAG ISHTAWHSNR TLYETCIEPW 


LS 

« Hide

Isoform 2 (I) [UniParc].

Checksum: 37EC25978B3FE96E
Show »

FASTA30134,055
Isoform 3 [UniParc].

Checksum: E83460052465B3A4
Show »

FASTA30834,819

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001191032.1. NM_001204103.1.
NP_005146.4. NM_005155.6.
NP_619731.2. NM_138717.2.
UniGeneHs.332138.
Hs.731888.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJAX-ray2.70A1-302[»]
ProteinModelPortalQ9UMR5.
SMRQ9UMR5. Positions 35-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114775. 27 interactions.
MINTMINT-4721124.

Chemistry

ChEMBLCHEMBL2189137.

Polymorphism databases

DMDM296453016.

Proteomic databases

PaxDbQ9UMR5.
PRIDEQ9UMR5.

Protocols and materials databases

DNASU9374.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324816; 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.
GeneID9374.
KEGGhsa:9374.
UCSCuc003nzx.3. human. [Q9UMR5-1]
uc010jtu.1. human. [Q9UMR5-2]

Organism-specific databases

CTD9374.
GeneCardsGC06P032122.
GC06Pi32132.
GC06Pj32069.
GC06Pk32096.
GC06Pl32160.
GC06Pm32197.
GC06Pn32078.
GC06Po32128.
HGNCHGNC:9326. PPT2.
HPAHPA000414.
MIM603298. gene.
neXtProtNX_Q9UMR5.
PharmGKBPA33689.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1075.
HOVERGENHBG019159.
InParanoidQ9UMR5.
KOK01074.
OMAQYINESH.
PhylomeDBQ9UMR5.
TreeFamTF323926.

Gene expression databases

ArrayExpressQ9UMR5.
BgeeQ9UMR5.
GenevestigatorQ9UMR5.

Family and domain databases

InterProIPR002472. Palm_thioest.
[Graphical view]
PfamPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSPR00414. PPTHIESTRASE.
ProtoNetSearch...

Other

EvolutionaryTraceQ9UMR5.
GeneWikiPPT2.
GenomeRNAi9374.
NextBio35116.
PROQ9UMR5.
SOURCESearch...

Entry information

Entry namePPT2_HUMAN
AccessionPrimary (citable) accession number: Q9UMR5
Secondary accession number(s): A2ABC9 expand/collapse secondary AC list , A2ABD1, A2ARM7, A2BFH7, A2BFH9, A2BFI2, A8K9L4, B0S868, G8JLE1, O14799, Q0P6K0, Q5JP13, Q5JP14, Q5JQF0, Q5SSX4, Q5SSX5, Q5SSX6, Q5STJ4, Q5STJ5, Q5STJ6, Q6FI80, Q99945
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 120 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM