Q9UMR5 (PPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysosomal thioesterase PPT2
Short name=PPT-2
EC=3.1.2.-

Alternative name(s):
S-thioesterase G14

Gene names

Name:

PPT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 AAB47495.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAB53659.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAG38577.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI17426.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI41763.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI41797.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAM24823.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAM25714.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAM26213.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAM26216.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ06588.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ09561.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ09617.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ10692.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	lysosome Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	palmitoyl-(protein) hydrolase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 302

275

Lysosomal thioesterase PPT2

PRO_0000025554

Sites

Active site

111

1

Nucleophile

Active site

228

1

Active site

283

1

Amino acid modifications

Glycosylation

60

1

N-linked (GlcNAc...) Potential

Glycosylation

190

1

N-linked (GlcNAc...) Ref.12

Glycosylation

206

1

N-linked (GlcNAc...) Potential

Glycosylation

245

1

N-linked (GlcNAc...) Potential

Glycosylation

289

1

N-linked (GlcNAc...) Potential

Disulfide bond

109 ↔ 117

Ref.12

Disulfide bond

165 ↔ 176

Ref.12

Disulfide bond

276 ↔ 296

Ref.12

Natural variations

Alternative sequence

256 – 300

45

VYLRD…CIEPW → PARPTHQSELLLLRLVCLKP PRRKKPACRVQRQSESWGPG LSCA in isoform 2.

VSP_005188

Natural variant

5

1

C → 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 variant

34

1

A → E. Ref.6 Ref.7 Ref.13
Corresponds to variant rs3096696 [ dbSNP | Ensembl ].

VAR_027108

Experimental info

Mutagenesis

111

1

S → A: Abolishes enzymatic activity. Ref.12

Mutagenesis

228

1

D → A: Abolishes enzymatic activity. Ref.12

Mutagenesis

283

1

H → A: Abolishes enzymatic activity. Ref.12

Mutagenesis

287

1

H → A: No effect on enzymatic activity. Ref.12

Sequence conflict

189

1

L → P in CAG38577. Ref.4

Secondary structure

1

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302

Helix Strand Turn

Details...

Beta strand

39 – 42

4

Helix

49 – 52

4

Helix

53 – 62

10

Beta strand

68 – 70

3

Helix

77 – 80

4

Helix

83 – 100

18

Beta strand

105 – 110

6

Helix

112 – 123

12

Beta strand

129 – 136

8

Helix

147 – 152

6

Helix

158 – 165

8

Helix

170 – 172

3

Helix

175 – 178

4

Helix

185 – 191

7

Helix

195 – 198

4

Helix

207 – 214

8

Beta strand

218 – 224

7

Beta strand

229 – 233

5

Helix

234 – 238

5

Helix

251 – 253

3

Helix

255 – 258

4

Turn

259 – 262

4

Helix

264 – 269

6

Beta strand

273 – 277

5

Turn

283 – 287

5

Helix

290 – 296

7

Helix

298 – 300

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 4. Checksum: E242D677970B4BEA	FASTA	302	34,225
	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
	Isoform 2 (I) [UniParc]. Checksum: 37EC25978B3FE96E	FASTA	301	34,055
	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 MEEQLPARPT HQSELLLLRL VCLKPPRRKK PACRVQRQSE SWGPGLSCAL S

References

	« Hide 'large scale' referencesShow '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. , 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 1), 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]	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. , 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. Different initiation.
CR533546 mRNA. Translation: CAG38577.1. Different initiation.
AK292729 mRNA. Translation: BAF85418.1.
U89336 Genomic DNA. Translation: AAB47495.1. Different initiation.
AL662828 Genomic DNA. Translation: CAI17424.1.
AL662828 Genomic DNA. Translation: CAI17426.2. Different initiation.
AL662828 Genomic DNA. Translation: CAM24823.1. Sequence problems.
AL662884 Genomic DNA. Translation: CAI18342.1.
AL662884 Genomic DNA. Translation: CAI18344.1.
AL662884 Genomic DNA. Translation: CAI41763.1. Different initiation.
AL845464 Genomic DNA. Translation: CAI41797.1. Different initiation.
AL845464 Genomic DNA. Translation: CAI41798.1.
AL845464 Genomic DNA. Translation: CAI41799.1.
AL662828 Genomic DNA. Translation: CAM24825.1.
AL845464 Genomic DNA. Translation: CAM25714.1. Sequence problems.
BX284686 Genomic DNA. Translation: CAM26213.1. Different initiation.
BX284686 Genomic DNA. Translation: CAM26215.1.
BX284686 Genomic DNA. Translation: CAM26216.1. Sequence problems.
BX284686 Genomic DNA. Translation: CAM26218.1.
BX927239 Genomic DNA. Translation: CAQ06588.1. Sequence problems.
BX927239 Genomic DNA. Translation: CAQ06590.1.
CR753803 Genomic DNA. Translation: CAQ09561.1. Sequence problems.
CR933878 Genomic DNA. Translation: CAQ09617.1. Sequence problems.
CR933878 Genomic DNA. Translation: CAQ09619.1.
CR812478 Genomic DNA. Translation: CAQ10692.1. Sequence problems.
CR812478 Genomic DNA. Translation: CAQ10694.1.
CH471081 Genomic DNA. Translation: EAX03597.1.
CH471081 Genomic DNA. Translation: EAX03591.1.
BC001355 mRNA. Translation: AAH01355.1.

IPI

IPI00021421.
IPI00216441.

RefSeq

NP_001191032.1. NM_001204103.1.
NP_005146.4. NM_005155.6.
NP_619731.2. NM_138717.2.

UniGene

Hs.332138.
Hs.731888.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PJA	X-ray	2.70	A	1-302	[»]

ProteinModelPortal

Q9UMR5.

SMR

Q9UMR5. Positions 35-302.

ModBase

Search...

Polymorphism databases

DMDM

296453016.

Proteomic databases

PaxDb

Q9UMR5.

PRIDE

Q9UMR5.

Protocols and materials databases

DNASU

9374.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324816; ENSP00000320528; ENSG00000221988.
ENST00000375137; ENSP00000364279; ENSG00000221988.
ENST00000375143; ENSP00000364285; ENSG00000221988.
ENST00000395523; ENSP00000378894; ENSG00000221988.
ENST00000399856; ENSP00000382748; ENSG00000206329.
ENST00000399859; ENSP00000382749; ENSG00000206329.
ENST00000399860; ENSP00000382750; ENSG00000206329.
ENST00000415972; ENSP00000408333; ENSG00000228116.
ENST00000420778; ENSP00000412827; ENSG00000168452.
ENST00000422988; ENSP00000406566; ENSG00000227600.
ENST00000424353; ENSP00000411007; ENSG00000231618.
ENST00000426325; ENSP00000387444; ENSG00000231618.
ENST00000427556; ENSP00000389930; ENSG00000168452.
ENST00000427642; ENSP00000409821; ENSG00000206329.
ENST00000433748; ENSP00000410001; ENSG00000206256.
ENST00000438385; ENSP00000395242; ENSG00000227600.
ENST00000440507; ENSP00000392885; ENSG00000231618.
ENST00000440533; ENSP00000403820; ENSG00000236649.
ENST00000442463; ENSP00000405631; ENSG00000227600.
ENST00000443321; ENSP00000392069; ENSG00000168452.
ENST00000445462; ENSP00000399879; ENSG00000236649.
ENST00000451460; ENSP00000404636; ENSG00000236649.
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.
ENST00000551482; ENSP00000448311; ENSG00000206329.
ENST00000552076; ENSP00000448072; ENSG00000227600.
ENST00000552922; ENSP00000447950; ENSG00000168452.

GeneID

9374.

KEGG

hsa:9374.

UCSC

uc003nzw.3. human.
uc010jtu.1. human.

Organism-specific databases

CTD

9374.

GeneCards

GC06P032122.

HGNC

HGNC:9326. PPT2.

HPA

HPA000414.

MIM

603298. gene.

neXtProt

NX_Q9UMR5.

PharmGKB

PA33689.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1075.

HOVERGEN

HBG019159.

InParanoid

Q9UMR5.

KO

K01074.

Gene expression databases

ArrayExpress

Q9UMR5.

Bgee

Q9UMR5.

Genevestigator

Q9UMR5.

Family and domain databases

InterPro

IPR002472. Palm_thioest.
[Graphical view]

Pfam

PF02089. Palm_thioest. 1 hit.
[Graphical view]

PRINTS

PR00414. PPTHIESTRASE.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9UMR5.

GenomeRNAi

9374.

NextBio

35116.

SOURCE

Search...

Entry information

Entry name

PPT2_HUMAN

Accession

Primary (citable) accession number: Q9UMR5
Secondary accession number(s): A2ABC9 , A2ABD1, A2ARM7, A2BFH7, A2BFH9, A2BFI2, A8K9L4, B0S868, 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 3, 2013
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.