P50897 (PPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Palmitoyl-protein thioesterase 1
Short name=PPT-1
EC=3.1.2.22

Alternative name(s):
Palmitoyl-protein hydrolase 1

Gene names

Name:	PPT1
Synonyms:	PPT

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	306 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 such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
Catalytic activity	Palmitoyl-[protein] + H2O = palmitate + [protein].
Subcellular location	Lysosome.
Involvement in disease	Neuronal ceroid lipofuscinosis 1 (CLN1) [MIM:256730]: A form of neuronal ceroid lipofuscinosis with variable age at onset. Infantile, late-infantile, juvenile, and adult onset have been reported. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN1 is referred to as granular osmiophilic deposits (GROD). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the palmitoyl-protein thioesterase family.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Neurodegeneration Neuronal ceroid lipofuscinosis
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from electronic annotation. Source: Compara apoptotic DNA fragmentation Inferred from direct assay PubMed 15929065. Source: UniProtKB associative learning Inferred from electronic annotation. Source: Compara brain development Inferred from mutant phenotype Ref.1. Source: UniProtKB cellular protein catabolic process Inferred from electronic annotation. Source: Compara cofactor metabolic process Inferred from mutant phenotype PubMed 16542649. Source: UniProtKB cofactor transport Inferred from mutant phenotype PubMed 16542649. Source: UniProtKB grooming behavior Inferred from electronic annotation. Source: Compara lysosomal lumen acidification Inferred from mutant phenotype PubMed 11722572. Source: UniProtKB membrane raft organization Inferred from mutant phenotype PubMed 15929065. Source: UniProtKB negative regulation of cell growth Inferred from mutant phenotype PubMed 10737604. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 10737604PubMed 11020216. Source: UniProtKB neuron development Traceable author statement PubMed 11136716. Source: UniProtKB neurotransmitter secretion Inferred from electronic annotation. Source: Compara pinocytosis Inferred from mutant phenotype PubMed 16542649. Source: MGI positive regulation of pinocytosis Inferred from mutant phenotype PubMed 16542649. Source: UniProtKB positive regulation of receptor-mediated endocytosis Inferred from mutant phenotype PubMed 16542649. Source: UniProtKB protein depalmitoylation Inferred from direct assay PubMed 10658183PubMed 10737604. Source: UniProtKB protein transport Inferred from mutant phenotype PubMed 10737604. Source: UniProtKB receptor-mediated endocytosis Inferred from mutant phenotype PubMed 16542649. Source: MGI regulation of phospholipase A2 activity Inferred from electronic annotation. Source: Compara regulation of synapse structure and activity Non-traceable author statement PubMed 11136716. Source: UniProtKB sphingolipid catabolic process Traceable author statement PubMed 16542649. Source: UniProtKB visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay Ref.1. Source: UniProtKB axon Inferred from direct assay PubMed 12483688. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from electronic annotation. Source: Compara extracellular region Inferred from direct assay PubMed 8895569. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara lysosome Inferred from direct assay PubMed 11020216PubMed 8895569. Source: UniProtKB membrane raft Inferred from direct assay PubMed 15929065. Source: UniProtKB neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 10992246. Source: UniProtKB synaptic vesicle Inferred from direct assay PubMed 12483688. Source: UniProtKB
Molecular_function	palmitoyl-(protein) hydrolase activity Inferred from direct assay PubMed 10658183PubMed 10737604. Source: UniProtKB palmitoyl-CoA hydrolase activity Inferred from direct assay PubMed 10658183. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P50897-1)

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: P50897-2)

The sequence of this isoform differs from the canonical sequence as follows:
     42-144: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

By similarity

Chain

28 – 306

279

Palmitoyl-protein thioesterase 1

PRO_0000025550

Sites

Active site

115

1

By similarity

Active site

233

1

By similarity

Active site

289

1

By similarity

Amino acid modifications

Glycosylation

197

1

N-linked (GlcNAc...) Ref.11

Glycosylation

212

1

N-linked (GlcNAc...) Ref.11

Glycosylation

232

1

N-linked (GlcNAc...) Ref.10 Ref.11

Disulfide bond

45 ↔ 46

Ref.13

Disulfide bond

96 ↔ 128

Ref.13

Disulfide bond

152 ↔ 160

Ref.13

Natural variations

Alternative sequence

42 – 144

103

Missing in isoform 2.

VSP_042033

Natural variant

38

1

W → C in CLN1. Ref.17

VAR_058434

Natural variant

39

1

H → Q in CLN1.

VAR_005548

Natural variant

42

1

G → E in CLN1.

VAR_005549

Natural variant

45

1

C → Y in CLN1. Ref.18

VAR_066874

Natural variant

75

1

T → P in CLN1; juvenile onset. Ref.14 Ref.18

VAR_005550

Natural variant

79

1

D → G in CLN1; juvenile onset. Ref.14 Ref.18

VAR_005551

Natural variant

108

1

G → R in CLN1; onset in adulthood. Ref.16 Ref.18

VAR_018511

Natural variant

109

1

Y → D in CLN1; late infantile form. Ref.18

VAR_005552

Natural variant

122

1

R → W in CLN1; seems to result in intracellular accumulation of the enzyme. Ref.1

VAR_005553

Natural variant

134

1

I → T. Ref.15
Corresponds to variant rs1800205 [ dbSNP | Ensembl ].

VAR_005554

Natural variant

138

1

S → L in CLN1. Ref.18

VAR_066875

Natural variant

152

1

C → Y in CLN1. Ref.18

VAR_066876

Natural variant

177

1

Q → E in CLN1; late infantile form. Ref.18

VAR_005555

Natural variant

181

1

V → L in CLN1.

VAR_005556

Natural variant

181

1

V → M in CLN1; late infantile form. Ref.18

VAR_005557

Natural variant

187

1

H → R in CLN1. Ref.18

VAR_066877

Natural variant

189

1

P → R in CLN1. Ref.18

VAR_066878

Natural variant

219

1

L → Q in CLN1; juvenile onset. Ref.14 Ref.18

VAR_005558

Natural variant

222

1

L → P in CLN1; late infantile form. Ref.18

VAR_066879

Natural variant

228

1

V → G in CLN1. Ref.18

VAR_066880

Natural variant

247

1

Y → H in CLN1. Ref.18

VAR_005559

Natural variant

250

1

G → V in CLN1. Ref.18

VAR_005560

Natural variant

296

1

W → R in CLN1. Ref.18

VAR_066881

Natural variant

305

1

L → P in CLN1. Ref.18

VAR_066882

Secondary structure

1

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306

Helix Strand Turn

Details...

Beta strand

35 – 38

4

Turn

48 – 50

3

Helix

51 – 61

11

Beta strand

67 – 69

3

Beta strand

73 – 75

3

Helix

76 – 85

10

Helix

88 – 101

14

Helix

103 – 105

3

Beta strand

109 – 114

6

Helix

116 – 127

12

Beta strand

133 – 140

8

Beta strand

153 – 155

3

Helix

157 – 170

14

Helix

174 – 177

4

Helix

181 – 185

5

Beta strand

189 – 191

3

Helix

192 – 198

7

Helix

202 – 205

4

Beta strand

208 – 210

3

Helix

213 – 220

8

Beta strand

223 – 230

8

Beta strand

234 – 238

5

Helix

239 – 243

5

Helix

258 – 260

3

Helix

262 – 265

4

Beta strand

268 – 270

3

Helix

271 – 276

6

Beta strand

280 – 288

9

Helix

294 – 300

7

Helix

302 – 305

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 69F8083FD1C15E92	FASTA	306	34,193
	10 20 30 40 50 60 MASPGCLWLL AVALLPWTCA SRALQHLDPP APLPLVIWHG MGDSCCNPLS MGAIKKMVEK 70 80 90 100 110 120 KIPGIYVLSL EIGKTLMEDV ENSFFLNVNS QVTTVCQALA KDPKLQQGYN AMGFSQGGQF 130 140 150 160 170 180 LRAVAQRCPS PPMINLISVG GQHQGVFGLP RCPGESSHIC DFIRKTLNAG AYSKVVQERL 190 200 210 220 230 240 VQAEYWHDPI KEDVYRNHSI FLADINQERG INESYKKNLM ALKKFVMVKF LNDSIVDPVD 250 260 270 280 290 300 SEWFGFYRSG QAKETIPLQE TSLYTQDRLG LKEMDNAGQL VFLATEGDHL QLSEEWFYAH IIPFLG
	Isoform 2 [UniParc]. Checksum: C73DB3FEBDEC8F32	FASTA	203	23,094
	10 20 30 40 50 60 MASPGCLWLL AVALLPWTCA SRALQHLDPP APLPLVIWHG MGVFGLPRCP GESSHICDFI 70 80 90 100 110 120 RKTLNAGAYS KVVQERLVQA EYWHDPIKED VYRNHSIFLA DINQERGINE SYKKNLMALK 130 140 150 160 170 180 KFVMVKFLND SIVDPVDSEW FGFYRSGQAK ETIPLQETSL YTQDRLGLKE MDNAGQLVFL 190 200 ATEGDHLQLS EEWFYAHIIP FLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis." Vesa J., Hellsten E., Verkruyse L.A., Camp L.A., Rapola J., Santavuori P., Hofmann S.L., Peltonen L. Nature 376:584-587(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT CLN1 TRP-122. Tissue: Brain.
[2]	"Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis." Crews C.M., Lane W.S., Schreiber S.L. Proc. Natl. Acad. Sci. U.S.A. 93:4316-4319(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis." Schriner J.E., Yi W., Hofmann S.L. Genomics 34:317-322(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Cerebellum and Testis.
[5]	"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).
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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). Tissue: Prostate.
[9]	"Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase." Lu J.-Y., Verkruyse L.A., Hofmann S.L. Proc. Natl. Acad. Sci. U.S.A. 93:10046-10050(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-232.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197; ASN-212 AND ASN-232, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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].
[13]	"Human palmitoyl-protein thioesterase 1." Structural genomics consortium (SGC) Submitted (APR-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 22-306, DISULFIDE BONDS.
[14]	"Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits." Mitchison H.M., Hofmann S.L., Becerra C.H.R., Munroe P.B., Lake B.D., Crow Y.J., Stephenson J.B.P., Williams R.E., Hofman I.L., Taschner P.E.M., Martin J.-J., Philippart M., Andermann E., Andermann F., Mole S.E., Gardiner R.M., O'Rawe A.M. Hum. Mol. Genet. 7:291-297(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CLN1 PRO-75; GLY-79 AND GLN-219.
[15]	"Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S." Das A.K., Becerra C.H.R., Yi W., Lu J.-Y., Siakotos A.N., Wisniewski K.E., Hofmann S.L. J. Clin. Invest. 102:361-370(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CLN1, VARIANT THR-134.
[16]	"Adult neuronal ceroid lipofuscinosis with palmitoyl-protein thioesterase deficiency: first adult-onset patients of a childhood disease." van Diggelen O.P., Thobois S., Tilikete C., Zabot M.-T., Keulemans J.L.M., van Bunderen P.A., Taschner P.E.M., Losekoot M., Voznyi Y.V. Ann. Neurol. 50:269-272(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CLN1 ARG-108.
[17]	"Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis." Kousi M., Siintola E., Dvorakova L., Vlaskova H., Turnbull J., Topcu M., Yuksel D., Gokben S., Minassian B.A., Elleder M., Mole S.E., Lehesjoki A.-E. Brain 132:810-819(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CLN1 CYS-38.
[18]	"Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses." Kousi M., Lehesjoki A.E., Mole S.E. Hum. Mutat. 33:42-63(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CLN1 TYR-45; PRO-75; GLY-79; ARG-108; ASP-109; LEU-138; TYR-152; GLU-177; MET-181; ARG-187; ARG-189; GLN-219; PRO-222; GLY-228; HIS-247; VAL-250; ARG-296 AND PRO-305.
+	Additional computationally mapped references.

Web resources

NCL CLN1

Neural Ceroid Lipofuscinoses mutation db

Mutations of the PPT1 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42809 Genomic DNA. Translation: AAA85337.1.
U44772 mRNA. Translation: AAB06236.1.
AF022211 , AF022203, AF022204, AF022205, AF022206, AF022207, AF022208, AF022209, AF022210 Genomic DNA. Translation: AAB72224.1.
AK302232 mRNA. Translation: BAG63586.1.
AK312287 mRNA. Translation: BAG35214.1.
CR542053 mRNA. Translation: CAG46850.1.
AL512599 Genomic DNA. Translation: CAI11025.1.
CH471059 Genomic DNA. Translation: EAX07237.1.
CH471059 Genomic DNA. Translation: EAX07238.1.
BC008426 mRNA. Translation: AAH08426.1.

IPI

IPI00002412.

PIR

I58097.

RefSeq

NP_000301.1. NM_000310.3.
NP_001136076.1. NM_001142604.1.

UniGene

Hs.3873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GRO	X-ray	2.53	A/B	22-306	[»]

ProteinModelPortal

P50897.

ModBase

Search...

Protein-protein interaction databases

IntAct

P50897. 6 interactions.

STRING

9606.ENSP00000394863.

PTM databases

PhosphoSite

P50897.

Polymorphism databases

DMDM

1709747.

Proteomic databases

PaxDb

P50897.

PRIDE

P50897.

Protocols and materials databases

DNASU

5538.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000433473; ENSP00000394863; ENSG00000131238.
ENST00000449045; ENSP00000392293; ENSG00000131238.
ENST00000529905; ENSP00000432053; ENSG00000131238.

GeneID

5538.

KEGG

hsa:5538.

UCSC

uc001cfb.2. human.

Organism-specific databases

CTD

5538.

GeneCards

GC01M040567.

HGNC

HGNC:9325. PPT1.

HPA

HPA021546.

MIM

256730. phenotype.
600722. gene.

neXtProt

NX_P50897.

Orphanet

228329. CLN1 disease.

PharmGKB

PA33688.

GenAtlas

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Phylogenomic databases

eggNOG

COG1075.

HOGENOM

HOG000199232.

HOVERGEN

HBG018186.

InParanoid

P50897.

KO

K01074.

OMA

YKEDRLG.

OrthoDB

EOG4TB4C0.

PhylomeDB

P50897.

Enzyme and pathway databases

BRENDA

3.1.2.22. 2681.

Gene expression databases

ArrayExpress

P50897.

Bgee

P50897.

CleanEx

HS_PPT1.

Genevestigator

P50897.

GermOnline

ENSG00000131238. Homo sapiens.

Family and domain databases

InterPro

IPR002472. Palm_thioest.
[Graphical view]

Pfam

PF02089. Palm_thioest. 1 hit.
[Graphical view]

PRINTS

PR00414. PPTHIESTRASE.

ProtoNet

Search...

Other

ChiTaRS

PPT1. human.

EvolutionaryTrace

P50897.

GenomeRNAi

5538.

NextBio

21454.

SOURCE

Search...

Entry information

Entry name

PPT1_HUMAN

Accession

Primary (citable) accession number: P50897
Secondary accession number(s): B4DY24, Q6FGQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 132 of the entry and version 1 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.