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P50897 (PPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length306 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 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

Ceroid lipofuscinosis, neuronal, 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 processSensory transduction
Vision
   Cellular componentLysosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Neuronal ceroid lipofuscinosis
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

apoptotic DNA fragmentation

Inferred from direct assay PubMed 15929065. Source: UniProtKB

associative learning

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

cellular protein catabolic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

lipid catabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

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 apoptotic process

Inferred from direct assay 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

nervous system development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

neuron development

Traceable author statement PubMed 11136716. Source: UniProtKB

neurotransmitter secretion

Inferred from electronic annotation. Source: Ensembl

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 catabolic process

Non-traceable author statement PubMed 10740217. 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: Ensembl

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_componentGolgi 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: Ensembl

extracellular region

Inferred from direct assay PubMed 8895569. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

nucleus

Inferred from direct assay PubMed 10992246. Source: UniProtKB

synaptic vesicle

Inferred from direct assay PubMed 12483688. Source: UniProtKB

   Molecular_functionpalmitoyl-(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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 306279Palmitoyl-protein thioesterase 1
PRO_0000025550

Sites

Active site1151 By similarity
Active site2331 By similarity
Active site2891 By similarity

Amino acid modifications

Glycosylation1971N-linked (GlcNAc...) Ref.11
Glycosylation2121N-linked (GlcNAc...) Ref.11
Glycosylation2321N-linked (GlcNAc...) Ref.10 Ref.11
Disulfide bond45 ↔ 46 Ref.13
Disulfide bond96 ↔ 128 Ref.13
Disulfide bond152 ↔ 160 Ref.13

Natural variations

Alternative sequence42 – 144103Missing in isoform 2.
VSP_042033
Natural variant381W → C in CLN1. Ref.17
VAR_058434
Natural variant391H → Q in CLN1.
VAR_005548
Natural variant421G → E in CLN1.
VAR_005549
Natural variant451C → Y in CLN1. Ref.18
VAR_066874
Natural variant751T → P in CLN1; juvenile onset. Ref.14 Ref.18
VAR_005550
Natural variant791D → G in CLN1; juvenile onset. Ref.14 Ref.18
VAR_005551
Natural variant1081G → R in CLN1; onset in adulthood. Ref.16 Ref.18
VAR_018511
Natural variant1091Y → D in CLN1; late infantile form. Ref.18
VAR_005552
Natural variant1221R → W in CLN1; seems to result in intracellular accumulation of the enzyme. Ref.1
Corresponds to variant rs137852695 [ dbSNP | Ensembl ].
VAR_005553
Natural variant1341I → T. Ref.15
Corresponds to variant rs1800205 [ dbSNP | Ensembl ].
VAR_005554
Natural variant1381S → L in CLN1. Ref.18
VAR_066875
Natural variant1521C → Y in CLN1. Ref.18
VAR_066876
Natural variant1771Q → E in CLN1; late infantile form. Ref.18
VAR_005555
Natural variant1811V → L in CLN1.
VAR_005556
Natural variant1811V → M in CLN1; late infantile form. Ref.18
VAR_005557
Natural variant1871H → R in CLN1. Ref.18
VAR_066877
Natural variant1891P → R in CLN1. Ref.18
VAR_066878
Natural variant2191L → Q in CLN1; juvenile onset. Ref.14 Ref.18
VAR_005558
Natural variant2221L → P in CLN1; late infantile form. Ref.18
VAR_066879
Natural variant2281V → G in CLN1. Ref.18
VAR_066880
Natural variant2471Y → H in CLN1. Ref.18
VAR_005559
Natural variant2501G → V in CLN1. Ref.18
VAR_005560
Natural variant2961W → R in CLN1. Ref.18
VAR_066881
Natural variant3051L → P in CLN1. Ref.18
VAR_066882

Secondary structure

........................................................ 306
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: 69F8083FD1C15E92

FASTA30634,193
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C73DB3FEBDEC8F32
Show »

FASTA20323,094

References

« Hide '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. 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] (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. expand/collapse author list , 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. 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 (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.
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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42809 Genomic DNA. Translation: AAA85337.1.
U44772 mRNA. Translation: AAB06236.1.
AF022211 expand/collapse EMBL AC list , 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.
CCDSCCDS44119.1. [P50897-2]
CCDS447.1. [P50897-1]
PIRI58097.
RefSeqNP_000301.1. NM_000310.3. [P50897-1]
NP_001136076.1. NM_001142604.1. [P50897-2]
UniGeneHs.3873.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GROX-ray2.53A/B22-306[»]
ProteinModelPortalP50897.
SMRP50897. Positions 30-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111530. 12 interactions.
IntActP50897. 6 interactions.
MINTMINT-3018663.
STRING9606.ENSP00000394863.

Chemistry

ChEMBLCHEMBL2331051.

PTM databases

PhosphoSiteP50897.

Polymorphism databases

DMDM1709747.

Proteomic databases

MaxQBP50897.
PaxDbP50897.
PRIDEP50897.

Protocols and materials databases

DNASU5538.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000433473; ENSP00000394863; ENSG00000131238. [P50897-1]
ENST00000449045; ENSP00000392293; ENSG00000131238. [P50897-2]
ENST00000529905; ENSP00000432053; ENSG00000131238. [P50897-1]
GeneID5538.
KEGGhsa:5538.
UCSCuc001cfb.2. human. [P50897-1]
uc010ojg.1. human. [P50897-2]

Organism-specific databases

CTD5538.
GeneCardsGC01M040567.
GeneReviewsPPT1.
HGNCHGNC:9325. PPT1.
HPAHPA021546.
MIM256730. phenotype.
600722. gene.
neXtProtNX_P50897.
Orphanet228329. CLN1 disease.
PharmGKBPA33688.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1075.
HOGENOMHOG000199232.
HOVERGENHBG018186.
InParanoidP50897.
KOK01074.
OMALQETTLY.
OrthoDBEOG776SQJ.
PhylomeDBP50897.
TreeFamTF323926.

Enzyme and pathway databases

BRENDA3.1.2.22. 2681.

Gene expression databases

ArrayExpressP50897.
BgeeP50897.
CleanExHS_PPT1.
GenevestigatorP50897.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002472. Palm_thioest.
[Graphical view]
PfamPF02089. Palm_thioest. 1 hit.
[Graphical view]
PRINTSPR00414. PPTHIESTRASE.
SUPFAMSSF53474. SSF53474. 1 hit.
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Other

ChiTaRSPPT1. human.
EvolutionaryTraceP50897.
GeneWikiPPT1.
GenomeRNAi5538.
NextBio21454.
PROP50897.
SOURCESearch...

Entry information

Entry namePPT1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 146 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM