Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01144
Entry Name
UniProt Accession
Theoretical PI
4.93
Molecular Weight
22148.77
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
DnaJ homolog subfamily C member 5
Protein Synonyms/Alias
Cysteine string protein; CSP;
Gene Name
DNAJC5
Gene Synonyms/Alias
CSP;
Created Date
14-AUG-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
113
Canonical
AKALFVFCGLLTCCY
[2]
S-Palmitoylation
118
Canonical
VFCGLLTCCYCCCCL
[1]
S-Palmitoylation
119
Canonical
FCGLLTCCYCCCCLC
[1]
S-Palmitoylation
121
Canonical
GLLTCCYCCCCLCCC
[1]
S-Palmitoylation
122
Canonical
LLTCCYCCCCLCCCF
[1]
S-Palmitoylation
123
Canonical
LTCCYCCCCLCCCFN
[1]
S-Palmitoylation
124
Canonical
TCCYCCCCLCCCFNC
[1]
S-Palmitoylation
126
Canonical
CYCCCCLCCCFNCCC
[1]
S-Palmitoylation
127
Canonical
YCCCCLCCCFNCCCG
[1]
S-Palmitoylation
128
Canonical
CCCCLCCCFNCCCGK
[1]
S-Palmitoylation
131
Canonical
CLCCCFNCCCGKCKP
[1]
S-Palmitoylation
132
Canonical
LCCCFNCCCGKCKPK
[1]
S-Palmitoylation
133
Canonical
CCCFNCCCGKCKPKA
[1]
S-Palmitoylation
136
Canonical
FNCCCGKCKPKAPEG
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Gundersen CB, Mastrogiacomo A, Faull K, Umbach JA. Extensive lipidation of aTorpedo cysteine string protein. J Biol Chem. 1994 Jul 29;269(30):19197-9. PubMedPMID: 8034679.[PMID:8034679]
[2] Zhang YQ, Chandra SS. Oligomerization of Cysteine String Protein alpha mutantscausing adult neuronal ceroid lipofuscinosis. Biochim Biophys Acta. 2014Nov;1842(11):2136-46. doi: 10.1016/j.bbadis.2014.07.009. Epub 2014 Jul 23. PubMedPMID: 25064588; PubMed Central PMCID: PMC4188699.[PMID:25064588]
Functional Description
May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity).
Sequence Annotation
Domain: 13 82 J.
Modified residue: 8 8 Phosphoserine.
Modified residue: 10 10 Phosphoserine.
Modified residue: 15 15 Phosphoserine.
Modified residue: 56 56 N6-acetyllysine.
Protein Length
198 AA.
Protein Sequence
(Canonical)
MADQRQRSLS TSGESLYHVL GLDKNATSDD IKKSYRKLAL KYHPDKNPDN PEAADKFKEI  60
NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF VFCGLLTCCY  120
CCCCLCCCFN CCCGKCKPKA PEGEETEFYV SPEDLEAQLQ SDEREATDTP IVIQPASATE  180
TTQLTADSHP SYHTDGFN                                                198
FASTA
(Canonical)
>LipidDB-9606-01144|Q9H3Z4
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEI
NNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVFCGLLTCCY
CCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATE
TTQLTADSHPSYHTDGFN
Gene Ontology
GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005739; C:mitochondrion; IDA:UniProt
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0008021; C:synaptic vesicle; IEA:Ensembl
GO:0008219; P:cell death; IEA:UniProtKB-KW
GO:0006887; P:exocytosis; NAS:ParkinsonsUK-UCL
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0007269; P:neurotransmitter secretion; TAS:Reactome
GO:0045055; P:regulated secretory pathway; TAS:ParkinsonsUK-UCL
GO:0007268; P:synaptic transmission; TAS:Reactome
GO:0016079; P:synaptic vesicle exocytosis; TAS:ParkinsonsUK-UCL
Interpro
InterPro; IPR001623; DnaJ_domain
InterPro; IPR018253; DnaJ_domain_CS
Pfam
Pfam; PF00226; DnaJ;
SMART
SMART; SM00271; DnaJ;
PROSITE
PROSITE; PS00636; DNAJ_1;
PROSITE; PS50076; DNAJ_2;
PRINTS
PRINTS; PR00625; JDOMAIN;