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Protein Page:
CLN3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CLN3 Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes. Defects in CLN3 are the cause of neuronal ceroid lipofuscinosis type 3 (CLN3); also known as Batten disease. A form of neuronal ceroid lipofuscinosis. 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 hallmark of CLN3 is the ultrastructural pattern of lipopigment with a fingerprint profile, which can have 3 different appearances: pure within a lysosomal residual body; in conjunction with curvilinear or rectilinear profiles; and as a small component within large membrane-bound lysosomal vacuoles. The combination of fingerprint profiles within lysosomal vacuoles is a regular feature of blood lymphocytes from patients with CLN3. Belongs to the battenin family. 5 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, multi-pass; Membrane protein, integral; Mitochondrial; Apoptosis; Chaperone; Autophagy; Vesicle protein
Cellular Component: Golgi apparatus; Golgi stack; neuron projection; mitochondrion; lysosomal membrane; lysosome; endoplasmic reticulum; early endosome; integral to membrane; autophagic vacuole; trans-Golgi network; caveola; lipid raft; Golgi membrane; synaptic vesicle; late endosome; cytoplasm; plasma membrane; integral to endoplasmic reticulum membrane; nucleus
Molecular Function: protein binding; unfolded protein binding
Biological Process: cell death; sphingomyelin metabolic process; autophagic vacuole fusion; macroautophagy; glucosylceramide metabolic process; negative regulation of macroautophagy; amyloid precursor protein catabolic process; neurotransmitter metabolic process; vesicle transport along microtubule; protein catabolic process; negative regulation of neuron apoptosis; neuromuscular process controlling balance; associative learning; negative regulation of proteolysis; amino acid metabolic process; receptor-mediated endocytosis; regulation of action potential; cytosolic calcium ion homeostasis; vacuolar transport; arginine transport; globoside metabolic process; galactosylceramide metabolic process; lysosome organization and biogenesis; ionotropic glutamate receptor signaling pathway; negative regulation of catalytic activity; lysosomal lumen acidification; protein processing; ceramide metabolic process; negative regulation of apoptosis
Reference #:  Q13286 (UniProtKB)
Alt. Names/Synonyms: Batten disease protein; Battenin; BTS; ceroid-lipofuscinosis, neuronal 3; CLN3; JNCL; MGC102840; Protein CLN3
Gene Symbols: CLN3
Molecular weight: 47,623 Da
Basal Isoelectric point: 5.93  Predict pI for various phosphorylation states
Select Structure to View Below

CLN3

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 27 S12-p AGSRRRFsDsEGEEt
0 36 S14-p SRRRFsDsEGEEtVP
0 16 T19-p sDsEGEEtVPEPRLP
0 1 T80 SHVDPGPTPIPHNSS
0 1 T80-ga SHVDPGPtPIPHNSS
0 1 S87 tPIPHNSSSRFDCNS
0 1 S94 SSRFDCNSVSTAAVL
0 1 S96 RFDCNSVSTAAVLLA
0 14 K262-ub RTEAPESkPGSSssL
0 1 S267-p ESkPGSSssLSLRER
0 1 S268-p SkPGSSssLSLRERW
0 1 T276-p LSLRERWtVFKGLLW
  CLN3 iso6  
S12 AGSRRRFSDSEGEET
S14 SRRRFSDSEGEETVP
T19 SDSEGEETVPEPRLP
T80-p SHVDPGPtPIPHNSs
T80 SHVDPGPTPIPHNSs
S87-p tPIPHNSsSRFDCNs
S94-p sSRFDCNsVSTAPPG
S96 RFDCNsVSTAPPGSR
K163 RTEAPESKPGSSSSL
S168 ESKPGSSSSLSLRER
S169 SKPGSSSSLSLRERW
T177 LSLRERWTVFKGLLW
  mouse

 
E12 AGSWRRLEDsEREEt
S14-p SWRRLEDsEREEtDS
T19-p EDsEREEtDSEPQAP
T80 SHVEPGPTPTPHNSS
T80 SHVEPGPTPTPHNSS
S87 TPTPHNSSSRFDCNS
S94 SSRFDCNSIsTAAVL
S96-p RFDCNSIsTAAVLLA
K262 GTETPESKPGASWDL
W267 ESKPGASWDLSLQER
D268 SKPGASWDLSLQERW
T276 LSLQERWTVFKGLLW
  rat

 
E12 ESSWRRLEDSEREET
S14 SWRRLEDSEREETDS
T19 EDSEREETDSEPQTP
T80 SHVEPGPTPMPHNSS
T80 SHVEPGPTPMPHNSS
S87 TPMPHNSSSRFDCNS
S94 SSRFDCNSISTAAVL
S96 RFDCNSISTAAVLLA
R262 GTETPESRPGTSWDL
W267 ESRPGTSWDLSLQER
D268 SRPGTSWDLSLQERW
T276 LSLQERWTVFKGLLR
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