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Q13286 (CLN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Battenin
Alternative name(s):
Batten disease protein
Protein CLN3
Gene names
Name:CLN3
Synonyms:BTS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes. Ref.20

Subunit structure

Interacts with DCTN1 and KIF3A. Interacts with RAB7A and RILP. Ref.20

Subcellular location

Lysosome membrane; Multi-pass membrane protein. Late endosome Ref.10 Ref.13 Ref.14 Ref.20.

Post-translational modification

Highly glycosylated. Ref.13

Farnesylation is important for trafficking to lysosomes.

Involvement in disease

Ceroid lipofuscinosis, neuronal, 3 (CLN3) [MIM:204200]: 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 neuronal ceroid lipofuscinosis type 3.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the battenin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentEndosome
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Neurodegeneration
Neuronal ceroid lipofuscinosis
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
Lipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaction potential

Inferred from sequence or structural similarity. Source: UniProtKB

amyloid precursor protein catabolic process

Inferred from direct assay PubMed 10924275. Source: UniProtKB

arginine transport

Inferred from direct assay PubMed 16251196. Source: UniProtKB

associative learning

Inferred from sequence or structural similarity. Source: UniProtKB

autophagic vacuole fusion

Inferred from sequence or structural similarity. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular amino acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

ceramide metabolic process

Inferred from direct assay PubMed 15240864. Source: UniProtKB

cytosolic calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

galactosylceramide metabolic process

Inferred from mutant phenotype PubMed 15240864. Source: UniProtKB

globoside metabolic process

Inferred from mutant phenotype PubMed 15240864. Source: UniProtKB

glucosylceramide metabolic process

Inferred from mutant phenotype PubMed 15240864. Source: UniProtKB

ionotropic glutamate receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

lysosomal lumen acidification

Inferred from mutant phenotype PubMed 11722572. Source: UniProtKB

lysosomal lumen pH elevation

Inferred from direct assay PubMed 10924275. Source: UniProtKB

lysosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

macroautophagy

Non-traceable author statement PubMed 9949212. Source: UniProtKB

membrane organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15240864. Source: UniProtKB

negative regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of macroautophagy

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

neuromuscular process controlling balance

Inferred from sequence or structural similarity. Source: UniProtKB

neurotransmitter metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein catabolic process

Non-traceable author statement PubMed 10740217. Source: UniProtKB

protein folding

Traceable author statement PubMed 8980123. Source: ProtInc

protein processing

Inferred from sequence or structural similarity. Source: UniProtKB

receptor-mediated endocytosis

Inferred from mutant phenotype PubMed 15471887. Source: UniProtKB

sphingomyelin metabolic process

Inferred from mutant phenotype PubMed 15240864. Source: UniProtKB

vacuolar transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

vesicle transport along microtubule

Inferred from mutant phenotype Ref.20. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15240864. Source: UniProtKB

Golgi membrane

Inferred from direct assay PubMed 10191111PubMed 9949212. Source: UniProtKB

Golgi stack

Inferred from direct assay PubMed 15240864. Source: UniProtKB

autophagic vacuole

Inferred from sequence or structural similarity. Source: UniProtKB

caveola

Inferred from direct assay PubMed 15240864. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 10191116. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 15240864. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 10191111. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from direct assay PubMed 12706816. Source: UniProtKB

integral component of membrane

Inferred from direct assay PubMed 10191112. Source: UniProtKB

late endosome

Inferred from direct assay Ref.20. Source: UniProtKB

lysosomal membrane

Inferred from direct assay Ref.14PubMed 9384607. Source: UniProtKB

lysosome

Inferred from direct assay PubMed 10924275. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 15240864. Source: UniProtKB

mitochondrion

Traceable author statement PubMed 8980123. Source: ProtInc

neuron projection

Inferred from direct assay PubMed 10332042. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 10191116. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 10191116PubMed 15240864. Source: UniProtKB

synaptic vesicle

Inferred from direct assay PubMed 10332042PubMed 11590129. Source: UniProtKB

trans-Golgi network

Inferred from direct assay PubMed 15240864. Source: UniProtKB

   Molecular_functionunfolded protein binding

Traceable author statement PubMed 8980123. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q13286-1)

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: Q13286-2)

The sequence of this isoform differs from the canonical sequence as follows:
     178-225: Missing.
Isoform 3 (identifier: Q13286-3)

The sequence of this isoform differs from the canonical sequence as follows:
     280-302: GLLWYIVPLVVVYFAEYFINQGL → VRMMAG
Isoform 4 (identifier: Q13286-4)

The sequence of this isoform differs from the canonical sequence as follows:
     322-438: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 5 (identifier: Q13286-5)

The sequence of this isoform differs from the canonical sequence as follows:
     155-264: Missing.
     353-438: CLNLVFLLAD...PLHDFLCQLS → MESRSVAQAGM
Isoform 6 (identifier: Q13286-6)

The sequence of this isoform differs from the canonical sequence as follows:
     99-127: AVLLADILPTLVIKLLAPLGLHLLPYSPR → PPGSRQWDLCCWKLRPGCLFSFCGDQPVC
     128-226: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435Battenin
PRO_0000089857
Propeptide436 – 4383Removed in mature form Probable
PRO_0000422290

Regions

Transmembrane38 – 5821Helical; Potential
Transmembrane99 – 11921Helical; Potential
Transmembrane128 – 14821Helical; Potential
Transmembrane180 – 20021Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane278 – 29821Helical; Potential
Transmembrane358 – 37821Helical; Potential
Transmembrane407 – 42721Helical; Potential

Amino acid modifications

Modified residue121Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19
Modified residue141Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19
Modified residue4351Cysteine methyl ester Probable
Lipidation4351S-farnesyl cysteine Ref.13
Glycosylation711N-linked (GlcNAc...) Ref.13
Glycosylation851N-linked (GlcNAc...) Ref.13
Glycosylation3101N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence99 – 12729AVLLA…PYSPR → PPGSRQWDLCCWKLRPGCLF SFCGDQPVC in isoform 6.
VSP_047631
Alternative sequence128 – 22699Missing in isoform 6.
VSP_047632
Alternative sequence155 – 264110Missing in isoform 5.
VSP_004169
Alternative sequence178 – 22548Missing in isoform 2.
VSP_004166
Alternative sequence280 – 30223GLLWY…INQGL → VRMMAG in isoform 3.
VSP_004167
Alternative sequence322 – 438117Missing in isoform 4.
VSP_004168
Alternative sequence353 – 43886CLNLV…LCQLS → MESRSVAQAGM in isoform 5.
VSP_004170
Natural variant1011L → P in CLN3. Ref.21 Ref.23
VAR_005131
Natural variant1341C → R in CLN3. Ref.23
VAR_066892
Natural variant1701L → P in CLN3. Ref.21 Ref.23
VAR_005132
Natural variant1871G → A in CLN3. Ref.23
VAR_066893
Natural variant1891G → R in CLN3. Ref.23
VAR_066894
Natural variant2951E → K in CLN3; the mutant is located to vesicles clustered in a perinuclear region. Ref.20 Ref.21 Ref.22 Ref.23
VAR_005133
Natural variant3301V → F in CLN3. Ref.21
VAR_005134
Natural variant3341R → C in CLN3. Ref.21
VAR_005135
Natural variant3341R → H in CLN3. Ref.21 Ref.23
VAR_005136

Experimental info

Sequence conflict2591P → L in BAG35838. Ref.5

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: BE25E973CEEC4FD5

FASTA43847,623
        10         20         30         40         50         60 
MGGCAGSRRR FSDSEGEETV PEPRLPLLDH QGAHWKNAVG FWLLGLCNNF SYVVMLSAAH 

        70         80         90        100        110        120 
DILSHKRTSG NQSHVDPGPT PIPHNSSSRF DCNSVSTAAV LLADILPTLV IKLLAPLGLH 

       130        140        150        160        170        180 
LLPYSPRVLV SGICAAGSFV LVAFSHSVGT SLCGVVFASI SSGLGEVTFL SLTAFYPRAV 

       190        200        210        220        230        240 
ISWWSSGTGG AGLLGALSYL GLTQAGLSPQ QTLLSMLGIP ALLLASYFLL LTSPEAQDPG 

       250        260        270        280        290        300 
GEEEAESAAR QPLIRTEAPE SKPGSSSSLS LRERWTVFKG LLWYIVPLVV VYFAEYFINQ 

       310        320        330        340        350        360 
GLFELLFFWN TSLSHAQQYR WYQMLYQAGV FASRSSLRCC RIRFTWALAL LQCLNLVFLL 

       370        380        390        400        410        420 
ADVWFGFLPS IYLVFLIILY EGLLGGAAYV NTFHNIALET SDEHREFAMA ATCISDTLGI 

       430 
SLSGLLALPL HDFLCQLS 

« Hide

Isoform 2 [UniParc].

Checksum: 30722C86911C70C0
Show »

FASTA39042,829
Isoform 3 [UniParc].

Checksum: 503A97EDF8B72CC3
Show »

FASTA42145,570
Isoform 4 [UniParc].

Checksum: 482F021A8FF39B63
Show »

FASTA32134,569
Isoform 5 [UniParc].

Checksum: 5FFBAA4622A8DF52
Show »

FASTA25328,016
Isoform 6 [UniParc].

Checksum: DD2C9A3D0A6B022D
Show »

FASTA33937,969

References

« Hide 'large scale' references
[1]"Isolation of a novel gene underlying Batten disease, CLN3."
Lerner T.J., Boustany R.-M.N., Anderson J.W., D'Arigo K.L., Schlumpf K., Buckler A.J., Gusella J.F., Haines J.L., Kremmidiotis G., Lensink I.L., Sutherland G.R., Callen D.F., Taschner P.E.M., de Vos N., van Ommen G.B., Breuning M.H., Doggett N.A., Meincke L.J. expand/collapse author list , Liu Z., Goodwin L.A., Tesmer J.G., Mitchison H.M., O'Rawe A.M., Munroe P.B., Jarvela I.E., Gardiner M.R., Mole S.E.
Cell 82:949-957(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Genomic structure and complete nucleotide sequence of the Batten disease gene, CLN3."
Mitchison H.M., Munroe P.B., O'Rawe A.M., Taschner P.E.M., de Vos N., Kremmidiotis G., Lensink I., Munk A.C., D'Arigo K.L., Anderson J.W., Lerner T.J., Moyzis R.K., Callen D.F., Breuning M.H., Doggett N.A., Gardiner R.M., Mole S.E.
Genomics 40:346-350(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Unique alternative spliced transcripts associated with the 56 chromosome haplotype allele of the Batten disease gene, CLN3."
LaFauci G., Papini M., Pullarkat R., Rubenstein R.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6).
[4]"Characterization of alternatively spliced transcripts of the Batten disease CLN3 gene in human lymphoblastoid cell lines."
LaFauci G., Kaczmarski W., Papini M., Pullarkat R.K., Wisniewski K.E., Zhong N., Rubenstein R.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 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. 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].
Tissue: Cerebellum.
[6]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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).
Tissue: Lung.
[10]"Expression studies of CLN3 protein (battenin) in fusion with the green fluorescent protein in mammalian cells in vitro."
Golabek A.A., Kaczmarski W., Kida E., Kaczmarski A., Michalewski M.P., Wisniewski K.E.
Mol. Genet. Metab. 66:277-282(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"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).
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes."
Storch S., Pohl S., Quitsch A., Falley K., Braulke T.
Traffic 8:431-444(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-71 AND ASN-85, ISOPRENYLATION AT CYS-435.
[14]"Integral and associated lysosomal membrane proteins."
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.
Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Placenta.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments."
Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K., Neefjes J., Olkkonen V.M., Jalanko A.
Cell. Mol. Life Sci. 69:2075-2089(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANTEROGRADE TRANSPORT OF LATE ENDOSOMES AND LYSOSOMES, SUBCELLULAR LOCATION, INTERACTION WITH DCTN1; KIF3A; RAB7A AND RILP, CHARACTERIZATION OF VARIANT CLN3 LYS-295.
[21]"Spectrum of mutations in the Batten disease gene, CLN3."
Munroe P.B., Mitchison H.M., O'Rawe A.M., Anderson J.W., Boustany R.-M.N., Lerner T.J., Taschner P.E.M., de Vos N., Breuning M.H., Gardiner R.M., Mole S.E.
Am. J. Hum. Genet. 61:310-316(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN3 PRO-101; PRO-170; LYS-295; PHE-330; CYS-334 AND HIS-334.
[22]"Molecular screening of Batten disease: identification of a missense mutation (E295K) in the CLN3 gene."
Zhong N., Wisniewski K.E., Kaczmarski A.L., Ju W., Xu W.M., Xu W.W., McLendon L., Liu B., Kaczmarski W., Brooks S.S., Brown W.T.
Hum. Genet. 102:57-62(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLN3 LYS-295.
[23]"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 CLN3 PRO-101; ARG-134; PRO-170; ALA-187; ARG-189; LYS-295 AND HIS-334.
+Additional computationally mapped references.

Web resources

NCL CLN3

Neural Ceroid Lipofuscinoses mutation db

Mutations of the CLN3 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32680 mRNA. Translation: AAB51075.1.
X99832 Genomic DNA. Translation: CAA68148.1.
AF015593 mRNA. Translation: AAD01555.1.
AF015598 mRNA. Translation: AAD01560.1.
AF077956 mRNA. Translation: AAD51478.1.
AF077957 mRNA. Translation: AAD51479.1.
AF077958 mRNA. Translation: AAD51480.1.
AF077959 mRNA. Translation: AAD51481.1.
AF077961 mRNA. Translation: AAD51483.1.
AF077962 mRNA. Translation: AAD51484.1.
AF077966 mRNA. Translation: AAD51488.1.
AF077960 mRNA. Translation: AAD51482.1.
AF077963 mRNA. Translation: AAD51485.1.
AF077965 mRNA. Translation: AAD51487.1.
AF077971 mRNA. Translation: AAD51493.1.
AF077972 mRNA. Translation: AAD51494.1.
AF078169 mRNA. Translation: AAD48543.1.
AK313002 mRNA. Translation: BAG35838.1.
AC002425 Genomic DNA. Translation: AAC05337.1.
AC002544 Genomic DNA. Translation: AAC27430.1.
AC138894 Genomic DNA. No translation available.
CH471279 Genomic DNA. Translation: EAW52281.1.
CH471279 Genomic DNA. Translation: EAW52286.1.
BC002394 mRNA. Translation: AAH02394.1.
BC004433 mRNA. Translation: AAH04433.1.
PIRA57219.
RefSeqNP_000077.1. NM_000086.2.
NP_001035897.1. NM_001042432.1.
UniGeneHs.534667.

3D structure databases

ProteinModelPortalQ13286.
SMRQ13286. Positions 98-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107612. 89 interactions.
IntActQ13286. 36 interactions.
STRING9606.ENSP00000353073.

PTM databases

PhosphoSiteQ13286.

Polymorphism databases

DMDM2498243.

Proteomic databases

PaxDbQ13286.
PRIDEQ13286.

Protocols and materials databases

DNASU1201.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354630; ENSP00000346650; ENSG00000188603. [Q13286-3]
ENST00000355477; ENSP00000347660; ENSG00000188603. [Q13286-2]
ENST00000357076; ENSP00000349586; ENSG00000188603. [Q13286-5]
ENST00000357806; ENSP00000350457; ENSG00000188603. [Q13286-6]
ENST00000359984; ENSP00000353073; ENSG00000188603. [Q13286-1]
ENST00000360019; ENSP00000353116; ENSG00000188603. [Q13286-1]
ENST00000565316; ENSP00000456117; ENSG00000188603. [Q13286-3]
ENST00000569030; ENSP00000454680; ENSG00000188603. [Q13286-5]
ENST00000569430; ENSP00000454229; ENSG00000188603. [Q13286-1]
GeneID1201.
KEGGhsa:1201.
UCSCuc002dpm.3. human. [Q13286-1]
uc002dpq.1. human. [Q13286-2]
uc010bye.1. human. [Q13286-3]

Organism-specific databases

CTD1201.
GeneCardsGC16M028488.
HGNCHGNC:2074. CLN3.
MIM204200. phenotype.
607042. gene.
neXtProtNX_Q13286.
Orphanet228346. CLN3 disease.
PharmGKBPA26601.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325947.
HOVERGENHBG017297.
InParanoidQ13286.
KOK12389.
OMANYGYVVM.
OrthoDBEOG7N8ZZQ.
PhylomeDBQ13286.
TreeFamTF314055.

Gene expression databases

BgeeQ13286.
CleanExHS_CLN3.
GenevestigatorQ13286.

Family and domain databases

InterProIPR003492. Battenin_disease_Cln3.
IPR018460. Battenin_disease_Cln3_subgr.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PANTHERPTHR10981. PTHR10981. 1 hit.
PfamPF02487. CLN3. 1 hit.
[Graphical view]
PIRSFPIRSF015974. CLN3_BTN1. 1 hit.
PRINTSPR01315. BATTENIN.
SUPFAMSSF103473. SSF103473. 1 hit.
ProtoNetSearch...

Other

GeneWikiCLN3.
GenomeRNAi1201.
NextBio4959.
PROQ13286.
SOURCESearch...

Entry information

Entry nameCLN3_HUMAN
AccessionPrimary (citable) accession number: Q13286
Secondary accession number(s): B2R7J1 expand/collapse secondary AC list , O00668, O95089, Q549S9, Q9UP09, Q9UP11, Q9UP12, Q9UP13, Q9UP14
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 135 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

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 16

Human chromosome 16: entries, gene names and cross-references to MIM