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Q13286

- CLN3_HUMAN

UniProt

Q13286 - CLN3_HUMAN

Protein

Battenin

Gene

CLN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. action potential Source: UniProtKB
    2. amyloid precursor protein catabolic process Source: UniProtKB
    3. arginine transport Source: UniProtKB
    4. associative learning Source: UniProtKB
    5. autophagic vacuole fusion Source: UniProtKB
    6. cell death Source: UniProtKB-KW
    7. cellular amino acid metabolic process Source: UniProtKB
    8. ceramide metabolic process Source: UniProtKB
    9. cytosolic calcium ion homeostasis Source: UniProtKB
    10. galactosylceramide metabolic process Source: UniProtKB
    11. globoside metabolic process Source: UniProtKB
    12. glucosylceramide metabolic process Source: UniProtKB
    13. ionotropic glutamate receptor signaling pathway Source: UniProtKB
    14. lysosomal lumen acidification Source: UniProtKB
    15. lysosomal lumen pH elevation Source: UniProtKB
    16. lysosome organization Source: UniProtKB
    17. macroautophagy Source: UniProtKB
    18. membrane organization Source: UniProtKB
    19. negative regulation of apoptotic process Source: UniProtKB
    20. negative regulation of catalytic activity Source: UniProtKB
    21. negative regulation of macroautophagy Source: UniProtKB
    22. negative regulation of neuron apoptotic process Source: UniProtKB
    23. negative regulation of proteolysis Source: UniProtKB
    24. neuromuscular process controlling balance Source: UniProtKB
    25. neurotransmitter metabolic process Source: UniProtKB
    26. protein catabolic process Source: UniProtKB
    27. protein processing Source: UniProtKB
    28. receptor-mediated endocytosis Source: UniProtKB
    29. sphingomyelin metabolic process Source: UniProtKB
    30. vacuolar transport Source: RefGenome
    31. vesicle transport along microtubule Source: UniProtKB

    Keywords - Biological processi

    Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Battenin
    Alternative name(s):
    Batten disease protein
    Protein CLN3
    Gene namesi
    Name:CLN3
    Synonyms:BTS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:2074. CLN3.

    Subcellular locationi

    GO - Cellular componenti

    1. autophagic vacuole Source: UniProtKB
    2. caveola Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. early endosome Source: UniProtKB
    5. endoplasmic reticulum Source: UniProtKB
    6. Golgi apparatus Source: UniProtKB
    7. Golgi membrane Source: UniProtKB
    8. Golgi stack Source: UniProtKB
    9. integral component of endoplasmic reticulum membrane Source: UniProtKB
    10. integral component of membrane Source: UniProtKB
    11. late endosome Source: UniProtKB
    12. lysosomal membrane Source: UniProtKB
    13. lysosome Source: UniProtKB
    14. membrane raft Source: UniProtKB
    15. mitochondrion Source: ProtInc
    16. neuron projection Source: UniProtKB
    17. nucleus Source: UniProtKB
    18. plasma membrane Source: UniProtKB
    19. synaptic vesicle Source: UniProtKB
    20. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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 3.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011L → P in CLN3. 2 Publications
    VAR_005131
    Natural varianti134 – 1341C → R in CLN3. 1 Publication
    VAR_066892
    Natural varianti170 – 1701L → P in CLN3. 2 Publications
    VAR_005132
    Natural varianti187 – 1871G → A in CLN3. 1 Publication
    VAR_066893
    Natural varianti189 – 1891G → R in CLN3. 1 Publication
    VAR_066894
    Natural varianti295 – 2951E → K in CLN3; the mutant is located to vesicles clustered in a perinuclear region. 3 Publications
    VAR_005133
    Natural varianti330 – 3301V → F in CLN3. 1 Publication
    VAR_005134
    Natural varianti334 – 3341R → C in CLN3. 1 Publication
    VAR_005135
    Natural varianti334 – 3341R → H in CLN3. 2 Publications
    VAR_005136

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Neuronal ceroid lipofuscinosis

    Organism-specific databases

    MIMi204200. phenotype.
    Orphaneti228346. CLN3 disease.
    PharmGKBiPA26601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435BatteninPRO_0000089857Add
    BLAST
    Propeptidei436 – 4383Removed in mature formCuratedPRO_0000422290

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine4 Publications
    Modified residuei14 – 141Phosphoserine4 Publications
    Glycosylationi71 – 711N-linked (GlcNAc...)1 Publication
    Glycosylationi85 – 851N-linked (GlcNAc...)1 Publication
    Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
    Modified residuei435 – 4351Cysteine methyl esterCurated
    Lipidationi435 – 4351S-farnesyl cysteine1 Publication

    Post-translational modificationi

    Highly glycosylated.1 Publication
    Farnesylation is important for trafficking to lysosomes.

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiQ13286.
    PaxDbiQ13286.
    PRIDEiQ13286.

    PTM databases

    PhosphoSiteiQ13286.

    Expressioni

    Gene expression databases

    BgeeiQ13286.
    CleanExiHS_CLN3.
    GenevestigatoriQ13286.

    Interactioni

    Subunit structurei

    Interacts with DCTN1 and KIF3A. Interacts with RAB7A and RILP.1 Publication

    Protein-protein interaction databases

    BioGridi107612. 89 interactions.
    IntActiQ13286. 36 interactions.
    STRINGi9606.ENSP00000353073.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13286.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei38 – 5821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei99 – 11921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei128 – 14821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei180 – 20021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei212 – 23221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei278 – 29821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei358 – 37821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei407 – 42721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the battenin family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG325947.
    HOVERGENiHBG017297.
    InParanoidiQ13286.
    KOiK12389.
    OMAiNYGYVVM.
    OrthoDBiEOG7N8ZZQ.
    PhylomeDBiQ13286.
    TreeFamiTF314055.

    Family and domain databases

    InterProiIPR003492. Battenin_disease_Cln3.
    IPR018460. Battenin_disease_Cln3_subgr.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view]
    PANTHERiPTHR10981. PTHR10981. 1 hit.
    PfamiPF02487. CLN3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015974. CLN3_BTN1. 1 hit.
    PRINTSiPR01315. BATTENIN.
    SUPFAMiSSF103473. SSF103473. 1 hit.

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q13286-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGGCAGSRRR FSDSEGEETV PEPRLPLLDH QGAHWKNAVG FWLLGLCNNF    50
    SYVVMLSAAH DILSHKRTSG NQSHVDPGPT PIPHNSSSRF DCNSVSTAAV 100
    LLADILPTLV IKLLAPLGLH LLPYSPRVLV SGICAAGSFV LVAFSHSVGT 150
    SLCGVVFASI SSGLGEVTFL SLTAFYPRAV ISWWSSGTGG AGLLGALSYL 200
    GLTQAGLSPQ QTLLSMLGIP ALLLASYFLL LTSPEAQDPG GEEEAESAAR 250
    QPLIRTEAPE SKPGSSSSLS LRERWTVFKG LLWYIVPLVV VYFAEYFINQ 300
    GLFELLFFWN TSLSHAQQYR WYQMLYQAGV FASRSSLRCC RIRFTWALAL 350
    LQCLNLVFLL ADVWFGFLPS IYLVFLIILY EGLLGGAAYV NTFHNIALET 400
    SDEHREFAMA ATCISDTLGI SLSGLLALPL HDFLCQLS 438
    Length:438
    Mass (Da):47,623
    Last modified:November 1, 1996 - v1
    Checksum:iBE25E973CEEC4FD5
    GO
    Isoform 2 (identifier: Q13286-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-225: Missing.

    Show »
    Length:390
    Mass (Da):42,829
    Checksum:i30722C86911C70C0
    GO
    Isoform 3 (identifier: Q13286-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         280-302: GLLWYIVPLVVVYFAEYFINQGL → VRMMAG

    Show »
    Length:421
    Mass (Da):45,570
    Checksum:i503A97EDF8B72CC3
    GO
    Isoform 4 (identifier: Q13286-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:321
    Mass (Da):34,569
    Checksum:i482F021A8FF39B63
    GO
    Isoform 5 (identifier: Q13286-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-264: Missing.
         353-438: CLNLVFLLAD...PLHDFLCQLS → MESRSVAQAGM

    Show »
    Length:253
    Mass (Da):28,016
    Checksum:i5FFBAA4622A8DF52
    GO
    Isoform 6 (identifier: Q13286-6) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:339
    Mass (Da):37,969
    Checksum:iDD2C9A3D0A6B022D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti259 – 2591P → L in BAG35838. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011L → P in CLN3. 2 Publications
    VAR_005131
    Natural varianti134 – 1341C → R in CLN3. 1 Publication
    VAR_066892
    Natural varianti170 – 1701L → P in CLN3. 2 Publications
    VAR_005132
    Natural varianti187 – 1871G → A in CLN3. 1 Publication
    VAR_066893
    Natural varianti189 – 1891G → R in CLN3. 1 Publication
    VAR_066894
    Natural varianti295 – 2951E → K in CLN3; the mutant is located to vesicles clustered in a perinuclear region. 3 Publications
    VAR_005133
    Natural varianti330 – 3301V → F in CLN3. 1 Publication
    VAR_005134
    Natural varianti334 – 3341R → C in CLN3. 1 Publication
    VAR_005135
    Natural varianti334 – 3341R → H in CLN3. 2 Publications
    VAR_005136

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei99 – 12729AVLLA…PYSPR → PPGSRQWDLCCWKLRPGCLF SFCGDQPVC in isoform 6. 1 PublicationVSP_047631Add
    BLAST
    Alternative sequencei128 – 22699Missing in isoform 6. 1 PublicationVSP_047632Add
    BLAST
    Alternative sequencei155 – 264110Missing in isoform 5. 1 PublicationVSP_004169Add
    BLAST
    Alternative sequencei178 – 22548Missing in isoform 2. 1 PublicationVSP_004166Add
    BLAST
    Alternative sequencei280 – 30223GLLWY…INQGL → VRMMAG in isoform 3. 1 PublicationVSP_004167Add
    BLAST
    Alternative sequencei322 – 438117Missing in isoform 4. 1 PublicationVSP_004168Add
    BLAST
    Alternative sequencei353 – 43886CLNLV…LCQLS → MESRSVAQAGM in isoform 5. 1 PublicationVSP_004170Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10632.1. [Q13286-1]
    PIRiA57219.
    RefSeqiNP_000077.1. NM_000086.2. [Q13286-1]
    NP_001035897.1. NM_001042432.1. [Q13286-1]
    UniGeneiHs.534667.

    Genome annotation databases

    EnsembliENST00000355477; ENSP00000347660; ENSG00000188603. [Q13286-2]
    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]
    GeneIDi1201.
    KEGGihsa:1201.
    UCSCiuc002dpm.3. human. [Q13286-1]
    uc002dpq.1. human. [Q13286-2]
    uc002dps.1. human.
    uc010bye.1. human. [Q13286-3]

    Polymorphism databases

    DMDMi2498243.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NCL CLN3

    Neural Ceroid Lipofuscinoses mutation db

    Mutations of the CLN3 gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10632.1. [Q13286-1 ]
    PIRi A57219.
    RefSeqi NP_000077.1. NM_000086.2. [Q13286-1 ]
    NP_001035897.1. NM_001042432.1. [Q13286-1 ]
    UniGenei Hs.534667.

    3D structure databases

    ProteinModelPortali Q13286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107612. 89 interactions.
    IntActi Q13286. 36 interactions.
    STRINGi 9606.ENSP00000353073.

    PTM databases

    PhosphoSitei Q13286.

    Polymorphism databases

    DMDMi 2498243.

    Proteomic databases

    MaxQBi Q13286.
    PaxDbi Q13286.
    PRIDEi Q13286.

    Protocols and materials databases

    DNASUi 1201.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355477 ; ENSP00000347660 ; ENSG00000188603 . [Q13286-2 ]
    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 ]
    GeneIDi 1201.
    KEGGi hsa:1201.
    UCSCi uc002dpm.3. human. [Q13286-1 ]
    uc002dpq.1. human. [Q13286-2 ]
    uc002dps.1. human.
    uc010bye.1. human. [Q13286-3 ]

    Organism-specific databases

    CTDi 1201.
    GeneCardsi GC16M028488.
    GeneReviewsi CLN3.
    HGNCi HGNC:2074. CLN3.
    MIMi 204200. phenotype.
    607042. gene.
    neXtProti NX_Q13286.
    Orphaneti 228346. CLN3 disease.
    PharmGKBi PA26601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325947.
    HOVERGENi HBG017297.
    InParanoidi Q13286.
    KOi K12389.
    OMAi NYGYVVM.
    OrthoDBi EOG7N8ZZQ.
    PhylomeDBi Q13286.
    TreeFami TF314055.

    Miscellaneous databases

    GeneWikii CLN3.
    GenomeRNAii 1201.
    NextBioi 4959.
    PROi Q13286.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13286.
    CleanExi HS_CLN3.
    Genevestigatori Q13286.

    Family and domain databases

    InterProi IPR003492. Battenin_disease_Cln3.
    IPR018460. Battenin_disease_Cln3_subgr.
    IPR016196. MFS_dom_general_subst_transpt.
    [Graphical view ]
    PANTHERi PTHR10981. PTHR10981. 1 hit.
    Pfami PF02487. CLN3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015974. CLN3_BTN1. 1 hit.
    PRINTSi PR01315. BATTENIN.
    SUPFAMi SSF103473. SSF103473. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. 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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. 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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiCLN3_HUMAN
    AccessioniPrimary (citable) accession number: Q13286
    Secondary accession number(s): B2R7J1
    , O00668, O95089, Q549S9, Q9UP09, Q9UP11, Q9UP12, Q9UP13, Q9UP14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3