Q13286 (CLN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Battenin

Alternative name(s):
Batten disease protein
Protein CLN3

Gene names

Name:	CLN3
Synonyms:	BTS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Neuronal ceroid lipofuscinosis 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 process	Transport
Cellular component	Endosome Lysosome Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Neurodegeneration Neuronal ceroid lipofuscinosis
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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 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 regulation of action potential Inferred from sequence or structural similarity. 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_component	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 early endosome Inferred from direct assay PubMed 15240864. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from direct assay PubMed 12706816. Source: UniProtKB late endosome Inferred from direct assay Ref.20. Source: UniProtKB lysosomal membrane Inferred from direct assay PubMed 9384607. 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 synaptic vesicle Inferred from direct assay PubMed 10332042PubMed 11590129. Source: UniProtKB trans-Golgi network Inferred from direct assay PubMed 15240864. Source: UniProtKB
Molecular_function	unfolded protein binding Traceable author statement PubMed 8980123. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 435	435	Battenin		PRO_0000089857
	Propeptide	436 – 438	3	Removed in mature form Probable		PRO_0000422290
Regions
	Transmembrane	38 – 58	21	Helical; Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Transmembrane	128 – 148	21	Helical; Potential
	Transmembrane	180 – 200	21	Helical; Potential
	Transmembrane	212 – 232	21	Helical; Potential
	Transmembrane	278 – 298	21	Helical; Potential
	Transmembrane	358 – 378	21	Helical; Potential
	Transmembrane	407 – 427	21	Helical; Potential
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19
	Modified residue	14	1	Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19
	Modified residue	435	1	Cysteine methyl ester Probable
	Lipidation	435	1	S-farnesyl cysteine Ref.13
	Glycosylation	71	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	85	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	155 – 264	110	Missing in isoform 5.		VSP_004169
	Alternative sequence	178 – 225	48	Missing in isoform 2.		VSP_004166
	Alternative sequence	280 – 302	23	GLLWY…INQGL → VRMMAG in isoform 3.		VSP_004167
	Alternative sequence	322 – 438	117	Missing in isoform 4.		VSP_004168
	Alternative sequence	353 – 438	86	CLNLV…LCQLS → MESRSVAQAGM in isoform 5.		VSP_004170
	Natural variant	101	1	L → P in CLN3. Ref.21 Ref.23		VAR_005131
	Natural variant	134	1	C → R in CLN3. Ref.23		VAR_066892
	Natural variant	170	1	L → P in CLN3. Ref.21 Ref.23		VAR_005132
	Natural variant	187	1	G → A in CLN3. Ref.23		VAR_066893
	Natural variant	189	1	G → R in CLN3. Ref.23		VAR_066894
	Natural variant	295	1	E → 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 variant	330	1	V → F in CLN3. Ref.21		VAR_005134
	Natural variant	334	1	R → C in CLN3. Ref.21		VAR_005135
	Natural variant	334	1	R → H in CLN3. Ref.21 Ref.23		VAR_005136
Experimental info
	Sequence conflict	259	1	P → L in BAG35838. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BE25E973CEEC4FD5	FASTA	438	47,623
	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
	Isoform 2 [UniParc]. Checksum: 30722C86911C70C0	FASTA	390	42,829
	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 SLTAFYPSYF 190 200 210 220 230 240 LLLTSPEAQD PGGEEEAESA ARQPLIRTEA PESKPGSSSS LSLRERWTVF KGLLWYIVPL 250 260 270 280 290 300 VVVYFAEYFI NQGLFELLFF WNTSLSHAQQ YRWYQMLYQA GVFASRSSLR CCRIRFTWAL 310 320 330 340 350 360 ALLQCLNLVF LLADVWFGFL PSIYLVFLII LYEGLLGGAA YVNTFHNIAL ETSDEHREFA 370 380 390 MAATCISDTL GISLSGLLAL PLHDFLCQLS
	Isoform 3 [UniParc]. Checksum: 503A97EDF8B72CC3	FASTA	421	45,570
	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 LRERWTVFKV RMMAGFELLF FWNTSLSHAQ 310 320 330 340 350 360 QYRWYQMLYQ AGVFASRSSL RCCRIRFTWA LALLQCLNLV FLLADVWFGF LPSIYLVFLI 370 380 390 400 410 420 ILYEGLLGGA AYVNTFHNIA LETSDEHREF AMAATCISDT LGISLSGLLA LPLHDFLCQL S
	Isoform 4 [UniParc]. Checksum: 482F021A8FF39B63	FASTA	321	34,569
	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 GLFELLFFWN TSLSHAQQYR W
	Isoform 5 [UniParc]. Checksum: 5FFBAA4622A8DF52	FASTA	253	28,016
	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 SLCGSSSSLS LRERWTVFKG LLWYIVPLVV 190 200 210 220 230 240 VYFAEYFINQ GLFELLFFWN TSLSHAQQYR WYQMLYQAGV FASRSSLRCC RIRFTWALAL 250 LQMESRSVAQ AGM

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 1).
[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]	"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. , 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. , 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. 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. BC002394 mRNA. Translation: AAH02394.1. BC004433 mRNA. Translation: AAH04433.1.
IPI	IPI00012448. IPI00217835. IPI00217836. IPI00217837. IPI00217838.
PIR	A57219.
RefSeq	NP_000077.1. NM_000086.2. NP_001035897.1. NM_001042432.1.
UniGene	Hs.534667.
3D structure databases
ProteinModelPortal	Q13286.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13286. 36 interactions.
STRING	9606.ENSP00000353073.
PTM databases
PhosphoSite	Q13286.
Polymorphism databases
DMDM	2498243.
Proteomic databases
PaxDb	Q13286.
PRIDE	Q13286.
Protocols and materials databases
DNASU	1201.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354630; ENSP00000346650; ENSG00000188603. ENST00000355477; ENSP00000347660; ENSG00000188603. ENST00000357076; ENSP00000349586; ENSG00000188603. ENST00000359984; ENSP00000353073; ENSG00000188603. ENST00000360019; ENSP00000353116; ENSG00000188603. ENST00000565316; ENSP00000456117; ENSG00000188603. ENST00000569030; ENSP00000454680; ENSG00000188603. ENST00000569430; ENSP00000454229; ENSG00000188603.
GeneID	1201.
KEGG	hsa:1201.
UCSC	uc002dpm.3. human. uc002dpq.1. human. uc010bye.1. human.
Organism-specific databases
CTD	1201.
GeneCards	GC16M028488.
HGNC	HGNC:2074. CLN3.
MIM	204200. phenotype. 607042. gene.
neXtProt	NX_Q13286.
Orphanet	228346. CLN3 disease.
PharmGKB	PA26601.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG325947.
HOVERGEN	HBG017297.
InParanoid	Q13286.
KO	K12389.
OMA	NYGYVVM.
OrthoDB	EOG4TF0KG.
PhylomeDB	Q13286.
Gene expression databases
ArrayExpress	Q13286.
Bgee	Q13286.
CleanEx	HS_CLN3.
Genevestigator	Q13286.
GermOnline	ENSG00000188603. Homo sapiens.
Family and domain databases
InterPro	IPR003492. Battenin_disease_Cln3. IPR018460. Battenin_disease_Cln3_subgr. IPR016196. MFS_dom_general_subst_transpt. [Graphical view]
PANTHER	PTHR10981. PTHR10981. 1 hit.
Pfam	PF02487. CLN3. 1 hit. [Graphical view]
PIRSF	PIRSF015974. CLN3_BTN1. 1 hit.
PRINTS	PR01315. BATTENIN.
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	1201.
NextBio	4959.
SOURCE	Search...

Entry information

Entry name

CLN3_HUMAN

Accession

Primary (citable) accession number: Q13286
Secondary accession number(s): B2R7J1 , O00668, Q549S9, Q9UP09, Q9UP11, Q9UP12, Q9UP13, Q9UP14

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.