| UniProt ID | CLN3_HUMAN | |
|---|---|---|
| UniProt AC | Q13286 | |
| Protein Name | Battenin | |
| Gene Name | CLN3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 438 | |
| Subcellular Localization |
Lysosome membrane Multi-pass membrane protein . Late endosome . Lysosome . |
|
| Protein Description | Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes.. | |
| Protein Sequence | MGGCAGSRRRFSDSEGEETVPEPRLPLLDHQGAHWKNAVGFWLLGLCNNFSYVVMLSAAHDILSHKRTSGNQSHVDPGPTPIPHNSSSRFDCNSVSTAAVLLADILPTLVIKLLAPLGLHLLPYSPRVLVSGICAAGSFVLVAFSHSVGTSLCGVVFASISSGLGEVTFLSLTAFYPRAVISWWSSGTGGAGLLGALSYLGLTQAGLSPQQTLLSMLGIPALLLASYFLLLTSPEAQDPGGEEEAESAARQPLIRTEAPESKPGSSSSLSLRERWTVFKGLLWYIVPLVVVYFAEYFINQGLFELLFFWNTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQCLNLVFLLADVWFGFLPSIYLVFLIILYEGLLGGAAYVNTFHNIALETSDEHREFAMAATCISDTLGISLSGLLALPLHDFLCQLS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 12 | Phosphorylation | AGSRRRFSDSEGEET CCCCCCCCCCCCCCC | 38.11 | 29255136 | |
| 14 | Phosphorylation | SRRRFSDSEGEETVP CCCCCCCCCCCCCCC | 46.43 | 29255136 | |
| 19 | Phosphorylation | SDSEGEETVPEPRLP CCCCCCCCCCCCCCC | 36.74 | 20044836 | |
| 68 | Phosphorylation | DILSHKRTSGNQSHV HHHHCCCCCCCCCCC | 45.87 | 22210691 | |
| 69 | Phosphorylation | ILSHKRTSGNQSHVD HHHCCCCCCCCCCCC | 39.52 | 22210691 | |
| 71 | N-linked_Glycosylation | SHKRTSGNQSHVDPG HCCCCCCCCCCCCCC | 39.69 | 17286803 | |
| 80 | O-linked_Glycosylation | SHVDPGPTPIPHNSS CCCCCCCCCCCCCCC | 39.50 | 30871613 | |
| 80 | Phosphorylation | SHVDPGPTPIPHNSS CCCCCCCCCCCCCCC | 39.50 | - | |
| 80 (in isoform 6) | Phosphorylation | - | 39.50 | - | |
| 85 | N-linked_Glycosylation | GPTPIPHNSSSRFDC CCCCCCCCCCCCCCC | 37.93 | 17286803 | |
| 87 | Phosphorylation | TPIPHNSSSRFDCNS CCCCCCCCCCCCCCC | 30.74 | 22210691 | |
| 87 (in isoform 6) | Phosphorylation | - | 30.74 | - | |
| 94 | Phosphorylation | SSRFDCNSVSTAAVL CCCCCCCCHHHHHHH | 24.63 | - | |
| 94 (in isoform 6) | Phosphorylation | - | 24.63 | - | |
| 125 | Phosphorylation | GLHLLPYSPRVLVSG CCCCCCCCCHHHHHH | 12.32 | - | |
| 163 | Ubiquitination | VFASISSGLGEVTFL HHHHHCCCCCCEEEE | 30.80 | 21890473 | |
| 214 (in isoform 2) | Ubiquitination | - | 3.00 | 21890473 | |
| 238 | Ubiquitination | LTSPEAQDPGGEEEA HHCCCCCCCCCHHHH | 51.35 | 21890473 | |
| 262 | Ubiquitination | RTEAPESKPGSSSSL ECCCCCCCCCCCCCC | 52.30 | 21890473 | |
| 262 (in isoform 4) | Ubiquitination | - | 52.30 | 21890473 | |
| 262 (in isoform 3) | Ubiquitination | - | 52.30 | 21890473 | |
| 262 (in isoform 1) | Ubiquitination | - | 52.30 | 21890473 | |
| 262 | Ubiquitination | RTEAPESKPGSSSSL ECCCCCCCCCCCCCC | 52.30 | 21890473 | |
| 262 | Ubiquitination | RTEAPESKPGSSSSL ECCCCCCCCCCCCCC | 52.30 | 21906983 | |
| 267 | Phosphorylation | ESKPGSSSSLSLRER CCCCCCCCCCCHHHH | 36.68 | - | |
| 268 | Phosphorylation | SKPGSSSSLSLRERW CCCCCCCCCCHHHHH | 24.75 | 17081983 | |
| 270 | Phosphorylation | PGSSSSLSLRERWTV CCCCCCCCHHHHHHH | 27.59 | 17081983 | |
| 276 | Phosphorylation | LSLRERWTVFKGLLW CCHHHHHHHHHHHHH | 23.45 | 24719451 | |
| 310 | N-linked_Glycosylation | FELLFFWNTSLSHAQ HHHHHHCCCCCCHHH | 18.03 | UniProtKB CARBOHYD | |
| 335 | Phosphorylation | AGVFASRSSLRCCRI HCCCCCCCCCHHHHH | 31.09 | 30631047 | |
| 336 | Phosphorylation | GVFASRSSLRCCRIR CCCCCCCCCHHHHHH | 20.79 | 30631047 | |
| 435 | Methylation | LPLHDFLCQLS---- CCHHHHHHHCC---- | 3.74 | - | |
| 435 | Farnesylation | LPLHDFLCQLS---- CCHHHHHHHCC---- | 3.74 | 17286803 | |
| 435 | Farnesylation | LPLHDFLCQLS---- CCHHHHHHHCC---- | 3.74 | 17286803 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CLN3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLN3_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CLN3_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00149 | Neuronal ceroid lipofuscinosis, including: Infantile Neuronal Ceroid Lipofuscinosis (INCL)/ Santavuo | |||||
| H00810 | Progressive myoclonic epilepsy (PME), including: Lafora disease (LBD); Unverricht-Lundborg disease ( | |||||
| OMIM Disease | ||||||
| 204200 | Ceroid lipofuscinosis, neuronal, 3 (CLN3) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "C-terminal prenylation of the CLN3 membrane glycoprotein is requiredfor efficient endosomal sorting to lysosomes."; Storch S., Pohl S., Quitsch A., Falley K., Braulke T.; Traffic 8:431-444(2007). Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-71 AND ASN-85, ANDISOPRENYLATION AT CYS-435. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, AND MASSSPECTROMETRY. | |
| "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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, AND MASSSPECTROMETRY. | |
| "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-14, AND MASSSPECTROMETRY. | |
| Prenylation | |
| Reference | PubMed |
| "C-terminal prenylation of the CLN3 membrane glycoprotein is requiredfor efficient endosomal sorting to lysosomes."; Storch S., Pohl S., Quitsch A., Falley K., Braulke T.; Traffic 8:431-444(2007). Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-71 AND ASN-85, ANDISOPRENYLATION AT CYS-435. | |
