UniProt ID | DC1L1_RAT | |
---|---|---|
UniProt AC | Q9QXU8 | |
Protein Name | Cytoplasmic dynein 1 light intermediate chain 1 | |
Gene Name | Dync1li1 | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 523 | |
Subcellular Localization | Cytoplasm . Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle pole. | |
Protein Description | Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity).. | |
Protein Sequence | MAAVGRVGSFGSSPPGLASTYASGPLANELASGSGGPAAGDDEDGQNLWSRILREVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGEDFPASPQRRATAAQEDRDDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKIEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVGGSPGGGAAGASTSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSPTTPPSPTEGEAS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | Phosphorylation | AAVGRVGSFGSSPPG CCCCCCCCCCCCCCC | 24.47 | 30240740 | |
12 | Phosphorylation | GRVGSFGSSPPGLAS CCCCCCCCCCCCHHH | 37.35 | 30240740 | |
13 | Phosphorylation | RVGSFGSSPPGLAST CCCCCCCCCCCHHHC | 35.18 | 30240740 | |
197 | Phosphorylation | LIRDFQEYVEPGEDF HHHHHHHHCCCCCCC | 10.18 | 28551015 | |
207 | Phosphorylation | PGEDFPASPQRRATA CCCCCCCCHHHHHHH | 23.08 | 23712012 | |
213 | Phosphorylation | ASPQRRATAAQEDRD CCHHHHHHHCHHCCC | 22.25 | 23984901 | |
222 | Phosphorylation | AQEDRDDSVVLPLGA CHHCCCCCEEEECCC | 20.58 | 23984901 | |
398 | Phosphorylation | AGRPVDASPRVPGGS CCCCCCCCCCCCCCC | 14.58 | - | |
405 | Phosphorylation | SPRVPGGSPRTPNRS CCCCCCCCCCCCCCC | 19.68 | 27097102 | |
408 | Phosphorylation | VPGGSPRTPNRSVSS CCCCCCCCCCCCCCC | 28.44 | 27097102 | |
412 | Phosphorylation | SPRTPNRSVSSNVAS CCCCCCCCCCCCCCC | 32.75 | 27097102 | |
414 | Phosphorylation | RTPNRSVSSNVASVS CCCCCCCCCCCCCCC | 19.90 | 27097102 | |
415 | Phosphorylation | TPNRSVSSNVASVSP CCCCCCCCCCCCCCC | 32.92 | 27097102 | |
419 | Phosphorylation | SVSSNVASVSPIPAG CCCCCCCCCCCCCCC | 20.88 | 27097102 | |
421 | Phosphorylation | SSNVASVSPIPAGSK CCCCCCCCCCCCCCC | 18.02 | 27097102 | |
427 | Phosphorylation | VSPIPAGSKKIDPNM CCCCCCCCCCCCCCC | 32.64 | 25575281 | |
450 | Phosphorylation | VLANFFNSLLSKKTG HHHHHHHHHHCCCCC | 26.07 | 16641100 | |
453 | Phosphorylation | NFFNSLLSKKTGSPG HHHHHHHCCCCCCCC | 37.08 | 25575281 | |
486 | Phosphorylation | LPPSAKKSGQKPVLS CCCCCCCCCCCCCHH | 45.83 | - | |
503 | Phosphorylation | HAELDRITRKPASVS HHHHHHHCCCCCCCC | 33.27 | 28689409 | |
508 | Phosphorylation | RITRKPASVSPTTPP HHCCCCCCCCCCCCC | 31.49 | 27097102 | |
510 | Phosphorylation | TRKPASVSPTTPPSP CCCCCCCCCCCCCCC | 17.65 | 28689409 | |
512 | Phosphorylation | KPASVSPTTPPSPTE CCCCCCCCCCCCCCC | 44.41 | 23712012 | |
513 | Phosphorylation | PASVSPTTPPSPTEG CCCCCCCCCCCCCCC | 36.26 | 23712012 | |
516 | Phosphorylation | VSPTTPPSPTEGEAS CCCCCCCCCCCCCCC | 45.73 | 23712012 | |
518 | Phosphorylation | PTTPPSPTEGEAS-- CCCCCCCCCCCCC-- | 62.04 | 23712012 | |
523 | Phosphorylation | SPTEGEAS------- CCCCCCCC------- | 36.13 | 23712012 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
213 | T | Phosphorylation | Kinase | PKACA | P17612 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DC1L1_RAT !! |
* 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 DC1L1_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of DC1L1_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-414; SER-421;SER-450; SER-510; THR-512; THR-513; SER-516 AND THR-518, AND MASSSPECTROMETRY. |