DCTN1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DCTN1_RAT
• UniProt AC: P28023
• Protein Name: Dynactin subunit 1
• Gene Name: Dctn1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1280
• Subcellular Localization: Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, spindle . Nucleus envelope . Cytoplasm, cel
• Protein Description: Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitement to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation..
• Protein Sequence: MAQSKRHMYNRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKILKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRDQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEAKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEESTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCSILISTMNKLATAMQEGEYDAERPPSKPPPVEPWPAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQTLLRKKEKEFEETMDALQADIDQLEAEKTELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGGTPGQAPGALPGPGPVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKFSLPPHEGPGGNLLSGALYRKTSQLLEKLNQLSTYTHVVDITRSSPACKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHGRLIS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	TPSGSRMSTEASARP CCCCCCCCCCCCCCC	23.22	12119357
20	Phosphorylation	PSGSRMSTEASARPL CCCCCCCCCCCCCCC	26.65	28432305
103	Phosphorylation	VFEDGADTTSPETPD EECCCCCCCCCCCCC	28.74	28432305
104	Phosphorylation	FEDGADTTSPETPDS ECCCCCCCCCCCCCC	42.71	28432305
105	Phosphorylation	EDGADTTSPETPDSS CCCCCCCCCCCCCCH	23.88	27097102
108	Phosphorylation	ADTTSPETPDSSASK CCCCCCCCCCCHHHH	35.46	27097102
111	Phosphorylation	TSPETPDSSASKILK CCCCCCCCHHHHHHH	29.07	27097102
112	Phosphorylation	SPETPDSSASKILKR CCCCCCCHHHHHHHH	43.89	27097102
114	Phosphorylation	ETPDSSASKILKREG CCCCCHHHHHHHHHC	23.37	27097102
145	Phosphorylation	KAPTARKTTTRRPKP CCCCCCCCCCCCCCC	28.04	-
146	Phosphorylation	APTARKTTTRRPKPT CCCCCCCCCCCCCCC	22.72	-
147	Phosphorylation	PTARKTTTRRPKPTR CCCCCCCCCCCCCCC	29.88	-
179	Phosphorylation	SASAGELSSSEPSTP CCCCCCCCCCCCCCC	27.76	-
203	Phosphorylation	IPTPALTSPGAAPPL CCCCCCCCCCCCCCC	23.37	30240740
212	Phosphorylation	GAAPPLPSPSKEEEG CCCCCCCCCCHHCCC	49.87	30240740
214	Phosphorylation	APPLPSPSKEEEGLR CCCCCCCCHHCCCHH	57.97	30240740
230	Acetylation	QVRDLEEKLETLRLK HHHHHHHHHHHHHHH	42.10	22902405
283	Acetylation	LKEAKEAKEALEAKE HHHHHHHHHHHHHHH	44.61	72626487
289	Acetylation	AKEALEAKERYMEEM HHHHHHHHHHHHHHH	33.09	22902405
319	Phosphorylation	MAEERAESLQQEVEA HHHHHHHHHHHHHHH	30.41	28432305
392	Acetylation	QEHVKLQKLMEKKNQ HHHHHHHHHHHHHHH	61.30	72598781
961	Acetylation	LKKSLKIKGEELSEA HHHHCCCCCHHHHHH	59.70	22902405
1153	Ubiquitination	LSGALYRKTSQLLEK HHHHHHHHHHHHHHH	38.68	-
1154	Phosphorylation	SGALYRKTSQLLEKL HHHHHHHHHHHHHHH	16.83	22673903
1155	Phosphorylation	GALYRKTSQLLEKLN HHHHHHHHHHHHHHH	23.13	22673903
1203	Acetylation	SLSDTIEKLKDEVLK HHHHHHHHHHHHHHH	57.92	22902405
1227	Phosphorylation	TVPTDFATFPSSAFL CCCCCCCCCCCHHHH	35.75	23984901
1230	Phosphorylation	TDFATFPSSAFLRAK CCCCCCCCHHHHHCC	30.06	23984901
1231	Phosphorylation	DFATFPSSAFLRAKE CCCCCCCHHHHHCCH	24.23	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
19	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
179	S	Phosphorylation	Kinase	PLK1	Q62673	Uniprot
212	S	Phosphorylation	Kinase	CDK1	P39951	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
145	T	Phosphorylation	Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome.	-
146	T	Phosphorylation	Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome.	-
147	T	Phosphorylation	Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome.	-
179	S	Phosphorylation	PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope and promotes its dissociation from microtubules during early mitosis and positively regulates nuclear envelope breakdown during prophase.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DCTN1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of DCTN1_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.