dbPTM

DCTN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DCTN1_MOUSE
UniProt AC	O08788
Protein Name	Dynactin subunit 1
Gene Name	Dctn1
Organism	Mus musculus (Mouse).
Sequence Length	1281
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	MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	RRHMSSRTPSGSRMS CCCCCCCCCCCCCCC	24.61	28059163
19	Phosphorylation	TPSGSRMSTEASARP CCCCCCCCCCCCCCC	23.22	30635358
20	Phosphorylation	PSGSRMSTEASARPL CCCCCCCCCCCCCCC	26.65	30635358
31	Phosphorylation	ARPLRVGSRVEVIGK CCCCCCCCEEEEECC	30.23	29176673
81	Glutathionylation	QGRKYFTCDEGHGIF CCEEEEEECCCCEEE	3.00	24333276
92	Phosphorylation	HGIFVRQSQIQVFED CEEEEEHHEEEEECC	20.77	25619855
103	Phosphorylation	VFEDGADTTSPETPD EECCCCCCCCCCCCC	28.74	25619855
104	Phosphorylation	FEDGADTTSPETPDS ECCCCCCCCCCCCCC	42.71	25619855
105	Phosphorylation	EDGADTTSPETPDSS CCCCCCCCCCCCCCH	23.88	25521595
108	Phosphorylation	ADTTSPETPDSSASK CCCCCCCCCCCHHHH	35.46	24925903
111	Phosphorylation	TSPETPDSSASKVLK CCCCCCCCHHHHHHH	29.07	25619855
112	Phosphorylation	SPETPDSSASKVLKR CCCCCCCHHHHHHHH	43.89	25619855
114	Phosphorylation	ETPDSSASKVLKREG CCCCCHHHHHHHHHC	25.83	25619855
145	Phosphorylation	KAPTARKTTTRRPKP CCCCCCCCCCCCCCC	28.04	-
146	Phosphorylation	APTARKTTTRRPKPT CCCCCCCCCCCCCCC	22.72	-
147	Phosphorylation	PTARKTTTRRPKPTR CCCCCCCCCCCCCCC	29.88	-
179	Phosphorylation	SASAGELSSSEPSTP CCCCCCCCCCCCCCC	27.76	-
212	Phosphorylation	GAAPPLPSPSKEEEG CCCCCCCCCCHHHHC	49.87	-
230	Acetylation	QVRDLEEKLETLRLK HHHCHHHHHHHHHHH	42.10	23236377
293	Phosphorylation	ALEAKERYMEEMADT HHHHHHHHHHHHHHH	15.23	25293948
300	Phosphorylation	YMEEMADTADAIEMA HHHHHHHHHHHHHHH	19.52	25293948
308	Phosphorylation	ADAIEMATLDKEMAE HHHHHHHHHCHHHHH	33.89	25293948
320	Phosphorylation	MAEERAESLQQEVEA HHHHHHHHHHHHHHH	30.41	25338131
351	Phosphorylation	AEIEEKGSDGAASSY HHHHHHCCCCCHHHH	43.89	25521595
356	Phosphorylation	KGSDGAASSYQLKQL HCCCCCHHHHHHHHH	29.10	30635358
357	Phosphorylation	GSDGAASSYQLKQLE CCCCCHHHHHHHHHH	16.51	30635358
417	Phosphorylation	ERLQEELSQAESTID HHHHHHHHHHHHHHH	30.53	29899451
421	Phosphorylation	EELSQAESTIDELKE HHHHHHHHHHHHHHH	33.41	29514104
541	Phosphorylation	LTNQQEASVERQQQP HHHHHHHHHHHHCCC	24.61	17203969
556	Ubiquitination	PPETFDFKIKFAETK CCCCCCEEEEEHHHH	46.99	22790023
618	Acetylation	LMPRLICKAELIRKQ HHHHHHHHHHHHHHH	37.59	22826441
693	Phosphorylation	GSLYPEMSAHERSLD HHHCHHCCHHHHHHH	25.47	28059163
722	Acetylation	VNVEPLTKAIKYYQH CCHHHHHHHHHHHHH	56.66	15605861
919	Phosphorylation	YDAERPPSKPPPVEL CCCCCCCCCCCCHHH	61.55	22817900
996	Phosphorylation	ERIEKVQTRLDETQT HHHHHHHHHHHHHHH	35.87	29109428
1003	Phosphorylation	TRLDETQTLLRKKEK HHHHHHHHHHHHHHH	34.87	29176673
1007	Acetylation	ETQTLLRKKEKDFEE HHHHHHHHHHHCHHH	66.31	2389433
1041	Phosphorylation	KQRLNSQSKRTIEGL HHHHHHHCCHHHHCC	24.75	29514104
1090	Phosphorylation	GPGLVKDSPLLLQQI CCCCCCCCHHHHHHH	16.24	25777480
1098	Phosphorylation	PLLLQQISAMRLHIS HHHHHHHHHHHHHHH	16.21	25777480
1155	Phosphorylation	AGALYRKTSQLLEKL HHHHHHHHHHHHHHH	16.83	29899451
1156	Phosphorylation	GALYRKTSQLLEKLN HHHHHHHHHHHHHHH	23.13	22817900
1161	Ubiquitination	KTSQLLEKLNQLSTH HHHHHHHHHHHCCCC	53.35	22790023
1175	Phosphorylation	HTHVVDITRSSPAAK CEEEEECCCCCCCCC	21.75	25338131
1183	Phosphorylation	RSSPAAKSPSAQLME CCCCCCCCHHHHHHH	21.25	28066266
1185	Phosphorylation	SPAAKSPSAQLMEQV CCCCCCHHHHHHHHH	35.42	28066266
1238	Ubiquitination	SSAFLRAKEEQQDDT CHHHHHCCHHHCCCC	56.18	22790023
1254	O-linked_Glycosylation	YMGKVTFSCAAGLGQ EEEEEEEECCCCCCH	8.09	55411787
1268	Phosphorylation	QRHRLVLTQEQLHQL HHHHEEECHHHHHHH	23.68	26239621

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
179	S	Phosphorylation	Kinase	PLK1	Q07832	Uniprot
212	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxl5	Q8C2S5	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DCTN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTZ_HUMAN	ACTR1A	physical	20360068
DCTN1_HUMAN	DCTN1	physical	20360068
DCTN3_HUMAN	DCTN3	physical	20360068
CDK1_HUMAN	CDK1	physical	20360068
ARP10_HUMAN	ACTR10	physical	20360068
ACTY_HUMAN	ACTR1B	physical	20360068
DCTN6_HUMAN	DCTN6	physical	20360068
DCTN4_HUMAN	DCTN4	physical	20360068
DCTN2_HUMAN	DCTN2	physical	20360068
DCTN5_HUMAN	DCTN5	physical	20360068
CAZA1_HUMAN	CAPZA1	physical	26496610
CAZA2_HUMAN	CAPZA2	physical	26496610
CAPZB_HUMAN	CAPZB	physical	26496610
DCTN1_HUMAN	DCTN1	physical	26496610
RT12_HUMAN	MRPS12	physical	26496610
TRIPB_HUMAN	TRIP11	physical	26496610
PTSS1_HUMAN	PTDSS1	physical	26496610
ACTY_HUMAN	ACTR1B	physical	26496610
ACTZ_HUMAN	ACTR1A	physical	26496610
DCTN2_HUMAN	DCTN2	physical	26496610
DCTN6_HUMAN	DCTN6	physical	26496610
CP250_HUMAN	CEP250	physical	26496610
DCTN3_HUMAN	DCTN3	physical	26496610
ANKL2_HUMAN	ANKLE2	physical	26496610
QCR8_HUMAN	UQCRQ	physical	26496610
CEP83_HUMAN	CEP83	physical	26496610
DC1L1_HUMAN	DYNC1LI1	physical	26496610
DCTN4_HUMAN	DCTN4	physical	26496610
KI16B_HUMAN	KIF16B	physical	26496610
ARP10_HUMAN	ACTR10	physical	26496610
DERL1_HUMAN	DERL1	physical	26496610
DLRB1_HUMAN	DYNLRB1	physical	26496610
DCTN5_HUMAN	DCTN5	physical	26496610

Drug and Disease Associations

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

Regulatory Network of DCTN1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541, AND MASSSPECTROMETRY.	17203969 [Abstract]

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