dbPTM

DC1I1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DC1I1_HUMAN
UniProt AC	O14576
Protein Name	Cytoplasmic dynein 1 intermediate chain 1
Gene Name	DYNC1I1
Organism	Homo sapiens (Human).
Sequence Length	645
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. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores..
Protein Sequence	MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVQPLHFLTWDTCYFHYLVPTPMSPSSKSVSTPSEAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVESKVGQDSELENQDKKQEVKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYNNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNNDTEVPTASVAIEGASALNRVRWAQAGKEVAVGDSEGRIWVYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDKSDLKA ------CCCHHHHHH	54.46	-
4	Acetylation	----MSDKSDLKAEL ----CCCHHHHHHHH	38.26	7705543
8	Acetylation	MSDKSDLKAELERKK CCCHHHHHHHHHHHH	44.82	7705553
14	Acetylation	LKAELERKKQRLAQI HHHHHHHHHHHHHHH	43.83	7705563
50	Phosphorylation	KEPVQDDSDLDRKRR HCCCCCCHHHHHHHH	48.65	23312004
77 (in isoform 2)	Phosphorylation	-	21.96	29691806
77 (in isoform 4)	Phosphorylation	-	21.96	29691806
77 (in isoform 3)	Phosphorylation	-	21.96	29691806
80	Phosphorylation	PLVQPLHFLTWDTCY CCCCCCEEEEECCCE	9.53	24719451
80 (in isoform 2)	Phosphorylation	-	9.53	26657352
80 (in isoform 3)	Phosphorylation	-	9.53	26657352
80 (in isoform 4)	Phosphorylation	-	9.53	26657352
82 (in isoform 3)	Phosphorylation	-	21.98	29691806
82 (in isoform 2)	Phosphorylation	-	21.98	29691806
82 (in isoform 4)	Phosphorylation	-	21.98	29691806
83 (in isoform 3)	Phosphorylation	-	10.89	29691806
83 (in isoform 2)	Phosphorylation	-	10.89	29691806
83 (in isoform 4)	Phosphorylation	-	10.89	29691806
97	Phosphorylation	YLVPTPMSPSSKSVS EECCCCCCCCCCCCC	23.88	-
99	Phosphorylation	VPTPMSPSSKSVSTP CCCCCCCCCCCCCCC	42.99	-
100	Phosphorylation	PTPMSPSSKSVSTPS CCCCCCCCCCCCCCC	32.13	23663014
102	Phosphorylation	PMSPSSKSVSTPSEA CCCCCCCCCCCCCCC	24.21	20068231
104	Phosphorylation	SPSSKSVSTPSEAGS CCCCCCCCCCCCCCC	41.51	20068231
105	Phosphorylation	PSSKSVSTPSEAGSQ CCCCCCCCCCCCCCC	28.78	18669648
107	Phosphorylation	SKSVSTPSEAGSQDS CCCCCCCCCCCCCCC	39.92	17525332
111	Phosphorylation	STPSEAGSQDSGDLG CCCCCCCCCCCCCCC	37.55	22817900
114	Phosphorylation	SEAGSQDSGDLGPLT CCCCCCCCCCCCCCE	26.94	24076635
154	O-linked_Glycosylation	KLGVSKVTQVDFLPR HCCCCCCEEEEECCH	26.98	28657654
165	Phosphorylation	FLPREVVSYSKETQT ECCHHHHCCCCCCCC	28.94	-
170	Phosphorylation	VVSYSKETQTPLATH HHCCCCCCCCCCCCC	41.29	28450419
172	Phosphorylation	SYSKETQTPLATHQS CCCCCCCCCCCCCCC	27.91	28450419
176	Phosphorylation	ETQTPLATHQSEEDE CCCCCCCCCCCCCCH	28.29	22617229
179	Phosphorylation	TPLATHQSEEDEEDE CCCCCCCCCCCHHHH	35.04	26657352
197	Phosphorylation	ESKVGQDSELENQDK HHHCCCCHHHCCHHH	35.87	-
274	Phosphorylation	VQAGANLSFNRQFYD CCCCCEEEECHHHCH	21.93	-
635	Phosphorylation	IRANRADSEEEGTVE HHHHCCCCCCCCCEE	46.02	28355574
640	Phosphorylation	ADSEEEGTVELSA-- CCCCCCCCEEECC--	17.68	28270605

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
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM58	Q8NG06	PMID:25241935

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DC1I1_HUMAN !!

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 DC1I1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYL2_HUMAN	DYNLL2	physical	16189514
DLRB1_HUMAN	DYNLRB1	physical	16189514
DYL1_HUMAN	DYNLL1	physical	12475239
DYLT1_HUMAN	DYNLT1	physical	12475239
DYLT3_HUMAN	DYNLT3	physical	12475239
CADM4_HUMAN	CADM4	physical	21900206
WDCP_HUMAN	C2orf44	physical	21900206
F110A_HUMAN	FAM110A	physical	21900206
KAT7_HUMAN	KAT7	physical	21900206
F16P1_HUMAN	FBP1	physical	21900206
TAOK1_HUMAN	TAOK1	physical	21900206
RUN3B_HUMAN	RUNDC3B	physical	21900206
CRCM_HUMAN	MCC	physical	21900206
FA83D_HUMAN	FAM83D	physical	21900206
RPGP1_HUMAN	RAP1GAP	physical	21900206
DCTN1_HUMAN	DCTN1	physical	21900206
DYL1_HUMAN	DYNLL1	physical	11148209
LIS1_HUMAN	PAFAH1B1	physical	18784752
KLC3_HUMAN	KLC3	physical	18784752
TBB3_HUMAN	TUBB3	physical	18784752
KCNA5_HUMAN	KCNA5	physical	16051887
LIS1_HUMAN	PAFAH1B1	physical	21652625
BICD2_HUMAN	BICD2	physical	22956769
DCTN1_HUMAN	DCTN1	physical	22956769
AMRA1_HUMAN	AMBRA1	physical	20921139
DYL1_HUMAN	DYNLL1	physical	20921139
BECN1_HUMAN	BECN1	physical	20921139
NDEL1_HUMAN	NDEL1	physical	22159412
DC1L2_HUMAN	DYNC1LI2	physical	28514442
WDR34_HUMAN	WDR34	physical	28514442
DYHC1_HUMAN	DYNC1H1	physical	28514442
DC1L1_HUMAN	DYNC1LI1	physical	28514442
DISC1_HUMAN	DISC1	physical	28514442
FA83D_HUMAN	FAM83D	physical	28514442
DC1I2_HUMAN	DYNC1I2	physical	28514442
RL23_HUMAN	RPL23	physical	28514442
CO039_HUMAN	C15orf39	physical	28514442
SAMD1_HUMAN	SAMD1	physical	28514442
MGAP_HUMAN	MGA	physical	28514442

Drug and Disease Associations

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

Regulatory Network of DC1I1_HUMAN

Related Literatures of Post-Translational Modification

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-635, AND MASSSPECTROMETRY.	19690332 [Abstract]