dbPTM

DC1I2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DC1I2_HUMAN
UniProt AC	Q13409
Protein Name	Cytoplasmic dynein 1 intermediate chain 2
Gene Name	DYNC1I2
Organism	Homo sapiens (Human).
Sequence Length	638
Subcellular Localization	Cytoplasm, cytoskeleton .
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. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes..
Protein Sequence	MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSDKSELKA ------CCCHHHHHH	54.46	29255136
2	Acetylation	------MSDKSELKA ------CCCHHHHHH	54.46	22814378
5	Phosphorylation	---MSDKSELKAELE ---CCCHHHHHHHHH	53.83	29255136
8	Ubiquitination	MSDKSELKAELERKK CCCHHHHHHHHHHHH	35.44	-
8	Malonylation	MSDKSELKAELERKK CCCHHHHHHHHHHHH	35.44	26320211
8	Acetylation	MSDKSELKAELERKK CCCHHHHHHHHHHHH	35.44	18586625
51	Phosphorylation	VAPVQEESDLEKKRR HHCCCCHHHHHHHHH	46.90	29255136
55	Acetylation	QEESDLEKKRREAEA CCHHHHHHHHHHHHH	59.90	23236377
55	Acetylation	QEESDLEKKRREAEA CCHHHHHHHHHHHHH	59.90	-
66 (in isoform 2)	Phosphorylation	-	18.13	23927012
66	Phosphorylation	EAEALLQSMGLTPES HHHHHHHHCCCCCCC	18.13	22199227
66 (in isoform 3)	Phosphorylation	-	18.13	23927012
66 (in isoform 6)	Phosphorylation	-	18.13	23927012
70	Phosphorylation	LLQSMGLTPESPIVF HHHHCCCCCCCCCEE	21.20	20068231
70 (in isoform 2)	Phosphorylation	-	21.20	30266825
70 (in isoform 3)	Phosphorylation	-	21.20	30266825
70 (in isoform 6)	Phosphorylation	-	21.20	30266825
73 (in isoform 3)	Phosphorylation	-	22.56	30266825
73 (in isoform 6)	Phosphorylation	-	22.56	30266825
73 (in isoform 7)	Phosphorylation	-	22.56	24076635
73 (in isoform 2)	Phosphorylation	-	22.56	30266825
73	Phosphorylation	SMGLTPESPIVFSEY HCCCCCCCCCEEEEE	22.56	18669648
78	Phosphorylation	PESPIVFSEYWVPPP CCCCCEEEEEECCCC	20.91	20068231
80	Phosphorylation	SPIVFSEYWVPPPMS CCCEEEEEECCCCCC	15.54	20068231
81 (in isoform 3)	Phosphorylation	-	7.65	23927012
81 (in isoform 6)	Phosphorylation	-	7.65	23927012
81 (in isoform 2)	Phosphorylation	-	7.65	23927012
83 (in isoform 3)	Phosphorylation	-	17.09	30266825
83 (in isoform 6)	Phosphorylation	-	17.09	30266825
83 (in isoform 2)	Phosphorylation	-	17.09	30266825
84 (in isoform 3)	Phosphorylation	-	27.83	25159151
84 (in isoform 2)	Phosphorylation	-	27.83	25159151
84 (in isoform 6)	Phosphorylation	-	27.83	25159151
86 (in isoform 3)	Phosphorylation	-	13.03	29743597
86 (in isoform 2)	Phosphorylation	-	13.03	29743597
86 (in isoform 6)	Phosphorylation	-	13.03	29743597
87	Phosphorylation	YWVPPPMSPSSKSVS EECCCCCCCCCCCCC	27.66	23663014
88 (in isoform 6)	Phosphorylation	-	36.05	25849741
88 (in isoform 3)	Phosphorylation	-	36.05	25849741
88 (in isoform 2)	Phosphorylation	-	36.05	25849741
89	Phosphorylation	VPPPMSPSSKSVSTP CCCCCCCCCCCCCCC	42.99	23663014
89 (in isoform 3)	Phosphorylation	-	42.99	25849741
89 (in isoform 2)	Phosphorylation	-	42.99	25849741
89 (in isoform 6)	Phosphorylation	-	42.99	25849741
90	Phosphorylation	PPPMSPSSKSVSTPS CCCCCCCCCCCCCCC	32.13	20068231
91 (in isoform 6)	Phosphorylation	-	60.25	22210691
91 (in isoform 3)	Phosphorylation	-	60.25	22210691
92	Phosphorylation	PMSPSSKSVSTPSEA CCCCCCCCCCCCCCC	24.21	30278072
94	Phosphorylation	SPSSKSVSTPSEAGS CCCCCCCCCCCCCCC	41.51	23927012
95 (in isoform 3)	Phosphorylation	-	28.78	30131370
95	Phosphorylation	PSSKSVSTPSEAGSQ CCCCCCCCCCCCCCC	28.78	23927012
95 (in isoform 6)	Phosphorylation	-	28.78	30131370
97	Phosphorylation	SKSVSTPSEAGSQDS CCCCCCCCCCCCCCC	39.92	23927012
98 (in isoform 3)	Phosphorylation	-	59.25	25849741
98 (in isoform 6)	Phosphorylation	-	59.25	25849741
99 (in isoform 7)	Phosphorylation	-	27.55	17081983
101	Phosphorylation	STPSEAGSQDSGDGA CCCCCCCCCCCCCCC	37.55	23927012
104 (in isoform 7)	Phosphorylation	-	31.01	29514088
104	Phosphorylation	SEAGSQDSGDGAVGS CCCCCCCCCCCCCCC	31.01	25159151
106 (in isoform 7)	Phosphorylation	-	45.92	22210691
107 (in isoform 7)	Phosphorylation	-	26.20	29514088
109 (in isoform 7)	Phosphorylation	-	9.76	22210691
111	Phosphorylation	SGDGAVGSRTLHWDT CCCCCCCCEEEECCC	18.59	23927012
113 (in isoform 7)	Phosphorylation	-	25.36	30131370
116 (in isoform 7)	Phosphorylation	-	17.20	25849741
118	Phosphorylation	SRTLHWDTDPSVLQL CEEEECCCCCHHEEE	44.62	30257219
121	Phosphorylation	LHWDTDPSVLQLHSD EECCCCCHHEEECCC	37.97	27732954
127	Phosphorylation	PSVLQLHSDSDLGRG CHHEEECCCCCCCCC	47.61	27732954
129	Ubiquitination	VLQLHSDSDLGRGPI HEEECCCCCCCCCCC	37.44	-
129	Phosphorylation	VLQLHSDSDLGRGPI HEEECCCCCCCCCCC	37.44	27732954
137	Ubiquitination	DLGRGPIKLGMAKIT CCCCCCCEEEEEEEE	41.96	-
160	O-linked_Glycosylation	IVTYTKETQTPVMAQ EEEEECCCCCCCCCC	39.02	23301498
162	Phosphorylation	TYTKETQTPVMAQPK EEECCCCCCCCCCCC	25.85	25159151
182	Acetylation	DDDVVAPKPPIEPEE CCCCCCCCCCCCHHH	54.40	26051181
182	Ubiquitination	DDDVVAPKPPIEPEE CCCCCCCCCCCCHHH	54.40	-
191	Ubiquitination	PIEPEEEKTLKKDEE CCCHHHHHCCCCCCC	63.54	-
192	Phosphorylation	IEPEEEKTLKKDEEN CCHHHHHCCCCCCCC	47.27	26657352
201	Phosphorylation	KKDEENDSKAPPHEL CCCCCCCCCCCCCCC	42.15	27251275
209	Phosphorylation	KAPPHELTEEEKQQI CCCCCCCCHHHHHHH	38.06	20071362
219	Phosphorylation	EKQQILHSEEFLSFF HHHHHHCCHHHHHHC	35.06	28348404
238	Phosphorylation	RIVERALSEQINIFF HHHHHHHHHHCCEEE	26.86	20068231
247	Phosphorylation	QINIFFDYSGRDLED HCCEEEECCCCCCCC	14.10	20068231
247	Ubiquitination	QINIFFDYSGRDLED HCCEEEECCCCCCCC	14.10	-
248	Phosphorylation	INIFFDYSGRDLEDK CCEEEECCCCCCCCC	29.24	20068231
255	Ubiquitination	SGRDLEDKEGEIQAG CCCCCCCCCCCCCCC	59.24	-
255	2-Hydroxyisobutyrylation	SGRDLEDKEGEIQAG CCCCCCCCCCCCCCC	59.24	-
264	Ubiquitination	GEIQAGAKLSLNRQF CCCCCCCEEEECHHH	37.38	-
269	Methylation	GAKLSLNRQFFDERW CCEEEECHHHHHHHH	39.72	-
422	Ubiquitination	LSHPQDSMELVHKQS HCCCHHHHHHHHHHH	6.59	-
427	Ubiquitination	DSMELVHKQSKAVAV HHHHHHHHHHCCEEE	49.11	-

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
Oops, there are no upstream regulatory protein records of DC1I2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
90	S	Phosphorylation		-
The phosphorylation status of Ser-90 appears to be involved in dynactin-dependent target binding.

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 DC1I2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYLT3_HUMAN	DYNLT3	physical	16189514
AKA12_HUMAN	AKAP12	physical	22863883
DDX1_HUMAN	DDX1	physical	22863883
DYHC1_HUMAN	DYNC1H1	physical	22863883
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3B_HUMAN	EIF3B	physical	22863883
EIFCL_HUMAN	EIF3CL	physical	22863883
EIF3K_HUMAN	EIF3K	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
YBOX1_HUMAN	YBX1	physical	22863883
DLRB1_HUMAN	DYNLRB1	physical	25416956
ADDA_HUMAN	ADD1	physical	26344197
ADDG_HUMAN	ADD3	physical	26344197
AHNK2_HUMAN	AHNAK2	physical	26344197
DCTN1_HUMAN	DCTN1	physical	26344197
DYHC1_HUMAN	DYNC1H1	physical	26344197
DC1L1_HUMAN	DYNC1LI1	physical	26344197
DC1L2_HUMAN	DYNC1LI2	physical	26344197
DLRB2_HUMAN	DYNLRB2	physical	26344197
PSA2_HUMAN	PSMA2	physical	26344197
PSA5_HUMAN	PSMA5	physical	26344197
PAPS1_HUMAN	PAPSS1	physical	28514442
DC1L2_HUMAN	DYNC1LI2	physical	28514442
DYHC1_HUMAN	DYNC1H1	physical	28514442
GNL1_HUMAN	GNL1	physical	28514442
LIS1_HUMAN	PAFAH1B1	physical	27173435
DYLT1_HUMAN	DYNLT1	physical	27173435

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 DC1I2_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-87 AND SER-104, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-94; THR-95;SER-101; SER-104 AND THR-162, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-94 AND SER-97, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-101, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.	17287340 [Abstract]
"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-87, AND MASSSPECTROMETRY.	15302935 [Abstract]

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