dbPTM

DCTN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DCTN2_HUMAN
UniProt AC	Q13561
Protein Name	Dynactin subunit 2
Gene Name	DCTN2
Organism	Homo sapiens (Human).
Sequence Length	401
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Membrane Peripheral membrane protein .
Protein Description	Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development..
Protein Sequence	MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELTSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGEYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVLLAKQLAALKQQLVASHLEKLLGPDAAINLTDPDGALAKRLLLQLEATKNSKGGSGGKTTGTPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELETAVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQSKVHQLYETIQRWSPIASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMIANSLKDNTTLLTQVQTTMRENLATVEGNFASIDERMKKLGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADPKYADL ------CCCCCCCCC	41.64	22814378
5	Ubiquitination	---MADPKYADLPGI ---CCCCCCCCCCCC	54.33	-
6	Phosphorylation	--MADPKYADLPGIA --CCCCCCCCCCCCC	15.67	25159151
20	Phosphorylation	ARNEPDVYETSDLPE CCCCCCCCCCCCCCC	22.37	27642862
22	Phosphorylation	NEPDVYETSDLPEDD CCCCCCCCCCCCCCC	15.17	28348404
23	Phosphorylation	EPDVYETSDLPEDDQ CCCCCCCCCCCCCCC	25.80	29496963
54	Phosphorylation	IVNPNAAYDKFKDKR EECCCHHHHHHCCCC	19.77	-
64	Phosphorylation	FKDKRVGTKGLDFSD HCCCCCCCCCCCHHH	21.05	28857561
65	Ubiquitination	KDKRVGTKGLDFSDR CCCCCCCCCCCHHHH	52.10	-
65	Methylation	KDKRVGTKGLDFSDR CCCCCCCCCCCHHHH	52.10	-
70	Phosphorylation	GTKGLDFSDRIGKTK CCCCCCHHHHCCCCC	26.16	25159151
72	Methylation	KGLDFSDRIGKTKRT CCCCHHHHCCCCCCC	38.06	-
75	Phosphorylation	DFSDRIGKTKRTGYE CHHHHCCCCCCCCCC	48.80	24719451
79	Phosphorylation	RIGKTKRTGYESGEY HCCCCCCCCCCCCCE	45.75	21945579
81	Phosphorylation	GKTKRTGYESGEYEM CCCCCCCCCCCCEEE	13.30	21945579
83	Phosphorylation	TKRTGYESGEYEMLG CCCCCCCCCCEEECC	28.57	21945579
86	Phosphorylation	TGYESGEYEMLGEGL CCCCCCCEEECCCCC	15.34	21945579
88	Phosphorylation	YESGEYEMLGEGLGV CCCCCEEECCCCCCC	5.96	24719451
88	Sulfoxidation	YESGEYEMLGEGLGV CCCCCEEECCCCCCC	5.96	30846556
98	Phosphorylation	EGLGVKETPQQKYQR CCCCCCCCHHHHHHH	22.22	21712546
102	Ubiquitination	VKETPQQKYQRLLHE CCCCHHHHHHHHHHH	37.80	-
102	2-Hydroxyisobutyrylation	VKETPQQKYQRLLHE CCCCHHHHHHHHHHH	37.80	-
114	Phosphorylation	LHEVQELTTEVEKIK HHHHHHHHHHHHHHH	21.84	29496907
115	Phosphorylation	HEVQELTTEVEKIKT HHHHHHHHHHHHHHH	51.13	-
119	Ubiquitination	ELTTEVEKIKTTVKE HHHHHHHHHHHHHHH	55.46	-
125	Ubiquitination	EKIKTTVKESATEEK HHHHHHHHHHCCCCC	43.81	-
127	Phosphorylation	IKTTVKESATEEKLT HHHHHHHHCCCCCCH	34.47	25159151
129	Phosphorylation	TTVKESATEEKLTPV HHHHHHCCCCCCHHH	54.69	23186163
132	2-Hydroxyisobutyrylation	KESATEEKLTPVLLA HHHCCCCCCHHHHHH	51.97	-
134	Phosphorylation	SATEEKLTPVLLAKQ HCCCCCCHHHHHHHH	23.55	21815630
140	Ubiquitination	LTPVLLAKQLAALKQ CHHHHHHHHHHHHHH	45.90	21890473
140	Acetylation	LTPVLLAKQLAALKQ CHHHHHHHHHHHHHH	45.90	25953088
145 (in isoform 2)	Ubiquitination	-	4.24	-
145	Ubiquitination	LAKQLAALKQQLVAS HHHHHHHHHHHHHHH	4.24	21890473
145	Ubiquitination	LAKQLAALKQQLVAS HHHHHHHHHHHHHHH	4.24	21890473
146	Ubiquitination	AKQLAALKQQLVASH HHHHHHHHHHHHHHH	31.13	21890473
146	2-Hydroxyisobutyrylation	AKQLAALKQQLVASH HHHHHHHHHHHHHHH	31.13	-
146	Acetylation	AKQLAALKQQLVASH HHHHHHHHHHHHHHH	31.13	25953088
151 (in isoform 2)	Ubiquitination	-	10.38	-
151	Ubiquitination	ALKQQLVASHLEKLL HHHHHHHHHHHHHHH	10.38	21890473
151	Ubiquitination	ALKQQLVASHLEKLL HHHHHHHHHHHHHHH	10.38	21890473
152	Phosphorylation	LKQQLVASHLEKLLG HHHHHHHHHHHHHHC	22.56	-
156	Ubiquitination	LVASHLEKLLGPDAA HHHHHHHHHHCCCCC	56.20	-
175	Ubiquitination	DPDGALAKRLLLQLE CCCCHHHHHHHHHHH	44.41	21906983
180 (in isoform 2)	Ubiquitination	-	36.91	-
180	Ubiquitination	LAKRLLLQLEATKNS HHHHHHHHHHHHCCC	36.91	21890473
184	Phosphorylation	LLLQLEATKNSKGGS HHHHHHHHCCCCCCC	22.76	26074081
187	Phosphorylation	QLEATKNSKGGSGGK HHHHHCCCCCCCCCC	33.94	26074081
191	Phosphorylation	TKNSKGGSGGKTTGT HCCCCCCCCCCCCCC	53.71	26074081
195	Phosphorylation	KGGSGGKTTGTPPDS CCCCCCCCCCCCCCC	33.46	21945579
196	Phosphorylation	GGSGGKTTGTPPDSS CCCCCCCCCCCCCCC	42.41	21945579
198	Phosphorylation	SGGKTTGTPPDSSLV CCCCCCCCCCCCCCE	29.56	22167270
202	Phosphorylation	TTGTPPDSSLVTYEL CCCCCCCCCCEEEEE	31.20	21945579
203	Phosphorylation	TGTPPDSSLVTYELH CCCCCCCCCEEEEEC	33.95	21945579
206	Phosphorylation	PPDSSLVTYELHSRP CCCCCCEEEEECCCC	19.30	21945579
207	Phosphorylation	PDSSLVTYELHSRPE CCCCCEEEEECCCCC	14.71	21945579
211	Phosphorylation	LVTYELHSRPEQDKF CEEEEECCCCCCCHH	63.25	21945579
217	Ubiquitination	HSRPEQDKFSQAAKV CCCCCCCHHHHHHHH	46.76	-
219	Phosphorylation	RPEQDKFSQAAKVAE CCCCCHHHHHHHHHH	25.34	23312004
223	Ubiquitination	DKFSQAAKVAELEKR CHHHHHHHHHHHHHH	45.02	-
232	Phosphorylation	AELEKRLTELETAVR HHHHHHHHHHHHHHC	42.42	-
249	Phosphorylation	QDAQNPLSAGLQGAC HHHCCCHHHHHHHHH	22.88	-
260	Phosphorylation	QGACLMETVELLQAK HHHHHHHHHHHHHHH	12.81	20068231
269	Phosphorylation	ELLQAKVSALDLAVL HHHHHHHHHHHHHHH	23.54	30622161
285	Phosphorylation	QVEARLQSVLGKVNE HHHHHHHHHHHHHHH	24.73	23312004
289	Malonylation	RLQSVLGKVNEIAKH HHHHHHHHHHHHHHC	37.41	26320211
289	Ubiquitination	RLQSVLGKVNEIAKH HHHHHHHHHHHHHHC	37.41	-
295	Acetylation	GKVNEIAKHKASVED HHHHHHHHCCCCHHC	51.83	26210075
297	Ubiquitination	VNEIAKHKASVEDAD HHHHHHCCCCHHCHH	41.47	21906983
302	Ubiquitination	KHKASVEDADTQSKV HCCCCHHCHHHHHHH	47.81	21890473
308	Ubiquitination	EDADTQSKVHQLYET HCHHHHHHHHHHHHH	33.64	2190698
308	2-Hydroxyisobutyrylation	EDADTQSKVHQLYET HCHHHHHHHHHHHHH	33.64	-
308	Acetylation	EDADTQSKVHQLYET HCHHHHHHHHHHHHH	33.64	23236377
313	Phosphorylation	QSKVHQLYETIQRWS HHHHHHHHHHHHHHC	12.40	21945579
313	Ubiquitination	QSKVHQLYETIQRWS HHHHHHHHHHHHHHC	12.40	21890473
315	Phosphorylation	KVHQLYETIQRWSPI HHHHHHHHHHHHCCH	14.62	21945579
320	Phosphorylation	YETIQRWSPIASTLP HHHHHHHCCHHHHHH	14.49	15570572
324	Phosphorylation	QRWSPIASTLPELVQ HHHCCHHHHHHHHHH	31.06	26074081
325	Phosphorylation	RWSPIASTLPELVQR HHCCHHHHHHHHHHH	36.99	24719451
368	Phosphorylation	ANSLKDNTTLLTQVQ HHHCCCCHHHHHHHH	29.02	23403867
369	Phosphorylation	NSLKDNTTLLTQVQT HHCCCCHHHHHHHHH	26.48	23403867
372	Phosphorylation	KDNTTLLTQVQTTMR CCCHHHHHHHHHHHH	29.79	23403867
376	Phosphorylation	TLLTQVQTTMRENLA HHHHHHHHHHHHHHH	24.57	23403867
377	Phosphorylation	LLTQVQTTMRENLAT HHHHHHHHHHHHHHH	9.35	23403867
378	Sulfoxidation	LTQVQTTMRENLATV HHHHHHHHHHHHHHH	6.01	21406390

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 DCTN2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DCTN2_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 DCTN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNAO_HUMAN	GNAO1	physical	16169070
BICD2_HUMAN	BICD2	physical	11483508
MRP_HUMAN	MARCKSL1	physical	10827182
KCNA5_HUMAN	KCNA5	physical	16051887
DCTN3_HUMAN	DCTN3	physical	22939629
MCM4_HUMAN	MCM4	physical	22939629
MCM7_HUMAN	MCM7	physical	22939629
PRS6B_HUMAN	PSMC4	physical	22939629
RPB1_HUMAN	POLR2A	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
RANB9_HUMAN	RANBP9	physical	22939629
STRN4_HUMAN	STRN4	physical	22939629
DLRB1_HUMAN	DYNLRB1	physical	22939629
RPB4_HUMAN	POLR2D	physical	22939629
PRS7_HUMAN	PSMC2	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
HS90B_HUMAN	HSP90AB1	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
MCM6_HUMAN	MCM6	physical	22939629
TPM4_HUMAN	TPM4	physical	22939629
GA45A_HUMAN	GADD45A	physical	21988832
IMA1_HUMAN	KPNA2	physical	21988832
ARP10_HUMAN	ACTR10	physical	22863883
ACTZ_HUMAN	ACTR1A	physical	22863883
ACTY_HUMAN	ACTR1B	physical	22863883
LEO1_HUMAN	LEO1	physical	22863883
LMNB1_HUMAN	LMNB1	physical	22863883
NUP43_HUMAN	NUP43	physical	22863883
RABE1_HUMAN	RABEP1	physical	22863883
SEH1_HUMAN	SEH1L	physical	22863883
BICD2_HUMAN	BICD2	physical	22956769
DC1I1_HUMAN	DYNC1I1	physical	22956769
DCTN1_HUMAN	DCTN1	physical	22956769
DCTN2_HUMAN	DCTN2	physical	25416956
BL1S6_HUMAN	BLOC1S6	physical	25416956
HAUS1_HUMAN	HAUS1	physical	25416956
CC172_HUMAN	CCDC172	physical	25416956
ACTY_HUMAN	ACTR1B	physical	26186194
ACTZ_HUMAN	ACTR1A	physical	26186194
DCTN1_HUMAN	DCTN1	physical	26186194
DCTN3_HUMAN	DCTN3	physical	26186194
ARP10_HUMAN	ACTR10	physical	26186194
DCTN4_HUMAN	DCTN4	physical	26186194
EXD2_HUMAN	EXD2	physical	26186194
CC138_HUMAN	CCDC138	physical	26186194
DCTN5_HUMAN	DCTN5	physical	26186194
DCTN6_HUMAN	DCTN6	physical	26186194
FBX28_HUMAN	FBXO28	physical	26186194
KLHL2_HUMAN	KLHL2	physical	26186194
BORC6_HUMAN	C17orf59	physical	26186194
TRM1L_HUMAN	TRMT1L	physical	26186194
TRI11_HUMAN	TRIM11	physical	26186194
ARMC1_HUMAN	ARMC1	physical	26344197
CAPZB_HUMAN	CAPZB	physical	26344197
DCTN1_HUMAN	DCTN1	physical	26344197
DCTN5_HUMAN	DCTN5	physical	26344197
DYHC1_HUMAN	DYNC1H1	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
PRS4_HUMAN	PSMC1	physical	26344197
SMRC1_HUMAN	SMARCC1	physical	26344197
SMRC2_HUMAN	SMARCC2	physical	26344197
ACTY_HUMAN	ACTR1B	physical	28514442
ARP10_HUMAN	ACTR10	physical	28514442
KLHL2_HUMAN	KLHL2	physical	28514442
BORC6_HUMAN	C17orf59	physical	28514442
CC138_HUMAN	CCDC138	physical	28514442
DCTN4_HUMAN	DCTN4	physical	28514442
DCTN3_HUMAN	DCTN3	physical	28514442
DCTN5_HUMAN	DCTN5	physical	28514442
ACTZ_HUMAN	ACTR1A	physical	28514442
FBX28_HUMAN	FBXO28	physical	28514442
EXD2_HUMAN	EXD2	physical	28514442
DCTN1_HUMAN	DCTN1	physical	27173435
DCTN3_HUMAN	DCTN3	physical	27173435
DCTN6_HUMAN	DCTN6	physical	27173435
DCTN4_HUMAN	DCTN4	physical	27173435
DCTN5_HUMAN	DCTN5	physical	27173435
AHI1_HUMAN	AHI1	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 DCTN2_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-83, AND MASSSPECTROMETRY.	19690332 [Abstract]