DCTN2_MOUSE - dbPTM
DCTN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCTN2_MOUSE
UniProt AC Q99KJ8
Protein Name Dynactin subunit 2
Gene Name Dctn2
Organism Mus musculus (Mouse).
Sequence Length 402
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 MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGDYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQNKVHQLYETIQRWSPVASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKRLGK
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 Orthologous
Protein Cluster
2Acetylation------MADPKYADL
------CCCCCCCCC		41.64-
6Phosphorylation--MADPKYADLPGIA
--CCCCCCCCCCCCC		15.6729514104
23PhosphorylationEPDVYETSDLPEDDQ
CCCCCCCCCCCCCCC		25.8025338131
42PhosphorylationAEELSSTSVEHIIVN
HHHHCCCCCEEEEEC		27.7025338131
70PhosphorylationGTKGLDFSDRIGKTK
CCCCCCHHHHCCCCC		26.16-
79PhosphorylationRIGKTKRTGYESGDY
HCCCCCCCCCCCCCC		45.7528833060
81PhosphorylationGKTKRTGYESGDYEM
CCCCCCCCCCCCCHH		13.3028833060
83PhosphorylationTKRTGYESGDYEMLG
CCCCCCCCCCCHHCC		28.6021082442
86PhosphorylationTGYESGDYEMLGEGL
CCCCCCCCHHCCCCC		13.5318034455
114PhosphorylationLHEVQELTTEVEKIK
HHHHHHHHHHHHHHH		21.8428576409
115PhosphorylationHEVQELTTEVEKIKT
HHHHHHHHHHHHHHH		51.1328576409
132UbiquitinationKESATEEKLTPVVLA
HHHCCCCCCHHHHHH		51.97-
134PhosphorylationSATEEKLTPVVLAKQ
HCCCCCCHHHHHHHH		25.71-
140SuccinylationLTPVVLAKQLAALKQ
CHHHHHHHHHHHHHH		41.5023806337
140AcetylationLTPVVLAKQLAALKQ
CHHHHHHHHHHHHHH		41.5023806337
140UbiquitinationLTPVVLAKQLAALKQ
CHHHHHHHHHHHHHH		41.50-
146AcetylationAKQLAALKQQLVASH
HHHHHHHHHHHHHHH		31.1322826441
175UbiquitinationDPDGALAKRLLLQLE
CCCCHHHHHHHHHHH		44.41-
220PhosphorylationRPEQDKFSQAAKVAE
CCCCCHHHHHHHHHH		25.3418779572
270PhosphorylationELLQAKVSALDLAVL
HHHHHHHHHHHHHHH		23.54-
300PhosphorylationEIAKHKASVEDADTQ
HHHHCCCCHHCHHHH		30.7325521595
314PhosphorylationQNKVHQLYETIQRWS
HHHHHHHHHHHHHHC		12.4025367039
316PhosphorylationKVHQLYETIQRWSPV
HHHHHHHHHHHHCCH		14.6223984901
321PhosphorylationYETIQRWSPVASTLP
HHHHHHHCCHHHHHH		16.2221082442
325PhosphorylationQRWSPVASTLPELVQ
HHHCCHHHHHHHHHH		30.6121183079
326PhosphorylationRWSPVASTLPELVQR
HHCCHHHHHHHHHHH		36.2718779572
373PhosphorylationKDNTALLTQVQTTMR
CHHHHHHHHHHHHHH		27.7829899451
378PhosphorylationLLTQVQTTMRENLAT
HHHHHHHHHHHHHHC		9.3529899451
385PhosphorylationTMRENLATVEGNFAS
HHHHHHHCCCCCCHH		23.4330635358
392PhosphorylationTVEGNFASIDARMKR
CCCCCCHHHHHHHHH		19.5022817900
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCTN2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHCBP_HUMANSHCBP1physical
20360068
DCTN5_HUMANDCTN5physical
20360068
KLHL2_HUMANKLHL2physical
20360068
ARP10_HUMANACTR10physical
20360068
DCTN2_HUMANDCTN2physical
20360068
KIF23_HUMANKIF23physical
20360068
DCTN6_HUMANDCTN6physical
20360068
DCTN4_HUMANDCTN4physical
20360068
DCTN1_HUMANDCTN1physical
20360068
ACTY_HUMANACTR1Bphysical
20360068
DCTN3_HUMANDCTN3physical
20360068
ACTZ_HUMANACTR1Aphysical
20360068
CAZA1_HUMANCAPZA1physical
26496610
CAZA2_HUMANCAPZA2physical
26496610
CAPZB_HUMANCAPZBphysical
26496610
DCTN1_HUMANDCTN1physical
26496610
TYB4_HUMANTMSB4Xphysical
26496610
EEA1_HUMANEEA1physical
26496610
ACTY_HUMANACTR1Bphysical
26496610
ACTZ_HUMANACTR1Aphysical
26496610
DCTN6_HUMANDCTN6physical
26496610
DCTN3_HUMANDCTN3physical
26496610
DCTN4_HUMANDCTN4physical
26496610
GOLM1_HUMANGOLM1physical
26496610
ARP10_HUMANACTR10physical
26496610
DCTN5_HUMANDCTN5physical
26496610
TRI47_HUMANTRIM47physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCTN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-86, AND MASSSPECTROMETRY.

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