DCTN3_HUMAN - dbPTM
DCTN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCTN3_HUMAN
UniProt AC O75935
Protein Name Dynactin subunit 3
Gene Name DCTN3 {ECO:0000312|EMBL:CAG46687.1}
Organism Homo sapiens (Human).
Sequence Length 186
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Cleavage furrow . Midbody . Localizes to punctate cytoplasmic structures and to the centrosome d
Protein Description Together with dynein may be involved in spindle assembly and cytokinesis..
Protein Sequence MAGLTDLQRLQARVEELERWVYGPGGARGSRKVADGLVKVQVALGNISSKRERVKILYKKIEDLIKYLDPEYIDRIAIPDASKLQFILAEEQFILSQVALLEQVNALVPMLDSAHIKAVPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAATQVKPAEE
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------MAGLTDLQR
------CCCCHHHHH
23.0022814378
5Phosphorylation---MAGLTDLQRLQA
---CCCCHHHHHHHH
33.4724043423
22PhosphorylationEELERWVYGPGGARG
HHHHHHHHCCCCCCC
15.6229496907
30PhosphorylationGPGGARGSRKVADGL
CCCCCCCHHHHCCCC
24.3124719451
32UbiquitinationGGARGSRKVADGLVK
CCCCCHHHHCCCCEE
43.3921906983
32 (in isoform 2)Ubiquitination-43.3921890473
32 (in isoform 1)Ubiquitination-43.3921890473
32 (in isoform 3)Ubiquitination-43.3921890473
50 (in isoform 2)Ubiquitination-52.0321890473
50 (in isoform 1)Ubiquitination-52.0321890473
50AcetylationALGNISSKRERVKIL
CCCCCCCHHHHHHHH
52.0325953088
50 (in isoform 3)Ubiquitination-52.0321890473
50UbiquitinationALGNISSKRERVKIL
CCCCCCCHHHHHHHH
52.0321890473
55 (in isoform 3)Ubiquitination-32.96-
55UbiquitinationSSKRERVKILYKKIE
CCHHHHHHHHHHHHH
32.96-
60 (in isoform 3)Ubiquitination-37.46-
60UbiquitinationRVKILYKKIEDLIKY
HHHHHHHHHHHHHHH
37.46-
66UbiquitinationKKIEDLIKYLDPEYI
HHHHHHHHHCCHHHH
47.24-
66 (in isoform 3)Ubiquitination-47.24-
67PhosphorylationKIEDLIKYLDPEYID
HHHHHHHHCCHHHHH
14.8930576142
72PhosphorylationIKYLDPEYIDRIAIP
HHHCCHHHHHHHCCC
17.3228152594
75MethylationLDPEYIDRIAIPDAS
CCHHHHHHHCCCCHH
15.64-
83 (in isoform 3)Ubiquitination-48.29-
120 (in isoform 3)Ubiquitination-32.30-
128 (in isoform 3)Ubiquitination-36.26-
148UbiquitinationVEITEESKALLEEYN
ECCCHHHHHHHHHHH
46.46-
154PhosphorylationSKALLEEYNKTTMLL
HHHHHHHHHHHHHHH
16.7522817900
156UbiquitinationALLEEYNKTTMLLSK
HHHHHHHHHHHHHHH
44.46-

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 DCTN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCTN3_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 DCTN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYLT3_HUMANDYNLT3physical
22939629
ARP10_HUMANACTR10physical
22863883
ACTZ_HUMANACTR1Aphysical
22863883
DCTN2_HUMANDCTN2physical
22863883
FLNB_HUMANFLNBphysical
22863883
CCAR2_HUMANCCAR2physical
22863883
LEO1_HUMANLEO1physical
22863883
LMNB1_HUMANLMNB1physical
22863883
TB182_HUMANTNKS1BP1physical
22863883
DCTN1_HUMANDCTN1physical
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 DCTN3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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