DYL2_HUMAN - dbPTM
DYL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYL2_HUMAN
UniProt AC Q96FJ2
Protein Name Dynein light chain 2, cytoplasmic
Gene Name DYNLL2
Organism Homo sapiens (Human).
Sequence Length 89
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. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity)..
Protein Sequence MSDRKAVIKNADMSEDMQQDAVDCATQAMEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
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
5Acetylation---MSDRKAVIKNAD
---CCCHHHHHHCCC		52.5819608861
5Ubiquitination---MSDRKAVIKNAD
---CCCHHHHHHCCC		52.5822817900
9AcetylationSDRKAVIKNADMSED
CCHHHHHHCCCCCHH		39.2125953088
9MalonylationSDRKAVIKNADMSED
CCHHHHHHCCCCCHH		39.2126320211
9UbiquitinationSDRKAVIKNADMSED
CCHHHHHHCCCCCHH		39.2122817900
14PhosphorylationVIKNADMSEDMQQDA
HHHCCCCCHHHHHHH		30.8728176443
26PhosphorylationQDAVDCATQAMEKYN
HHHHHHHHHHHHHCC		24.1628176443
31UbiquitinationCATQAMEKYNIEKDI
HHHHHHHHCCCHHHH		30.4323000965
31AcetylationCATQAMEKYNIEKDI
HHHHHHHHCCCHHHH		30.4325038526
32PhosphorylationATQAMEKYNIEKDIA
HHHHHHHCCCHHHHH		14.2028152594
36AcetylationMEKYNIEKDIAAYIK
HHHCCCHHHHHHHHH		51.1123954790
36UbiquitinationMEKYNIEKDIAAYIK
HHHCCCHHHHHHHHH		51.1123000965
41PhosphorylationIEKDIAAYIKKEFDK
CHHHHHHHHHHHHHC		12.3028152594
43UbiquitinationKDIAAYIKKEFDKKY
HHHHHHHHHHHHCCC		33.3123000965
44UbiquitinationDIAAYIKKEFDKKYN
HHHHHHHHHHHCCCC		54.8023000965
48UbiquitinationYIKKEFDKKYNPTWH
HHHHHHHCCCCCCCE		63.5823000965
49UbiquitinationIKKEFDKKYNPTWHC
HHHHHHCCCCCCCEE		52.7023000965
49SumoylationIKKEFDKKYNPTWHC
HHHHHHCCCCCCCEE		52.70-
49SumoylationIKKEFDKKYNPTWHC
HHHHHHCCCCCCCEE		52.70-
49MethylationIKKEFDKKYNPTWHC
HHHHHHCCCCCCCEE		52.70-
50PhosphorylationKKEFDKKYNPTWHCI
HHHHHCCCCCCCEEE		31.9228152594
53PhosphorylationFDKKYNPTWHCIVGR
HHCCCCCCCEEEECC		24.9728857561
64PhosphorylationIVGRNFGSYVTHETK
EECCCCHHHCCCCHH		16.5828152594
65PhosphorylationVGRNFGSYVTHETKH
ECCCCHHHCCCCHHH		15.1125159151
67PhosphorylationRNFGSYVTHETKHFI
CCCHHHCCCCHHHHH		13.0325884760
70PhosphorylationGSYVTHETKHFIYFY
HHHCCCCHHHHHHEE		23.3923186163
88PhosphorylationVAILLFKSG------
HHHHHHHCC------		42.2628112733
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 DYL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYL2_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 DYL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLGP1_HUMANDLGAP1physical
10844022
MYO5A_HUMANMYO5Aphysical
10844022
DLG4_HUMANDLG4physical
10844022
DLG2_HUMANDLG2physical
10844022
BMF_HUMANBMFphysical
14561217
B2L11_HUMANBCL2L11physical
14561217
DYL2_HUMANDYNLL2physical
14561217
BMF_HUMANBMFphysical
11546872
PAK1_HUMANPAK1physical
21988832
MORN3_HUMANMORN3physical
25416956
CL040_HUMANC12orf40physical
25416956
IHO1_HUMANCCDC36physical
25416956
PCBP1_HUMANPCBP1physical
26344197
SKAP1_HUMANSKAP1physical
21516116
WDR34_HUMANWDR34physical
27173435
RN214_HUMANRNF214physical
27173435
NRF1_HUMANNRF1physical
27173435
MORC3_HUMANMORC3physical
27173435
GEPH_HUMANGPHNphysical
27173435
GLYM_HUMANSHMT2physical
27173435
CIZ1_HUMANCIZ1physical
27173435
NEK9_HUMANNEK9physical
27173435
PAPD1_HUMANMTPAPphysical
27173435
TLK2_HUMANTLK2physical
27173435
DBLOH_HUMANDIABLOphysical
27173435
XIAP_HUMANXIAPphysical
27173435
DDHD1_HUMANDDHD1physical
27173435
EPN4_HUMANCLINT1physical
27173435
AMOT_HUMANAMOTphysical
27173435
AMRA1_HUMANAMBRA1physical
27173435
SKP1_HUMANSKP1physical
27173435
DC1I2_HUMANDYNC1I2physical
27173435
WDR60_HUMANWDR60physical
27173435
OFD1_HUMANOFD1physical
27173435
RAF1_HUMANRAF1physical
27173435
FTM_HUMANRPGRIP1Lphysical
27173435
DZAN1_HUMANDZANK1physical
27173435
PP1B_HUMANPPP1CBphysical
27173435
DYLT1_HUMANDYNLT1physical
27173435
SSNA1_HUMANSSNA1physical
27173435
LCA5_HUMANLCA5physical
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 DYL2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND MASS SPECTROMETRY.

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