DYLT1_HUMAN - dbPTM
DYLT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYLT1_HUMAN
UniProt AC P63172
Protein Name Dynein light chain Tctex-type 1
Gene Name DYNLT1
Organism Homo sapiens (Human).
Sequence Length 113
Subcellular Localization Golgi apparatus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Localizes to mitotic spindles..
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. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. May also be a accessory component of axonemal dynein.; Plays a role in neuronal morphogenesis; the function is independent of cytoplasmic dynein and seems to be coupled to regulation of the actin cytoskeleton by enhancing Rac1 activity. The function in neurogenesis may be regulated by association with a G-protein beta-gamma dimer. May function as a receptor-independent activator of heterotrimeric G-protein signaling; the activation appears to be independent of a nucleotide exchange. Plays a role in regulating neurogenesis; inhibits the genesis of neurons from precursor cells during cortical development presumably by antagonizing ARHGEF2. Involved in the regulation of mitotic spindle orientation (By similarity). Unrelated to the role in retrograde microtubule-associated movement may play a role in the dimerization of cytoplasmic proteins/domains such as for ACVR2B. Binds to the cytoplasmic domain of ACVR2B and, in vitro, inhibits ACVR2B signaling. [PubMed: 27502274; (Microbial infection) Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site.]
Protein Sequence MEDYQAAEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI
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
1Acetylation-------MEDYQAAE
-------CCCHHHHH
8.8022223895
4Phosphorylation----MEDYQAAEETA
----CCCHHHHHHHC
6.1725106551
10PhosphorylationDYQAAEETAFVVDEV
CHHHHHHHCEEHHHH
19.5325106551
18PhosphorylationAFVVDEVSNIVKEAI
CEEHHHHHHHHHHHH
20.8425867546
24UbiquitinationVSNIVKEAIESAIGG
HHHHHHHHHHHHHCC
12.7222817900
38UbiquitinationGNAYQHSKVNQWTTN
CCCCCCHHHCHHHHH
42.9821963094
42UbiquitinationQHSKVNQWTTNVVEQ
CCHHHCHHHHHHHHH
10.4523000965
45UbiquitinationKVNQWTTNVVEQTLS
HHCHHHHHHHHHHHH
28.5823000965
48UbiquitinationQWTTNVVEQTLSQLT
HHHHHHHHHHHHHHH
33.3023000965
56UbiquitinationQTLSQLTKLGKPFKY
HHHHHHHHCCCCCEE
64.9321890473
56UbiquitinationQTLSQLTKLGKPFKY
HHHHHHHHCCCCCEE
64.9323000965
59UbiquitinationSQLTKLGKPFKYIVT
HHHHHCCCCCEEEEE
58.6923000965
62UbiquitinationTKLGKPFKYIVTCVI
HHCCCCCEEEEEEEE
42.4623000965
79PhosphorylationKNGAGLHTASSCFWD
CCCCCEEEEEECEEC
33.02-
81PhosphorylationGAGLHTASSCFWDSS
CCCEEEEEECEECCC
28.88-
82PhosphorylationAGLHTASSCFWDSST
CCEEEEEECEECCCC
15.7422817900
94PhosphorylationSSTDGSCTVRWENKT
CCCCCCEEEEECCCC
18.1421394082

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 DYLT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DYLT1_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 DYLT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG3_HUMANBAG3physical
21252941
SODC_HUMANSOD1physical
21252941
A4_HUMANAPPphysical
21832049
YES_HUMANYES1physical
22939629
RAVR1_HUMANRAVER1physical
22939629
THIO_HUMANTXNphysical
21988832
TBA3C_HUMANTUBA3Cphysical
21988832
DYHC1_HUMANDYNC1H1physical
26344197
LMNA_HUMANLMNAphysical
26344197
LMNB2_HUMANLMNB2physical
26344197
PSA_HUMANNPEPPSphysical
26344197
SUMO3_HUMANSUMO3physical
26344197
AAK1_HUMANAAK1physical
26638075
ADDG_HUMANADD3physical
26638075
ARFG3_HUMANARFGAP3physical
26638075
ARFP1_HUMANARFIP1physical
26638075
RHG21_HUMANARHGAP21physical
26638075
BLM_HUMANBLMphysical
26638075
EMSY_HUMANC11orf30physical
26638075
CATIN_HUMANCACTINphysical
26638075
WDCP_HUMANC2orf44physical
26638075
CP110_HUMANCCP110physical
26638075
CDCA2_HUMANCDCA2physical
26638075
CHD8_HUMANCHD8physical
26638075
CIZ1_HUMANCIZ1physical
26638075
CKAP2_HUMANCKAP2physical
26638075
CPVL_HUMANCPVLphysical
26638075
CT2NL_HUMANCTTNBP2NLphysical
26638075
CUL4B_HUMANCUL4Bphysical
26638075
DCTN1_HUMANDCTN1physical
26638075
DNJB6_HUMANDNAJB6physical
26638075
DYST_HUMANDSTphysical
26638075
DVL2_HUMANDVL2physical
26638075
DYHC1_HUMANDYNC1H1physical
26638075
DC1I2_HUMANDYNC1I2physical
26638075
DC1L1_HUMANDYNC1LI1physical
26638075
DC1L2_HUMANDYNC1LI2physical
26638075
DLRB1_HUMANDYNLRB1physical
26638075
ELF2_HUMANELF2physical
26638075
TASOR_HUMANFAM208Aphysical
26638075
HECD1_HUMANHECTD1physical
26638075
K1671_HUMANKIAA1671physical
26638075
KLF12_HUMANKLF12physical
26638075
LIN54_HUMANLIN54physical
26638075
LRIF1_HUMANLRIF1physical
26638075
LUZP1_HUMANLUZP1physical
26638075
MA7D3_HUMANMAP7D3physical
26638075
GWL_HUMANMASTLphysical
26638075
KMT2A_HUMANKMT2Aphysical
26638075
MOC2B_HUMANMOCS2physical
26638075
MOC2A_HUMANMOCS2physical
26638075
GCR_HUMANNR3C1physical
26638075
NUFP2_HUMANNUFIP2physical
26638075
NUP50_HUMANNUP50physical
26638075
PKHA5_HUMANPLEKHA5physical
26638075
PMS1_HUMANPMS1physical
26638075
PP4C_HUMANPPP4Cphysical
26638075
RFIP1_HUMANRAB11FIP1physical
26638075
RPGF6_HUMANRAPGEF6physical
26638075
SP130_HUMANSAP130physical
26638075
TC1D2_HUMANTCTEX1D2physical
26638075
ASPP2_HUMANTP53BP2physical
26638075
WDR34_HUMANWDR34physical
26638075
WDR60_HUMANWDR60physical
26638075
ZN318_HUMANZNF318physical
26638075
ADDA_HUMANADD1physical
26638075
ARGL1_HUMANARGLU1physical
26638075
KNL1_HUMANCASC5physical
26638075
MPIP3_HUMANCDC25Cphysical
26638075
DGC14_HUMANDGCR14physical
26638075
ETFA_HUMANETFAphysical
26638075
ETFB_HUMANETFBphysical
26638075
EXOC4_HUMANEXOC4physical
26638075
GAB1_HUMANGAB1physical
26638075
HCFC1_HUMANHCFC1physical
26638075
IBTK_HUMANIBTKphysical
26638075
IQEC1_HUMANIQSEC1physical
26638075
KDM1A_HUMANKDM1Aphysical
26638075
TALD3_HUMANKIAA0586physical
26638075
MS18A_HUMANMIS18Aphysical
26638075
MTUS1_HUMANMTUS1physical
26638075
CND2_HUMANNCAPHphysical
26638075
NDEL1_HUMANNDEL1physical
26638075
NFRKB_HUMANNFRKBphysical
26638075
NRBP_HUMANNRBP1physical
26638075
OGT1_HUMANOGTphysical
26638075
MINT_HUMANSPENphysical
26638075
SYNRG_HUMANSYNRGphysical
26638075
TEX2_HUMANTEX2physical
26638075
WAPL_HUMANWAPALphysical
26638075
ZC3HE_HUMANZC3H14physical
26638075
ZBT21_HUMANZBTB21physical
26638075
TC1D2_HUMANTCTEX1D2physical
27173435
DYLT3_HUMANDYNLT3physical
27173435
DLRB1_HUMANDYNLRB1physical
27173435
DYHC1_HUMANDYNC1H1physical
27173435
LIS1_HUMANPAFAH1B1physical
27173435
ANM1_HUMANPRMT1physical
27173435
WDR34_HUMANWDR34physical
27173435
DLRB2_HUMANDYNLRB2physical
27173435
MARE2_HUMANMAPRE2physical
27173435
VIME_HUMANVIMphysical
27173435

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYLT1_HUMAN

loading...

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 MET-1, AND MASS SPECTROMETRY.

TOP