DLRB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DLRB1_HUMAN
• UniProt AC: Q9NP97
• Protein Name: Dynein light chain roadblock-type 1
• Gene Name: DYNLRB1
• Organism: Homo sapiens (Human).
• Sequence Length: 96
• 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..
• Protein Sequence: MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE

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
2	Acetylation	------MAEVEETLK ------CHHHHHHHH	29.55	-
9	Ubiquitination	AEVEETLKRLQSQKG HHHHHHHHHHHHCCC	59.49	-
15	Ubiquitination	LKRLQSQKGVQGIIV HHHHHHCCCCCEEEE	67.31	20972266
15 (in isoform 1)	Ubiquitination	-	67.31	21890473
40	Phosphorylation	TMDNPTTTQYASLMH CCCCCCHHHHHHHHH	23.28	28348404
44	Phosphorylation	PTTTQYASLMHSFIL CCHHHHHHHHHHHHH	22.69	28348404
48	Phosphorylation	QYASLMHSFILKARS HHHHHHHHHHHHHHH	10.46	28348404
52	Ubiquitination	LMHSFILKARSTVRD HHHHHHHHHHHCCCC	36.62	21890473
52 (in isoform 1)	Ubiquitination	-	36.62	21890473
67	Phosphorylation	IDPQNDLTFLRIRSK CCCCCCEEEEEEEEC	24.40	21712546
73	Phosphorylation	LTFLRIRSKKNEIMV EEEEEEEECCCEEEE	45.68	-
75	Ubiquitination	FLRIRSKKNEIMVAP EEEEEECCCEEEECC	62.14	21906983
75 (in isoform 1)	Ubiquitination	-	62.14	21890473
84	Ubiquitination	EIMVAPDKDYFLIVI EEEECCCCCEEEEEE	53.95	2190698
84 (in isoform 1)	Ubiquitination	-	53.95	21890473
86	Phosphorylation	MVAPDKDYFLIVIQN EECCCCCEEEEEEEC	13.16	-

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
73	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DLRB1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DLRB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYHC1_HUMAN	DYNC1H1	physical	22939629
DYL1_HUMAN	DYNLL1	physical	22939629
FLNC_HUMAN	FLNC	physical	22939629
DYLT1_HUMAN	DYNLT1	physical	22939629
PLOD3_HUMAN	PLOD3	physical	22939629
SEPT2_HUMAN	SEPT2	physical	22939629
LTOR2_HUMAN	LAMTOR2	physical	22939629
SAFB1_HUMAN	SAFB	physical	22939629
RT26_HUMAN	MRPS26	physical	22939629
DC1I2_HUMAN	DYNC1I2	physical	22863883
DC1L1_HUMAN	DYNC1LI1	physical	22863883
DC1L2_HUMAN	DYNC1LI2	physical	22863883
TC1D2_HUMAN	TCTEX1D2	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.

Related Literatures of Post-Translational Modification

Acetylation

"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.
PubMed: 19413330