DOC2A_HUMAN - dbPTM
DOC2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DOC2A_HUMAN
UniProt AC Q14183
Protein Name Double C2-like domain-containing protein alpha
Gene Name DOC2A
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Lysosome. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Peripheral membrane protein . Cell junction, synapse, synaptosome. Colocalizes to synaptic vesicles.
Protein Description Calcium sensor which most probably regulates fusion of vesicles with membranes. Binds calcium and phospholipids. May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in calcium-dependent spontaneous release of neurotransmitter in absence of action potentials in neuronal cells. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells..
Protein Sequence MRGRRGDRMTINIQEHMAINVCPGPIRPIRQISDYFPRGPGPEGGGGGGGEAPAHLVPLALAPPAALLGATTPEDGAEVDSYDSDDATALGTLEFDLLYDRASCTLHCSILRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTQRNTLNPVWNEDLTYSGITDDDITHKVLRIAVCDEDKLSHNEFIGEIRVPLRRLKPSQKKHFNICLERQVPLASPSSMSAALRGISCYLKELEQAEQGQGLLEERGRILLSLSYSSRRRGLLVGILRCAHLAAMDVNGYSDPYVKTYLRPDVDKKSKHKTCVKKKTLNPEFNEEFFYEIELSTLATKTLEVTVWDYDIGKSNDFIGGVSLGPGARGEARKHWSDCLQQPDAALERWHTLTSELPPAAGALSSA
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
139UbiquitinationHLLPGACKANKLKTK
HCCCCCHHHCCCCCC
55.2329967540
162PhosphorylationVWNEDLTYSGITDDD
CCCCCCCCCCCCCHH
16.5227642862
171PhosphorylationGITDDDITHKVLRIA
CCCCHHHHHEEEEEE
23.73-
204PhosphorylationPLRRLKPSQKKHFNI
CHHHCCHHHCCCEEE
53.7130631047
221PhosphorylationERQVPLASPSSMSAA
ECCCCCCCHHHHHHH
32.7629978859
223PhosphorylationQVPLASPSSMSAALR
CCCCCCHHHHHHHHH
35.8629978859
224PhosphorylationVPLASPSSMSAALRG
CCCCCHHHHHHHHHH
21.8229978859
226PhosphorylationLASPSSMSAALRGIS
CCCHHHHHHHHHHHH
16.6129978859
233PhosphorylationSAALRGISCYLKELE
HHHHHHHHHHHHHHH
10.2628555341
258PhosphorylationERGRILLSLSYSSRR
HHCEEEEEECCHHHH
16.3029759185
260PhosphorylationGRILLSLSYSSRRRG
CEEEEEECCHHHHCC
21.4229759185
262PhosphorylationILLSLSYSSRRRGLL
EEEEECCHHHHCCHH
17.6229759185
263PhosphorylationLLSLSYSSRRRGLLV
EEEECCHHHHCCHHH
22.9029759185
294PhosphorylationSDPYVKTYLRPDVDK
CCHHHHHHCCCCCCC
8.59-
313PhosphorylationKTCVKKKTLNPEFNE
CCCCCCCCCCHHHCH
40.42-
329PhosphorylationFFYEIELSTLATKTL
HEEEEEHHHCCCCEE
14.48-
333PhosphorylationIELSTLATKTLEVTV
EEHHHCCCCEEEEEE
27.89-

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 DOC2A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DOC2A_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 DOC2A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UN13B_HUMANUNC13Bphysical
9195900
UN13B_HUMANUNC13Bphysical
9736751
GDS1_HUMANRAP1GDS1physical
24722188
UBS3B_HUMANUBASH3Bphysical
24722188
TT21B_HUMANTTC21Bphysical
26186194
DOC2B_HUMANDOC2Bphysical
26186194
UBS3B_HUMANUBASH3Bphysical
26186194
KCD21_HUMANKCTD21physical
26186194
DOC2B_HUMANDOC2Bphysical
28514442
TT21B_HUMANTTC21Bphysical
28514442
KCD21_HUMANKCTD21physical
28514442
UBS3B_HUMANUBASH3Bphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DOC2A_HUMAN

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Related Literatures of Post-Translational Modification

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