PRLD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PRLD1_HUMAN
• UniProt AC: Q9Y255
• Protein Name: PRELI domain-containing protein 1, mitochondrial
• Gene Name: PRELID1
• Organism: Homo sapiens (Human).
• Sequence Length: 219
• Subcellular Localization: Mitochondrion. Mitochondrion intermembrane space .
• Protein Description: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane. Regulates the mitochondrial apoptotic pathway in primary Th cells. Regulates Th cell differentiation by down-regulating STAT6 thereby reducing IL-4-induced Th2 cell number. May be important for the development of vital and immunocompetent organs..
• Protein Sequence: MVKYFLGQSVLRSSWDQVFAAFWQRYPNPYSKHVLTEDIVHREVTPDQKLLSRRLLTKTNRMPRWAERLFPANVAHSVYVLEDSIVDPQNQTMTTFTWNINHARLMVVEERCVYCVNSDNSGWTEIRREAWVSSSLFGVSRAVQEFGLARFKSNVTKTMKGFEYILAKLQGEAPSKTLVETAKEAKEKAKETALAATEKAKDLASKAATKKQQQQQQFV

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
4	Phosphorylation	----MVKYFLGQSVL ----CCCCCCCHHHH	7.82	-
9	Phosphorylation	VKYFLGQSVLRSSWD CCCCCCHHHHHHCHH	22.71	-
13	Phosphorylation	LGQSVLRSSWDQVFA CCHHHHHHCHHHHHH	31.46	-
14	Phosphorylation	GQSVLRSSWDQVFAA CHHHHHHCHHHHHHH	28.39	-
49	Ubiquitination	REVTPDQKLLSRRLL CCCCCCHHHHHHHHH	59.79	21906983
49	Ubiquitination	REVTPDQKLLSRRLL CCCCCCHHHHHHHHH	59.79	-
52	Phosphorylation	TPDQKLLSRRLLTKT CCCHHHHHHHHHHHC	26.28	-
57	Phosphorylation	LLSRRLLTKTNRMPR HHHHHHHHHCCCCCH	40.18	-
58	Ubiquitination	LSRRLLTKTNRMPRW HHHHHHHHCCCCCHH	43.71	27667366
118	Phosphorylation	RCVYCVNSDNSGWTE EEEEEECCCCCCCEE	20.12	22210691
152	Ubiquitination	EFGLARFKSNVTKTM HHCHHHHHCCCCHHH	35.25	27667366
157	Ubiquitination	RFKSNVTKTMKGFEY HHHCCCCHHHCHHHH	42.19	27667366
160	Ubiquitination	SNVTKTMKGFEYILA CCCCHHHCHHHHHHH	66.72	-
160	Ubiquitination	SNVTKTMKGFEYILA CCCCHHHCHHHHHHH	66.72	-
164	Phosphorylation	KTMKGFEYILAKLQG HHHCHHHHHHHHHCC	10.04	29496907
168	Ubiquitination	GFEYILAKLQGEAPS HHHHHHHHHCCCCCC	37.59	21906983
175	Phosphorylation	KLQGEAPSKTLVETA HHCCCCCCCCHHHHH	45.37	24670416
176	Ubiquitination	LQGEAPSKTLVETAK HCCCCCCCCHHHHHH	44.83	21906983
177	Phosphorylation	QGEAPSKTLVETAKE CCCCCCCCHHHHHHH	40.13	22210691
181	Phosphorylation	PSKTLVETAKEAKEK CCCCHHHHHHHHHHH	35.23	22210691
188	Ubiquitination	TAKEAKEKAKETALA HHHHHHHHHHHHHHH	65.14	33845483
190	Ubiquitination	KEAKEKAKETALAAT HHHHHHHHHHHHHHH	67.67	29967540
199	Ubiquitination	TALAATEKAKDLASK HHHHHHHHHHHHHHH	57.28	33845483
200	Ubiquitination	ALAATEKAKDLASKA HHHHHHHHHHHHHHH	12.36	29967540
211	Ubiquitination	ASKAATKKQQQQQQF HHHHHHHHHHHHHHC	49.32	29967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PRLD1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PRLD1_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 PRLD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIA1_HUMAN	TRIAP1	physical	26186194
PRLD1_HUMAN	PRELID1	physical	27499296
TRIA1_HUMAN	TRIAP1	physical	27499296
STML2_HUMAN	STOML2	physical	27499296
ADCK1_HUMAN	ADCK1	physical	27499296
STAR7_HUMAN	STARD7	physical	27499296

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.