dbPTM

PHLA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PHLA2_HUMAN
UniProt AC	Q53GA4
Protein Name	Pleckstrin homology-like domain family A member 2
Gene Name	PHLDA2
Organism	Homo sapiens (Human).
Sequence Length	152
Subcellular Localization	Cytoplasm. Membrane Peripheral membrane protein.
Protein Description	Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids (By similarity)..
Protein Sequence	MKSPDEVLREGELEKRSDSLFQLWKKKRGVLTSDRLSLFPASPRARPKELRFHSILKVDCVERTGKYVYFTIVTTDHKEIDFRCAGESCWNAAIALALIDFQNRRALQDFRSRQERTAPAAPAEDAVAAAAAAPSEPSEPSRPSPQPKPRTP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Ubiquitination	------MKSPDEVLR ------CCCHHHHHH	71.36	21906983
3	Phosphorylation	-----MKSPDEVLRE -----CCCHHHHHHH	35.96	25159151
15	Ubiquitination	LREGELEKRSDSLFQ HHHCCHHHHCCHHHH	70.58	21906983
17	Phosphorylation	EGELEKRSDSLFQLW HCCHHHHCCHHHHHH	42.49	23898821
19	Phosphorylation	ELEKRSDSLFQLWKK CHHHHCCHHHHHHHH	32.12	27499020
25	Ubiquitination	DSLFQLWKKKRGVLT CHHHHHHHHHCCCCC	57.94	21906983
26	Ubiquitination	SLFQLWKKKRGVLTS HHHHHHHHHCCCCCC	35.80	22817900
27	Ubiquitination	LFQLWKKKRGVLTSD HHHHHHHHCCCCCCC	51.13	22817900
32	Phosphorylation	KKKRGVLTSDRLSLF HHHCCCCCCCCHHCC	26.61	22199227
33	Phosphorylation	KKRGVLTSDRLSLFP HHCCCCCCCCHHCCC	19.30	22199227
37	Phosphorylation	VLTSDRLSLFPASPR CCCCCCHHCCCCCCC	28.94	22199227
42	Phosphorylation	RLSLFPASPRARPKE CHHCCCCCCCCCCCH	18.37	29255136
54	Phosphorylation	PKELRFHSILKVDCV CCHHCCCEEEEEEEE	27.23	24719451
57	Ubiquitination	LRFHSILKVDCVERT HCCCEEEEEEEEEEC	34.06	21963094
66	Ubiquitination	DCVERTGKYVYFTIV EEEEECCCEEEEEEE	30.81	22817900
117	Phosphorylation	FRSRQERTAPAAPAE HHHHHHCCCCCCCHH	35.92	23403867
135	Phosphorylation	AAAAAAPSEPSEPSR HHHHHCCCCCCCCCC	58.37	28176443
138	Phosphorylation	AAAPSEPSEPSRPSP HHCCCCCCCCCCCCC	59.07	29255136
141	Phosphorylation	PSEPSEPSRPSPQPK CCCCCCCCCCCCCCC	53.42	29255136
144	Phosphorylation	PSEPSRPSPQPKPRT CCCCCCCCCCCCCCC	34.75	29255136
151	Phosphorylation	SPQPKPRTP------ CCCCCCCCC------	41.71	28176443

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 PHLA2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PHLA2_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 PHLA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PHLA2_HUMAN !!

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 PHLA2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-135; SER-138 ANDSER-141, AND MASS SPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-144 AND THR-151,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-42; SER-141 ANDSER-144, AND MASS SPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	16964243 [Abstract]