ADAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ADAP1_HUMAN
• UniProt AC: O75689
• Protein Name: Arf-GAP with dual PH domain-containing protein 1
• Gene Name: ADAP1
• Organism: Homo sapiens (Human).
• Sequence Length: 374
• Subcellular Localization: Nucleus. Cytoplasm. Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase.
• Protein Description: GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4)..
• Protein Sequence: MAKERRRAVLELLQRPGNARCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWEEAQVEFMASHGNDAARARFESKVPSFYYRPTPSDCQLLREQWIRAKYERQEFIYPEKQEPYSAGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHHWPHGITIVTPDRKFLFACETESDQREWVAAFQKAVDRPMLPQEYAVEAHFKHKP

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
51	Ubiquitination	CSGIHRNIPQVSKVK CCCHHCCCCCCCCCE	2.26	21906983
87	Phosphorylation	AARARFESKVPSFYY HHHHHHHHCCCCEEE	35.92	22817900
123	Ubiquitination	QEFIYPEKQEPYSAG HCCCCCCCCCCCCCC	56.29	21906983
134	Ubiquitination	YSAGYREGFLWKRGR CCCCCCCCCCEECCC	17.59	21906983
204	Phosphorylation	VTYLKDNSTRNIFIY EEEECCCCCCEEEEE	38.59	24719451
205	Phosphorylation	TYLKDNSTRNIFIYH EEECCCCCCEEEEEE	33.71	25849741
216	Ubiquitination	FIYHEDGKEIVDWFN EEEECCCHHHHHHHH	57.50	-
232	Phosphorylation	LRAARFHYLQVAFPG HHHHHCCEEEEECCC	8.98	-
272	Acetylation	KQTEGFRKRWFTMDD CCCCCCHHEEEECCC	52.28	19608861
276	Phosphorylation	GFRKRWFTMDDRRLM CCHHEEEECCCCEEE	16.84	14702039
283	Acetylation	TMDDRRLMYFKDPLD ECCCCEEEEECCHHH	3.33	19608861
284	Phosphorylation	MDDRRLMYFKDPLDA CCCCEEEEECCHHHH	16.45	27811184
329	Phosphorylation	PHGITIVTPDRKFLF CCCEEEECCCCCEEE	18.67	26091039
364	Phosphorylation	RPMLPQEYAVEAHFK CCCCCHHHHHHHHCC	15.65	-

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
87	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
87	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
87	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
87	S	Phosphorylation	Kinase	PKC	-	Uniprot
276	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
276	T	Phosphorylation	Kinase	PRKCE	Q02156	GPS
276	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
276	T	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ADAP1_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 ADAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KPCI_HUMAN	PRKCI	physical	12893243
KPCZ_HUMAN	PRKCZ	physical	12893243
PK3CA_HUMAN	PIK3CA	physical	12893243
KPCD1_HUMAN	PRKD1	physical	12893243
KC1A_HUMAN	CSNK1A1	physical	11278595
NUCL_HUMAN	NCL	physical	12565890
AN32A_HUMAN	ANP32A	physical	12565890
RANB9_HUMAN	RANBP9	physical	18298663
NUCL_HUMAN	NCL	physical	18298663
SDCB2_HUMAN	SDCBP2	physical	25416956

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

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Centaurin-alpha(1) associates with and is phosphorylated by isoformsof protein kinase C.";
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D.,Wakefield R.I.D., Johannes F.-J., Aitken A.;
Biochem. Biophys. Res. Commun. 307:459-465(2003).
Cited for: INTERACTION WITH PRKCA; PRKCI; PRKCZ AND PRKD1, AND PHOSPHORYLATION ATSER-87 AND THR-276.
PubMed: 12893243