RAP1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAP1A_HUMAN
• UniProt AC: P62834
• Protein Name: Ras-related protein Rap-1A
• Gene Name: RAP1A
• Organism: Homo sapiens (Human).
• Sequence Length: 184
• Subcellular Localization: Cell membrane ; Lipid-anchor . Cytoplasm . Cytoplasm, perinuclear region . Cell junction. Early endosome. Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junc
• Protein Description: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions..
• Protein Sequence: MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL

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
5	Ubiquitination	---MREYKLVVLGSG ---CCEEEEEEECCC	30.01	21890473
11	Phosphorylation	YKLVVLGSGGVGKSA EEEEEECCCCCCCHH	28.36	25159151
17	Phosphorylation	GSGGVGKSALTVQFV CCCCCCCHHHHHHEE	23.68	20068231
31	Ubiquitination	VQGIFVEKYDPTIED EEEEEEEECCCCCCH	50.04	21890473
32	Phosphorylation	QGIFVEKYDPTIEDS EEEEEEECCCCCCHH	17.41	20860994
35	Phosphorylation	FVEKYDPTIEDSYRK EEEECCCCCCHHHHH	33.82	23403867
39	Phosphorylation	YDPTIEDSYRKQVEV CCCCCCHHHHHHCEE	17.66	23401153
40	Phosphorylation	DPTIEDSYRKQVEVD CCCCCHHHHHHCEEH	33.86	23403867
58	Phosphorylation	CMLEILDTAGTEQFT HHHHHHHHCCCHHHH	24.44	27732954
61	Phosphorylation	EILDTAGTEQFTAMR HHHHHCCCHHHHHHH	24.93	27732954
65	Phosphorylation	TAGTEQFTAMRDLYM HCCCHHHHHHHHHHH	21.16	27732954
88	Phosphorylation	VYSITAQSTFNDLQD EEEEEECCCCCCHHH	32.28	26657352
106	Phosphorylation	QILRVKDTEDVPMIL HHHCCCCCCCCCEEE	28.50	28555341
117	Ubiquitination	PMILVGNKCDLEDER CEEEECCCCCCCCCE	24.17	-
128	Ubiquitination	EDERVVGKEQGQNLA CCCEECCHHHHHHHH	34.94	-
149	Ubiquitination	AFLESSAKSKINVNE HHHHHHCCCCCCHHH	54.98	-
151	Ubiquitination	LESSAKSKINVNEIF HHHHCCCCCCHHHHH	37.28	-
159	Phosphorylation	INVNEIFYDLVRQIN CCHHHHHHHHHHHHH	17.65	25147952
168	Acetylation	LVRQINRKTPVEKKK HHHHHHHCCCCCCCC	53.33	27452117
180	Phosphorylation	KKKPKKKSCLLL--- CCCCCCCCCCCC---	20.90	9867809
181	Methylation	KKPKKKSCLLL---- CCCCCCCCCCC----	4.22	1899909
181	Geranylgeranylation	KKPKKKSCLLL---- CCCCCCCCCCC----	4.22	1899909
181	Geranylgeranylation	KKPKKKSCLLL---- CCCCCCCCCCC----	4.22	1899909

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
180	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
180	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
180	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAP1A_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 RAP1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TSC2_HUMAN	TSC2	physical	12842888
RUN3A_HUMAN	RUNDC3A	physical	9523700
AFAD_HUMAN	MLLT4	physical	10922060
GNDS_HUMAN	RALGDS	physical	10922060
RAF1_HUMAN	RAF1	physical	7862125
RAF1_HUMAN	RAF1	physical	7791872
RAF1_HUMAN	RAF1	physical	9867809
NTRK1_HUMAN	NTRK1	physical	11466412
RPGF2_HUMAN	RAPGEF2	physical	10934204
GBB1_HUMAN	GNB1	physical	20048162
RADIL_HUMAN	RADIL	physical	20048162
GDIR1_HUMAN	ARHGDIA	physical	26344197
CDC42_HUMAN	CDC42	physical	26344197
ECHM_HUMAN	ECHS1	physical	26344197
RAB5A_HUMAN	RAB5A	physical	26344197
RAB5B_HUMAN	RAB5B	physical	26344197
RAB5C_HUMAN	RAB5C	physical	26344197
RAB7A_HUMAN	RAB7A	physical	26344197
RAB8A_HUMAN	RAB8A	physical	26344197
RAB8B_HUMAN	RAB8B	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
BIN1_HUMAN	BIN1	physical	15207703
BMX_HUMAN	BMX	physical	15207703
SMCA2_HUMAN	SMARCA2	physical	15207703
TR10C_HUMAN	TNFRSF10C	physical	15207703
ELOA1_HUMAN	TCEB3	physical	15207703
FADD_HUMAN	FADD	physical	15207703
FAF1_HUMAN	FAF1	physical	15207703
TNR6_HUMAN	FAS	physical	15207703
HDAC1_HUMAN	HDAC1	physical	15207703
HSP74_HUMAN	HSPA4	physical	15207703
BRAF_HUMAN	BRAF	physical	16507992

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

Methylation

"The COOH-terminal domain of the Rap1A (Krev-1) protein isisoprenylated and supports transformation by an H-Ras:Rap1A chimericprotein.";
Buss J.E., Quilliam L.A., Kato K., Casey P.J., Solski P.A., Wong G.,Clark R., McCormick F., Bokoch G.M., Der C.J.;
Mol. Cell. Biol. 11:1523-1530(1991).
Cited for: ISOPRENYLATION AT CYS-181, AND METHYLATION AT CYS-181.
PubMed: 1899909

Prenylation

"The COOH-terminal domain of the Rap1A (Krev-1) protein isisoprenylated and supports transformation by an H-Ras:Rap1A chimericprotein.";
Buss J.E., Quilliam L.A., Kato K., Casey P.J., Solski P.A., Wong G.,Clark R., McCormick F., Bokoch G.M., Der C.J.;
Mol. Cell. Biol. 11:1523-1530(1991).
Cited for: ISOPRENYLATION AT CYS-181, AND METHYLATION AT CYS-181.
PubMed: 1899909