dbPTM

RAP2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAP2B_HUMAN
UniProt AC	P61225
Protein Name	Ras-related protein Rap-2b
Gene Name	RAP2B
Organism	Homo sapiens (Human).
Sequence Length	183
Subcellular Localization	Recycling endosome membrane Lipid-anchor Cytoplasmic side . Associated with red blood cells-released vesicles.
Protein Description	Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. Involved in EGFR and CHRM3 signaling pathways through stimulation of PLCE1. May play a role in cytoskeletal rearrangements and regulate cell spreading through activation of the effector TNIK. May regulate membrane vesiculation in red blood cells..
Protein Sequence	MREYKVVVLGSGGVGKSALTVQFVTGSFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYERVPMILVGNKVDLEGEREVSYGEGKALAEEWSCPFMETSAKNKASVDELFAEIVRQMNYAAQPNGDEGCCSACVIL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MREYKVVVLGS ----CCEEEEEEECC	9.94	-
5	Ubiquitination	---MREYKVVVLGSG ---CCEEEEEEECCC	24.65	23000965
11	Phosphorylation	YKVVVLGSGGVGKSA EEEEEECCCCCCCCE	28.36	20058876
17	Phosphorylation	GSGGVGKSALTVQFV CCCCCCCCEEEEEEE	23.68	20068231
25	Phosphorylation	ALTVQFVTGSFIEKY EEEEEEEECCHHHHC	28.53	28348404
27	Phosphorylation	TVQFVTGSFIEKYDP EEEEEECCHHHHCCC	17.43	28348404
31	Ubiquitination	VTGSFIEKYDPTIED EECCHHHHCCCCHHH	50.57	21987572
40	Phosphorylation	DPTIEDFYRKEIEVD CCCHHHHHHCCCCCC	32.85	-
42	Ubiquitination	TIEDFYRKEIEVDSS CHHHHHHCCCCCCCC	52.22	29901268
48	Phosphorylation	RKEIEVDSSPSVLEI HCCCCCCCCHHHHHH	49.69	28060719
49	Phosphorylation	KEIEVDSSPSVLEIL CCCCCCCCHHHHHHH	19.41	20068231
51	Phosphorylation	IEVDSSPSVLEILDT CCCCCCHHHHHHHHC	41.08	20068231
58	Phosphorylation	SVLEILDTAGTEQFA HHHHHHHCCCCHHHH	24.44	28060719
61	Phosphorylation	EILDTAGTEQFASMR HHHHCCCCHHHHHHH	24.93	30108239
66	Phosphorylation	AGTEQFASMRDLYIK CCCHHHHHHHHEEEE	18.68	30108239
71	Phosphorylation	FASMRDLYIKNGQGF HHHHHHEEEECCCEE	17.71	28270605
106	Phosphorylation	QIIRVKRYERVPMIL HEEEEEECEECCEEE	11.45	-
111	Sulfoxidation	KRYERVPMILVGNKV EECEECCEEEECCEE	3.19	21406390
117	Ubiquitination	PMILVGNKVDLEGER CEEEECCEECCCCCE	31.06	23503661
127	Phosphorylation	LEGEREVSYGEGKAL CCCCEEECCCCCHHH	23.75	20068231
128	Phosphorylation	EGEREVSYGEGKALA CCCEEECCCCCHHHH	25.11	20068231
132	Ubiquitination	EVSYGEGKALAEEWS EECCCCCHHHHHHHC	35.61	21963094
148	Ubiquitination	PFMETSAKNKASVDE CCCCCCCCCCCCHHH	59.76	22817900
150	Ubiquitination	METSAKNKASVDELF CCCCCCCCCCHHHHH	41.13	21906983
152	Phosphorylation	TSAKNKASVDELFAE CCCCCCCCHHHHHHH	31.54	27050516
166	Phosphorylation	EIVRQMNYAAQPNGD HHHHHCCCCCCCCCC	9.66	22817900
176	S-palmitoylation	QPNGDEGCCSACVIL CCCCCCCCCCEEEEC	1.23	18582561
177	S-palmitoylation	PNGDEGCCSACVIL- CCCCCCCCCEEEEC-	4.20	18582561
180	Methylation	DEGCCSACVIL---- CCCCCCEEEEC----	0.82	8424780
180	Geranylgeranylation	DEGCCSACVIL---- CCCCCCEEEEC----	0.82	8424780
180	Geranylgeranylation	DEGCCSACVIL---- CCCCCCEEEEC----	0.82	8424780

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 RAP2B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAP2B_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 RAP2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RUN3A_HUMAN	RUNDC3A	physical	16189514
RPGF2_HUMAN	RAPGEF2	physical	10934204
RUN3A_HUMAN	RUNDC3A	physical	25416956
RASF5_HUMAN	RASSF5	physical	25416956
TCPZ_HUMAN	CCT6A	physical	26344197
RIN1_HUMAN	RIN1	physical	27173435

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 RAP2B_HUMAN

Related Literatures of Post-Translational Modification

Prenylation
Reference	PubMed
"Prenyl group identification of rap2 proteins: a ras superfamilymember other than ras that is farnesylated."; Farrell F.X., Yamamoto K., Lapetina E.G.; Biochem. J. 289:349-355(1993). Cited for: ISOPRENYLATION AT CYS-180.	8424780 [Abstract]