dbPTM

RALA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RALA_HUMAN
UniProt AC	P11233
Protein Name	Ras-related protein Ral-A
Gene Name	RALA
Organism	Homo sapiens (Human).
Sequence Length	206
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side. Cleavage furrow . Midbody, Midbody ring . Predominantly at the cell surface in the absence of LPA. In the presence of LPA, colocalizes with LPAR1 and LPAR2 in endocytic vesicles (PubMed:19306925). May
Protein Description	Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. [PubMed: 20005108 Key regulator of LPAR1 signaling and competes with GRK2 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells]
Protein Sequence	MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MAANKPKGQNSLAL -CCCCCCCCCCCCCC	74.80	33845483
11	Phosphorylation	NKPKGQNSLALHKVI CCCCCCCCCCCEEEE	13.71	30266825
16	Malonylation	QNSLALHKVIMVGSG CCCCCCEEEEEECCC	34.02	26320211
19	Sulfoxidation	LALHKVIMVGSGGVG CCCEEEEEECCCCCC	2.90	21406390
22	Phosphorylation	HKVIMVGSGGVGKSA EEEEEECCCCCCHHH	22.44	25159151
43	Phosphorylation	YDEFVEDYEPTKADS HHHHHHCCCCCCCHH	15.42	25884760
46	O-linked_Glycosylation	FVEDYEPTKADSYRK HHHCCCCCCCHHCCC	27.24	8858106
50	Phosphorylation	YEPTKADSYRKKVVL CCCCCCHHCCCEEEE	31.53	24719451
51	Phosphorylation	EPTKADSYRKKVVLD CCCCCHHCCCEEEEC	27.31	-
54	Ubiquitination	KADSYRKKVVLDGEE CCHHCCCEEEECCCE	28.69	22053931
75	Phosphorylation	DTAGQEDYAAIRDNY CCCCCCCHHHHHHCC	9.36	25884760
82	Phosphorylation	YAAIRDNYFRSGEGF HHHHHHCCEECCCCE	12.50	-
85	Phosphorylation	IRDNYFRSGEGFLCV HHHCCEECCCCEEEE	31.15	-
115	2-Hydroxyisobutyrylation	REQILRVKEDENVPF HHHHHCCCCCCCCCE	53.68	-
128	Ubiquitination	PFLLVGNKSDLEDKR CEEEECCHHHHCCHH	39.14	24816145
129	Phosphorylation	FLLVGNKSDLEDKRQ EEEECCHHHHCCHHC	51.97	23312004
134	Ubiquitination	NKSDLEDKRQVSVEE CHHHHCCHHCCCHHH	35.04	33845483
138	Phosphorylation	LEDKRQVSVEEAKNR HCCHHCCCHHHHHHH	18.57	25159151
143	Ubiquitination	QVSVEEAKNRAEQWN CCCHHHHHHHHHHHC	50.69	33845483
153	Phosphorylation	AEQWNVNYVETSAKT HHHHCCCEEECCHHH	8.72	22817900
159	Ubiquitination	NYVETSAKTRANVDK CEEECCHHHCCCHHH	38.01	23000965
159	Ubiquitination	NYVETSAKTRANVDK CEEECCHHHCCCHHH	38.01	21890473
166	2-Hydroxyisobutyrylation	KTRANVDKVFFDLMR HHCCCHHHHHHHHHH	36.34	-
179	Ubiquitination	MREIRARKMEDSKEK HHHHHHHHHHHHHHH	45.73	24816145
183	Phosphorylation	RARKMEDSKEKNGKK HHHHHHHHHHHHCHH	29.43	17540176
183	Dephosphorylation	RARKMEDSKEKNGKK HHHHHHHHHHHHCHH	29.43	17540176
194	Phosphorylation	NGKKKRKSLAKRIRE HCHHHHHHHHHHHHH	37.28	17540176
194	Dephosphorylation	NGKKKRKSLAKRIRE HCHHHHHHHHHHHHH	37.28	17540176
203	Methylation	AKRIRERCCIL---- HHHHHHHHCCC----	1.13	-
203	Geranylgeranylation	AKRIRERCCIL---- HHHHHHHHCCC----	1.13	1903399
203	Geranylgeranylation	AKRIRERCCIL---- HHHHHHHHCCC----	1.13	1903399

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
194	S	Phosphorylation	Kinase	AURKA	O14965	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TSC2_HUMAN	TSC2	physical	12842888
RBP1_HUMAN	RALBP1	physical	7673236
RBP1_HUMAN	RALBP1	physical	7623849
RBP1_HUMAN	RALBP1	physical	9422736
PLD1_HUMAN	PLD1	physical	9207251
PLD1_HUMAN	PLD1	physical	9688545
ARF1_HUMAN	ARF1	physical	9688545
ARF6_HUMAN	ARF6	physical	12509462
EXOC4_RAT	Exoc4	physical	11406615
EXOC3_RAT	Exoc3	physical	11406615
RBP1_RAT	Ralbp1	physical	11406615
PP2AA_HUMAN	PPP2CA	physical	17540176
2AAB_HUMAN	PPP2R1B	physical	17540176
PLCD1_HUMAN	PLCD1	physical	15817490
RAB34_HUMAN	RAB34	physical	24056301
LSM2_HUMAN	LSM2	physical	24056301
PIHD2_HUMAN	PIH1D2	physical	24056301
UBP33_HUMAN	USP33	physical	24056301
GLSL_HUMAN	GLS2	physical	11167825
ATP5J_HUMAN	ATP5J	physical	26496610
FLNB_HUMAN	FLNB	physical	26496610
ALAT1_HUMAN	GPT	physical	26496610
MCM5_HUMAN	MCM5	physical	26496610
ARK72_HUMAN	AKR7A2	physical	26496610
ZNHI3_HUMAN	ZNHIT3	physical	26496610
VPS4B_HUMAN	VPS4B	physical	26496610
CAPON_HUMAN	NOS1AP	physical	26496610
INT7_HUMAN	INTS7	physical	26496610
RHOF_HUMAN	RHOF	physical	26496610
CEP55_HUMAN	CEP55	physical	26496610
FBH1_HUMAN	FBXO18	physical	26496610
K2013_HUMAN	KIAA2013	physical	26496610
RBP1_HUMAN	RALBP1	physical	10364219

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 RALA_HUMAN

Related Literatures of Post-Translational Modification

Prenylation
Reference	PubMed
"Geranylgeranyltransferase I inhibitors target RalB to inhibitanchorage-dependent growth and induce apoptosis and RalA to inhibitanchorage-independent growth."; Falsetti S.C., Wang D.A., Peng H., Carrico D., Cox A.D., Der C.J.,Hamilton A.D., Sebti S.M.; Mol. Cell. Biol. 27:8003-8014(2007). Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION, ISOPRENYLATION AT CYS-203, ANDMUTAGENESIS OF CYS-203 AND LEU-206.	17875936 [Abstract]
"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteinsencoded by rac1, rac2, and ralA."; Kinsella B.T., Erdman R.A., Maltese W.A.; J. Biol. Chem. 266:9786-9794(1991). Cited for: ISOPRENYLATION AT CYS-203.	1903399 [Abstract]