dbPTM

RALB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RALB_HUMAN
UniProt AC	P11234
Protein Name	Ras-related protein Ral-B
Gene Name	RALB
Organism	Homo sapiens (Human).
Sequence Length	206
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Midbody . During late cytokinesis, enriched at the midbody.
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 (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis. [PubMed: 17875936 In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission]
Protein Sequence	MAANKSKGQSSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEHESFTATAEFREQILRVKAEEDKIPLLVVGNKSDLEERRQVPVEEARSKAEEWGVQYVETSAKTRANVDKVFFDLMREIRTKKMSENKDKNGKKSSKNKKSFKERCCLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAANKSKGQSSLA --CCCCCCCCCCCHH	41.65	28857561
7	Ubiquitination	-MAANKSKGQSSLAL -CCCCCCCCCCCHHC	63.68	-
10	Phosphorylation	ANKSKGQSSLALHKV CCCCCCCCCHHCEEE	35.67	23312004
11	Phosphorylation	NKSKGQSSLALHKVI CCCCCCCCHHCEEEE	15.13	23312004
20 (in isoform 2)	Phosphorylation	-	3.66	22210691
21 (in isoform 2)	Phosphorylation	-	11.82	22210691
22	Phosphorylation	HKVIMVGSGGVGKSA EEEEEECCCCCCHHH	22.44	25159151
43	Phosphorylation	YDEFVEDYEPTKADS HHHHHHCCCCCCCHH	15.42	25884760
47	Ubiquitination	VEDYEPTKADSYRKK HHCCCCCCCHHCCCE	61.99	-
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
76	Ubiquitination	TAGQEDYAAIRDNYF CCCCCCHHHHHHCCE	14.56	-
82	Phosphorylation	YAAIRDNYFRSGEGF HHHHHHCCEECCCCE	12.50	-
85	Phosphorylation	IRDNYFRSGEGFLLV HHHCCEECCCCEEEE	31.15	-
104	Phosphorylation	EHESFTATAEFREQI CCCCCEECHHHHHHH	24.54	-
120	Ubiquitination	RVKAEEDKIPLLVVG HHHCCCCCCCEEEEC	49.88	-
129	Ubiquitination	PLLVVGNKSDLEERR CEEEECCHHHHHHHH	39.14	-
146	Ubiquitination	PVEEARSKAEEWGVQ CHHHHHHHHHHHCCE	55.02	-
154	Phosphorylation	AEEWGVQYVETSAKT HHHHCCEEEECCCCC	9.61	-
160	Ubiquitination	QYVETSAKTRANVDK EEEECCCCCCCCHHH	38.01	21906983
179	Acetylation	LMREIRTKKMSENKD HHHHHHHHHHHCCCC	36.31	71195
180	Acetylation	MREIRTKKMSENKDK HHHHHHHHHHCCCCC	47.23	7303101
182	Ubiquitination	EIRTKKMSENKDKNG HHHHHHHHCCCCCCC	47.07	-
190	Acetylation	ENKDKNGKKSSKNKK CCCCCCCCCCCCCHH	59.90	71199
198	Phosphorylation	KSSKNKKSFKERCCL CCCCCHHCHHHHHCC	43.06	20940393
203	Methylation	KKSFKERCCLL---- HHCHHHHHCCC----	1.69	-
203	Geranylgeranylation	KKSFKERCCLL---- HHCHHHHHCCC----	1.69	17875936
203	Geranylgeranylation	KKSFKERCCLL---- HHCHHHHHCCC----	1.69	17875936

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
198	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
198	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBP1_HUMAN	RALBP1	physical	16189514
EXOC8_HUMAN	EXOC8	physical	14525976
RBP1_HUMAN	RALBP1	physical	7673236
UBP33_HUMAN	USP33	physical	24056301
EXOC2_HUMAN	EXOC2	physical	24056301
EXOC8_HUMAN	EXOC8	physical	24056301
EXOC8_HUMAN	EXOC8	physical	21241894
ULK1_HUMAN	ULK1	physical	21241894
BAKOR_HUMAN	ATG14	physical	21241894
UVRAG_HUMAN	UVRAG	physical	21241894
EXOC2_HUMAN	EXOC2	physical	21241894
TPP2_HUMAN	TPP2	physical	28514442
MK14_HUMAN	MAPK14	physical	28514442
AMD_HUMAN	PAM	physical	28514442
P5CS_HUMAN	ALDH18A1	physical	28514442
AN13A_HUMAN	ANKRD13A	physical	28514442
ODB2_HUMAN	DBT	physical	28514442
XPO5_HUMAN	XPO5	physical	28514442
EXOC2_HUMAN	EXOC2	physical	27173435
HAUS4_HUMAN	HAUS4	physical	27173435
OCAD1_HUMAN	OCIAD1	physical	27173435
EI24_HUMAN	EI24	physical	27173435
HAUS1_HUMAN	HAUS1	physical	27173435
EXOC3_HUMAN	EXOC3	physical	27173435
EXOC1_HUMAN	EXOC1	physical	27173435
EXOC4_HUMAN	EXOC4	physical	27173435
EXOC8_HUMAN	EXOC8	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 RALB_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]