dbPTM

RBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBP1_HUMAN
UniProt AC	Q15311
Protein Name	RalA-binding protein 1
Gene Name	RALBP1
Organism	Homo sapiens (Human).
Sequence Length	655
Subcellular Localization	Membrane Peripheral membrane protein .
Protein Description	Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin..
Protein Sequence	MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSSESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAKAEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTECFLPPT ------CCCCCCCCC	41.27	28464451
2	Acetylation	------MTECFLPPT ------CCCCCCCCC	41.27	19413330
9	Phosphorylation	TECFLPPTSSPSEHR CCCCCCCCCCCCCCC	39.64	23401153
10	Phosphorylation	ECFLPPTSSPSEHRR CCCCCCCCCCCCCCC	46.13	29255136
11	Phosphorylation	CFLPPTSSPSEHRRV CCCCCCCCCCCCCCC	34.62	23401153
13	Phosphorylation	LPPTSSPSEHRRVEH CCCCCCCCCCCCCCC	48.24	29255136
22	Phosphorylation	HRRVEHGSGLTRTPS CCCCCCCCCCCCCCC	32.32	23898821
25	Phosphorylation	VEHGSGLTRTPSSEE CCCCCCCCCCCCCCC	35.70	23898821
27	Phosphorylation	HGSGLTRTPSSEEIS CCCCCCCCCCCCCCC	23.45	29255136
29	Phosphorylation	SGLTRTPSSEEISPT CCCCCCCCCCCCCCC	50.17	29255136
30	Phosphorylation	GLTRTPSSEEISPTK CCCCCCCCCCCCCCC	40.21	29255136
34	Phosphorylation	TPSSEEISPTKFPGL CCCCCCCCCCCCCCC	29.78	25159151
36	Phosphorylation	SSEEISPTKFPGLYR CCCCCCCCCCCCCCC	38.23	30278072
42	Phosphorylation	PTKFPGLYRTGEPSP CCCCCCCCCCCCCCC	16.43	23403867
44	Phosphorylation	KFPGLYRTGEPSPPH CCCCCCCCCCCCCCC	32.13	30266825
48	Phosphorylation	LYRTGEPSPPHDILH CCCCCCCCCCCCCCC	46.92	25159151
62	Phosphorylation	HEPPDVVSDDEKDHG CCCCCCCCCCCCCCC	38.91	29255136
82	Phosphorylation	FKKKEKRTEGYAAFQ CCCCCCCCCCCCCCC	44.84	23927012
85	Phosphorylation	KEKRTEGYAAFQEDS CCCCCCCCCCCCCCC	6.63	23927012
92	Phosphorylation	YAAFQEDSSGDEAES CCCCCCCCCCCCCCC	35.15	23927012
93	Phosphorylation	AAFQEDSSGDEAESP CCCCCCCCCCCCCCH	63.69	25159151
99	Phosphorylation	SSGDEAESPSKMKRS CCCCCCCCHHHCCCC	41.33	23927012
101	Phosphorylation	GDEAESPSKMKRSKG CCCCCCHHHCCCCCC	55.45	23927012
106	Phosphorylation	SPSKMKRSKGIHVFK CHHHCCCCCCEEEEC	29.71	23312004
116	Phosphorylation	IHVFKKPSFSKKKEK EEEECCCCCCCHHHH	51.54	21955146
118	Phosphorylation	VFKKPSFSKKKEKDF EECCCCCCCHHHHCC	48.15	21955146
147	Ubiquitination	KHKEEKHKEKKSKDL HHHHHHHHHHHHHCC	80.46	22817900
149	Ubiquitination	KEEKHKEKKSKDLTA HHHHHHHHHHHCCCH	68.12	22817900
150	Ubiquitination	EEKHKEKKSKDLTAA HHHHHHHHHHCCCHH	64.92	22817900
151	Phosphorylation	EKHKEKKSKDLTAAD HHHHHHHHHCCCHHH	42.33	23312004
152	Ubiquitination	KHKEKKSKDLTAADV HHHHHHHHCCCHHHH	66.68	21906983
161	Ubiquitination	LTAADVVKQWKEKKK CCHHHHHHHHHHHHC	50.73	23000965
164	Ubiquitination	ADVVKQWKEKKKKKK HHHHHHHHHHHCCCC	58.10	23000965
166	Ubiquitination	VVKQWKEKKKKKKPI HHHHHHHHHCCCCCC	67.19	23000965
167	Ubiquitination	VKQWKEKKKKKKPIQ HHHHHHHHCCCCCCC	71.55	23000965
201	Phosphorylation	LADAVERTMMYDGIR HHHHHHHHHHCCCCC	7.87	29978859
204	Phosphorylation	AVERTMMYDGIRLPA HHHHHHHCCCCCCCH	10.53	27642862
219	Phosphorylation	VFRECIDYVEKYGMK HHHHHHHHHHHHCCC	7.21	-
234	Phosphorylation	CEGIYRVSGIKSKVD CCEEEEECCHHHHHH	26.29	24719451
244	Ubiquitination	KSKVDELKAAYDREE HHHHHHHHHHHCCCC	28.99	29967540
252	Phosphorylation	AAYDREESTNLEDYE HHHCCCCCCCHHHCC	20.17	22817900
253	Phosphorylation	AYDREESTNLEDYEP HHCCCCCCCHHHCCH	47.29	22817900
258	Phosphorylation	ESTNLEDYEPNTVAS CCCCHHHCCHHHHHH	24.74	27642862
265	Phosphorylation	YEPNTVASLLKQYLR CCHHHHHHHHHHHHH	29.87	24719451
268	Ubiquitination	NTVASLLKQYLRDLP HHHHHHHHHHHHHCC	42.04	29967540
270	Phosphorylation	VASLLKQYLRDLPEN HHHHHHHHHHHCCHH	11.34	19413330
280	Phosphorylation	DLPENLLTKELMPRF HCCHHHCCHHHHHHH	26.16	19413330
281	Ubiquitination	LPENLLTKELMPRFE CCHHHCCHHHHHHHH	49.14	24816145
297	Phosphorylation	ACGRTTETEKVQEFQ HHCCCCCHHHHHHHH	38.73	22817900
299	Ubiquitination	GRTTETEKVQEFQRL CCCCCHHHHHHHHHH	57.55	29967540
353	Phosphorylation	LSPTVQISNRVLYVF ECCEEEECCCHHHHH	11.07	22817900
421	Ubiquitination	RDLQGGIKDLSKEER HHHCCCCCCCCHHHH	56.76	24816145
454	Ubiquitination	KRQECETKIAQEIAS HHHHHHHHHHHHHHH	17.47	-
461	Phosphorylation	KIAQEIASLSKEDVS HHHHHHHHCCHHHCC	38.55	30266825
463	Phosphorylation	AQEIASLSKEDVSKE HHHHHHCCHHHCCHH	31.35	19664994
468	Phosphorylation	SLSKEDVSKEEMNEN HCCHHHCCHHHHCCC	46.82	25850435
469	Ubiquitination	LSKEDVSKEEMNENE CCHHHCCHHHHCCCH	58.50	-
509	Phosphorylation	FLRRQIASEKEEIER HHHHHHHCCHHHHHH	51.32	22817900
511	Ubiquitination	RRQIASEKEEIERLR HHHHHCCHHHHHHHH	59.14	24816145
600	Ubiquitination	LLQMQRAKAEQQAQE HHHHHHHHHHHHHHH	55.43	29967540
632	Ubiquitination	VLEPKAAKEQPKAGK CCCHHHHHCCCCCCC	62.84	24816145
645	Phosphorylation	GKEPAKPSPSRDRKE CCCCCCCCCCCCCCC	34.50	23927012
647	Phosphorylation	EPAKPSPSRDRKETS CCCCCCCCCCCCCCC	51.67	30266825

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
118	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
297	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
353	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
509	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	PELI1	Q96FA3	PMID:19734906

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBP1_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 RBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCNB1_HUMAN	CCNB1	physical	12775724
HOOK2_HUMAN	HOOK2	physical	16189514
RALA_HUMAN	RALA	physical	14525976
RALB_HUMAN	RALB	physical	14525976
NUMB_HUMAN	NUMB	physical	12775724
TF3A_HUMAN	GTF3A	physical	12775724
EPN1_HUMAN	EPN1	physical	12775724
REPS2_HUMAN	REPS2	physical	9422736
RPB1_HUMAN	POLR2A	physical	22939629
GPSM1_HUMAN	GPSM1	physical	23718855
RALB_HUMAN	RALB	physical	21241894
GSE1_HUMAN	GSE1	physical	25416956
TFPT_HUMAN	TFPT	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
TBRG1_HUMAN	TBRG1	physical	25416956
CA216_HUMAN	C1orf216	physical	25416956
ZBT38_HUMAN	ZBTB38	physical	25416956
ZN707_HUMAN	ZNF707	physical	25416956
EPN1_HUMAN	EPN1	physical	20709745
EPN2_HUMAN	EPN2	physical	20709745
EPN3_HUMAN	EPN3	physical	20709745
REPS1_HUMAN	REPS1	physical	26344197
GPS2_HUMAN	GPS2	physical	21516116
CEP57_HUMAN	CEP57	physical	21516116
RALA_HUMAN	RALA	physical	25241761
TRAF2_HUMAN	TRAF2	physical	25241761
NEMO_HUMAN	IKBKG	physical	25241761
RALA_HUMAN	RALA	physical	10364219
REPS1_HUMAN	REPS1	physical	28514442
MSD4_HUMAN	MSANTD4	physical	28514442
REPS2_HUMAN	REPS2	physical	28514442
KIFC1_HUMAN	KIFC1	physical	28514442
SAPC2_HUMAN	SAPCD2	physical	28514442
GPS2_HUMAN	GPS2	physical	28514442
GOGA4_HUMAN	GOLGA4	physical	28514442
CCDC6_HUMAN	CCDC6	physical	28514442
PP4R1_HUMAN	PPP4R1	physical	28514442
SKI_HUMAN	SKI	physical	28514442
GCC1_HUMAN	GCC1	physical	28514442
CACO1_HUMAN	CALCOCO1	physical	28514442
JUND_HUMAN	JUND	physical	28514442
ANR26_HUMAN	ANKRD26	physical	28514442
JUN_HUMAN	JUN	physical	28514442
AAK1_HUMAN	AAK1	physical	28514442
PHLB3_HUMAN	PHLDB3	physical	28514442
BMP2K_HUMAN	BMP2K	physical	28514442
ZHANG_HUMAN	CREBZF	physical	28514442
CP250_HUMAN	CEP250	physical	28514442
SEP10_HUMAN	SEPT10	physical	28514442
CE164_HUMAN	CEP164	physical	28514442
GOPC_HUMAN	GOPC	physical	28514442
KIF7_HUMAN	KIF7	physical	28514442
HOOK3_HUMAN	HOOK3	physical	28514442
CROCC_HUMAN	CROCC	physical	28514442
RUFY1_HUMAN	RUFY1	physical	28514442
CBY1_HUMAN	CBY1	physical	28514442
TFPT_HUMAN	TFPT	physical	28514442
AP2A1_HUMAN	AP2A1	physical	28514442
CK5P2_HUMAN	CDK5RAP2	physical	28514442
ALBU_HUMAN	ALB	physical	28514442

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
DB00564	Carbamazepine
DB00997	Doxorubicin
DB00398	Sorafenib
DB00541	Vincristine

Regulatory Network of RBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-92; SER-93 ANDSER-645, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-29; SER-30;SER-34; SER-92; SER-93; TYR-270; THR-280 AND SER-463, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-62, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-29, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASSSPECTROMETRY.	17081983 [Abstract]