dbPTM

RBM4B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM4B_HUMAN
UniProt AC	Q9BQ04
Protein Name	RNA-binding protein 4B
Gene Name	RBM4B
Organism	Homo sapiens (Human).
Sequence Length	359
Subcellular Localization	Nucleus. Nucleus, nucleolus.
Protein Description	Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA (By similarity)..
Protein Sequence	MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKASTKLHVGNISPTCTNQELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPVDRTGRVADFTEQYNEQYGAVRTPYTMGYGESMYYNDAYGALDYYKRYRVRSYEAVAAAAAASAYNYAEQTMSHLPQVQSTTVTSHLNSTSVDPYDRHLLPNSGAAATSAAMAAAAATTSSYYGRDRSPLRRAAAMLPTVGEGYGYGPESELSQASAATRNSLYDMARYEREQYVDRARYSAF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MVKLFIGNLP -----CCEEEECCCC	36.06	21890473
3	Sumoylation	-----MVKLFIGNLP -----CCEEEECCCC	36.06	-
3	Sumoylation	-----MVKLFIGNLP -----CCEEEECCCC	36.06	-
25	Phosphorylation	IRSLFEQYGKVLECD HHHHHHHHCCCEECE	16.24	29496907
27	Ubiquitination	SLFEQYGKVLECDII HHHHHHCCCEECEEH	38.42	-
27	Acetylation	SLFEQYGKVLECDII HHHHHHCCCEECEEH	38.42	26051181
31	S-nitrosocysteine	QYGKVLECDIIKNYG HHCCCEECEEHHCCE	3.88	-
31	S-nitrosylation	QYGKVLECDIIKNYG HHCCCEECEEHHCCE	3.88	19483679
35	Ubiquitination	VLECDIIKNYGFVHI CEECEEHHCCEEEEE	44.44	-
35	Acetylation	VLECDIIKNYGFVHI CEECEEHHCCEEEEE	44.44	26051181
37	Phosphorylation	ECDIIKNYGFVHIED ECEEHHCCEEEEECC	13.62	25159151
45	Ubiquitination	GFVHIEDKTAAEDAI EEEEECCCCHHHHHH	27.55	-
45	Acetylation	GFVHIEDKTAAEDAI EEEEECCCCHHHHHH	27.55	25953088
59	Acetylation	IRNLHHYKLHGVNIN HHHHHHHEECCEEEE	29.65	25825284
59	Ubiquitination	IRNLHHYKLHGVNIN HHHHHHHEECCEEEE	29.65	-
70	Phosphorylation	VNINVEASKNKSKAS EEEEEEECCCCCCCC	24.21	-
71	Sumoylation	NINVEASKNKSKAST EEEEEECCCCCCCCC	75.37	-
71	Ubiquitination	NINVEASKNKSKAST EEEEEECCCCCCCCC	75.37	-
71	Acetylation	NINVEASKNKSKAST EEEEEECCCCCCCCC	75.37	25953088
71	Sumoylation	NINVEASKNKSKAST EEEEEECCCCCCCCC	75.37	-
73	Ubiquitination	NVEASKNKSKASTKL EEEECCCCCCCCCEE	58.00	-
86	Phosphorylation	KLHVGNISPTCTNQE EEEECCCCCCCCCHH	20.39	25159151
88	Phosphorylation	HVGNISPTCTNQELR EECCCCCCCCCHHHH	25.77	22617229
90	Phosphorylation	GNISPTCTNQELRAK CCCCCCCCCHHHHHH	42.27	29632367
97	Sumoylation	TNQELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	-
97	Acetylation	TNQELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	27452117
97	Sumoylation	TNQELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	-
97	Ubiquitination	TNQELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	-
101	Phosphorylation	LRAKFEEYGPVIECD HHHHHHHHCCEEEEE	21.38	22817900
111	Ubiquitination	VIECDIVKDYAFVHM EEEEEEEECEEEEEH	45.41	-
113	Phosphorylation	ECDIVKDYAFVHMER EEEEEECEEEEEHHH	9.02	28796482
129	Methylation	EDAVEAIRGLDNTEF HHHHHHHHCCCCCCC	46.82	-
139	Acetylation	DNTEFQGKRMHVQLS CCCCCCCEEEEEEEE	35.45	23749302
139	Ubiquitination	DNTEFQGKRMHVQLS CCCCCCCEEEEEEEE	35.45	-
146	Phosphorylation	KRMHVQLSTSRLRTA EEEEEEEECCCCCCC	13.77	28857561
147	Phosphorylation	RMHVQLSTSRLRTAP EEEEEEECCCCCCCC	26.85	28555341
152	Phosphorylation	LSTSRLRTAPGMGDQ EECCCCCCCCCCCCC	41.62	21406692
160	Phosphorylation	APGMGDQSGCYRCGK CCCCCCCCCCCCCCC	35.25	21406692
163	Phosphorylation	MGDQSGCYRCGKEGH CCCCCCCCCCCCCCC	16.68	21406692
173	Ubiquitination	GKEGHWSKECPVDRT CCCCCCCCCCCCCCC	59.13	-
187	Phosphorylation	TGRVADFTEQYNEQY CCCCCHHHHHHHHHH	23.79	28796482
190	Phosphorylation	VADFTEQYNEQYGAV CCHHHHHHHHHHCCC	17.90	28796482
194	Phosphorylation	TEQYNEQYGAVRTPY HHHHHHHHCCCCCCC	10.81	28796482
201	Phosphorylation	YGAVRTPYTMGYGES HCCCCCCCCCCCCCC	14.56	-
205	Phosphorylation	RTPYTMGYGESMYYN CCCCCCCCCCCCCCC	13.60	-
208	Phosphorylation	YTMGYGESMYYNDAY CCCCCCCCCCCCCCC	14.02	-
210	Phosphorylation	MGYGESMYYNDAYGA CCCCCCCCCCCCCCC	14.38	-
215	Phosphorylation	SMYYNDAYGALDYYK CCCCCCCCCCHHHHH	13.04	-
299	Phosphorylation	AATTSSYYGRDRSPL HHHHHHHCCCCCCHH	13.97	27642862
304	Phosphorylation	SYYGRDRSPLRRAAA HHCCCCCCHHHHHHH	32.35	30266825
315	Phosphorylation	RAAAMLPTVGEGYGY HHHHHCCCCCCCCCC	36.86	26074081
320	Phosphorylation	LPTVGEGYGYGPESE CCCCCCCCCCCCHHH	11.67	26074081
322	Phosphorylation	TVGEGYGYGPESELS CCCCCCCCCCHHHHH	22.48	26074081
326	Phosphorylation	GYGYGPESELSQASA CCCCCCHHHHHHHCH	47.15	26074081
338	Phosphorylation	ASAATRNSLYDMARY HCHHHHHHHHHHHHH	25.64	28796482
340	Phosphorylation	AATRNSLYDMARYER HHHHHHHHHHHHHHH	11.95	25884760
350	Phosphorylation	ARYEREQYVDRARYS HHHHHHHHHHHHHHC	10.28	-
356	Phosphorylation	QYVDRARYSAF---- HHHHHHHHCCC----	11.90	-
357	Phosphorylation	YVDRARYSAF----- HHHHHHHCCC-----	20.04	22210691

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 RBM4B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM4B_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 RBM4B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
SMYD1_HUMAN	SMYD1	physical	23455924
NIP7_HUMAN	NIP7	physical	26186194
KNOP1_HUMAN	KNOP1	physical	26186194
POP1_HUMAN	POP1	physical	26186194
RPP29_HUMAN	POP4	physical	26186194
CBX6_HUMAN	CBX6	physical	26186194
SPB1_HUMAN	FTSJ3	physical	26186194
MYEF2_HUMAN	MYEF2	physical	26186194
RL3_HUMAN	RPL3	physical	26186194
Z324A_HUMAN	ZNF324	physical	26186194
UTP18_HUMAN	UTP18	physical	26186194
STAU2_HUMAN	STAU2	physical	26186194
STAU1_HUMAN	STAU1	physical	26186194
ZFR_HUMAN	ZFR	physical	26186194
RL5_HUMAN	RPL5	physical	26186194
NOP16_HUMAN	NOP16	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
RS3A_HUMAN	RPS3A	physical	26186194
RL18_HUMAN	RPL18	physical	26186194
CDC5L_HUMAN	CDC5L	physical	26186194
SON_HUMAN	SON	physical	26186194
NUFP1_HUMAN	NUFIP1	physical	26186194
ZCHC8_HUMAN	ZCCHC8	physical	26186194
RBM4_HUMAN	RBM4	physical	26186194
TOP2A_HUMAN	TOP2A	physical	26186194
BRX1_HUMAN	BRIX1	physical	26186194
RLP24_HUMAN	RSL24D1	physical	26186194
RRS1_HUMAN	RRS1	physical	26186194
NSD2_HUMAN	WHSC1	physical	26186194
RL15_HUMAN	RPL15	physical	26186194
NOG2_HUMAN	GNL2	physical	26186194
HASP_HUMAN	GSG2	physical	26186194
FCF1_HUMAN	FCF1	physical	26186194
FA83H_HUMAN	FAM83H	physical	26186194
MPP10_HUMAN	MPHOSPH10	physical	26186194
RPP38_HUMAN	RPP38	physical	26186194
MKRN2_HUMAN	MKRN2	physical	26186194
RPP25_HUMAN	RPP25	physical	26186194
IMP3_HUMAN	IMP3	physical	26186194
ANGE2_HUMAN	ANGEL2	physical	26186194
RPP40_HUMAN	RPP40	physical	26186194
UTP4_HUMAN	CIRH1A	physical	26186194
TRBP2_HUMAN	TARBP2	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
ZC3HA_HUMAN	ZC3H10	physical	26186194
REPI1_HUMAN	REPIN1	physical	26186194
NMNA1_HUMAN	NMNAT1	physical	26186194
RBM4_HUMAN	RBM4	physical	28514442
RPP25_HUMAN	RPP25	physical	28514442
NUFP1_HUMAN	NUFIP1	physical	28514442
RPP40_HUMAN	RPP40	physical	28514442
HASP_HUMAN	GSG2	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
MYEF2_HUMAN	MYEF2	physical	28514442
TOP2A_HUMAN	TOP2A	physical	28514442
ZCHC8_HUMAN	ZCCHC8	physical	28514442
ANGE2_HUMAN	ANGEL2	physical	28514442
MKRN2_HUMAN	MKRN2	physical	28514442
FCF1_HUMAN	FCF1	physical	28514442
FA83H_HUMAN	FAM83H	physical	28514442
Z324A_HUMAN	ZNF324	physical	28514442
ZFR_HUMAN	ZFR	physical	28514442
RPP38_HUMAN	RPP38	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
POP1_HUMAN	POP1	physical	28514442
STAU1_HUMAN	STAU1	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
NMNA1_HUMAN	NMNAT1	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
There are no disease associations of PTM sites.

Regulatory Network of RBM4B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-304, AND MASSSPECTROMETRY.	17081983 [Abstract]