dbPTM

RBM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM3_HUMAN
UniProt AC	P98179
Protein Name	RNA-binding protein 3
Gene Name	RBM3
Organism	Homo sapiens (Human).
Sequence Length	157
Subcellular Localization	Nucleus. Cytoplasm. Cell projection, dendrite. Localizes in mRNA granules in dentrites..
Protein Description	Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation (By similarity)..
Protein Sequence	MSSEEGKLFVGGLNFNTDEQALEDHFSSFGPISEVVVVKDRETQRSRGFGFITFTNPEHASVAMRAMNGESLDGRQIRVDHAGKSARGTRGGGFGAHGRGRSYSRGGGDQGYGSGRYYDSRPGGYGYGYGRSRDYNGRNQGGYDRYSGGNYRDNYDN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSEEGKLF ------CCCCCCCEE	46.59	28464451
3	Phosphorylation	-----MSSEEGKLFV -----CCCCCCCEEE	38.07	28464451
27	Phosphorylation	QALEDHFSSFGPISE HHHHHHHHCCCCCCE	22.72	27251275
28	Phosphorylation	ALEDHFSSFGPISEV HHHHHHHCCCCCCEE	33.02	24275569
43	Phosphorylation	VVVKDRETQRSRGFG EEEECCCCCCCCCEE	30.12	-
47	Methylation	DRETQRSRGFGFITF CCCCCCCCCEEEEEE	46.80	24129315
53	Phosphorylation	SRGFGFITFTNPEHA CCCEEEEEECCHHHH	23.34	28555341
61	Phosphorylation	FTNPEHASVAMRAMN ECCHHHHHHHHHHHC	16.59	28857561
64	Sulfoxidation	PEHASVAMRAMNGES HHHHHHHHHHHCCCC	2.35	30846556
65	Methylation	EHASVAMRAMNGESL HHHHHHHHHHCCCCC	22.43	115490727
71	Phosphorylation	MRAMNGESLDGRQIR HHHHCCCCCCCCEEE	32.91	29255136
87	Methylation	DHAGKSARGTRGGGF ECCCCCCCCCCCCCC	54.85	18960571
87	Dimethylation	DHAGKSARGTRGGGF ECCCCCCCCCCCCCC	54.85	-
90	Dimethylation	GKSARGTRGGGFGAH CCCCCCCCCCCCCCC	44.58	-
90	Methylation	GKSARGTRGGGFGAH CCCCCCCCCCCCCCC	44.58	12018995
99	Methylation	GGFGAHGRGRSYSRG CCCCCCCCCCCCCCC	27.73	12019005
99	Dimethylation	GGFGAHGRGRSYSRG CCCCCCCCCCCCCCC	27.73	-
101	Dimethylation	FGAHGRGRSYSRGGG CCCCCCCCCCCCCCC	30.94	-
101	Methylation	FGAHGRGRSYSRGGG CCCCCCCCCCCCCCC	30.94	12019015
102	Phosphorylation	GAHGRGRSYSRGGGD CCCCCCCCCCCCCCC	30.22	27251275
103	Phosphorylation	AHGRGRSYSRGGGDQ CCCCCCCCCCCCCCC	10.88	-
104	Phosphorylation	HGRGRSYSRGGGDQG CCCCCCCCCCCCCCC	26.20	23898821
105	Methylation	GRGRSYSRGGGDQGY CCCCCCCCCCCCCCC	39.27	24129315
105	Asymmetric dimethylarginine	GRGRSYSRGGGDQGY CCCCCCCCCCCCCCC	39.27	-
112	Phosphorylation	RGGGDQGYGSGRYYD CCCCCCCCCCCCCCC	11.50	-
116	Methylation	DQGYGSGRYYDSRPG CCCCCCCCCCCCCCC	28.65	80702199
117	Phosphorylation	QGYGSGRYYDSRPGG CCCCCCCCCCCCCCC	18.36	21945579
118	Phosphorylation	GYGSGRYYDSRPGGY CCCCCCCCCCCCCCC	13.19	21945579
120	Phosphorylation	GSGRYYDSRPGGYGY CCCCCCCCCCCCCCC	25.01	21945579
121	Methylation	SGRYYDSRPGGYGYG CCCCCCCCCCCCCCC	30.87	24129315
125	Phosphorylation	YDSRPGGYGYGYGRS CCCCCCCCCCCCCCC	17.06	21945579
127	Phosphorylation	SRPGGYGYGYGRSRD CCCCCCCCCCCCCCC	9.93	21945579
129	Phosphorylation	PGGYGYGYGRSRDYN CCCCCCCCCCCCCCC	10.81	21945579
131	Methylation	GYGYGYGRSRDYNGR CCCCCCCCCCCCCCC	21.75	24129315
131	Dimethylation	GYGYGYGRSRDYNGR CCCCCCCCCCCCCCC	21.75	-
132	Phosphorylation	YGYGYGRSRDYNGRN CCCCCCCCCCCCCCC	25.74	24719451
133	Methylation	GYGYGRSRDYNGRNQ CCCCCCCCCCCCCCC	49.42	18966545
135	Phosphorylation	GYGRSRDYNGRNQGG CCCCCCCCCCCCCCC	20.57	-
138	Methylation	RSRDYNGRNQGGYDR CCCCCCCCCCCCCCC	28.76	18601017
143	Phosphorylation	NGRNQGGYDRYSGGN CCCCCCCCCCCCCCC	12.22	21945579
145	Methylation	RNQGGYDRYSGGNYR CCCCCCCCCCCCCCC	21.02	58859235
146	Phosphorylation	NQGGYDRYSGGNYRD CCCCCCCCCCCCCCC	14.58	21945579
147	Phosphorylation	QGGYDRYSGGNYRDN CCCCCCCCCCCCCCC	40.91	23401153
151	Phosphorylation	DRYSGGNYRDNYDN- CCCCCCCCCCCCCC-	23.71	21945579
155	Phosphorylation	GGNYRDNYDN----- CCCCCCCCCC-----	22.58	21945579

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
147	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
105	R	Methylation
Arg-105 is dimethylated, probably to asymmetric dimethylarginine.

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 RBM3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RM12_HUMAN	MRPL12	physical	22939629
ROA1_HUMAN	HNRNPA1	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
RBY1A_HUMAN	RBMY1A1	physical	25416956
SNRPA_HUMAN	SNRPA	physical	25416956
RBMX_HUMAN	RBMX	physical	25416956
RBY1F_HUMAN	RBMY1F	physical	25416956
KHDR2_HUMAN	KHDRBS2	physical	25416956
SYYM_HUMAN	YARS2	physical	28514442
FABD_HUMAN	MCAT	physical	28514442
PAI2B_HUMAN	PAIP2B	physical	28514442
NAGK_HUMAN	NAGK	physical	28514442
NGRN_HUMAN	NGRN	physical	28514442
THUM3_HUMAN	THUMPD3	physical	28514442
NIF3L_HUMAN	NIF3L1	physical	28514442
SYAM_HUMAN	AARS2	physical	28514442
ANM5_HUMAN	PRMT5	physical	28514442
RENT1_HUMAN	UPF1	physical	26472337
F120A_HUMAN	FAM120A	physical	26472337
IF2B2_HUMAN	IGF2BP2	physical	26472337
SEPR_HUMAN	FAP	physical	26472337
DYN2_HUMAN	DNM2	physical	26472337
CDV3_HUMAN	CDV3	physical	26472337
RT31_HUMAN	MRPS31	physical	26472337
ELOB_HUMAN	TCEB2	physical	26472337
SF3A2_HUMAN	SF3A2	physical	26472337
PTCD1_HUMAN	PTCD1	physical	26472337
ELAV2_HUMAN	ELAVL2	physical	26472337
CASC3_HUMAN	CASC3	physical	26472337
ACHE_HUMAN	CHRNE	physical	26472337
1433E_HUMAN	YWHAE	physical	26472337
CALC_HUMAN	CALCA	physical	26472337
CALCA_HUMAN	CALCA	physical	26472337
NCBP2_HUMAN	NCBP2	physical	26472337
UBP34_HUMAN	USP34	physical	26472337
TCPD_HUMAN	CCT4	physical	26472337
RO60_HUMAN	TROVE2	physical	26472337
KLD10_HUMAN	KLHDC10	physical	26472337
ILF3_HUMAN	ILF3	physical	26472337
RFA1_HUMAN	RPA1	physical	26472337
RT29_HUMAN	DAP3	physical	26472337
WDR74_HUMAN	WDR74	physical	26472337
RT09_HUMAN	MRPS9	physical	26472337
IF2B3_HUMAN	IGF2BP3	physical	26472337
ILF2_HUMAN	ILF2	physical	26472337
UBR3_HUMAN	UBR3	physical	26472337
IKBZ_HUMAN	NFKBIZ	physical	26472337
RT28_HUMAN	MRPS28	physical	26472337
ELOC_HUMAN	TCEB1	physical	26472337
MOV10_HUMAN	MOV10	physical	26472337
TITIN_HUMAN	TTN	physical	26472337
FWCH2_HUMAN	FLYWCH2	physical	26472337
MGN_HUMAN	MAGOH	physical	26472337
TCPG_HUMAN	CCT3	physical	26472337
FABP5_HUMAN	FABP5	physical	26472337
KIF27_HUMAN	KIF27	physical	26472337
RM01_HUMAN	MRPL1	physical	26472337
RM52_HUMAN	MRPL52	physical	26472337
PLAK_HUMAN	JUP	physical	26472337
TMM94_HUMAN	KIAA0195	physical	26472337
PRKRA_HUMAN	PRKRA	physical	26472337
DDX6L_HUMAN	DDX60L	physical	26472337
RALYL_HUMAN	RALYL	physical	26472337
CC070_HUMAN	C3orf70	physical	26472337
RAE1_HUMAN	CHM	physical	26472337
RL39_HUMAN	RPL39	physical	26472337
RT18B_HUMAN	MRPS18B	physical	26472337
AP1G2_HUMAN	AP1G2	physical	26472337
C2AIL_HUMAN	CDKN2AIPNL	physical	26472337
RT06_HUMAN	MRPS6	physical	26472337
ZCHC3_HUMAN	ZCCHC3	physical	26472337
RM12_HUMAN	MRPL12	physical	26472337
RET3_HUMAN	RBP3	physical	26472337
RBM8A_HUMAN	RBM8A	physical	26472337
ELAV1_HUMAN	ELAVL1	physical	26472337

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 RBM3_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-105, AND MASS SPECTROMETRY.	15782174 [Abstract]
Phosphorylation
Reference	PubMed
"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-147, AND MASSSPECTROMETRY.	18669648 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND TYR-155, ANDMASS SPECTROMETRY.	15144186 [Abstract]

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