dbPTM

RBM24_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM24_HUMAN
UniProt AC	Q9BX46
Protein Name	RNA-binding protein 24 {ECO:0000305}
Gene Name	RBM24 {ECO:0000312\|HGNC:HGNC:21539}
Organism	Homo sapiens (Human).
Sequence Length	236
Subcellular Localization	Nucleus . Cytoplasm .
Protein Description	Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation. [PubMed: 20977548]
Protein Sequence	MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGEIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAAAGYVTAGGYGYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MHTTQKDTTYTKIFV CCCCCCCCCCEEEEE	28.83	24043423
9	Phosphorylation	HTTQKDTTYTKIFVG CCCCCCCCCEEEEEC	39.05	24043423
10	Phosphorylation	TTQKDTTYTKIFVGG CCCCCCCCEEEEECC	14.23	29116813
11	Phosphorylation	TQKDTTYTKIFVGGL CCCCCCCEEEEECCC	18.64	29116813
46 (in isoform 2)	Ubiquitination	-	27.58	21906983
62	Methylation	GFVTMADRAAAERAC EEEEHHHHHHHHHHC	19.31	-
70	Ubiquitination	AAAERACKDPNPIID HHHHHHCCCCCCCCC	75.20	-
80	Ubiquitination	NPIIDGRKANVNLAY CCCCCCCCCCCCEEE	50.25	-
87	Phosphorylation	KANVNLAYLGAKPRI CCCCCEEECCCCCCC	14.61	18187866
91	Ubiquitination	NLAYLGAKPRIMQPG CEEECCCCCCCCCCC	32.79	-
91 (in isoform 1)	Ubiquitination	-	32.79	21906983
181	Phosphorylation	DQYPYAASPAAAGYV HCCCCCCCHHHCCCE	13.60	-

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 RBM24_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RBM24_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 RBM24_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPIPL_HUMAN	EPPK1	physical	26186194
PLAK_HUMAN	JUP	physical	26186194
SPB13_HUMAN	SERPINB13	physical	26186194
CALL5_HUMAN	CALML5	physical	26186194
H2AY_HUMAN	H2AFY	physical	26186194
TRI29_HUMAN	TRIM29	physical	26186194
RBM38_HUMAN	RBM38	physical	26186194
CALL3_HUMAN	CALML3	physical	26186194
SPB5_HUMAN	SERPINB5	physical	26186194
PKP1_HUMAN	PKP1	physical	26186194
INVO_HUMAN	IVL	physical	26186194
ANR40_HUMAN	ANKRD40	physical	26186194
PAI2_HUMAN	SERPINB2	physical	26186194
CRYAB_HUMAN	CRYAB	physical	26186194
EVPL_HUMAN	EVPL	physical	26186194
PKP3_HUMAN	PKP3	physical	26186194
PEPL_HUMAN	PPL	physical	26186194
TYPH_HUMAN	TYMP	physical	26186194
PLCD1_HUMAN	PLCD1	physical	26186194
DMKN_HUMAN	DMKN	physical	26186194
QSOX1_HUMAN	QSOX1	physical	26186194
RBM38_HUMAN	RBM38	physical	28514442
DMKN_HUMAN	DMKN	physical	28514442
INVO_HUMAN	IVL	physical	28514442
TRI29_HUMAN	TRIM29	physical	28514442
PAI2_HUMAN	SERPINB2	physical	28514442
SPB5_HUMAN	SERPINB5	physical	28514442
CRYAB_HUMAN	CRYAB	physical	28514442
PKP3_HUMAN	PKP3	physical	28514442
PEPL_HUMAN	PPL	physical	28514442
SPB13_HUMAN	SERPINB13	physical	28514442
PLCD1_HUMAN	PLCD1	physical	28514442
ANR40_HUMAN	ANKRD40	physical	28514442
TYPH_HUMAN	TYMP	physical	28514442
EVPL_HUMAN	EVPL	physical	28514442
CALL5_HUMAN	CALML5	physical	28514442
EPIPL_HUMAN	EPPK1	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442
CALL3_HUMAN	CALML3	physical	28514442
SPB3_HUMAN	SERPINB3	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 RBM24_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-87, AND MASSSPECTROMETRY.	18187866 [Abstract]