SLBP_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SLBP_DROME
• UniProt AC: Q9VAN6
• Protein Name: Histone RNA hairpin-binding protein
• Gene Name: Slbp
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 276
• Protein Description: Involved in histone pre-mRNA 3' processing and couples histone mRNA production with the cell cycle. Both maternal and zygotic proteins play an essential and vital function for development..
• Protein Sequence: MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHNSYTSSTSSSSSYTEADPAILSRRQKQIDYGKNTAAYERYVEMVPKDERTRDHPRTPNKYGKYSRRAFDGLVKIWRKSLHIYDPPTQARDTAKDSNSDSDSD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	KGSGSLNSSASSISI CCCCCCCCCCCCCEE	32.35	22817900
24	Phosphorylation	GSGSLNSSASSISID CCCCCCCCCCCCEEE	30.97	22817900
29	Phosphorylation	NSSASSISIDVKPTM CCCCCCCEEECCHHH	18.06	18327897
54	Phosphorylation	FGHSDEASSSLNSSA HCCCHHHHHHHCCCH	20.57	22817900
59	Phosphorylation	EASSSLNSSAASCGS HHHHHHCCCHHHHHH	27.01	22817900
63	Phosphorylation	SLNSSAASCGSLAKK HHCCCHHHHHHHHCC	20.80	22817900
72	Phosphorylation	GSLAKKETADGNLES HHHHCCCCCCCCCCC	38.64	22817900
118	Phosphorylation	TPYKRRHSFTPPSNE CCCCCCCCCCCCCCC	29.07	19429919
120	Phosphorylation	YKRRHSFTPPSNENS CCCCCCCCCCCCCCC	36.99	22817900
123	Phosphorylation	RHSFTPPSNENSRSN CCCCCCCCCCCCCCC	58.96	19429919
127	Phosphorylation	TPPSNENSRSNSPNS CCCCCCCCCCCCCCC	30.79	22817900
131	Phosphorylation	NENSRSNSPNSSNSS CCCCCCCCCCCCCCC	27.06	29892262
134	Phosphorylation	SRSNSPNSSNSSANG CCCCCCCCCCCCCCC	33.99	29892262
160	Phosphorylation	HSRNSKKSGNFRAHK CCCCCCCCCCCCCCC	42.58	22817900
176	Phosphorylation	EKRVRHNSYTSSTSS CCCCCCCCCCCCCCC	24.54	19429919
177	Phosphorylation	KRVRHNSYTSSTSSS CCCCCCCCCCCCCCC	18.89	23607784
178	Phosphorylation	RVRHNSYTSSTSSSS CCCCCCCCCCCCCCC	18.93	19429919
179	Phosphorylation	VRHNSYTSSTSSSSS CCCCCCCCCCCCCCC	24.32	19429919
180	Phosphorylation	RHNSYTSSTSSSSSY CCCCCCCCCCCCCCC	25.22	19429919
182	Phosphorylation	NSYTSSTSSSSSYTE CCCCCCCCCCCCCCC	30.12	19060867
183	Phosphorylation	SYTSSTSSSSSYTEA CCCCCCCCCCCCCCC	34.04	21082442
184	Phosphorylation	YTSSTSSSSSYTEAD CCCCCCCCCCCCCCC	24.07	21082442
185	Phosphorylation	TSSTSSSSSYTEADP CCCCCCCCCCCCCCH	29.34	21082442
220	Ubiquitination	RYVEMVPKDERTRDH HHHHCCCCCCCCCCC	61.89	31113955
230	Phosphorylation	RTRDHPRTPNKYGKY CCCCCCCCCCCCCCH	35.35	25749252

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SLBP_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SLBP_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SLBP_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NACA_DROME	Nacalpha	physical	22036573

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-29; SER-118;THR-120; SER-123; SER-127; SER-131; TYR-177 AND SER-182, AND MASSSPECTROMETRY.
PubMed: 18327897