dbPTM

SLBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SLBP_HUMAN
UniProt AC	Q14493
Protein Name	Histone RNA hairpin-binding protein
Gene Name	SLBP
Organism	Homo sapiens (Human).
Sequence Length	270
Subcellular Localization	Cytoplasm. Nucleus. Polyribosome-associated. Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase. Through the S phase, partially redistributes to the cytoplasm. Binding to histone mRNA is necessary for cytoplasmic
Protein Description	RNA-binding protein involved in the histone pre-mRNA processing. Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression. Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis. Binds to the 5' side of the stem-loop structure of histone pre-mRNAs..
Protein Sequence	MACRPRSPPRHQSRCDGDASPPSPARWSLGRKRRADGRRWRPEDAEEAEHRGAERRPESFTTPEGPKPRSRCSDWASAVEEDEMRTRVNKEMARYKRKLLINDFGRERKSSSGSSDSKESMSTVPADFETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPKTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIHPVDLESAESSSEPQTSSQDDFDVYSGTPTKVRHMDSQVEDEFDLEACLTEPLRDFSAMS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MACRPRSPPRHQSR -CCCCCCCCCCCCCC	41.77	23401153
7 (in isoform 2)	Phosphorylation	-	41.77	27762562
13	Phosphorylation	RSPPRHQSRCDGDAS CCCCCCCCCCCCCCC	28.84	28450419
20	Phosphorylation	SRCDGDASPPSPARW CCCCCCCCCCCCCHH	41.92	29255136
23	Phosphorylation	DGDASPPSPARWSLG CCCCCCCCCCHHHCC	34.28	19664994
23 (in isoform 2)	Phosphorylation	-	34.28	25159151
28	Phosphorylation	PPSPARWSLGRKRRA CCCCCHHHCCCCCCC	18.52	23090842
59	Phosphorylation	GAERRPESFTTPEGP CCCCCCCCCCCCCCC	30.49	29255136
61	Phosphorylation	ERRPESFTTPEGPKP CCCCCCCCCCCCCCC	51.20	29255136
62	Phosphorylation	RRPESFTTPEGPKPR CCCCCCCCCCCCCCC	19.82	29255136
67	Ubiquitination	FTTPEGPKPRSRCSD CCCCCCCCCCCCCCH	65.01	-
70	Phosphorylation	PEGPKPRSRCSDWAS CCCCCCCCCCCHHHH	46.28	26074081
73	Phosphorylation	PKPRSRCSDWASAVE CCCCCCCCHHHHHHC	34.77	26074081
77	Phosphorylation	SRCSDWASAVEEDEM CCCCHHHHHHCHHHH	28.70	26552605
98	Sumoylation	EMARYKRKLLINDFG HHHHHHHHHHHHCCC	43.42	-
98	Ubiquitination	EMARYKRKLLINDFG HHHHHHHHHHHHCCC	43.42	-
98	Sumoylation	EMARYKRKLLINDFG HHHHHHHHHHHHCCC	43.42	28112733
110	Phosphorylation	DFGRERKSSSGSSDS CCCCCCCCCCCCCCC	35.64	28176443
111	Phosphorylation	FGRERKSSSGSSDSK CCCCCCCCCCCCCCC	41.58	27273156
112	Phosphorylation	GRERKSSSGSSDSKE CCCCCCCCCCCCCCH	50.19	26074081
114	Phosphorylation	ERKSSSGSSDSKESM CCCCCCCCCCCCHHH	32.68	30576142
115	Phosphorylation	RKSSSGSSDSKESMS CCCCCCCCCCCHHHC	49.80	28176443
117	Phosphorylation	SSSGSSDSKESMSTV CCCCCCCCCHHHCCC	40.03	23401153
120	Phosphorylation	GSSDSKESMSTVPAD CCCCCCHHHCCCCCC	23.05	29116813
122	Phosphorylation	SDSKESMSTVPADFE CCCCHHHCCCCCCCC	35.22	-
123	Phosphorylation	DSKESMSTVPADFET CCCHHHCCCCCCCCC	23.13	30576142
133	Phosphorylation	ADFETDESVLMRRQK CCCCCCHHHHHHHHH	24.30	-
137	Methylation	TDESVLMRRQKQINY CCHHHHHHHHHHHHC	33.44	30761027
140	Ubiquitination	SVLMRRQKQINYGKN HHHHHHHHHHHCCCC	51.86	-
146	Ubiquitination	QKQINYGKNTIAYDR HHHHHCCCCCHHHHH	40.32	-
146	Sumoylation	QKQINYGKNTIAYDR HHHHHCCCCCHHHHH	40.32	-
146	Sumoylation	QKQINYGKNTIAYDR HHHHHCCCCCHHHHH	40.32	-
153	Methylation	KNTIAYDRYIKEVPR CCCHHHHHHHHHCHH	23.54	115368087
156	Ubiquitination	IAYDRYIKEVPRHLR HHHHHHHHHCHHHHC	43.66	-
171	Phosphorylation	QPGIHPKTPNKFKKY CCCCCCCCCCHHHHC	36.22	23401153
178	Phosphorylation	TPNKFKKYSRRSWDQ CCCHHHHCCCCCHHH	14.17	-
179	Phosphorylation	PNKFKKYSRRSWDQQ CCHHHHCCCCCHHHH	30.05	22617229
182	Phosphorylation	FKKYSRRSWDQQIKL HHHCCCCCHHHHHHH	33.62	30266825
217	Phosphorylation	IHPVDLESAESSSEP ECCCCHHHCCCCCCC	44.63	26074081
220	Phosphorylation	VDLESAESSSEPQTS CCHHHCCCCCCCCCC	38.59	26074081
221	Phosphorylation	DLESAESSSEPQTSS CHHHCCCCCCCCCCC	30.17	26074081
222	Phosphorylation	LESAESSSEPQTSSQ HHHCCCCCCCCCCCC	63.68	26074081
226	Phosphorylation	ESSSEPQTSSQDDFD CCCCCCCCCCCCCCC	40.85	26074081
227	Phosphorylation	SSSEPQTSSQDDFDV CCCCCCCCCCCCCCC	22.28	26074081
228	Phosphorylation	SSEPQTSSQDDFDVY CCCCCCCCCCCCCCC	40.80	26074081
235	Phosphorylation	SQDDFDVYSGTPTKV CCCCCCCCCCCCCEE	11.83	26074081
236	Phosphorylation	QDDFDVYSGTPTKVR CCCCCCCCCCCCEEE	35.72	26074081
238	Phosphorylation	DFDVYSGTPTKVRHM CCCCCCCCCCEEECC	23.11	29496963
240	Phosphorylation	DVYSGTPTKVRHMDS CCCCCCCCEEECCCC	41.85	28464451
247	Phosphorylation	TKVRHMDSQVEDEFD CEEECCCCCCCCCCC	28.66	28464451
260	Phosphorylation	FDLEACLTEPLRDFS CCHHHHHCCCCHHHH	35.13	24719451
270	Phosphorylation	LRDFSAMS------- CHHHHCCC-------	36.47	26074081

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
61	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
61	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
61	T	Phosphorylation	Kinase	CK2	-	Uniprot
62	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
61	T	Phosphorylation	12588979
Phosphorylated on Thr-61 and Thr-62 in the S-phase.
61	T	Phosphorylation	12588979
Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by CK2.
62	T	Phosphorylation	12588979
Phosphorylated on Thr-61 and Thr-62 in the S-phase.
62	T	Phosphorylation	12588979
Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by CK2.
62	T	Phosphorylation	12588979
Phosphorylation of Thr-62 is required for its degradation by the proteasome at the end of the S phase.
171	T	Phosphorylation	23186163
Phosphorylation at Thr-171 increases affinity for histone mRNAs.

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 SLBP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERI1_HUMAN	ERI1	physical	14536070
ZN473_HUMAN	ZNF473	physical	11782445
RENT1_HUMAN	UPF1	physical	16086026
FEM1A_HUMAN	FEM1A	physical	28118078
FEM1B_HUMAN	FEM1B	physical	28118078
FEM1C_HUMAN	FEM1C	physical	28118078
CUL2_HUMAN	CUL2	physical	28118078
NCBP1_HUMAN	NCBP1	physical	28118078
CTIF_HUMAN	CTIF	physical	28118078
CCNF_HUMAN	CCNF	physical	28118078
CCNA2_HUMAN	CCNA2	physical	28118078
RENT1_HUMAN	UPF1	physical	28118078
DCA11_HUMAN	DCAF11	physical	27254819
CUL4A_HUMAN	CUL4A	physical	27254819
CCNF_HUMAN	CCNF	physical	27773672
SKP1_HUMAN	SKP1	physical	27773672
CDK1_HUMAN	CDK1	physical	27773672
CDK2_HUMAN	CDK2	physical	27773672
CCNA2_HUMAN	CCNA2	physical	27773672
IF4G1_HUMAN	EIF4G1	physical	27773672
RENT1_HUMAN	UPF1	physical	27773672
TUT7_HUMAN	ZCCHC6	physical	27773672
MI4GD_HUMAN	MIF4GD	physical	27773672
NCBP1_HUMAN	NCBP1	physical	27773672
CSK21_HUMAN	CSNK2A1	physical	27773672
CSK22_HUMAN	CSNK2A2	physical	27773672
CUL1_HUMAN	CUL1	physical	27773672
CTIF_HUMAN	CTIF	physical	27773672

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 SLBP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-20 AND SER-23, 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-20; SER-23 AND SER-182,AND MASS SPECTROMETRY.	18669648 [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-20 AND SER-23, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradationof stem-loop binding protein at the end of S phase."; Koseoglu M.M., Graves L.M., Marzluff W.F.; Mol. Cell. Biol. 28:4469-4479(2008). Cited for: PHOSPHORYLATION AT THR-61 AND THR-62, MUTAGENESIS OF THR-61; THR-62;59-SER--PRO-63 AND 96-LYS--LEU-99, AND IDENTIFICATION BY MASSSPECTROMETRY.	18490441 [Abstract]
"Phosphorylation of stem-loop binding protein (SLBP) on two threoninestriggers degradation of SLBP, the sole cell cycle-regulated factorrequired for regulation of histone mRNA processing, at the end of Sphase."; Zheng L., Dominski Z., Yang X.-C., Elms P., Raska C.S., Borchers C.H.,Marzluff W.F.; Mol. Cell. Biol. 23:1590-1601(2003). Cited for: FUNCTION, ASSOCIATION WITH POLYRIBOSOMES, SUBCELLULAR LOCATION,PHOSPHORYLATION AT THR-61 AND THR-62, RNA-BINDING, MUTAGENESIS OFSER-59; THR-61; THR-62; PRO-63 AND 96-LYS--LEU-99, AND IDENTIFICATIONBY MASS SPECTROMETRY.	12588979 [Abstract]

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