dbPTM

SSBP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSBP3_HUMAN
UniProt AC	Q9BWW4
Protein Name	Single-stranded DNA-binding protein 3
Gene Name	SSBP3
Organism	Homo sapiens (Human).
Sequence Length	388
Subcellular Localization	Nucleus.
Protein Description	May be involved in transcription regulation of the alpha 2(I) collagen gene where it binds to the single-stranded polypyrimidine sequences in the promoter region..
Protein Sequence	MFAKGKGSAVPSDGQAREKLALYVYEYLLHVGAQKSAQTFLSEIRWEKNITLGEPPGFLHSWWCVFWDLYCAAPERRDTCEHSSEAKAFHDYSAAAAPSPVLGNIPPNDGMPGGPIPPGFFQGPPGSQPSPHAQPPPHNPSSMMGPHSQPFMSPRYAGGPRPPIRMGNQPPGGVPGTQPLLPNSMDPTRQQGHPNMGGSMQRMNPPRGMGPMGPGPQNYGSGMRPPPNSLGPAMPGINMGPGAGRPWPNPNSANSIPYSSSSPGTYVGPPGGGGPPGTPIMPSPADSTNSSDNIYTMINPVPPGGSRSNFPMGPGSDGPMGGMGGMEPHHMNGSLGSGDIDGLPKNSPNNISGISNPPGTPRDDGELGGNFLHSFQNDNYSPSMTMSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MFAKGKGS -------CCCCCCCC	7.13	22814378
4	Ubiquitination	----MFAKGKGSAVP ----CCCCCCCCCCC	50.30	-
6	Ubiquitination	--MFAKGKGSAVPSD --CCCCCCCCCCCCC	49.32	-
6 (in isoform 3)	Ubiquitination	-	49.32	21906983
6 (in isoform 2)	Ubiquitination	-	49.32	21906983
6 (in isoform 1)	Ubiquitination	-	49.32	21906983
8	Phosphorylation	MFAKGKGSAVPSDGQ CCCCCCCCCCCCCCH	29.58	29396449
19	Ubiquitination	SDGQAREKLALYVYE CCCHHHHHHHHHHHH	33.24	-
23	Phosphorylation	AREKLALYVYEYLLH HHHHHHHHHHHHHHH	8.72	18080319
25	Phosphorylation	EKLALYVYEYLLHVG HHHHHHHHHHHHHHC	5.82	18080319
36	Phosphorylation	LHVGAQKSAQTFLSE HHHCCHHHHHHHHHH	17.33	22210691
42	Phosphorylation	KSAQTFLSEIRWEKN HHHHHHHHHHHHHCC	27.13	24719451
128 (in isoform 2)	Methylation	-	48.70	-
155	Asymmetric dimethylarginine	SQPFMSPRYAGGPRP CCCCCCCCCCCCCCC	26.99	-
155	Methylation	SQPFMSPRYAGGPRP CCCCCCCCCCCCCCC	26.99	24129315
156	Phosphorylation	QPFMSPRYAGGPRPP CCCCCCCCCCCCCCC	17.00	22817900
161	Asymmetric dimethylarginine	PRYAGGPRPPIRMGN CCCCCCCCCCCCCCC	53.56	-
161	Methylation	PRYAGGPRPPIRMGN CCCCCCCCCCCCCCC	53.56	24129315
165	Asymmetric dimethylarginine	GGPRPPIRMGNQPPG CCCCCCCCCCCCCCC	32.50	-
165	Methylation	GGPRPPIRMGNQPPG CCCCCCCCCCCCCCC	32.50	24129315
202	Methylation	NMGGSMQRMNPPRGM CCCCCCCCCCCCCCC	20.43	97795479
265	O-linked_Glycosylation	YSSSSPGTYVGPPGG CCCCCCCCCCCCCCC	20.58	29485866
316	Phosphorylation	NFPMGPGSDGPMGGM CCCCCCCCCCCCCCC	42.39	28348404
320 (in isoform 2)	Phosphorylation	-	9.91	-
325 (in isoform 2)	Phosphorylation	-	14.37	-
327 (in isoform 3)	Phosphorylation	-	44.77	-
332 (in isoform 3)	Phosphorylation	-	32.32	-
333 (in isoform 2)	Phosphorylation	-	19.37	-
334	Phosphorylation	EPHHMNGSLGSGDID CCCCCCCCCCCCCCC	25.26	26074081
337	Phosphorylation	HMNGSLGSGDIDGLP CCCCCCCCCCCCCCC	38.29	26074081
340 (in isoform 3)	Phosphorylation	-	5.30	-
347	Phosphorylation	IDGLPKNSPNNISGI CCCCCCCCCCCCCCC	34.82	19664994
352	Phosphorylation	KNSPNNISGISNPPG CCCCCCCCCCCCCCC	32.00	30266825
354 (in isoform 2)	Phosphorylation	-	2.62	-
355	Phosphorylation	PNNISGISNPPGTPR CCCCCCCCCCCCCCC	46.97	30266825
360 (in isoform 2)	Phosphorylation	-	22.41	-
360	Phosphorylation	GISNPPGTPRDDGEL CCCCCCCCCCCCCCC	22.41	22167270
361 (in isoform 3)	Phosphorylation	-	43.55	-
367 (in isoform 3)	Phosphorylation	-	15.10	-
374	Phosphorylation	LGGNFLHSFQNDNYS CCHHHHHHHCCCCCC	30.58	21406692
380	Phosphorylation	HSFQNDNYSPSMTMS HHHCCCCCCCCCEEC	25.48	20363803
381	Phosphorylation	SFQNDNYSPSMTMSV HHCCCCCCCCCEECC	19.43	26055452
383	Phosphorylation	QNDNYSPSMTMSV-- CCCCCCCCCEECC--	22.42	23663014
385	Phosphorylation	DNYSPSMTMSV---- CCCCCCCEECC----	15.61	30177828
387	Phosphorylation	YSPSMTMSV------ CCCCCEECC------	18.60	26055452

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
23	Y	Phosphorylation	Kinase	LCK	P06239	PSP
25	Y	Phosphorylation	Kinase	LCK	P06239	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SSBP3_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 SSBP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANKE1_HUMAN	ANKEF1	physical	20211142
A4_HUMAN	APP	physical	21832049
I36RA_HUMAN	IL36RN	physical	25416956
TBC23_HUMAN	TBC1D23	physical	25416956
NXT2_HUMAN	NXT2	physical	25416956
LDB1_HUMAN	LDB1	physical	26186194
RRP44_HUMAN	DIS3	physical	26186194
LHX1_HUMAN	LHX1	physical	26186194
ISL2_HUMAN	ISL2	physical	26186194
ISL1_HUMAN	ISL1	physical	26186194
LMO4_HUMAN	LMO4	physical	26186194
ISL2_HUMAN	ISL2	physical	28514442
LDB1_HUMAN	LDB1	physical	28514442
ISL1_HUMAN	ISL1	physical	28514442
LMO4_HUMAN	LMO4	physical	28514442
RRP44_HUMAN	DIS3	physical	28514442
LHX1_HUMAN	LHX1	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 SSBP3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-352; THR-360;SER-381 AND SER-387, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-347; SER-352 ANDTHR-360, AND MASS SPECTROMETRY.	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-381 AND SER-387, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-360, ANDMASS SPECTROMETRY.	18220336 [Abstract]