dbPTM

FUBP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FUBP3_HUMAN
UniProt AC	Q96I24
Protein Name	Far upstream element-binding protein 3
Gene Name	FUBP3
Organism	Homo sapiens (Human).
Sequence Length	572
Subcellular Localization	Nucleus .
Protein Description	May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression..
Protein Sequence	MAELVQGQSAPVGMKAEGFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGVGNQLGALVHQRTVITEEFKVPDKMVGFIIGRGGEQISRIQAESGCKIQIASESSGIPERPCVLTGTPESIEQAKRLLGQIVDRCRNGPGFHNDIDSNSTIQEILIPASKVGLVIGRGGETIKQLQERTGVKMVMIQDGPLPTGADKPLRITGDAFKVQQAREMVLEIIREKDQADFRGVRGDFNSRMGGGSIEVSVPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERAAQVMGPPDRCQHAAHIISELILTAQERDGFGGLAAARGRGRGRGDWSVGAPGGVQEITYTVPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNSDPNLRRFTIRGVPQQIEVARQLIDEKVGGTNLGAPGAFGQSPFSQPPAPPHQNTFPPRSSGCFPNMAAKVNGNPHSTPVSGPPAFLTQGWGSTYQAWQQPTQQVPSQQSQPQSSQPNYSKAWEDYYKKQSHAASAAPQASSPPDYTMAWAEYYRQQVAFYGQTLGQAQAHSQEQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAELVQGQS ------CCCCCCCCC	20.87	22223895
9	Phosphorylation	AELVQGQSAPVGMKA CCCCCCCCCCCCCCH	41.17	25002506
15	Sumoylation	QSAPVGMKAEGFVDA CCCCCCCCHHHHHHH	37.04	-
15	Acetylation	QSAPVGMKAEGFVDA CCCCCCCCHHHHHHH	37.04	23954790
15	Sumoylation	QSAPVGMKAEGFVDA CCCCCCCCHHHHHHH	37.04	28112733
15	Ubiquitination	QSAPVGMKAEGFVDA CCCCCCCCHHHHHHH	37.04	-
27 (in isoform 2)	Ubiquitination	-	23.34	21890473
32	Acetylation	RVRQIAAKIDSIPHL HHHHHHHHHHCCCCC	37.72	23954790
32	Ubiquitination	RVRQIAAKIDSIPHL HHHHHHHHHHCCCCC	37.72	-
35	Phosphorylation	QIAAKIDSIPHLNNS HHHHHHHCCCCCCCC	41.30	21945579
42	Phosphorylation	SIPHLNNSTPLVDPS CCCCCCCCCCCCCHH	30.26	21945579
43	Phosphorylation	IPHLNNSTPLVDPSV CCCCCCCCCCCCHHH	23.82	21945579
49	Phosphorylation	STPLVDPSVYGYGVQ CCCCCCHHHHCCCCC	24.41	21945579
51	Phosphorylation	PLVDPSVYGYGVQKR CCCCHHHHCCCCCCC	14.68	21945579
53	Phosphorylation	VDPSVYGYGVQKRPL CCHHHHCCCCCCCCC	9.09	21945579
57	Ubiquitination	VYGYGVQKRPLDDGV HHCCCCCCCCCCCCH	54.28	21890473
57	Acetylation	VYGYGVQKRPLDDGV HHCCCCCCCCCCCCH	54.28	26051181
57	Sumoylation	VYGYGVQKRPLDDGV HHCCCCCCCCCCCCH	54.28	28112733
57	Ubiquitination	VYGYGVQKRPLDDGV HHCCCCCCCCCCCCH	54.28	21890473
57 (in isoform 1)	Ubiquitination	-	54.28	21890473
76	Phosphorylation	GALVHQRTVITEEFK HHHHHCEEEECEECC	15.08	28674151
79	Phosphorylation	VHQRTVITEEFKVPD HHCEEEECEECCCCC	25.73	30108239
83	Acetylation	TVITEEFKVPDKMVG EEECEECCCCCCCEE	57.02	26051181
83	Ubiquitination	TVITEEFKVPDKMVG EEECEECCCCCCCEE	57.02	-
87	Ubiquitination	EEFKVPDKMVGFIIG EECCCCCCCEEEEEC	29.43	21890473
87	Acetylation	EEFKVPDKMVGFIIG EECCCCCCCEEEEEC	29.43	25953088
87	Ubiquitination	EEFKVPDKMVGFIIG EECCCCCCCEEEEEC	29.43	21890473
87 (in isoform 1)	Ubiquitination	-	29.43	21890473
95	Methylation	MVGFIIGRGGEQISR CEEEEECCCCHHHHH	39.26	-
109	S-nitrosocysteine	RIQAESGCKIQIASE HHHHHCCCEEEEEEC	4.96	-
109	S-nitrosylation	RIQAESGCKIQIASE HHHHHCCCEEEEEEC	4.96	19483679
128	Phosphorylation	PERPCVLTGTPESIE CCCCEEECCCHHHHH	20.72	28348404
130	Phosphorylation	RPCVLTGTPESIEQA CCEEECCCHHHHHHH	20.74	25159151
138	Acetylation	PESIEQAKRLLGQIV HHHHHHHHHHHHHHH	43.18	26051181
138	Ubiquitination	PESIEQAKRLLGQIV HHHHHHHHHHHHHHH	43.18	-
147	Methylation	LLGQIVDRCRNGPGF HHHHHHHHHHCCCCC	15.48	-
149	Methylation	GQIVDRCRNGPGFHN HHHHHHHHCCCCCCC	52.62	-
160	Phosphorylation	GFHNDIDSNSTIQEI CCCCCCCCCCCHHHH	32.77	20873877
162	O-linked_Glycosylation	HNDIDSNSTIQEILI CCCCCCCCCHHHHEE	30.73	30059200
162	Phosphorylation	HNDIDSNSTIQEILI CCCCCCCCCHHHHEE	30.73	20873877
163	Phosphorylation	NDIDSNSTIQEILIP CCCCCCCCHHHHEEE	30.81	28555341
172	O-linked_Glycosylation	QEILIPASKVGLVIG HHHEEEHHHCEEEEC	23.63	30059200
180	Methylation	KVGLVIGRGGETIKQ HCEEEECCCCHHHHH	38.53	-
184	Phosphorylation	VIGRGGETIKQLQER EECCCCHHHHHHHHH	36.43	20068230
186	Ubiquitination	GRGGETIKQLQERTG CCCCHHHHHHHHHHC	52.99	-
195	Ubiquitination	LQERTGVKMVMIQDG HHHHHCCCEEEEECC	27.41	-
210	Ubiquitination	PLPTGADKPLRITGD CCCCCCCCCCEEECC	45.47	-
220	Acetylation	RITGDAFKVQQAREM EEECCCHHHHHHHHH	40.63	25953088
220	Ubiquitination	RITGDAFKVQQAREM EEECCCHHHHHHHHH	40.63	-
227	Sulfoxidation	KVQQAREMVLEIIRE HHHHHHHHHHHHHHH	3.30	21406390
235	Acetylation	VLEIIREKDQADFRG HHHHHHHHCHHCCCC	45.34	25953088
241	Methylation	EKDQADFRGVRGDFN HHCHHCCCCCCCCCC	43.15	-
244	Methylation	QADFRGVRGDFNSRM HHCCCCCCCCCCCCC	41.61	-
251	Sulfoxidation	RGDFNSRMGGGSIEV CCCCCCCCCCCCEEE	6.16	21406390
255	Phosphorylation	NSRMGGGSIEVSVPR CCCCCCCCEEEECCC	20.89	21406692
259	Phosphorylation	GGGSIEVSVPRFAVG CCCCEEEECCCEEEE	17.39	21406692
278	Ubiquitination	RNGEMIKKIQNDAGV CCHHHHHHHCCCCCC	38.30	-
286	Methylation	IQNDAGVRIQFKPDD HCCCCCCCEEECCCC	18.97	-
290	Acetylation	AGVRIQFKPDDGISP CCCCEEECCCCCCCH	31.03	26051181
296	Phosphorylation	FKPDDGISPERAAQV ECCCCCCCHHHHHHH	26.66	29255136
299	Methylation	DDGISPERAAQVMGP CCCCCHHHHHHHHCC	38.31	-
304	Sulfoxidation	PERAAQVMGPPDRCQ HHHHHHHHCCCCHHH	4.42	21406390
309	Methylation	QVMGPPDRCQHAAHI HHHCCCCHHHHHHHH	27.98	-
337	Methylation	FGGLAAARGRGRGRG CCHHHHHCCCCCCCC	30.52	-
339	Methylation	GLAAARGRGRGRGDW HHHHHCCCCCCCCCC	26.53	-
341	Methylation	AAARGRGRGRGDWSV HHHCCCCCCCCCCCC	30.21	-
343	Methylation	ARGRGRGRGDWSVGA HCCCCCCCCCCCCCC	38.24	-
347	Phosphorylation	GRGRGDWSVGAPGGV CCCCCCCCCCCCCCE	18.53	27251275
358	Phosphorylation	PGGVQEITYTVPADK CCCEEEEEEEEEHHH	16.64	-
359	Phosphorylation	GGVQEITYTVPADKC CCEEEEEEEEEHHHC	16.05	-
360	Phosphorylation	GVQEITYTVPADKCG CEEEEEEEEEHHHCC	16.03	-
372	Ubiquitination	KCGLVIGKGGENIKS HCCEEECCCCCCHHH	53.25	-
378	Ubiquitination	GKGGENIKSINQQSG CCCCCCHHHHHHCCC	57.79	21890473
378	Acetylation	GKGGENIKSINQQSG CCCCCCHHHHHHCCC	57.79	26051181
378	Ubiquitination	GKGGENIKSINQQSG CCCCCCHHHHHHCCC	57.79	21890473
378 (in isoform 1)	Ubiquitination	-	57.79	21890473
406	Phosphorylation	DPNLRRFTIRGVPQQ CCCCCCEEECCHHHH	14.14	24719451
408	Methylation	NLRRFTIRGVPQQIE CCCCEEECCHHHHHH	36.68	-
428	Phosphorylation	IDEKVGGTNLGAPGA HHHHHCCCCCCCCCC	22.72	26074081
439	Phosphorylation	APGAFGQSPFSQPPA CCCCCCCCCCCCCCC	28.43	25159151
442	Phosphorylation	AFGQSPFSQPPAPPH CCCCCCCCCCCCCCC	45.20	28555341
452	Phosphorylation	PAPPHQNTFPPRSSG CCCCCCCCCCCCCCC	30.83	26074081
457	O-linked_Glycosylation	QNTFPPRSSGCFPNM CCCCCCCCCCCCCCC	36.53	30059200
457	Phosphorylation	QNTFPPRSSGCFPNM CCCCCCCCCCCCCCC	36.53	25159151
458	Phosphorylation	NTFPPRSSGCFPNMA CCCCCCCCCCCCCCC	40.64	25159151
518	Sumoylation	SSQPNYSKAWEDYYK CCCCCHHHHHHHHHH	47.35	-
523	Phosphorylation	YSKAWEDYYKKQSHA HHHHHHHHHHHHHHH	12.98	26074081
524	Phosphorylation	SKAWEDYYKKQSHAA HHHHHHHHHHHHHHH	24.83	26074081
525	Ubiquitination	KAWEDYYKKQSHAAS HHHHHHHHHHHHHHH	37.80	21890473
525	Ubiquitination	KAWEDYYKKQSHAAS HHHHHHHHHHHHHHH	37.80	21890473
525 (in isoform 1)	Ubiquitination	-	37.80	21890473
526	Ubiquitination	AWEDYYKKQSHAASA HHHHHHHHHHHHHHC	40.69	-
528	Phosphorylation	EDYYKKQSHAASAAP HHHHHHHHHHHHCCC	24.79	26074081
532	O-linked_Glycosylation	KKQSHAASAAPQASS HHHHHHHHCCCCCCC	26.25	30059200
532	Phosphorylation	KKQSHAASAAPQASS HHHHHHHHCCCCCCC	26.25	17081983
538	Phosphorylation	ASAAPQASSPPDYTM HHCCCCCCCCCCCHH	37.82	23401153
539	Phosphorylation	SAAPQASSPPDYTMA HCCCCCCCCCCCHHH	43.39	23401153
543	Phosphorylation	QASSPPDYTMAWAEY CCCCCCCCHHHHHHH	12.28	17081983
544	Phosphorylation	ASSPPDYTMAWAEYY CCCCCCCHHHHHHHH	14.06	21712546
550	Phosphorylation	YTMAWAEYYRQQVAF CHHHHHHHHHHHHHH	9.01	26074081
551	Phosphorylation	TMAWAEYYRQQVAFY HHHHHHHHHHHHHHH	8.08	26074081
558	Phosphorylation	YRQQVAFYGQTLGQA HHHHHHHHHCCHHHH	9.89	23403867
561	Phosphorylation	QVAFYGQTLGQAQAH HHHHHHCCHHHHHHH	28.61	22167270
569	O-linked_Glycosylation	LGQAQAHSQEQ---- HHHHHHHHCCC----	38.13	30059200
569	Phosphorylation	LGQAQAHSQEQ---- HHHHHHHHCCC----	38.13	22167270

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 FUBP3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FUBP3_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 FUBP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
NUP62_HUMAN	NUP62	physical	22939629
DPP8_HUMAN	DPP8	physical	22863883
QKI_HUMAN	QKI	physical	25416956
CATD_HUMAN	CTSD	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
NQO1_HUMAN	NQO1	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
SMRC1_HUMAN	SMARCC1	physical	26344197
QKI_HUMAN	QKI	physical	21516116

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 FUBP3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
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-569, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.	19369195 [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-296, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASSSPECTROMETRY.	17525332 [Abstract]