dbPTM

FUBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FUBP1_HUMAN
UniProt AC	Q96AE4
Protein Name	Far upstream element-binding protein 1
Gene Name	FUBP1
Organism	Homo sapiens (Human).
Sequence Length	644
Subcellular Localization	Nucleus .
Protein Description	Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription..
Protein Sequence	MADYSTVPPPSSGSAGGGGGGGGGGGVNDAFKDALQRARQIAAKIGGDAGTSLNSNDYGYGGQKRPLEDGDQPDAKKVAPQNDSFGTQLPPMHQQQSRSVMTEEYKVPDGMVGFIIGRGGEQISRIQQESGCKIQIAPDSGGLPERSCMLTGTPESVQSAKRLLDQIVEKGRPAPGFHHGDGPGNAVQEIMIPASKAGLVIGKGGETIKQLQERAGVKMVMIQDGPQNTGADKPLRITGDPYKVQQAKEMVLELIRDQGGFREVRNEYGSRIGGNEGIDVPIPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGTTPERIAQITGPPDRCQHAAEIITDLLRSVQAGNPGGPGPGGRGRGRGQGNWNMGPPGGLQEFNFIVPTGKTGLIIGKGGETIKSISQQSGARIELQRNPPPNADPNMKLFTIRGTPQQIDYARQLIEEKIGGPVNPLGPPVPHGPHGVPGPHGPPGPPGPGTPMGPYNPAPYNPGPPGPAPHGPPAPYAPQGWGNAYPHWQQQAPPDPAKAGTDPNSAAWAAYYAHYYQQQAQPPPAAPAGAPTTTQTNGQGDQQNPAPAGQVDYTKAWEEYYKKMGQAVPAPTGAPPGGQPDYSAAWAEYYRQQAAYYAQTSPQGMPQHPPAPQGQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADYSTVPP ------CCCCCCCCC	25.17	19413330
4	Phosphorylation	----MADYSTVPPPS ----CCCCCCCCCCC	9.19	18491316
5	Phosphorylation	---MADYSTVPPPSS ---CCCCCCCCCCCC	24.39	27251275
6	Phosphorylation	--MADYSTVPPPSSG --CCCCCCCCCCCCC	30.70	27251275
11	Phosphorylation	YSTVPPPSSGSAGGG CCCCCCCCCCCCCCC	53.78	25159151
12	Phosphorylation	STVPPPSSGSAGGGG CCCCCCCCCCCCCCC	42.41	25159151
14	Phosphorylation	VPPPSSGSAGGGGGG CCCCCCCCCCCCCCC	26.20	25159151
32	Ubiquitination	GGVNDAFKDALQRAR CHHHHHHHHHHHHHH	43.76	-
44	Acetylation	RARQIAAKIGGDAGT HHHHHHHHHCCCCCC	32.63	23954790
44	Ubiquitination	RARQIAAKIGGDAGT HHHHHHHHHCCCCCC	32.63	21906983
44 (in isoform 1)	Ubiquitination	-	32.63	21890473
44 (in isoform 2)	Ubiquitination	-	32.63	21890473
51	Phosphorylation	KIGGDAGTSLNSNDY HHCCCCCCCCCCCCC	31.59	21945579
52	Phosphorylation	IGGDAGTSLNSNDYG HCCCCCCCCCCCCCC	25.33	21945579
55	Phosphorylation	DAGTSLNSNDYGYGG CCCCCCCCCCCCCCC	36.05	21945579
58	Phosphorylation	TSLNSNDYGYGGQKR CCCCCCCCCCCCCCC	19.25	21945579
60	Phosphorylation	LNSNDYGYGGQKRPL CCCCCCCCCCCCCCC	16.32	21945579
64	Acetylation	DYGYGGQKRPLEDGD CCCCCCCCCCCCCCC	60.29	26051181
64	Ubiquitination	DYGYGGQKRPLEDGD CCCCCCCCCCCCCCC	60.29	21906983
64 (in isoform 1)	Ubiquitination	-	60.29	21890473
64 (in isoform 2)	Ubiquitination	-	60.29	21890473
76	Acetylation	DGDQPDAKKVAPQND CCCCCCHHHCCCCCC	55.98	25953088
76	Ubiquitination	DGDQPDAKKVAPQND CCCCCCHHHCCCCCC	55.98	21906983
76 (in isoform 1)	Ubiquitination	-	55.98	21890473
76 (in isoform 2)	Ubiquitination	-	55.98	21890473
77	Acetylation	GDQPDAKKVAPQNDS CCCCCHHHCCCCCCC	45.40	7378677
77	Ubiquitination	GDQPDAKKVAPQNDS CCCCCHHHCCCCCCC	45.40	-
84	Phosphorylation	KVAPQNDSFGTQLPP HCCCCCCCCCCCCCC	32.88	20068231
84 (in isoform 2)	Phosphorylation	-	32.88	28674419
87	Phosphorylation	PQNDSFGTQLPPMHQ CCCCCCCCCCCCHHH	25.56	20068231
87 (in isoform 2)	Phosphorylation	-	25.56	20068231
98 (in isoform 2)	Phosphorylation	-	29.00	21857030
99	Phosphorylation	MHQQQSRSVMTEEYK HHHHHCCCCCCCEEC	22.84	23911959
102	Phosphorylation	QQSRSVMTEEYKVPD HHCCCCCCCEECCCC	24.41	28450419
105	Phosphorylation	RSVMTEEYKVPDGMV CCCCCCEECCCCCCE	15.85	21406692
118	Methylation	MVGFIIGRGGEQISR CEEEEECCCCHHHHH	39.26	-
133	Acetylation	IQQESGCKIQIAPDS HHHHHCCEEEECCCC	40.97	25953088
133	Ubiquitination	IQQESGCKIQIAPDS HHHHHCCEEEECCCC	40.97	-
140	Phosphorylation	KIQIAPDSGGLPERS EEEECCCCCCCCCCC	33.43	30266825
147	Phosphorylation	SGGLPERSCMLTGTP CCCCCCCCEECCCCH	11.39	23403867
148	Glutathionylation	GGLPERSCMLTGTPE CCCCCCCEECCCCHH	3.03	22555962
148	S-nitrosylation	GGLPERSCMLTGTPE CCCCCCCEECCCCHH	3.03	22126794
149	Sulfoxidation	GLPERSCMLTGTPES CCCCCCEECCCCHHH	3.86	21406390
151	Phosphorylation	PERSCMLTGTPESVQ CCCCEECCCCHHHHH	16.48	30266825
153	Phosphorylation	RSCMLTGTPESVQSA CCEECCCCHHHHHHH	20.74	22167270
156	Phosphorylation	MLTGTPESVQSAKRL ECCCCHHHHHHHHHH	27.02	30266825
159	Phosphorylation	GTPESVQSAKRLLDQ CCHHHHHHHHHHHHH	33.33	23927012
161	Acetylation	PESVQSAKRLLDQIV HHHHHHHHHHHHHHH	49.15	25953088
161	Ubiquitination	PESVQSAKRLLDQIV HHHHHHHHHHHHHHH	49.15	-
170	Acetylation	LLDQIVEKGRPAPGF HHHHHHHCCCCCCCC	49.69	25953088
196	Acetylation	EIMIPASKAGLVIGK EEEEEHHHCCEEECC	48.88	25953088
202 (in isoform 2)	Ubiquitination	-	18.31	21890473
203	Ubiquitination	KAGLVIGKGGETIKQ HCCEEECCCCHHHHH	53.25	21906983
203 (in isoform 1)	Ubiquitination	-	53.25	21890473
207	Phosphorylation	VIGKGGETIKQLQER EECCCCHHHHHHHHH	36.43	22817900
208 (in isoform 2)	Ubiquitination	-	2.02	21890473
209	Ubiquitination	GKGGETIKQLQERAG CCCCHHHHHHHHHHC	52.99	-
209 (in isoform 1)	Ubiquitination	-	52.99	21890473
218	Acetylation	LQERAGVKMVMIQDG HHHHHCCCEEEEECC	25.51	25953088
218	Ubiquitination	LQERAGVKMVMIQDG HHHHHCCCEEEEECC	25.51	-
219	Sulfoxidation	QERAGVKMVMIQDGP HHHHCCCEEEEECCC	1.99	28183972
221	Sulfoxidation	RAGVKMVMIQDGPQN HHCCCEEEEECCCCC	1.72	28183972
229	Phosphorylation	IQDGPQNTGADKPLR EECCCCCCCCCCCCE	28.62	20068231
233	Acetylation	PQNTGADKPLRITGD CCCCCCCCCCEECCC	45.47	26051181
242	Phosphorylation	LRITGDPYKVQQAKE CEECCCCHHHHHHHH	28.65	28152594
243	Acetylation	RITGDPYKVQQAKEM EECCCCHHHHHHHHH	38.67	23749302
243	Malonylation	RITGDPYKVQQAKEM EECCCCHHHHHHHHH	38.67	26320211
243	Ubiquitination	RITGDPYKVQQAKEM EECCCCHHHHHHHHH	38.67	-
250	Sulfoxidation	KVQQAKEMVLELIRD HHHHHHHHHHHHHHH	4.03	28183972
268	Phosphorylation	FREVRNEYGSRIGGN HHHHHHHHHCCCCCC	24.77	30576142
270	Phosphorylation	EVRNEYGSRIGGNEG HHHHHHHCCCCCCCC	21.59	21712546
300	Ubiquitination	RNGEMIKKIQNDAGV CCHHHHHHHCCCCCC	38.30	-
308	Methylation	IQNDAGVRIQFKPDD HCCCCCCCEEECCCC	18.97	-
311 (in isoform 2)	Ubiquitination	-	13.27	21890473
312	Sumoylation	AGVRIQFKPDDGTTP CCCCEEECCCCCCCH	31.03	-
312	Acetylation	AGVRIQFKPDDGTTP CCCCEEECCCCCCCH	31.03	23954790
312	Malonylation	AGVRIQFKPDDGTTP CCCCEEECCCCCCCH	31.03	26320211
312	Sumoylation	AGVRIQFKPDDGTTP CCCCEEECCCCCCCH	31.03	-
312	Ubiquitination	AGVRIQFKPDDGTTP CCCCEEECCCCCCCH	31.03	-
312 (in isoform 1)	Ubiquitination	-	31.03	21890473
317	Phosphorylation	QFKPDDGTTPERIAQ EECCCCCCCHHHHHH	46.29	29214152
318	Phosphorylation	FKPDDGTTPERIAQI ECCCCCCCHHHHHHH	28.78	28674419
321	Methylation	DDGTTPERIAQITGP CCCCCHHHHHHHHCC	30.65	-
331	Methylation	QITGPPDRCQHAAEI HHHCCCHHHHHHHHH	27.98	-
359	Dimethylation	GGPGPGGRGRGRGQG CCCCCCCCCCCCCCC	37.23	-
359	Methylation	GGPGPGGRGRGRGQG CCCCCCCCCCCCCCC	37.23	24129315
361	Dimethylation	PGPGGRGRGRGQGNW CCCCCCCCCCCCCCC	30.21	-
361	Methylation	PGPGGRGRGRGQGNW CCCCCCCCCCCCCCC	30.21	24129315
363	Dimethylation	PGGRGRGRGQGNWNM CCCCCCCCCCCCCCC	32.66	-
363	Methylation	PGGRGRGRGQGNWNM CCCCCCCCCCCCCCC	32.66	24129315
394	Acetylation	KTGLIIGKGGETIKS CCEEEECCCCHHHHH	54.02	25953088
394	Malonylation	KTGLIIGKGGETIKS CCEEEECCCCHHHHH	54.02	26320211
394	Succinylation	KTGLIIGKGGETIKS CCEEEECCCCHHHHH	54.02	23954790
394	Ubiquitination	KTGLIIGKGGETIKS CCEEEECCCCHHHHH	54.02	-
398	Phosphorylation	IIGKGGETIKSISQQ EECCCCHHHHHHHHH	36.66	-
399 (in isoform 2)	Ubiquitination	-	2.61	21890473
400	Acetylation	GKGGETIKSISQQSG CCCCHHHHHHHHHCC	49.51	23236377
400	Ubiquitination	GKGGETIKSISQQSG CCCCHHHHHHHHHCC	49.51	21906983
400 (in isoform 1)	Ubiquitination	-	49.51	21890473
424 (in isoform 2)	Ubiquitination	-	4.93	21890473
425	Acetylation	PNADPNMKLFTIRGT CCCCCCCEEEEECCC	47.27	23236377
425	Ubiquitination	PNADPNMKLFTIRGT CCCCCCCEEEEECCC	47.27	2189047
425 (in isoform 1)	Ubiquitination	-	47.27	21890473
428	Phosphorylation	DPNMKLFTIRGTPQQ CCCCEEEEECCCHHH	21.87	29214152
430	Methylation	NMKLFTIRGTPQQID CCEEEEECCCHHHHH	39.62	-
432	Phosphorylation	KLFTIRGTPQQIDYA EEEEECCCHHHHHHH	14.21	25159151
438	Nitration	GTPQQIDYARQLIEE CCHHHHHHHHHHHHH	12.81	-
438	Phosphorylation	GTPQQIDYARQLIEE CCHHHHHHHHHHHHH	12.81	28152594
446	Ubiquitination	ARQLIEEKIGGPVNP HHHHHHHHHCCCCCC	33.58	-
589	Phosphorylation	YTKAWEEYYKKMGQA HHHHHHHHHHHHCCC	14.74	28152594
590	Phosphorylation	TKAWEEYYKKMGQAV HHHHHHHHHHHCCCC	13.86	28152594
591	Acetylation	KAWEEYYKKMGQAVP HHHHHHHHHHCCCCC	35.07	23749302
591	Succinylation	KAWEEYYKKMGQAVP HHHHHHHHHHCCCCC	35.07	23954790
592	Ubiquitination	AWEEYYKKMGQAVPA HHHHHHHHHCCCCCC	31.94	-
601	O-linked_Glycosylation	GQAVPAPTGAPPGGQ CCCCCCCCCCCCCCC	48.35	32119511
601	Phosphorylation	GQAVPAPTGAPPGGQ CCCCCCCCCCCCCCC	48.35	21945579
611	Phosphorylation	PPGGQPDYSAAWAEY CCCCCCCCHHHHHHH	13.59	21945579
612	Phosphorylation	PGGQPDYSAAWAEYY CCCCCCCHHHHHHHH	20.91	21945579
618	Phosphorylation	YSAAWAEYYRQQAAY CHHHHHHHHHHHHHH	9.01	-
619	Phosphorylation	SAAWAEYYRQQAAYY HHHHHHHHHHHHHHH	8.08	-
625	Phosphorylation	YYRQQAAYYAQTSPQ HHHHHHHHHHCCCCC	11.44	21945579
626	Phosphorylation	YRQQAAYYAQTSPQG HHHHHHHHHCCCCCC	6.36	21945579
629	Phosphorylation	QAAYYAQTSPQGMPQ HHHHHHCCCCCCCCC	33.91	26846344
630	Phosphorylation	AAYYAQTSPQGMPQH HHHHHCCCCCCCCCC	11.80	26846344

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
58	Y	Phosphorylation	Kinase	SRC	P12931	PSP
268	Y	Phosphorylation	Kinase	SRC	P12931	PSP
625	Y	Phosphorylation	Kinase	SRC	P12931	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:16672220

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FUBP1_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 FUBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CELF1_HUMAN	CELF1	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
VIME_HUMAN	VIM	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
SMN_HUMAN	SMN1	physical	10734235
CCNH_HUMAN	CCNH	physical	11239393
TF2H1_HUMAN	GTF2H1	physical	11239393
UBP22_HUMAN	USP22	physical	21779003
RM32_HUMAN	MRPL32	physical	22939629
RM41_HUMAN	MRPL41	physical	22939629
KPYM_HUMAN	PKM	physical	22939629
RM38_HUMAN	MRPL38	physical	22939629
RM02_HUMAN	MRPL2	physical	22939629
RM46_HUMAN	MRPL46	physical	22939629
ITA5_HUMAN	ITGA5	physical	22939629
RS15_HUMAN	RPS15	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
PCBP1_HUMAN	PCBP1	physical	22939629
CERS2_HUMAN	CERS2	physical	22939629
RM42_HUMAN	MRPL42	physical	22939629
PGM1_HUMAN	PGM1	physical	22939629
PDCD6_HUMAN	PDCD6	physical	22939629
ACOC_HUMAN	ACO1	physical	22863883
CNN2_HUMAN	CNN2	physical	22863883
DD19A_HUMAN	DDX19A	physical	22863883
GRPE1_HUMAN	GRPEL1	physical	22863883
H2B1O_HUMAN	HIST1H2BO	physical	22863883
LEG1_HUMAN	LGALS1	physical	22863883
PLD3_HUMAN	PLD3	physical	22863883
PPP5_HUMAN	PPP5C	physical	22863883
ANX11_HUMAN	ANXA11	physical	26344197
ANXA2_HUMAN	ANXA2	physical	26344197
CCD58_HUMAN	CCDC58	physical	26344197
CHRD1_HUMAN	CHORDC1	physical	26344197
DUT_HUMAN	DUT	physical	26344197
FUBP3_HUMAN	FUBP3	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
NDKA_HUMAN	NME1	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PPIC_HUMAN	PPIC	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
RAB1A_HUMAN	RAB1A	physical	26344197
SIN3A_HUMAN	SIN3A	physical	26344197
SMRC1_HUMAN	SMARCC1	physical	26344197
SMRC2_HUMAN	SMARCC2	physical	26344197
PRKN_HUMAN	PARK2	physical	16672220

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 FUBP1_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-52; SER-55; THR-153 AND SER-630, AND MASSSPECTROMETRY.	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-630, AND MASSSPECTROMETRY.	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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-52; SER-55; THR-153 AND SER-630, 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-140; THR-153 ANDSER-630, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153 AND SER-630, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-153, AND MASSSPECTROMETRY.	16964243 [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 TYR-626, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58, AND MASSSPECTROMETRY.	15592455 [Abstract]