dbPTM

REQU_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	REQU_HUMAN
UniProt AC	Q92785
Protein Name	Zinc finger protein ubi-d4
Gene Name	DPF2
Organism	Homo sapiens (Human).
Sequence Length	391
Subcellular Localization	Nucleus. Cytoplasm. 30% nuclear. 70% cytoplasmic.
Protein Description	May be a transcription factor required for the apoptosis response following survival factor withdrawal from myeloid cells. Might also have a role in the development and maturation of lymphoid cells..
Protein Sequence	MAAVVENVVKLLGEQYYKDAMEQCHNYNARLCAERSVRLPFLDSQTGVAQSNCYIWMEKRHRGPGLASGQLYSYPARRWRKKRRAHPPEDPRLSFPSIKPDTDQTLKKEGLISQDGSSLEALLRTDPLEKRGAPDPRVDDDSLGEFPVTNSRARKRILEPDDFLDDLDDEDYEEDTPKRRGKGKSKGKGVGSARKKLDASILEDRDKPYACDICGKRYKNRPGLSYHYAHSHLAEEEGEDKEDSQPPTPVSQRSEEQKSKKGPDGLALPNNYCDFCLGDSKINKKTGQPEELVSCSDCGRSGHPSCLQFTPVMMAAVKTYRWQCIECKCCNICGTSENDDQLLFCDDCDRGYHMYCLTPSMSEPPEGSWSCHLCLDLLKEKASIYQNQNSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAVVENVV ------CHHHHHHHH	14.68	19413330
10	Ubiquitination	AVVENVVKLLGEQYY HHHHHHHHHHHHHHH	33.44	-
10	Sumoylation	AVVENVVKLLGEQYY HHHHHHHHHHHHHHH	33.44	28112733
10	Sumoylation	AVVENVVKLLGEQYY HHHHHHHHHHHHHHH	33.44	-
18	Acetylation	LLGEQYYKDAMEQCH HHHHHHHHHHHHHHH	33.79	26051181
38	Methylation	LCAERSVRLPFLDSQ HHHHHCCCCCEECCC	37.58	115387911
59	Ubiquitination	NCYIWMEKRHRGPGL CEEEEEEECCCCCCC	37.08	-
59	Ubiquitination	NCYIWMEKRHRGPGL CEEEEEEECCCCCCC	37.08	-
62	Methylation	IWMEKRHRGPGLASG EEEEECCCCCCCCCC	57.97	115491075
68	Phosphorylation	HRGPGLASGQLYSYP CCCCCCCCCCCCCCC	31.92	28796482
72	Phosphorylation	GLASGQLYSYPARRW CCCCCCCCCCCHHHH	9.77	28796482
73	Phosphorylation	LASGQLYSYPARRWR CCCCCCCCCCHHHHH	32.98	28796482
74	Phosphorylation	ASGQLYSYPARRWRK CCCCCCCCCHHHHHH	6.32	28796482
77	Methylation	QLYSYPARRWRKKRR CCCCCCHHHHHHHHC	33.90	115491059
78	Methylation	LYSYPARRWRKKRRA CCCCCHHHHHHHHCC	39.39	115491067
92	Methylation	AHPPEDPRLSFPSIK CCCCCCCCCCCCCCC	56.11	115491051
94	Phosphorylation	PPEDPRLSFPSIKPD CCCCCCCCCCCCCCC	36.07	25159151
97	Phosphorylation	DPRLSFPSIKPDTDQ CCCCCCCCCCCCCCC	41.03	17287340
99	Ubiquitination	RLSFPSIKPDTDQTL CCCCCCCCCCCCCHH	40.97	-
99	Sumoylation	RLSFPSIKPDTDQTL CCCCCCCCCCCCCHH	40.97	-
99	Sumoylation	RLSFPSIKPDTDQTL CCCCCCCCCCCCCHH	40.97	28112733
99	Ubiquitination	RLSFPSIKPDTDQTL CCCCCCCCCCCCCHH	40.97	-
105	Phosphorylation	IKPDTDQTLKKEGLI CCCCCCCHHHHCCCC	43.27	28555341
107	Sumoylation	PDTDQTLKKEGLISQ CCCCCHHHHCCCCCC	52.76	-
107	Sumoylation	PDTDQTLKKEGLISQ CCCCCHHHHCCCCCC	52.76	28112733
108	Ubiquitination	DTDQTLKKEGLISQD CCCCHHHHCCCCCCC	61.19	21890473
108	Ubiquitination	DTDQTLKKEGLISQD CCCCHHHHCCCCCCC	61.19	21890473
108	Sumoylation	DTDQTLKKEGLISQD CCCCHHHHCCCCCCC	61.19	28112733
113	Phosphorylation	LKKEGLISQDGSSLE HHHCCCCCCCCCHHH	27.54	21712546
117	Phosphorylation	GLISQDGSSLEALLR CCCCCCCCHHHHHHC	39.79	30266825
118	Phosphorylation	LISQDGSSLEALLRT CCCCCCCHHHHHHCC	35.44	30266825
125	Phosphorylation	SLEALLRTDPLEKRG HHHHHHCCCHHHHCC	41.77	29496963
130	Ubiquitination	LRTDPLEKRGAPDPR HCCCHHHHCCCCCCC	64.91	-
130	Ubiquitination	LRTDPLEKRGAPDPR HCCCHHHHCCCCCCC	64.91	-
142	Phosphorylation	DPRVDDDSLGEFPVT CCCCCCCCCCCCCCC	45.31	29255136
142 (in isoform 2)	Phosphorylation	-	45.31	29743597
149	Phosphorylation	SLGEFPVTNSRARKR CCCCCCCCCHHHHHH	27.93	23927012
151	Phosphorylation	GEFPVTNSRARKRIL CCCCCCCHHHHHHCC	20.25	23927012
155	Acetylation	VTNSRARKRILEPDD CCCHHHHHHCCCCCC	42.69	26051181
172	Phosphorylation	DDLDDEDYEEDTPKR HCCCCCCCCCCCCCC	21.12	28176443
176	Phosphorylation	DEDYEEDTPKRRGKG CCCCCCCCCCCCCCC	33.71	19664994
178	Sumoylation	DYEEDTPKRRGKGKS CCCCCCCCCCCCCCC	57.74	28112733
178	Ubiquitination	DYEEDTPKRRGKGKS CCCCCCCCCCCCCCC	57.74	-
184	Acetylation	PKRRGKGKSKGKGVG CCCCCCCCCCCCCCH	53.10	7589121
185	Phosphorylation	KRRGKGKSKGKGVGS CCCCCCCCCCCCCHH	56.14	26074081
186	Acetylation	RRGKGKSKGKGVGSA CCCCCCCCCCCCHHH	69.03	18528575
188	Acetylation	GKGKSKGKGVGSARK CCCCCCCCCCHHHHH	54.91	7589131
195	Acetylation	KGVGSARKKLDASIL CCCHHHHHHHCHHHH	58.36	23749302
195	Methylation	KGVGSARKKLDASIL CCCHHHHHHHCHHHH	58.36	18528583
196	Sumoylation	GVGSARKKLDASILE CCHHHHHHHCHHHHC	46.15	28112733
196	Ubiquitination	GVGSARKKLDASILE CCHHHHHHHCHHHHC	46.15	-
196	Methylation	GVGSARKKLDASILE CCHHHHHHHCHHHHC	46.15	115976525
197	Ubiquitination	VGSARKKLDASILED CHHHHHHHCHHHHCC	8.14	-
200	Phosphorylation	ARKKLDASILEDRDK HHHHHCHHHHCCCCC	27.63	23401153
216	Acetylation	YACDICGKRYKNRPG CEECCCCCCCCCCCC	48.41	25953088
218	Phosphorylation	CDICGKRYKNRPGLS ECCCCCCCCCCCCCC	18.99	23312004
225	Phosphorylation	YKNRPGLSYHYAHSH CCCCCCCCHHHHHHH	18.77	23927012
226	Phosphorylation	KNRPGLSYHYAHSHL CCCCCCCHHHHHHHH	12.14	27422710
228	Phosphorylation	RPGLSYHYAHSHLAE CCCCCHHHHHHHHCH	9.58	23927012
231	Phosphorylation	LSYHYAHSHLAEEEG CCHHHHHHHHCHHHC	16.42	23927012
244	Phosphorylation	EGEDKEDSQPPTPVS HCCCCCCCCCCCCHH	45.75	29255136
248	Phosphorylation	KEDSQPPTPVSQRSE CCCCCCCCCHHHCCH	42.90	20164059
251	Phosphorylation	SQPPTPVSQRSEEQK CCCCCCHHHCCHHHH	22.53	23927012
254	Phosphorylation	PTPVSQRSEEQKSKK CCCHHHCCHHHHHCC	37.54	23090842
261	Acetylation	SEEQKSKKGPDGLAL CHHHHHCCCCCCCCC	80.78	23749302
261	Ubiquitination	SEEQKSKKGPDGLAL CHHHHHCCCCCCCCC	80.78	-
272	Phosphorylation	GLALPNNYCDFCLGD CCCCCCCCCCCCCCC	10.47	23312004
280	Phosphorylation	CDFCLGDSKINKKTG CCCCCCCCHHCCCCC	33.37	25159151
281	Sumoylation	DFCLGDSKINKKTGQ CCCCCCCHHCCCCCC	55.85	28112733
285	Ubiquitination	GDSKINKKTGQPEEL CCCHHCCCCCCCHHH	54.09	-
305	Phosphorylation	CGRSGHPSCLQFTPV CCCCCCCCHHHHHHH	23.06	-
310	Phosphorylation	HPSCLQFTPVMMAAV CCCHHHHHHHHHHHH	11.30	25159151
318	Acetylation	PVMMAAVKTYRWQCI HHHHHHHHHHCEEEE	34.80	25953088
358	Phosphorylation	GYHMYCLTPSMSEPP CEEEEEECCCCCCCC	15.12	25159151
381	Ubiquitination	CLDLLKEKASIYQNQ HHHHHHHHHHHHHCC	45.93	21890473
385	Phosphorylation	LKEKASIYQNQNSS- HHHHHHHHHCCCCC-	10.02	23312004
390	Phosphorylation	SIYQNQNSS------ HHHHCCCCC------	27.88	25159151
391	Phosphorylation	IYQNQNSS------- HHHCCCCC-------	52.36	25159151

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
176	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAF_HUMAN	BANF1	physical	19759913
SMRC1_HUMAN	SMARCC1	physical	20460684
SMCA2_HUMAN	SMARCA2	physical	20460684
SMCA4_HUMAN	SMARCA4	physical	20460684
SMRD1_HUMAN	SMARCD1	physical	20460684
SNF5_HUMAN	SMARCB1	physical	20460684
TF65_HUMAN	RELA	physical	20460684
RELB_HUMAN	RELB	physical	20460684
REL_HUMAN	REL	physical	20460684
NFKB1_HUMAN	NFKB1	physical	20460684
NFKB2_HUMAN	NFKB2	physical	20460684
TF65_HUMAN	RELA	physical	22334708
NFKB1_HUMAN	NFKB1	physical	22334708
SMCA2_HUMAN	SMARCA2	physical	22334708
SMCA4_HUMAN	SMARCA4	physical	22334708
SMRC1_HUMAN	SMARCC1	physical	22334708
FHL2_HUMAN	FHL2	physical	18255255
LDOC1_HUMAN	LDOC1	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
SMCE1_HUMAN	SMARCE1	physical	26186194
ARI1A_HUMAN	ARID1A	physical	26186194
ARI1B_HUMAN	ARID1B	physical	26186194
SMRC2_HUMAN	SMARCC2	physical	26186194
SMRC1_HUMAN	SMARCC1	physical	26186194
SMCA2_HUMAN	SMARCA2	physical	26186194
SMCA4_HUMAN	SMARCA4	physical	26186194
SMRD3_HUMAN	SMARCD3	physical	26186194
SMRD2_HUMAN	SMARCD2	physical	26186194
SMRD1_HUMAN	SMARCD1	physical	26186194
SNF5_HUMAN	SMARCB1	physical	26186194
BCL7A_HUMAN	BCL7A	physical	26186194
BCL7C_HUMAN	BCL7C	physical	26186194
BCL7B_HUMAN	BCL7B	physical	26186194
ACL6A_HUMAN	ACTL6A	physical	26186194
ACL6B_HUMAN	ACTL6B	physical	26186194
SSXT_HUMAN	SS18	physical	26186194
CREST_HUMAN	SS18L1	physical	26186194
ARI1A_HUMAN	ARID1A	physical	26344197
ARI1B_HUMAN	ARID1B	physical	26344197
SMRD1_HUMAN	SMARCD1	physical	28514442
SMRC2_HUMAN	SMARCC2	physical	28514442
ARI1B_HUMAN	ARID1B	physical	28514442
SMCA2_HUMAN	SMARCA2	physical	28514442
SMRD3_HUMAN	SMARCD3	physical	28514442
CREST_HUMAN	SS18L1	physical	28514442
SMRD2_HUMAN	SMARCD2	physical	28514442
SMCE1_HUMAN	SMARCE1	physical	28514442
BCL7B_HUMAN	BCL7B	physical	28514442
SMCA4_HUMAN	SMARCA4	physical	28514442
SNF5_HUMAN	SMARCB1	physical	28514442
SSXT_HUMAN	SS18	physical	28514442
SMRC1_HUMAN	SMARCC1	physical	28514442
ARI1A_HUMAN	ARID1A	physical	28514442
ACL6B_HUMAN	ACTL6B	physical	28514442
ACL6A_HUMAN	ACTL6A	physical	28514442
H31_HUMAN	HIST1H3A	physical	27775714

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 REQU_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-142, 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-142; TYR-172 ANDTHR-176, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-142, 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-142; THR-176 ANDSER-200, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-97 AND SER-142,AND MASS SPECTROMETRY.	17287340 [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-142, AND MASSSPECTROMETRY.	17081983 [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 SER-142, AND MASSSPECTROMETRY.	15302935 [Abstract]