CNBP_HUMAN - dbPTM
CNBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNBP_HUMAN
UniProt AC P62633
Protein Name Cellular nucleic acid-binding protein
Gene Name CNBP
Organism Homo sapiens (Human).
Sequence Length 177
Subcellular Localization Cytoplasm. Endoplasmic reticulum.
Protein Description Single-stranded DNA-binding protein, with specificity to the sterol regulatory element (SRE). Involved in sterol-mediated repression..
Protein Sequence MSSNECFKCGRSGHWARECPTGGGRGRGMRSRGRGGFTSDRGFQFVSSSLPDICYRCGESGHLAKDCDLQEDACYNCGRGGHIAKDCKEPKREREQCCYNCGKPGHLARDCDHADEQKCYSCGEFGHIQKDCTKVKCYRCGETGHVAINCSKTSEVNCYRCGESGHLARECTIEATA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSSNECFKC
------CCCCCCCCC
41.7022814378
2Phosphorylation------MSSNECFKC
------CCCCCCCCC
41.7027251275
3Phosphorylation-----MSSNECFKCG
-----CCCCCCCCCC
35.0424719451
3 (in isoform 6)Phosphorylation-35.0424719451
8MethylationMSSNECFKCGRSGHW
CCCCCCCCCCCCCCC
47.6583040663
8AcetylationMSSNECFKCGRSGHW
CCCCCCCCCCCCCCC
47.65-
8UbiquitinationMSSNECFKCGRSGHW
CCCCCCCCCCCCCCC
47.65-
8SuccinylationMSSNECFKCGRSGHW
CCCCCCCCCCCCCCC
47.6523954790
8AcetylationMSSNECFKCGRSGHW
CCCCCCCCCCCCCCC
47.6523749302
8UbiquitinationMSSNECFKCGRSGHW
CCCCCCCCCCCCCCC
47.65-
11MethylationNECFKCGRSGHWARE
CCCCCCCCCCCCCCC
49.27115920677
12 (in isoform 6)Phosphorylation-21.9424719451
12PhosphorylationECFKCGRSGHWAREC
CCCCCCCCCCCCCCC
21.9426657352
25DimethylationECPTGGGRGRGMRSR
CCCCCCCCCCCCCCC
34.60-
25MethylationECPTGGGRGRGMRSR
CCCCCCCCCCCCCCC
34.6024726729
27MethylationPTGGGRGRGMRSRGR
CCCCCCCCCCCCCCC
34.0824726729
27DimethylationPTGGGRGRGMRSRGR
CCCCCCCCCCCCCCC
34.08-
30MethylationGGRGRGMRSRGRGGF
CCCCCCCCCCCCCCC
26.4854560907
32 (in isoform 5)Methylation-28.5924129315
32 (in isoform 2)Methylation-28.5924129315
32 (in isoform 8)Methylation-28.5924129315
32DimethylationRGRGMRSRGRGGFTS
CCCCCCCCCCCCCCC
28.59-
32MethylationRGRGMRSRGRGGFTS
CCCCCCCCCCCCCCC
28.5924394347
34 (in isoform 5)Methylation-40.7424129315
34 (in isoform 2)Methylation-40.7424129315
34DimethylationRGMRSRGRGGFTSDR
CCCCCCCCCCCCCHH
40.74-
34MethylationRGMRSRGRGGFTSDR
CCCCCCCCCCCCCHH
40.7412018949
34 (in isoform 8)Methylation-40.7424129315
41 (in isoform 8)Phosphorylation-47.8229116813
41 (in isoform 2)Phosphorylation-47.8229116813
41 (in isoform 5)Phosphorylation-47.8229116813
47PhosphorylationDRGFQFVSSSLPDIC
HHCCHHHHCCCCHHH
18.5922617229
47 (in isoform 6)Phosphorylation-18.5927251275
48AcetylationRGFQFVSSSLPDICY
HCCHHHHCCCCHHHH
30.50-
48PhosphorylationRGFQFVSSSLPDICY
HCCHHHHCCCCHHHH
30.5028348404
48UbiquitinationRGFQFVSSSLPDICY
HCCHHHHCCCCHHHH
30.50-
48 (in isoform 6)Phosphorylation-30.5027251275
49PhosphorylationGFQFVSSSLPDICYR
CCHHHHCCCCHHHHH
36.0922617229
49 (in isoform 6)Phosphorylation-36.0924719451
54GlutathionylationSSSLPDICYRCGESG
HCCCCHHHHHCCCCC
1.9822555962
55PhosphorylationSSLPDICYRCGESGH
CCCCHHHHHCCCCCC
14.8520068231
65UbiquitinationGESGHLAKDCDLQED
CCCCCCCCCCCCCCC
66.31-
65AcetylationGESGHLAKDCDLQED
CCCCCCCCCCCCCCC
66.3123749302
68AcetylationGHLAKDCDLQEDACY
CCCCCCCCCCCCCCH
62.61-
73 (in isoform 8)Methylation-9.2824129315
75PhosphorylationDLQEDACYNCGRGGH
CCCCCCCHHCCCCCC
18.4028796482
79MethylationDACYNCGRGGHIAKD
CCCHHCCCCCCHHCC
50.5524129315
80 (in isoform 4)Methylation-19.8124129315
85AcetylationGRGGHIAKDCKEPKR
CCCCCHHCCCCCCCH
64.1623749302
86UbiquitinationRGGHIAKDCKEPKRE
CCCCHHCCCCCCCHH
39.43-
86AcetylationRGGHIAKDCKEPKRE
CCCCHHCCCCCCCHH
39.43-
97AcetylationPKREREQCCYNCGKP
CCHHHHHHHHHCCCC
1.9719608861
97UbiquitinationPKREREQCCYNCGKP
CCHHHHHHHHHCCCC
1.9719608861
97GlutathionylationPKREREQCCYNCGKP
CCHHHHHHHHHCCCC
1.9722555962
98AcetylationKREREQCCYNCGKPG
CHHHHHHHHHCCCCC
2.4619608861
98UbiquitinationKREREQCCYNCGKPG
CHHHHHHHHHCCCCC
2.4619608861
99PhosphorylationREREQCCYNCGKPGH
HHHHHHHHHCCCCCC
22.5521945579
101UbiquitinationREQCCYNCGKPGHLA
HHHHHHHCCCCCCHH
2.75-
103UbiquitinationQCCYNCGKPGHLARD
HHHHHCCCCCCHHCC
50.45-
103AcetylationQCCYNCGKPGHLARD
HHHHHCCCCCCHHCC
50.4523749302
104UbiquitinationCCYNCGKPGHLARDC
HHHHCCCCCCHHCCC
22.2619608861
104AcetylationCCYNCGKPGHLARDC
HHHHCCCCCCHHCCC
22.2619608861
105AcetylationCYNCGKPGHLARDCD
HHHCCCCCCHHCCCC
31.7419608861
105UbiquitinationCYNCGKPGHLARDCD
HHHCCCCCCHHCCCC
31.7419608861
113UbiquitinationHLARDCDHADEQKCY
CHHCCCCCCCCHHCC
41.22-
117UbiquitinationDCDHADEQKCYSCGE
CCCCCCCHHCCCCCC
41.49-
118AcetylationCDHADEQKCYSCGEF
CCCCCCHHCCCCCCC
32.8525953088
118UbiquitinationCDHADEQKCYSCGEF
CCCCCCHHCCCCCCC
32.85-
119GlutathionylationDHADEQKCYSCGEFG
CCCCCHHCCCCCCCC
2.7822555962
120PhosphorylationHADEQKCYSCGEFGH
CCCCHHCCCCCCCCC
17.6525394399
121PhosphorylationADEQKCYSCGEFGHI
CCCHHCCCCCCCCCC
25.7228348404
123 (in isoform 6)Phosphorylation-27.5927251275
130UbiquitinationGEFGHIQKDCTKVKC
CCCCCCCCCCCEEEE
54.92-
130AcetylationGEFGHIQKDCTKVKC
CCCCCCCCCCCEEEE
54.9225953088
135UbiquitinationIQKDCTKVKCYRCGE
CCCCCCEEEEEECCC
2.52-
143PhosphorylationKCYRCGETGHVAINC
EEEECCCCCCEEEEC
20.1923312004
151PhosphorylationGHVAINCSKTSEVNC
CCEEEECCCCCCEEE
34.1820068231
152AcetylationHVAINCSKTSEVNCY
CEEEECCCCCCEEEE
59.2725953088
152UbiquitinationHVAINCSKTSEVNCY
CEEEECCCCCCEEEE
59.27-
153 (in isoform 6)Phosphorylation-17.5227251275
153PhosphorylationVAINCSKTSEVNCYR
EEEECCCCCCEEEEE
17.5221945579
154PhosphorylationAINCSKTSEVNCYRC
EEECCCCCCEEEEEC
43.1921945579
159PhosphorylationKTSEVNCYRCGESGH
CCCCEEEEECCCCCC
12.0721945579
164PhosphorylationNCYRCGESGHLAREC
EEEECCCCCCEEEEE
19.4521945579
166 (in isoform 6)Phosphorylation-26.1224719451
172PhosphorylationGHLARECTIEATA--
CCEEEEEEEEECC--
19.6626437602
174 (in isoform 6)Phosphorylation-23.0924719451
176PhosphorylationRECTIEATA------
EEEEEEECC------
21.8027251275
178 (in isoform 6)Phosphorylation-24719451

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 CNBP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNBP_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 CNBP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF2B1_HUMANIGF2BP1physical
17353931
RL3_HUMANRPL3physical
17353931
HNRPC_HUMANHNRNPCphysical
17353931
PURA_HUMANPURAphysical
17353931
RS3A_HUMANRPS3Aphysical
17353931
DHX9_HUMANDHX9physical
17353931
ROAA_HUMANHNRNPABphysical
17353931
RL34_HUMANRPL34physical
17353931
IF2B3_HUMANIGF2BP3physical
17353931
BRX1_HUMANBRIX1physical
17353931
RL23A_HUMANRPL23Aphysical
17353931
RBMX_HUMANRBMXphysical
17353931
HNRPR_HUMANHNRNPRphysical
17353931
RL31_HUMANRPL31physical
17353931
RL35A_HUMANRPL35Aphysical
17353931
RS16_HUMANRPS16physical
17353931
ABC3C_HUMANAPOBEC3Cphysical
17353931
RFA3_HUMANRPA3physical
17353931
RL36_HUMANRPL36physical
17353931
RS19_HUMANRPS19physical
17353931
ERH_HUMANERHphysical
17353931
EBP2_HUMANEBNA1BP2physical
17353931
HNRL1_HUMANHNRNPUL1physical
17353931
HNRPQ_HUMANSYNCRIPphysical
17353931
ROA3_HUMANHNRNPA3physical
17353931
RL1D1_HUMANRSL1D1physical
17353931
RT29_HUMANDAP3physical
17353931
FKTN_HUMANFKTNphysical
21232131
MYH4_HUMANMYH4physical
21232131
BZW2_HUMANBZW2physical
22863883
PABP3_HUMANPABPC3physical
26344197
PABP4_HUMANPABPC4physical
26344197
TRI56_HUMANTRIM56physical
28514442
H11_HUMANHIST1H1Aphysical
28514442
NLE1_HUMANNLE1physical
28514442
ZN275_HUMANZNF275physical
28514442
CENPR_HUMANITGB3BPphysical
28514442
RL18_HUMANRPL18physical
28514442
RL36_HUMANRPL36physical
28514442
RPF2_HUMANRPF2physical
28514442
RL26L_HUMANRPL26L1physical
28514442
DDX31_HUMANDDX31physical
28514442
RLA0_HUMANRPLP0physical
28514442
RL27_HUMANRPL27physical
28514442
NOG1_HUMANGTPBP4physical
28514442
BRX1_HUMANBRIX1physical
28514442
RLA2_HUMANRPLP2physical
28514442
NOG2_HUMANGNL2physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
RPF1_HUMANRPF1physical
28514442
RL4_HUMANRPL4physical
28514442
RL10A_HUMANRPL10Aphysical
28514442
RL18A_HUMANRPL18Aphysical
28514442
PUM3_HUMANKIAA0020physical
28514442
ZN689_HUMANZNF689physical
28514442
STAU1_HUMANSTAU1physical
28514442
RL32_HUMANRPL32physical
28514442
RS8_HUMANRPS8physical
28514442
CENPN_HUMANCENPNphysical
28514442
RL37A_HUMANRPL37Aphysical
28514442
PK1IP_HUMANPAK1IP1physical
28514442
RL13_HUMANRPL13physical
28514442
RL14_HUMANRPL14physical
28514442
RRS1_HUMANRRS1physical
28514442
RL15_HUMANRPL15physical
28514442
CENPU_HUMANCENPUphysical
28514442
ZN184_HUMANZNF184physical
28514442
NSD2_HUMANWHSC1physical
28514442
ZN800_HUMANZNF800physical
28514442
RL12_HUMANRPL12physical
28514442
GLYR1_HUMANGLYR1physical
28514442
RS6_HUMANRPS6physical
28514442
RLP24_HUMANRSL24D1physical
28514442
RRP8_HUMANRRP8physical
28514442
RL6_HUMANRPL6physical
28514442
TTF1_HUMANTTF1physical
28514442
ZFP62_HUMANZFP62physical
28514442
ZN512_HUMANZNF512physical
28514442
DDX27_HUMANDDX27physical
28514442
REPI1_HUMANREPIN1physical
28514442
RLA1_HUMANRPLP1physical
28514442
ZNF48_HUMANZNF48physical
28514442
RL30_HUMANRPL30physical
28514442
RL7_HUMANRPL7physical
28514442
RS13_HUMANRPS13physical
28514442
RL8_HUMANRPL8physical
28514442
CH033_HUMANC8orf33physical
28514442
NSA2_HUMANNSA2physical
28514442
RBM34_HUMANRBM34physical
28514442
ZSC25_HUMANZSCAN25physical
28514442
DDX24_HUMANDDX24physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
EBP2_HUMANEBNA1BP2physical
28514442
SURF6_HUMANSURF6physical
28514442
SPB1_HUMANFTSJ3physical
28514442
NIP7_HUMANNIP7physical
28514442
RL11_HUMANRPL11physical
28514442
DKC1_HUMANDKC1physical
28514442
RL5_HUMANRPL5physical
28514442
RL3_HUMANRPL3physical
28514442
NOL12_HUMANNOL12physical
28514442
NOP56_HUMANNOP56physical
28514442
RL35A_HUMANRPL35Aphysical
28514442
POP1_HUMANPOP1physical
28514442
NOP2_HUMANNOP2physical
28514442
DHX30_HUMANDHX30physical
28514442
DDX21_HUMANDDX21physical
28514442
FCF1_HUMANFCF1physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
MAK16_HUMANMAK16physical
28514442
RL13A_HUMANRPL13Aphysical
28514442
RBM28_HUMANRBM28physical
28514442
RL7L_HUMANRPL7L1physical
28514442
LLPH_HUMANLLPHphysical
28514442
PAPD5_HUMANPAPD5physical
28514442
ABT1_HUMANABT1physical
28514442
ZN771_HUMANZNF771physical
28514442
NOP53_HUMANGLTSCR2physical
28514442
CC137_HUMANCCDC137physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602668Dystrophia myotonica 2 (DM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNBP_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASS SPECTROMETRY.

TOP