RFOX2_HUMAN - dbPTM
RFOX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFOX2_HUMAN
UniProt AC O43251
Protein Name RNA binding protein fox-1 homolog 2
Gene Name RBFOX2
Organism Homo sapiens (Human).
Sequence Length 390
Subcellular Localization Nucleus. Cytoplasm.
Protein Description RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seems to act as a coregulatory factor of ER-alpha..
Protein Sequence MQNEPLTPGYHGFPARDSQGNQEPTTTPDAMVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTGEHNLTLYGSTQAHGEQSSNSPSTQNGSLTTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKMVTPYANGWKLSPVVGAVYGPELYAASSFQADVSLGNDAAVPLSGRGGINTYIPLISLPLVPGFPYPTAATTAAAFRGAHLRGRGRTVYGAVRAVPPTAIPAYPGVVYQDGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPYHALAPAASYGVGAVASLYRGGYSRFAPY
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
7Phosphorylation-MQNEPLTPGYHGFP
-CCCCCCCCCCCCCC
25.9428985074
10PhosphorylationNEPLTPGYHGFPARD
CCCCCCCCCCCCCCC
10.4424275569
15 (in isoform 10)Phosphorylation-26.17-
15 (in isoform 2)Phosphorylation-26.17-
15 (in isoform 3)Phosphorylation-26.17-
15 (in isoform 4)Phosphorylation-26.17-
15 (in isoform 5)Phosphorylation-26.17-
15 (in isoform 9)Phosphorylation-26.17-
26 (in isoform 6)Phosphorylation-47.2326657352
26PhosphorylationQGNQEPTTTPDAMVQ
CCCCCCCCCCCCCCC
47.2327251275
26 (in isoform 8)Phosphorylation-47.2326657352
37PhosphorylationAMVQPFTTIPFPPPP
CCCCCCEECCCCCCC
27.34-
50 (in isoform 8)Phosphorylation-39.6621406692
50 (in isoform 6)Phosphorylation-39.6621406692
67 (in isoform 8)Phosphorylation-35.6230266825
67PhosphorylationYAGQTGEHNLTLYGS
CCCCCCCCEEEEEEC
35.6227251275
67 (in isoform 6)Phosphorylation-35.6230266825
70 (in isoform 6)Phosphorylation-24.2121955146
70 (in isoform 8)Phosphorylation-24.2121955146
106PhosphorylationAQTDGQQSQTQSSEN
CCCCCCCCCCCCCCC
27.57-
119PhosphorylationENSESKSTPKRLHVS
CCCCCCCCCCEEEEC
36.24-
130UbiquitinationLHVSNIPFRFRDPDL
EEECCCCCCCCCHHH
11.6121890473
138MethylationRFRDPDLRQMFGQFG
CCCCHHHHHHHHHHC
33.04-
138 (in isoform 3)Phosphorylation-33.0429083192
142 (in isoform 3)Phosphorylation-19.3029083192
147UbiquitinationMFGQFGKILDVEIIF
HHHHHCCEEEEEEEE
3.9821890473
150 (in isoform 10)Ubiquitination-5.2221890473
150 (in isoform 4)Ubiquitination-5.2221890473
150 (in isoform 5)Ubiquitination-5.2221890473
150UbiquitinationQFGKILDVEIIFNER
HHCCEEEEEEEEECC
5.2221890473
151 (in isoform 2)Ubiquitination-29.9921890473
151 (in isoform 9)Ubiquitination-29.9921890473
151UbiquitinationFGKILDVEIIFNERG
HCCEEEEEEEEECCC
29.9921890473
156UbiquitinationDVEIIFNERGSKGFG
EEEEEEECCCCCCEE
47.9021890473
157UbiquitinationVEIIFNERGSKGFGF
EEEEEECCCCCCEEE
56.6521890473
160UbiquitinationIFNERGSKGFGFVTF
EEECCCCCCEEEEEE
62.17-
160 (in isoform 7)Ubiquitination-62.1721890473
160 (in isoform 1)Ubiquitination-62.1721890473
163UbiquitinationERGSKGFGFVTFENS
CCCCCCEEEEEECCC
25.4521890473
169UbiquitinationFGFVTFENSADADRA
EEEEEECCCCCHHHH
38.0032142685
170UbiquitinationGFVTFENSADADRAR
EEEEECCCCCHHHHH
21.9632142685
172UbiquitinationVTFENSADADRAREK
EEECCCCCHHHHHHH
49.1521890473
173UbiquitinationTFENSADADRAREKL
EECCCCCHHHHHHHH
14.1221890473
179UbiquitinationDADRAREKLHGTVVE
CHHHHHHHHCCEEEE
39.9832142685
179AcetylationDADRAREKLHGTVVE
CHHHHHHHHCCEEEE
39.9819817231
180UbiquitinationADRAREKLHGTVVEG
HHHHHHHHCCEEEEC
3.7432142685
183PhosphorylationAREKLHGTVVEGRKI
HHHHHCCEEEECCEE
15.6123532336
194UbiquitinationGRKIEVNNATARVMT
CCEEEECCCEEEEEC
43.7932142685
195UbiquitinationRKIEVNNATARVMTN
CEEEECCCEEEEECC
9.4621890473
199MethylationVNNATARVMTNKKMV
ECCCEEEEECCCCCE
5.28-
207PhosphorylationMTNKKMVTPYANGWK
ECCCCCEECCCCCEE
13.6921815630
220UbiquitinationWKLSPVVGAVYGPEL
EECCCCCCEECCHHH
15.0121890473
220 (in isoform 6)Ubiquitination-15.0121890473
221UbiquitinationKLSPVVGAVYGPELY
ECCCCCCEECCHHHH
4.6321890473
221 (in isoform 8)Ubiquitination-4.6321890473
239UbiquitinationSFQADVSLGNDAAVP
CEECCCCCCCCCCEE
8.1532142685
240UbiquitinationFQADVSLGNDAAVPL
EECCCCCCCCCCEEC
23.5932142685
249 (in isoform 3)Methylation-39.6824129315
249UbiquitinationDAAVPLSGRGGINTY
CCCEECCCCCCCCCC
39.6832142685
250UbiquitinationAAVPLSGRGGINTYI
CCEECCCCCCCCCCE
36.4732142685
264UbiquitinationIPLISLPLVPGFPYP
EECEECCCCCCCCCC
9.8432142685
265UbiquitinationPLISLPLVPGFPYPT
ECEECCCCCCCCCCC
4.0432142685
267 (in isoform 5)Methylation-28.7824129315
268 (in isoform 9)Methylation-4.2524129315
275SumoylationFPYPTAATTAAAFRG
CCCCCHHHHHHHHCC
17.95-
277 (in isoform 7)Methylation-7.7624129315
281MethylationATTAAAFRGAHLRGR
HHHHHHHCCHHHCCC
36.3454558687
286MethylationAFRGAHLRGRGRTVY
HHCCHHHCCCCCEEE
23.9354558693
293PhosphorylationRGRGRTVYGAVRAVP
CCCCCEEEEEEECCC
9.9628152594
297Asymmetric dimethylarginineRTVYGAVRAVPPTAI
CEEEEEEECCCCCCC
29.36-
297MethylationRTVYGAVRAVPPTAI
CEEEEEEECCCCCCC
29.36-
329MethylationYGGYAAYRYAQPATA
CCCEEEEECCCCHHH
18.6524129315
329Asymmetric dimethylarginineYGGYAAYRYAQPATA
CCCEEEEECCCCHHH
18.65-
342MethylationTATAATAAAAAAAAY
HHHHHHHHHHHHHHH
8.02-
347MethylationTAAAAAAAAYSDGYG
HHHHHHHHHHHCCCC
11.38-
380PhosphorylationVGAVASLYRGGYSRF
HHHHHHHHCCCCCCC
12.52-
381Asymmetric dimethylarginineGAVASLYRGGYSRFA
HHHHHHHCCCCCCCC
37.04-
381MethylationGAVASLYRGGYSRFA
HHHHHHHCCCCCCCC
37.0412018239
386Asymmetric dimethylarginineLYRGGYSRFAPY---
HHCCCCCCCCCC---
24.22-
386MethylationLYRGGYSRFAPY---
HHCCCCCCCCCC---
24.2216188267
390MethylationGYSRFAPY-------
CCCCCCCC-------
27.97-
442Methylation-----------------------------------------------------------
-----------------------------------------------------------
-
447Methylation----------------------------------------------------------------
----------------------------------------------------------------
-

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 RFOX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFOX2_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 RFOX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHXF2_HUMANRHOXF2physical
16189514
DMRTB_HUMANDMRTB1physical
16189514
ESR1_HUMANESR1physical
11875103
ESR2_HUMANESR2physical
11875103
RFOX2_HUMANRBFOX2physical
20211142
BRD7_HUMANBRD7physical
20211142
DEDD2_HUMANDEDD2physical
20211142
RU1C_HUMANSNRPCphysical
22365833
SF3A1_HUMANSF3A1physical
22365833
U2AF2_HUMANU2AF2physical
22365833
RBM23_HUMANRBM23physical
22365833
ELAV1_HUMANELAVL1physical
22365833
RBM22_HUMANRBM22physical
22365833
DDX5_HUMANDDX5physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
SMN_HUMANSMN1physical
22365833
HNRPF_HUMANHNRNPFphysical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
RBM42_HUMANRBM42physical
22365833
PTBP1_HUMANPTBP1physical
22365833
QKI_HUMANQKIphysical
22365833
KHDR1_HUMANKHDRBS1physical
22365833
RFOX2_HUMANRBFOX2physical
22365833
VAC14_HUMANVAC14physical
25416956
BOLL_HUMANBOLLphysical
25416956
CA094_HUMANC1orf94physical
25416956
NAF1_HUMANNAF1physical
25416956
MISSL_HUMANMAPK1IP1Lphysical
25416956
ANM5_HUMANPRMT5physical
26186194
IF4G3_HUMANEIF4G3physical
26186194
MBNL1_HUMANMBNL1physical
26186194
RBPMS_HUMANRBPMSphysical
26186194
RBPS2_HUMANRBPMS2physical
26186194
LAR4B_HUMANLARP4Bphysical
26186194
PUM1_HUMANPUM1physical
26186194
PUM2_HUMANPUM2physical
26186194
RBM38_HUMANRBM38physical
26186194
DPH2_HUMANDPH2physical
26186194
GPTC8_HUMANGPATCH8physical
26186194
FND3B_HUMANFNDC3Bphysical
26186194
QKI_HUMANQKIphysical
26186194
F136A_HUMANFAM136Aphysical
26186194
PRC2A_HUMANPRRC2Aphysical
26186194
ATX2_HUMANATXN2physical
26186194
COPRS_HUMANCOPRSphysical
26186194
JMJD4_HUMANJMJD4physical
26186194
ICLN_HUMANCLNS1Aphysical
26186194
ANR40_HUMANANKRD40physical
26186194
DAZP2_HUMANDAZAP2physical
26186194
RBMS1_HUMANRBMS1physical
26186194
RIOK1_HUMANRIOK1physical
26186194
MSI2H_HUMANMSI2physical
26186194
OTUD4_HUMANOTUD4physical
26186194
HXA5_HUMANHOXA5physical
26186194
UBAP2_HUMANUBAP2physical
26186194
PKHB1_HUMANPLEKHB1physical
26186194
TIM29_HUMANC19orf52physical
26186194
PJA1_HUMANPJA1physical
26186194
FBX7_HUMANFBXO7physical
26186194
BCS1_HUMANBCS1Lphysical
26186194
PARL_HUMANPARLphysical
26186194
RBPMS_HUMANRBPMSphysical
28514442
FND3B_HUMANFNDC3Bphysical
28514442
RBM38_HUMANRBM38physical
28514442
PUM2_HUMANPUM2physical
28514442
COPRS_HUMANCOPRSphysical
28514442
PUM1_HUMANPUM1physical
28514442
DPH2_HUMANDPH2physical
28514442
JMJD4_HUMANJMJD4physical
28514442
ATX2_HUMANATXN2physical
28514442
RBPS2_HUMANRBPMS2physical
28514442
DAZP2_HUMANDAZAP2physical
28514442
PKHB1_HUMANPLEKHB1physical
28514442
ANM5_HUMANPRMT5physical
28514442
RIOK1_HUMANRIOK1physical
28514442
ANR40_HUMANANKRD40physical
28514442
ICLN_HUMANCLNS1Aphysical
28514442
GPTC8_HUMANGPATCH8physical
28514442
TIM29_HUMANC19orf52physical
28514442
MBNL1_HUMANMBNL1physical
28514442
RBMS1_HUMANRBMS1physical
28514442
BCS1_HUMANBCS1Lphysical
28514442
RBMS2_HUMANRBMS2physical
28514442
FBX7_HUMANFBXO7physical
28514442
PARL_HUMANPARLphysical
28514442
IF4G3_HUMANEIF4G3physical
28514442
MSI2H_HUMANMSI2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RFOX2_HUMAN

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Related Literatures of Post-Translational Modification

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