IKZF2_HUMAN - dbPTM
IKZF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IKZF2_HUMAN
UniProt AC Q9UKS7
Protein Name Zinc finger protein Helios
Gene Name IKZF2
Organism Homo sapiens (Human).
Sequence Length 526
Subcellular Localization Nucleus.
Protein Description Associates with Ikaros at centromeric heterochromatin..
Protein Sequence METEAIDGYITCDNELSPEREHSNMAIDLTSSTPNGQHASPSHMTSTNSVKLEMQSDEECDRKPLSREDEIRGHDEGSSLEEPLIESSEVADNRKVQELQGEGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCSYACRRRDALTGHLRTHSVGKPHKCNYCGRSYKQRSSLEEHKERCHNYLQNVSMEAAGQVMSHHVPPMEDCKEQEPIMDNNISLVPFERPAVIEKLTGNMGKRKSSTPQKFVGEKLMRFSYPDIHFDMNLTYEKEAELMQSHMMDQAINNAITYLGAEALHPLMQHPPSTIAEVAPVISSAYSQVYHPNRIERPISRETADSHENNMDGPISLIRPKSRPQEREASPSNSCLDSTDSESSHDDHQSYQGHPALNPKRKQSPAYMKEDVKALDTTKAPKGSLKDIYKVFNGEGEQIRAFKCEHCRVLFLDHVMYTIHMGCHGYRDPLECNICGYRSQDRYEFSSHIVRGEHTFH
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
3Phosphorylation-----METEAIDGYI
-----CCCCEECEEE		29.4426074081
9PhosphorylationETEAIDGYITCDNEL
CCCEECEEEECCCCC		6.8426074081
11PhosphorylationEAIDGYITCDNELSP
CEECEEEECCCCCCC		12.8126074081
17PhosphorylationITCDNELSPEREHSN
EECCCCCCCCCCCCC		20.6630108239
23PhosphorylationLSPEREHSNMAIDLT
CCCCCCCCCCEEECC		24.4526074081
30PhosphorylationSNMAIDLTSSTPNGQ
CCCEEECCCCCCCCC		19.5126074081
31PhosphorylationNMAIDLTSSTPNGQH
CCEEECCCCCCCCCC		39.2426074081
32PhosphorylationMAIDLTSSTPNGQHA
CEEECCCCCCCCCCC		42.5226074081
33PhosphorylationAIDLTSSTPNGQHAS
EEECCCCCCCCCCCC		22.1230108239
40PhosphorylationTPNGQHASPSHMTST
CCCCCCCCCCCCCCC		25.4730108239
42PhosphorylationNGQHASPSHMTSTNS
CCCCCCCCCCCCCCC		24.3230108239
45PhosphorylationHASPSHMTSTNSVKL
CCCCCCCCCCCCCEE		27.2926074081
46PhosphorylationASPSHMTSTNSVKLE
CCCCCCCCCCCCEEE		20.3026074081
47PhosphorylationSPSHMTSTNSVKLEM
CCCCCCCCCCCEEEE		23.5026074081
49PhosphorylationSHMTSTNSVKLEMQS
CCCCCCCCCEEEECC		22.2526074081
56PhosphorylationSVKLEMQSDEECDRK
CCEEEECCCCCCCCC		45.7523401153
63AcetylationSDEECDRKPLSREDE
CCCCCCCCCCCHHHH		36.7425953088
63UbiquitinationSDEECDRKPLSREDE
CCCCCCCCCCCHHHH		36.74-
66PhosphorylationECDRKPLSREDEIRG
CCCCCCCCHHHHHCC		42.0026657352
78PhosphorylationIRGHDEGSSLEEPLI
HCCCCCCCCCCCCCC		29.6923401153
79PhosphorylationRGHDEGSSLEEPLIE
CCCCCCCCCCCCCCC		51.1330266825
87PhosphorylationLEEPLIESSEVADNR
CCCCCCCCCHHHCCH		25.4627251275
88PhosphorylationEEPLIESSEVADNRK
CCCCCCCCHHHCCHH		24.2530576142
95UbiquitinationSEVADNRKVQELQGE
CHHHCCHHHHHHCCC		55.30-
95SumoylationSEVADNRKVQELQGE
CHHHCCHHHHHHCCC		55.3028112733
111AcetylationGIRLPNGKLKCDVCG
CEECCCCCEEECCCE		51.9525953088
135PhosphorylationMVHKRSHTGERPFHC
EEECCCCCCCCCCCC		41.82-
148PhosphorylationHCNQCGASFTQKGNL
CCCCCCCCEECCCCC		17.7017924679
160UbiquitinationGNLLRHIKLHSGEKP
CCCCEEEEECCCCCC		33.74-
163PhosphorylationLRHIKLHSGEKPFKC
CEEEEECCCCCCCCC		60.1123401153
166SumoylationIKLHSGEKPFKCPFC
EEECCCCCCCCCCCC		60.32-
166UbiquitinationIKLHSGEKPFKCPFC
EEECCCCCCCCCCCC		60.32-
166AcetylationIKLHSGEKPFKCPFC
EEECCCCCCCCCCCC		60.3272618283
166SumoylationIKLHSGEKPFKCPFC
EEECCCCCCCCCCCC		60.32-
174PhosphorylationPFKCPFCSYACRRRD
CCCCCCCHHHHHCHH		19.0217924679
175PhosphorylationFKCPFCSYACRRRDA
CCCCCCHHHHHCHHH		15.7617924679
200PhosphorylationGKPHKCNYCGRSYKQ
CCCCCCCCCCCCHHH		13.02-
200 (in isoform 4)Phosphorylation-13.02-
209PhosphorylationGRSYKQRSSLEEHKE
CCCHHHCCCHHHHHH		36.46-
210PhosphorylationRSYKQRSSLEEHKER
CCHHHCCCHHHHHHH		41.82-
215UbiquitinationRSSLEEHKERCHNYL
CCCHHHHHHHHHHHH		50.57-
226PhosphorylationHNYLQNVSMEAAGQV
HHHHHHCCHHHHHHH		20.6026074081
235PhosphorylationEAAGQVMSHHVPPME
HHHHHHHHCCCCCHH		16.1630576142
256PhosphorylationPIMDNNISLVPFERP
CCCCCCEEEEECCCH		25.9930576142
262UbiquitinationISLVPFERPAVIEKL
EEEEECCCHHHHHHH		25.5119608861
262AcetylationISLVPFERPAVIEKL
EEEEECCCHHHHHHH		25.5119608861
268UbiquitinationERPAVIEKLTGNMGK
CCHHHHHHHHCCCCC		39.98-
270PhosphorylationPAVIEKLTGNMGKRK
HHHHHHHHCCCCCCC		37.2626074081
275UbiquitinationKLTGNMGKRKSSTPQ
HHHCCCCCCCCCCCC		45.98-
275AcetylationKLTGNMGKRKSSTPQ
HHHCCCCCCCCCCCC		45.9825953088
278PhosphorylationGNMGKRKSSTPQKFV
CCCCCCCCCCCCHHH		43.4026074081
279PhosphorylationNMGKRKSSTPQKFVG
CCCCCCCCCCCHHHH		47.3326074081
280PhosphorylationMGKRKSSTPQKFVGE
CCCCCCCCCCHHHHH		36.5126074081
283UbiquitinationRKSSTPQKFVGEKLM
CCCCCCCHHHHHHHH		43.13-
283AcetylationRKSSTPQKFVGEKLM
CCCCCCCHHHHHHHH		43.1325953088
288UbiquitinationPQKFVGEKLMRFSYP
CCHHHHHHHHHCCCC		41.4719608861
288AcetylationPQKFVGEKLMRFSYP
CCHHHHHHHHHCCCC		41.4719608861
293PhosphorylationGEKLMRFSYPDIHFD
HHHHHHCCCCCEEEE		25.95-
342O-linked_GlycosylationPLMQHPPSTIAEVAP
HHHHCCCCHHHHHHH		36.5829351928
352PhosphorylationAEVAPVISSAYSQVY
HHHHHHHHHHHHHCC		14.7826074081
353PhosphorylationEVAPVISSAYSQVYH
HHHHHHHHHHHHCCC		21.8026074081
355PhosphorylationAPVISSAYSQVYHPN
HHHHHHHHHHCCCCC		11.1126074081
356PhosphorylationPVISSAYSQVYHPNR
HHHHHHHHHCCCCCC		16.9426074081
359PhosphorylationSSAYSQVYHPNRIER
HHHHHHCCCCCCCCC		12.1526074081
369PhosphorylationNRIERPISRETADSH
CCCCCCCCHHHCCCC		27.0930266825
372PhosphorylationERPISRETADSHENN
CCCCCHHHCCCCCCC		34.3523401153
375PhosphorylationISRETADSHENNMDG
CCHHHCCCCCCCCCC		30.1822115753
385PhosphorylationNNMDGPISLIRPKSR
CCCCCCCEEECCCCC		22.3726074081
390UbiquitinationPISLIRPKSRPQERE
CCEEECCCCCCCCCC		49.61-
391PhosphorylationISLIRPKSRPQEREA
CEEECCCCCCCCCCC		52.4526074081
399PhosphorylationRPQEREASPSNSCLD
CCCCCCCCCCCCCCC		24.9026074081
401PhosphorylationQEREASPSNSCLDST
CCCCCCCCCCCCCCC		38.5926074081
403PhosphorylationREASPSNSCLDSTDS
CCCCCCCCCCCCCCC		22.0126074081
408PhosphorylationSNSCLDSTDSESSHD
CCCCCCCCCCCCCCC		43.1230576142
419PhosphorylationSSHDDHQSYQGHPAL
CCCCCHHHHCCCCCC		18.9226074081
420PhosphorylationSHDDHQSYQGHPALN
CCCCHHHHCCCCCCC		16.3726074081
433PhosphorylationLNPKRKQSPAYMKED
CCCCCCCCCCHHHHH		17.9623401153
436PhosphorylationKRKQSPAYMKEDVKA
CCCCCCCHHHHHHHH		16.4729978859
438UbiquitinationKQSPAYMKEDVKALD
CCCCCHHHHHHHHHC		37.78-
442SumoylationAYMKEDVKALDTTKA
CHHHHHHHHHCCCCC		56.40-
442UbiquitinationAYMKEDVKALDTTKA
CHHHHHHHHHCCCCC		56.40-
442SumoylationAYMKEDVKALDTTKA
CHHHHHHHHHCCCCC		56.4028112733
446PhosphorylationEDVKALDTTKAPKGS
HHHHHHCCCCCCCCC		30.9228122231
447PhosphorylationDVKALDTTKAPKGSL
HHHHHCCCCCCCCCH		25.5217081983
448UbiquitinationVKALDTTKAPKGSLK
HHHHCCCCCCCCCHH		65.86-
448SumoylationVKALDTTKAPKGSLK
HHHHCCCCCCCCCHH		65.8628112733
451UbiquitinationLDTTKAPKGSLKDIY
HCCCCCCCCCHHHHH		67.02-
453PhosphorylationTTKAPKGSLKDIYKV
CCCCCCCCHHHHHHH		38.0730108239
455UbiquitinationKAPKGSLKDIYKVFN
CCCCCCHHHHHHHHC		43.72-
459UbiquitinationGSLKDIYKVFNGEGE
CCHHHHHHHHCCCCC		40.46-
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 IKZF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IKZF2_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 IKZF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC4_HUMANHDAC4physical
12943985
SIN3A_HUMANSIN3Aphysical
12015313
SIN3B_HUMANSIN3Bphysical
12015313
CHD4_HUMANCHD4physical
12015313
HDAC2_HUMANHDAC2physical
12015313
HDAC5_HUMANHDAC5physical
12015313
IKZF1_HUMANIKZF1physical
9560339
IKZF3_HUMANIKZF3physical
9560339
IKZF2_HUMANIKZF2physical
9560339
LONF1_HUMANLONRF1physical
25416956
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 IKZF2_HUMAN

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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-288, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-56; SER-78 AND SER-79,AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND TYR-175, ANDMASS SPECTROMETRY.

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