IKZF3_HUMAN - dbPTM
IKZF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IKZF3_HUMAN
UniProt AC Q9UKT9
Protein Name Zinc finger protein Aiolos
Gene Name IKZF3
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner..
Protein Sequence MEDIQTNAELKSTQEQSVPAESAAVLNDYSLTKSHEMENVDSGEGPANEDEDIGDDSMKVKDEYSERDENVLKSEPMGNAEEPEIPYSYSREYNEYENIKLERHVVSFDSSRPTSGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRTFLQSTDPGDTASAEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDVNYNSSYMYEKESELIQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSMYPIALTRAEMSNGAPQELEKKSIHLPEKSVPSERGLSPNNSGHDSTDTDSNHEERQNHIYQQNHMVLSRARNGMPLLKEVPRSYELLKPPPICPRDSVKVINKEGEVMDVYRCDHCRVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRALLK
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
6 (in isoform 7)Phosphorylation-36.4124043423
6 (in isoform 8)Phosphorylation-36.4124043423
12PhosphorylationQTNAELKSTQEQSVP
HHHHHHHCCCCCCCC
48.2027282143
12 (in isoform 7)Phosphorylation-48.2024043423
12 (in isoform 8)Phosphorylation-48.2024043423
13PhosphorylationTNAELKSTQEQSVPA
HHHHHHCCCCCCCCH
34.2427282143
13 (in isoform 7)Phosphorylation-34.2424043423
13 (in isoform 8)Phosphorylation-34.2424043423
17PhosphorylationLKSTQEQSVPAESAA
HHCCCCCCCCHHHHH
29.3427282143
17 (in isoform 7)Phosphorylation-29.3424043423
17 (in isoform 8)Phosphorylation-29.3424043423
18UbiquitinationKSTQEQSVPAESAAV
HCCCCCCCCHHHHHH
5.3524816145
22PhosphorylationEQSVPAESAAVLNDY
CCCCCHHHHHHHHCC
24.5130108239
23 (in isoform 7)Phosphorylation-7.9724043423
23 (in isoform 8)Phosphorylation-7.9724043423
26UbiquitinationPAESAAVLNDYSLTK
CHHHHHHHHCCCCCC
3.28-
26UbiquitinationPAESAAVLNDYSLTK
CHHHHHHHHCCCCCC
3.2829967540
42PhosphorylationHEMENVDSGEGPANE
EECCCCCCCCCCCCC
34.1723401153
57PhosphorylationDEDIGDDSMKVKDEY
CCCCCCCCCCCCHHH
25.8330108239
61SumoylationGDDSMKVKDEYSERD
CCCCCCCCHHHHHHH
39.0528112733
63UbiquitinationDSMKVKDEYSERDEN
CCCCCCHHHHHHHHC
45.2822817900
64PhosphorylationSMKVKDEYSERDENV
CCCCCHHHHHHHHCC
26.4327251275
65PhosphorylationMKVKDEYSERDENVL
CCCCHHHHHHHHCCC
24.9030108239
66UbiquitinationKVKDEYSERDENVLK
CCCHHHHHHHHCCCC
64.3529967540
73SumoylationERDENVLKSEPMGNA
HHHHCCCCCCCCCCC
48.7928112733
73UbiquitinationERDENVLKSEPMGNA
HHHHCCCCCCCCCCC
48.79-
74PhosphorylationRDENVLKSEPMGNAE
HHHCCCCCCCCCCCC
42.6550564293
83UbiquitinationPMGNAEEPEIPYSYS
CCCCCCCCCCCCCCC
36.0024816145
88PhosphorylationEEPEIPYSYSREYNE
CCCCCCCCCCCCCCC
15.9830108239
90PhosphorylationPEIPYSYSREYNEYE
CCCCCCCCCCCCCCC
16.8250564299
91UbiquitinationEIPYSYSREYNEYEN
CCCCCCCCCCCCCCC
42.0329967540
93PhosphorylationPYSYSREYNEYENIK
CCCCCCCCCCCCCEE
16.5123025827
96PhosphorylationYSREYNEYENIKLER
CCCCCCCCCCEEEEE
15.6123025827
100SumoylationYNEYENIKLERHVVS
CCCCCCEEEEEEEEE
56.74-
100SumoylationYNEYENIKLERHVVS
CCCCCCEEEEEEEEE
56.7428112733
100UbiquitinationYNEYENIKLERHVVS
CCCCCCEEEEEEEEE
56.7429967540
102UbiquitinationEYENIKLERHVVSFD
CCCCEEEEEEEEEEC
35.4222817900
107PhosphorylationKLERHVVSFDSSRPT
EEEEEEEEECCCCCC
23.4223401153
114UbiquitinationSFDSSRPTSGKMNCD
EECCCCCCCCCCCCC
49.34-
115UbiquitinationFDSSRPTSGKMNCDV
ECCCCCCCCCCCCCC
38.81-
115PhosphorylationFDSSRPTSGKMNCDV
ECCCCCCCCCCCCCC
38.8146161063
122UbiquitinationSGKMNCDVCGLSCIS
CCCCCCCCCCCEEEE
2.80-
122UbiquitinationSGKMNCDVCGLSCIS
CCCCCCCCCCCEEEE
2.8024816145
130UbiquitinationCGLSCISFNVLMVHK
CCCEEEEEEEEEEEC
3.5729967540
139PhosphorylationVLMVHKRSHTGERPF
EEEEECCCCCCCCCC
30.1528450419
139 (in isoform 15)Phosphorylation-30.15-
139 (in isoform 2)Phosphorylation-30.15-
141PhosphorylationMVHKRSHTGERPFQC
EEECCCCCCCCCCCC
41.8228450419
141 (in isoform 15)Phosphorylation-41.82-
141 (in isoform 2)Phosphorylation-41.82-
141 (in isoform 5)Phosphorylation-41.82-
146 (in isoform 15)Phosphorylation-18.95-
146 (in isoform 2)Phosphorylation-18.95-
150UbiquitinationERPFQCNQCGASFTQ
CCCCCCCCCCCCEEC
34.3522817900
150 (in isoform 5)Ubiquitination-34.3521906983
154PhosphorylationQCNQCGASFTQKGNL
CCCCCCCCEECCCCC
17.7027080861
156PhosphorylationNQCGASFTQKGNLLR
CCCCCCEECCCCCEE
27.2027080861
158UbiquitinationCGASFTQKGNLLRHI
CCCCEECCCCCEEEE
46.8622817900
169PhosphorylationLRHIKLHTGEKPFKC
EEEEEEECCCCCEEE
58.4318669648
170UbiquitinationRHIKLHTGEKPFKCH
EEEEEECCCCCEEEE
30.1324816145
172UbiquitinationIKLHTGEKPFKCHLC
EEEECCCCCEEEEEC
58.04-
172SumoylationIKLHTGEKPFKCHLC
EEEECCCCCEEEEEC
58.04-
172SumoylationIKLHTGEKPFKCHLC
EEEECCCCCEEEEEC
58.04-
172UbiquitinationIKLHTGEKPFKCHLC
EEEECCCCCEEEEEC
58.0422817900
178UbiquitinationEKPFKCHLCNYACQR
CCCEEEEECCHHHHC
2.5824816145
182UbiquitinationKCHLCNYACQRRDAL
EEEECCHHHHCCHHH
2.96-
182UbiquitinationKCHLCNYACQRRDAL
EEEECCHHHHCCHHH
2.9622817900
186UbiquitinationCNYACQRRDALTGHL
CCHHHHCCHHHCCCC
14.0029967540
189UbiquitinationACQRRDALTGHLRTH
HHHCCHHHCCCCCCC
7.4522817900
189 (in isoform 2)Ubiquitination-7.4521906983
190PhosphorylationCQRRDALTGHLRTHS
HHCCHHHCCCCCCCC
25.0329083192
192UbiquitinationRRDALTGHLRTHSVE
CCHHHCCCCCCCCCC
13.6024816145
195PhosphorylationALTGHLRTHSVEKPY
HHCCCCCCCCCCCCC
25.5129083192
197UbiquitinationTGHLRTHSVEKPYKC
CCCCCCCCCCCCCCC
31.21-
197PhosphorylationTGHLRTHSVEKPYKC
CCCCCCCCCCCCCCC
31.2129083192
200UbiquitinationLRTHSVEKPYKCEFC
CCCCCCCCCCCCCCC
52.0329967540
202PhosphorylationTHSVEKPYKCEFCGR
CCCCCCCCCCCCCCC
39.0629083192
203UbiquitinationHSVEKPYKCEFCGRS
CCCCCCCCCCCCCCC
35.50-
206UbiquitinationEKPYKCEFCGRSYKQ
CCCCCCCCCCCCHHC
8.2022817900
206 (in isoform 3)Ubiquitination-8.2021906983
208UbiquitinationPYKCEFCGRSYKQRS
CCCCCCCCCCHHCCC
27.2222817900
209UbiquitinationYKCEFCGRSYKQRSS
CCCCCCCCCHHCCCC
37.6824816145
211UbiquitinationCEFCGRSYKQRSSLE
CCCCCCCHHCCCCHH
15.1322817900
215PhosphorylationGRSYKQRSSLEEHKE
CCCHHCCCCHHHHHH
36.46-
216PhosphorylationRSYKQRSSLEEHKER
CCHHCCCCHHHHHHH
41.82-
217UbiquitinationSYKQRSSLEEHKERC
CHHCCCCHHHHHHHH
10.6429967540
221UbiquitinationRSSLEEHKERCRTFL
CCCHHHHHHHHHHHH
50.57-
226UbiquitinationEHKERCRTFLQSTDP
HHHHHHHHHHHCCCC
32.1224816145
230PhosphorylationRCRTFLQSTDPGDTA
HHHHHHHCCCCCCCC
36.6030108239
231PhosphorylationCRTFLQSTDPGDTAS
HHHHHHCCCCCCCCH
33.0030108239
231UbiquitinationCRTFLQSTDPGDTAS
HHHHHHCCCCCCCCH
33.0024816145
234UbiquitinationFLQSTDPGDTASAEA
HHHCCCCCCCCHHHH
47.9529967540
236PhosphorylationQSTDPGDTASAEARH
HCCCCCCCCHHHHHH
28.5530108239
238PhosphorylationTDPGDTASAEARHIK
CCCCCCCHHHHHHHH
28.8330108239
239UbiquitinationDPGDTASAEARHIKA
CCCCCCHHHHHHHHH
16.4129967540
245SumoylationSAEARHIKAEMGSER
HHHHHHHHHHHCCHH
31.97-
245AcetylationSAEARHIKAEMGSER
HHHHHHHHHHHCCHH
31.9730586829
245SumoylationSAEARHIKAEMGSER
HHHHHHHHHHHCCHH
31.9728112733
245UbiquitinationSAEARHIKAEMGSER
HHHHHHHHHHHCCHH
31.9721906983
245 (in isoform 1)Ubiquitination-31.9721906983
247UbiquitinationEARHIKAEMGSERAL
HHHHHHHHHCCHHHH
38.7922817900
250PhosphorylationHIKAEMGSERALVLD
HHHHHHCCHHHHHHH
23.6926714015
261PhosphorylationLVLDRLASNVAKRKS
HHHHHHHHHHHHHHC
36.1125003641
265UbiquitinationRLASNVAKRKSSMPQ
HHHHHHHHHHCCCCH
56.9524816145
268PhosphorylationSNVAKRKSSMPQKFI
HHHHHHHCCCCHHHC
35.5824719451
269PhosphorylationNVAKRKSSMPQKFIG
HHHHHHCCCCHHHCC
37.2024719451
273AcetylationRKSSMPQKFIGEKRH
HHCCCCHHHCCCCCE
32.8325953088
273UbiquitinationRKSSMPQKFIGEKRH
HHCCCCHHHCCCCCE
32.8329967540
286PhosphorylationRHCFDVNYNSSYMYE
CEEEECCCCCHHHHH
19.1017053785
286UbiquitinationRHCFDVNYNSSYMYE
CEEEECCCCCHHHHH
19.1022817900
290PhosphorylationDVNYNSSYMYEKESE
ECCCCCHHHHHHHHH
11.97171903
295UbiquitinationSSYMYEKESELIQTR
CHHHHHHHHHHHHHH
37.1922817900
326PhosphorylationALRPLVQTPPAPTSE
HHHHHHCCCCCCCHH
24.6226074081
334UbiquitinationPPAPTSEMVPVISSM
CCCCCHHCCCCHHHH
4.0722817900
334 (in isoform 5)Ubiquitination-4.0721906983
342UbiquitinationVPVISSMYPIALTRA
CCCHHHHHHHEEHHH
8.0722817900
351UbiquitinationIALTRAEMSNGAPQE
HEEHHHHHCCCCCHH
3.5322817900
351 (in isoform 6)Ubiquitination-3.5321906983
352PhosphorylationALTRAEMSNGAPQEL
EEHHHHHCCCCCHHH
24.5030108239
356UbiquitinationAEMSNGAPQELEKKS
HHHCCCCCHHHHHHC
29.5822817900
361UbiquitinationGAPQELEKKSIHLPE
CCCHHHHHHCCCCCC
65.53-
362UbiquitinationAPQELEKKSIHLPEK
CCHHHHHHCCCCCCC
45.31-
363PhosphorylationPQELEKKSIHLPEKS
CHHHHHHCCCCCCCC
26.7226714015
369AcetylationKSIHLPEKSVPSERG
HCCCCCCCCCCCCCC
55.6125953088
369UbiquitinationKSIHLPEKSVPSERG
HCCCCCCCCCCCCCC
55.61-
370PhosphorylationSIHLPEKSVPSERGL
CCCCCCCCCCCCCCC
37.2830108239
373PhosphorylationLPEKSVPSERGLSPN
CCCCCCCCCCCCCCC
37.4626714015
373UbiquitinationLPEKSVPSERGLSPN
CCCCCCCCCCCCCCC
37.4622817900
373 (in isoform 2)Ubiquitination-37.4621906983
378PhosphorylationVPSERGLSPNNSGHD
CCCCCCCCCCCCCCC
28.5323401153
382PhosphorylationRGLSPNNSGHDSTDT
CCCCCCCCCCCCCCC
44.1130108239
386PhosphorylationPNNSGHDSTDTDSNH
CCCCCCCCCCCCCCH
23.6230108239
387PhosphorylationNNSGHDSTDTDSNHE
CCCCCCCCCCCCCHH
49.3130108239
389PhosphorylationSGHDSTDTDSNHEER
CCCCCCCCCCCHHHH
41.2230108239
390UbiquitinationGHDSTDTDSNHEERQ
CCCCCCCCCCHHHHH
50.6922817900
390 (in isoform 3)Ubiquitination-50.6921906983
390 (in isoform 4)Ubiquitination-50.6921906983
391PhosphorylationHDSTDTDSNHEERQN
CCCCCCCCCHHHHHH
42.0230108239
395UbiquitinationDTDSNHEERQNHIYQ
CCCCCHHHHHHHHHH
52.6022817900
401PhosphorylationEERQNHIYQQNHMVL
HHHHHHHHHHHHHHH
9.1128674151
409PhosphorylationQQNHMVLSRARNGMP
HHHHHHHHHHHCCCH
16.6924043423
419UbiquitinationRNGMPLLKEVPRSYE
HCCCHHHCCCCCCHH
65.43-
425PhosphorylationLKEVPRSYELLKPPP
HCCCCCCHHHCCCCC
16.3327642862
429UbiquitinationPRSYELLKPPPICPR
CCCHHHCCCCCCCCC
69.0122817900
429 (in isoform 1)Ubiquitination-69.0121906983
438PhosphorylationPPICPRDSVKVINKE
CCCCCCCCEEEECCC
25.7230108239
444UbiquitinationDSVKVINKEGEVMDV
CCEEEECCCCCEEEE
56.84-

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
-KUbiquitinationE3 ubiquitin ligaseCRBNQ96SW2
PMID:29496670

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IKZF3_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 IKZF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_HUMANSIN3Aphysical
12015313
SIN3B_HUMANSIN3Bphysical
12015313
HDAC2_HUMANHDAC2physical
12015313
HDAC4_HUMANHDAC4physical
12015313
HDAC5_HUMANHDAC5physical
12015313
HDAC7_HUMANHDAC7physical
12015313
CHD4_HUMANCHD4physical
12015313
IKZF4_HUMANIKZF4physical
10978333
IKZF5_HUMANIKZF5physical
10978333
RASH_HUMANHRASphysical
10369681
B2CL1_HUMANBCL2L1physical
11714801
FOXP3_HUMANFOXP3physical
20676092
IKZF3_HUMANIKZF3physical
25416956
ABLM3_HUMANABLIM3physical
25416956
PP16B_HUMANPPP1R16Bphysical
25416956
DPOLM_HUMANPOLMphysical
25416956
OSGI1_HUMANOSGIN1physical
25416956
CHCH2_HUMANCHCHD2physical
25416956
SPG21_HUMANSPG21physical
25416956
OAZ3_HUMANOAZ3physical
25416956
CA109_HUMANC1orf109physical
25416956
MGN2_HUMANMAGOHBphysical
25416956
FANCL_HUMANFANCLphysical
25416956
TB22B_HUMANTBC1D22Bphysical
25416956
RCOR3_HUMANRCOR3physical
25416956
PCID2_HUMANPCID2physical
25416956
CABP5_HUMANCABP5physical
25416956
PPL13_HUMANLGALS14physical
25416956
EXOS5_HUMANEXOSC5physical
25416956
STALP_HUMANSTAMBPL1physical
25416956
TPC6A_HUMANTRAPPC6Aphysical
25416956
ARMC7_HUMANARMC7physical
25416956
TSSK3_HUMANTSSK3physical
25416956
ING5_HUMANING5physical
25416956
ZGPAT_HUMANZGPATphysical
25416956
FBF1_HUMANFBF1physical
25416956
ATPF2_HUMANATPAF2physical
25416956
EFHC1_HUMANEFHC1physical
25416956
RM53_HUMANMRPL53physical
25416956
EXOC8_HUMANEXOC8physical
25416956
TEKT4_HUMANTEKT4physical
25416956
TSTD2_HUMANTSTD2physical
25416956
NATD1_HUMANNATD1physical
25416956
MORN3_HUMANMORN3physical
25416956
TRI42_HUMANTRIM42physical
25416956
ARMC8_HUMANARMC8physical
26186194
IKZF4_HUMANIKZF4physical
26186194
SETMR_HUMANSETMARphysical
26186194
DGC14_HUMANDGCR14physical
26186194
GID4_HUMANGID4physical
26186194
MD1L1_HUMANMAD1L1physical
26186194
LDOC1_HUMANLDOC1physical
21516116
NATD1_HUMANNATD1physical
21516116
STK26_HUMANSTK26physical
21516116
MGN2_HUMANMAGOHBphysical
21516116
AAKB2_HUMANPRKAB2physical
21516116
RCOR3_HUMANRCOR3physical
21516116
UBC9_HUMANUBE2Iphysical
21516116
SUMO1_HUMANSUMO1physical
21516116
ATPF2_HUMANATPAF2physical
21516116
TCAF1_HUMANFAM115Aphysical
21516116
PRDM1_HUMANPRDM1physical
26823144
IKZF1_HUMANIKZF1physical
26823144
CRBN_HUMANCRBNphysical
27294876
IKZF4_HUMANIKZF4physical
28514442
SETMR_HUMANSETMARphysical
28514442
DGC14_HUMANDGCR14physical
28514442
P66B_HUMANGATAD2Bphysical
28514442

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 IKZF3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-169, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-286 AND TYR-290, ANDMASS SPECTROMETRY.

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