dbPTM

IKZF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IKZF1_HUMAN
UniProt AC	Q13422
Protein Name	DNA-binding protein Ikaros
Gene Name	IKZF1
Organism	Homo sapiens (Human).
Sequence Length	519
Subcellular Localization	Nucleus . In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation even
Protein Description	Transcription regulator of hematopoietic cell differentiation. [PubMed: 17934067 Binds gamma-satellite DNA]
Protein Sequence	MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	ADEGQDMSQVSGKES CCCCCCHHHCCCCCC	35.40	27251275
13	Phosphorylation	GQDMSQVSGKESPPV CCCHHHCCCCCCCCC	36.19	27251275
17	Phosphorylation	SQVSGKESPPVSDTP HHCCCCCCCCCCCCC	37.68	26074081
21	Phosphorylation	GKESPPVSDTPDEGD CCCCCCCCCCCCCCC	41.35	24905233
23	Phosphorylation	ESPPVSDTPDEGDEP CCCCCCCCCCCCCCC	25.73	24905233
38	Phosphorylation	MPIPEDLSTTSGGQQ CCCCCCCCCCCCCCC	41.79	24905233
39	Phosphorylation	PIPEDLSTTSGGQQS CCCCCCCCCCCCCCC	32.07	24905233
40	Phosphorylation	IPEDLSTTSGGQQSS CCCCCCCCCCCCCCC	23.23	24905233
41	Phosphorylation	PEDLSTTSGGQQSSK CCCCCCCCCCCCCCC	40.80	24905233
46	Phosphorylation	TTSGGQQSSKSDRVV CCCCCCCCCCCCEEE	31.67	24905233
47	Phosphorylation	TSGGQQSSKSDRVVA CCCCCCCCCCCEEEE	31.66	24905233
55	Phosphorylation	KSDRVVASNVKVETQ CCCEEEEECEEEEEC	30.46	23186163
58	Sumoylation	RVVASNVKVETQSDE EEEEECEEEEECCHH	38.31	-
58	Sumoylation	RVVASNVKVETQSDE EEEEECEEEEECCHH	38.31	-
61	Phosphorylation	ASNVKVETQSDEENG EECEEEEECCHHHCC	36.04	23401153
63	Phosphorylation	NVKVETQSDEENGRA CEEEEECCHHHCCCC	55.18	23401153
83	Methylation	EECAEDLRMLDASGE HHHHHHHHHHCCCCC	35.62	115386363
88	O-linked_Glycosylation	DLRMLDASGEKMNGS HHHHHCCCCCCCCCC	47.34	29351928
88	Phosphorylation	DLRMLDASGEKMNGS HHHHHCCCCCCCCCC	47.34	30576142
91	Ubiquitination	MLDASGEKMNGSHRD HHCCCCCCCCCCCCC	40.99	-
95	Phosphorylation	SGEKMNGSHRDQGSS CCCCCCCCCCCCCCC	15.45	-
101	Phosphorylation	GSHRDQGSSALSGVG CCCCCCCCCCCCCCC	13.55	21082442
105	Phosphorylation	DQGSSALSGVGGIRL CCCCCCCCCCCCEEC	31.02	-
116	Acetylation	GIRLPNGKLKCDICG CEECCCCCEECCCCE	51.95	25953088
138	Phosphorylation	VLMVHKRSHTGERPF EEEEECCCCCCCCCC	30.15	28450419
140	Phosphorylation	MVHKRSHTGERPFQC EEECCCCCCCCCCCC	41.82	28450419
153	Phosphorylation	QCNQCGASFTQKGNL CCCCCCCCCCCCCCE	17.70	27080861
155	Phosphorylation	NQCGASFTQKGNLLR CCCCCCCCCCCCEEE	27.20	27080861
157	Ubiquitination	CGASFTQKGNLLRHI CCCCCCCCCCEEEEE	46.86	-
165	Ubiquitination	GNLLRHIKLHSGEKP CCEEEEEEECCCCCC	33.74	-
168	Phosphorylation	LRHIKLHSGEKPFKC EEEEEECCCCCCEEE	60.11	23401153
171	Sumoylation	IKLHSGEKPFKCHLC EEECCCCCCEEEEEC	60.32	-
171	Acetylation	IKLHSGEKPFKCHLC EEECCCCCCEEEEEC	60.32	-
171	Sumoylation	IKLHSGEKPFKCHLC EEECCCCCCEEEEEC	60.32	-
171	Ubiquitination	IKLHSGEKPFKCHLC EEECCCCCCEEEEEC	60.32	-
174	Ubiquitination	HSGEKPFKCHLCNYA CCCCCCEEEEECCHH	29.31	-
196	Phosphorylation	TGHLRTHSVGKPHKC CCCCCCCCCCCCCCC	31.77	-
196 (in isoform 7)	Phosphorylation	-	31.77	-
196 (in isoform 8)	Phosphorylation	-	31.77	-
214	Phosphorylation	GRSYKQRSSLEEHKE CCCHHHCCCHHHHHH	36.46	-
215	Phosphorylation	RSYKQRSSLEEHKER CCHHHCCCHHHHHHH	41.82	-
220	Ubiquitination	RSSLEEHKERCHNYL CCCHHHHHHHHHHHH	50.57	-
226	Phosphorylation	HKERCHNYLESMGLP HHHHHHHHHHHCCCC	6.54	22210691
241	Sumoylation	GTLYPVIKEETNHSE CCHHHHHHHCCCCHH	50.13	-
241	Sumoylation	GTLYPVIKEETNHSE CCHHHHHHHCCCCHH	50.13	-
241	Ubiquitination	GTLYPVIKEETNHSE CCHHHHHHHCCCCHH	50.13	-
244	Phosphorylation	YPVIKEETNHSEMAE HHHHHHCCCCHHHHH	39.05	22210691
247	Phosphorylation	IKEETNHSEMAEDLC HHHCCCCHHHHHHHH	31.01	22210691
249	Sulfoxidation	EETNHSEMAEDLCKI HCCCCHHHHHHHHHH	5.77	21406390
255	Ubiquitination	EMAEDLCKIGSERSL HHHHHHHHHCHHHHH	58.35	-
258	Phosphorylation	EDLCKIGSERSLVLD HHHHHHCHHHHHHHH	33.05	30576142
261	Phosphorylation	CKIGSERSLVLDRLA HHHCHHHHHHHHHHH	20.83	23401153
269	Phosphorylation	LVLDRLASNVAKRKS HHHHHHHHHHHHHHC	36.11	25003641
273	Acetylation	RLASNVAKRKSSMPQ HHHHHHHHHHCCCCH	56.95	25953088
273	Ubiquitination	RLASNVAKRKSSMPQ HHHHHHHHHHCCCCH	56.95	-
276	Phosphorylation	SNVAKRKSSMPQKFL HHHHHHHCCCCHHHC	35.58	24719451
277	Phosphorylation	NVAKRKSSMPQKFLG HHHHHHCCCCHHHCC	37.20	24719451
281	Acetylation	RKSSMPQKFLGDKGL HHCCCCHHHCCCCCC	36.36	25953088
281	Ubiquitination	RKSSMPQKFLGDKGL HHCCCCHHHCCCCCC	36.36	-
286	Acetylation	PQKFLGDKGLSDTPY CHHHCCCCCCCCCCC	61.01	25953088
286	Ubiquitination	PQKFLGDKGLSDTPY CHHHCCCCCCCCCCC	61.01	-
289	Phosphorylation	FLGDKGLSDTPYDSS HCCCCCCCCCCCCCC	48.37	30576142
291	Phosphorylation	GDKGLSDTPYDSSAS CCCCCCCCCCCCCCC	22.00	30576142
293	Phosphorylation	KGLSDTPYDSSASYE CCCCCCCCCCCCCHH	30.46	30108239
295	Phosphorylation	LSDTPYDSSASYEKE CCCCCCCCCCCHHHH	23.20	23401153
296	Phosphorylation	SDTPYDSSASYEKEN CCCCCCCCCCHHHHH	20.52	30108239
298	Phosphorylation	TPYDSSASYEKENEM CCCCCCCCHHHHHHH	35.45	23401153
299	Phosphorylation	PYDSSASYEKENEMM CCCCCCCHHHHHHHH	30.64	30576142
301	Ubiquitination	DSSASYEKENEMMKS CCCCCHHHHHHHHHH	58.57	-
321	Phosphorylation	AINNAINYLGAESLR HHHHHHHHCCHHHHH	10.62	-
326	Phosphorylation	INYLGAESLRPLVQT HHHCCHHHHHCCCCC	29.19	26074081
333	Phosphorylation	SLRPLVQTPPGGSEV HHHCCCCCCCCCCCC	24.79	28464451
338	Phosphorylation	VQTPPGGSEVVPVIS CCCCCCCCCCCCEEC	32.88	26074081
345	Phosphorylation	SEVVPVISPMYQLHK CCCCCEECCCEECCC	12.12	28464451
348	Phosphorylation	VPVISPMYQLHKPLA CCEECCCEECCCCCC	16.00	26074081
358	Phosphorylation	HKPLAEGTPRSNHSA CCCCCCCCCCCCCCC	13.66	30576142
361	O-linked_Glycosylation	LAEGTPRSNHSAQDS CCCCCCCCCCCCCCH	39.85	29351928
361	Phosphorylation	LAEGTPRSNHSAQDS CCCCCCCCCCCCCCH	39.85	23401153
364	Phosphorylation	GTPRSNHSAQDSAVE CCCCCCCCCCCHHHH	31.69	23071339
368	O-linked_Glycosylation	SNHSAQDSAVENLLL CCCCCCCHHHHHHHH	23.33	29351928
368	Phosphorylation	SNHSAQDSAVENLLL CCCCCCCHHHHHHHH	23.33	28674151
377	Phosphorylation	VENLLLLSKAKLVPS HHHHHHHHHCEECCC	30.45	21082442
378	Acetylation	ENLLLLSKAKLVPSE HHHHHHHHCEECCCC	49.89	25953088
378	Ubiquitination	ENLLLLSKAKLVPSE HHHHHHHHCEECCCC	49.89	-
380	Acetylation	LLLLSKAKLVPSERE HHHHHHCEECCCCCC	54.47	25953088
380	Ubiquitination	LLLLSKAKLVPSERE HHHHHHCEECCCCCC	54.47	-
384	Phosphorylation	SKAKLVPSEREASPS HHCEECCCCCCCCCC	41.63	28450419
389	Phosphorylation	VPSEREASPSNSCQD CCCCCCCCCCCCCCC	24.90	23401153
391	Phosphorylation	SEREASPSNSCQDST CCCCCCCCCCCCCCC	38.59	30576142
393	Phosphorylation	REASPSNSCQDSTDT CCCCCCCCCCCCCCC	19.93	28450419
397	Phosphorylation	PSNSCQDSTDTESNN CCCCCCCCCCCCCCC	11.42	28450419
398	Phosphorylation	SNSCQDSTDTESNNE CCCCCCCCCCCCCCH	56.05	30576142
400	Phosphorylation	SCQDSTDTESNNEEQ CCCCCCCCCCCCHHH	41.21	30576142
402	Phosphorylation	QDSTDTESNNEEQRS CCCCCCCCCCHHHHH	47.23	28450419
409	Phosphorylation	SNNEEQRSGLIYLTN CCCHHHHHHEEEECC	37.33	28796482
413	Phosphorylation	EQRSGLIYLTNHIAP HHHHHEEEECCCHHH	16.71	28796482
415	Phosphorylation	RSGLIYLTNHIAPHA HHHEEEECCCHHHHH	14.05	28796482
427	Phosphorylation	PHARNGLSLKEEHRA HHHHCCCCCCHHHHH	38.50	23401153
429	Sumoylation	ARNGLSLKEEHRAYD HHCCCCCCHHHHHHH	58.65	-
429	Acetylation	ARNGLSLKEEHRAYD HHCCCCCCHHHHHHH	58.65	25953088
429	Sumoylation	ARNGLSLKEEHRAYD HHCCCCCCHHHHHHH	58.65	-
429	Ubiquitination	ARNGLSLKEEHRAYD HHCCCCCCHHHHHHH	58.65	-
435	Phosphorylation	LKEEHRAYDLLRAAS CCHHHHHHHHHHHHH	13.69	27642862
442	Phosphorylation	YDLLRAASENSQDAL HHHHHHHHHCCHHHH	36.00	23401153
445	Phosphorylation	LRAASENSQDALRVV HHHHHHCCHHHHHEE	25.94	23401153
453	Phosphorylation	QDALRVVSTSGEQMK HHHHHEEECCCCCCE	17.63	20049867
454	Phosphorylation	DALRVVSTSGEQMKV HHHHEEECCCCCCEE	29.19	20049867
455	Phosphorylation	ALRVVSTSGEQMKVY HHHEEECCCCCCEEE	32.59	20049867
460	Acetylation	STSGEQMKVYKCEHC ECCCCCCEEEECCCC	41.95	25953088
460	Ubiquitination	STSGEQMKVYKCEHC ECCCCCCEEEECCCC	41.95	-
462	Phosphorylation	SGEQMKVYKCEHCRV CCCCCEEEECCCCEE	12.38	20049867

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
214	S	Phosphorylation	Kinase	BTK	Q06187	PSP
215	S	Phosphorylation	Kinase	BTK	Q06187	PSP
361	S	Phosphorylation	Kinase	SYK	P43405	PSP
364	S	Phosphorylation	Kinase	SYK	P43405	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	CRBN	Q96SW2	PMID:24292625

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
13	S	Phosphorylation	22106042
Phosphorylation/dephosphorylation events on Ser-13 and Ser-295 regulate TDT expression during thymocyte differentiation.
140	T	Phosphorylation	22106042
Phosphorylation on Thr-140 is required for DNA and pericentromeric location during mitosis.
295	S	Phosphorylation	22106042
Phosphorylation/dephosphorylation events on Ser-13 and Ser-295 regulate TDT expression during thymocyte differentiation.
361	S	Phosphorylation	19690332
Phosphorylation at Ser-361 and Ser-364 downstream of SYK induces nuclear translocation.
364	S	Phosphorylation	19690332
Phosphorylation at Ser-361 and Ser-364 downstream of SYK induces nuclear translocation.

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 IKZF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCOR2_HUMAN	NCOR2	physical	11959865
TBP_HUMAN	TBP	physical	11959865
TF2B_HUMAN	GTF2B	physical	11959865
SIN3B_MOUSE	Sin3b	physical	10357820
SIN3A_MOUSE	Sin3a	physical	10357820
IKZF3_MOUSE	Ikzf3	physical	10357820
HDAC1_MOUSE	Hdac1	physical	10357820
CHD4_HUMAN	CHD4	physical	12015313
SIN3A_HUMAN	SIN3A	physical	12015313
SIN3B_HUMAN	SIN3B	physical	12015313
HDAC2_HUMAN	HDAC2	physical	12015313
HDAC4_HUMAN	HDAC4	physical	12015313
HDAC5_HUMAN	HDAC5	physical	12015313
HDAC7_HUMAN	HDAC7	physical	12015313
IKZF4_HUMAN	IKZF4	physical	10978333
IKZF5_HUMAN	IKZF5	physical	10978333
GATA1_HUMAN	GATA1	physical	19114560
CHD4_HUMAN	CHD4	physical	11003653
IKZF3_HUMAN	IKZF3	physical	10204490
HDAC1_HUMAN	HDAC1	physical	10204490
HDAC2_HUMAN	HDAC2	physical	10204490
RBBP4_HUMAN	RBBP4	physical	10204490
CHD3_HUMAN	CHD3	physical	10204490
SMCA4_HUMAN	SMARCA4	physical	10204490
TDG_HUMAN	TDG	physical	21988832
CRBN_HUMAN	CRBN	physical	24292623
IKZF1_HUMAN	IKZF1	physical	25416956
MCRS1_HUMAN	MCRS1	physical	25416956
MD2L2_HUMAN	MAD2L2	physical	25416956
GLRX3_HUMAN	GLRX3	physical	25416956
NEK6_HUMAN	NEK6	physical	25416956
MO4L1_HUMAN	MORF4L1	physical	25416956
PNKP_HUMAN	PNKP	physical	25416956
SNW1_HUMAN	SNW1	physical	25416956
ISCU_HUMAN	ISCU	physical	25416956
LSM4_HUMAN	LSM4	physical	25416956
FA50B_HUMAN	FAM50B	physical	25416956
ZN581_HUMAN	ZNF581	physical	25416956
SYT17_HUMAN	SYT17	physical	25416956
CA109_HUMAN	C1orf109	physical	25416956
RYDEN_HUMAN	C19orf66	physical	25416956
LMO3_HUMAN	LMO3	physical	25416956
CBX8_HUMAN	CBX8	physical	25416956
SH24A_HUMAN	SH2D4A	physical	25416956
KIF9_HUMAN	KIF9	physical	25416956
AEN_HUMAN	AEN	physical	25416956
CH033_HUMAN	C8orf33	physical	25416956
SCNM1_HUMAN	SCNM1	physical	25416956
NOC4L_HUMAN	NOC4L	physical	25416956
ARMC7_HUMAN	ARMC7	physical	25416956
F214B_HUMAN	FAM214B	physical	25416956
F161A_HUMAN	FAM161A	physical	25416956
SPC1L_HUMAN	SPATC1L	physical	25416956
FRMD6_HUMAN	FRMD6	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
ZMAT2_HUMAN	ZMAT2	physical	25416956
ALKB3_HUMAN	ALKBH3	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
CA174_HUMAN	C1orf174	physical	25416956
CTBP2_HUMAN	CTBP2	physical	21516116
DCX_HUMAN	DCX	physical	21516116
FA50B_HUMAN	FAM50B	physical	21516116
RA51D_HUMAN	RAD51D	physical	21516116
MPPD2_HUMAN	MPPED2	physical	21516116
F214B_HUMAN	FAM214B	physical	21516116
IKZF3_HUMAN	IKZF3	physical	26823144
IKZF3_HUMAN	IKZF3	physical	28514442
MIB2_HUMAN	MIB2	physical	28514442
IKZF2_HUMAN	IKZF2	physical	28514442
KLD10_HUMAN	KLHDC10	physical	28514442
IKZF4_HUMAN	IKZF4	physical	28514442
POC1A_HUMAN	POC1A	physical	28514442
FOXK2_HUMAN	FOXK2	physical	28514442
CHD3_HUMAN	CHD3	physical	28514442
IKZF5_HUMAN	IKZF5	physical	28514442
CHD4_HUMAN	CHD4	physical	28514442
FOXK1_HUMAN	FOXK1	physical	28514442
WDR76_HUMAN	WDR76	physical	28514442
MCRS1_HUMAN	MCRS1	physical	28514442
APBP2_HUMAN	APPBP2	physical	28514442
ANR27_HUMAN	ANKRD27	physical	28514442
ZMY19_HUMAN	ZMYND19	physical	28514442
KLDC3_HUMAN	KLHDC3	physical	28514442
NFS1_HUMAN	NFS1	physical	28514442
MTA3_HUMAN	MTA3	physical	28514442
CUL2_HUMAN	CUL2	physical	28514442
FL2D_HUMAN	WTAP	physical	28514442
BTBD1_HUMAN	BTBD1	physical	28514442
DHB4_HUMAN	HSD17B4	physical	28514442
WDR26_HUMAN	WDR26	physical	28514442
MTA1_HUMAN	MTA1	physical	28514442
CTBP2_HUMAN	CTBP2	physical	28514442
P66A_HUMAN	GATAD2A	physical	28514442
MKLN1_HUMAN	MKLN1	physical	28514442
P66B_HUMAN	GATAD2B	physical	28514442
RMD5A_HUMAN	RMND5A	physical	28514442
RBP10_HUMAN	RANBP10	physical	28514442
MTA2_HUMAN	MTA2	physical	28514442
ARMC8_HUMAN	ARMC8	physical	28514442
GALC_HUMAN	GALC	physical	28514442
POTEI_HUMAN	POTEI	physical	28514442
FOXP1_HUMAN	FOXP1	physical	27588474

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 IKZF1_HUMAN

Related Literatures of Post-Translational Modification

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-63; SER-361; SER-364;SER-377 AND SER-442, AND MASS SPECTROMETRY.	19690332 [Abstract]

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