dbPTM

IREB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IREB2_HUMAN
UniProt AC	P48200
Protein Name	Iron-responsive element-binding protein 2
Gene Name	IREB2
Organism	Homo sapiens (Human).
Sequence Length	963
Subcellular Localization	Cytoplasm.
Protein Description	RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA..
Protein Sequence	MDAPKAGYAFEYLIETLNDSSHKKFFDVSKLGTKYDVLPYSIRVLLEAAVRNCDGFLMKKEDVMNILDWKTKQSNVEVPFFPARVLLQDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSKCAIQNAPNPGGGDLQKAGKLSPVKVQPKKLPCRGQTTCRGSCDSGELGRNSGTFSSQIENTPILCPFHLQPVPEPETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTGMAHQINLEYLSRVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGCELTGSSNPFVTSIDVVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLKHLEHTGFSKAKLESMETYLKAVKLFRNDQNSSGEPEYSQVIQINLNSIVPSVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQIAAEKQKDIVSIHYEGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVEAGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSICVGNTAPLSDAVLNAVKQGDLVTCGILSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGTDPTGKNIYLHDIWPSREEVHRVEEEHVILSMFKALKDKIEMGNKRWNSLEAPDSVLFPWDLKSTYIRCPSFFDKLTKEPIALQAIENAHVLLYLGDSVTTDHISPAGSIARNSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFIGKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLQFLPGENADSLGLSGRETFSLTFPEELSPGITLNIQTSTGKVFSVIASFEDDVEITLYKHGGLLNFVARKFS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MDAPKAGYAFEY ---CCCCCHHHHHHH	57.05	-
5	Ubiquitination	---MDAPKAGYAFEY ---CCCCCHHHHHHH	57.05	-
23	Ubiquitination	TLNDSSHKKFFDVSK HCCCCCCCCCEEHHH	53.90	-
23	Ubiquitination	TLNDSSHKKFFDVSK HCCCCCCCCCEEHHH	53.90	21890473
24	Ubiquitination	LNDSSHKKFFDVSKL CCCCCCCCCEEHHHC	45.93	-
24	Ubiquitination	LNDSSHKKFFDVSKL CCCCCCCCCEEHHHC	45.93	-
30	Ubiquitination	KKFFDVSKLGTKYDV CCCEEHHHCCCCCCC	51.27	-
30	Ubiquitination	KKFFDVSKLGTKYDV CCCEEHHHCCCCCCC	51.27	-
34	Ubiquitination	DVSKLGTKYDVLPYS EHHHCCCCCCCCCHH	37.34	-
34	Ubiquitination	DVSKLGTKYDVLPYS EHHHCCCCCCCCCHH	37.34	-
40	Phosphorylation	TKYDVLPYSIRVLLE CCCCCCCHHHHHHHH	16.75	22817900
41	Phosphorylation	KYDVLPYSIRVLLEA CCCCCCHHHHHHHHH	11.28	24719451
59	Ubiquitination	NCDGFLMKKEDVMNI CCCCEEECHHHHHHH	55.98	-
59	Ubiquitination	NCDGFLMKKEDVMNI CCCCEEECHHHHHHH	55.98	-
60	Ubiquitination	CDGFLMKKEDVMNIL CCCEEECHHHHHHHH	45.22	-
60	Ubiquitination	CDGFLMKKEDVMNIL CCCEEECHHHHHHHH	45.22	-
70	Ubiquitination	VMNILDWKTKQSNVE HHHHHCCCCCCCCCC	45.57	-
70	Ubiquitination	VMNILDWKTKQSNVE HHHHHCCCCCCCCCC	45.57	-
72	Ubiquitination	NILDWKTKQSNVEVP HHHCCCCCCCCCCCC	48.26	-
72	Ubiquitination	NILDWKTKQSNVEVP HHHCCCCCCCCCCCC	48.26	-
107	Ubiquitination	AAMREAVKTLGGDPE HHHHHHHHHHCCCHH	45.11	21890473
107	Ubiquitination	AAMREAVKTLGGDPE HHHHHHHHHHCCCHH	45.11	-
108	Phosphorylation	AMREAVKTLGGDPEK HHHHHHHHHCCCHHH	24.84	27251275
115	Ubiquitination	TLGGDPEKVHPACPT HHCCCHHHCCCCCCC	51.75	-
115	Ubiquitination	TLGGDPEKVHPACPT HHCCCHHHCCCCCCC	51.75	-
136	Ubiquitination	SLQIDFSKCAIQNAP CEEEEHHHCHHCCCC	27.90	-
136	Ubiquitination	SLQIDFSKCAIQNAP CEEEEHHHCHHCCCC	27.90	-
152	Ubiquitination	PGGGDLQKAGKLSPV CCCCCHHHCCCCCCC	67.42	-
152	Ubiquitination	PGGGDLQKAGKLSPV CCCCCHHHCCCCCCC	67.42	-
155	Acetylation	GDLQKAGKLSPVKVQ CCHHHCCCCCCCEEC	51.13	164571
157	Phosphorylation	LQKAGKLSPVKVQPK HHHCCCCCCCEECCC	31.00	22617229
157	Phosphorylation	LQKAGKLSPVKVQPK HHHCCCCCCCEECCC	31.00	19691289
160	Ubiquitination	AGKLSPVKVQPKKLP CCCCCCCEECCCCCC	38.24	-
160	Acetylation	AGKLSPVKVQPKKLP CCCCCCCEECCCCCC	38.24	164573
172	Phosphorylation	KLPCRGQTTCRGSCD CCCCCCCCCCCCCCC	30.59	29083192
173	Phosphorylation	LPCRGQTTCRGSCDS CCCCCCCCCCCCCCC	7.72	25159151
175	Methylation	CRGQTTCRGSCDSGE CCCCCCCCCCCCCCC	37.66	115480475
177	Phosphorylation	GQTTCRGSCDSGELG CCCCCCCCCCCCCCC	8.73	21815630
178	S-nitrosocysteine	QTTCRGSCDSGELGR CCCCCCCCCCCCCCC	5.56	-
178	S-nitrosylation	QTTCRGSCDSGELGR CCCCCCCCCCCCCCC	5.56	22178444
180	Phosphorylation	TCRGSCDSGELGRNS CCCCCCCCCCCCCCC	38.19	21712546
187	Phosphorylation	SGELGRNSGTFSSQI CCCCCCCCCCCHHHC	37.54	25627689
216	Ubiquitination	PEPETVLKNQEVEFG CCCCHHCCCCEEECC	52.85	-
216	Ubiquitination	PEPETVLKNQEVEFG CCCCHHCCCCEEECC	52.85	-
233	Ubiquitination	RERLQFFKWSSRVFK HHHHHHHHHCCCCCC	47.67	21890473
233	Ubiquitination	RERLQFFKWSSRVFK HHHHHHHHHCCCCCC	47.67	21890473
233	Ubiquitination	RERLQFFKWSSRVFK HHHHHHHHHCCCCCC	47.67	-
240	Ubiquitination	KWSSRVFKNVAVIPP HHCCCCCCCEEEECC	47.88	-
240	Ubiquitination	KWSSRVFKNVAVIPP HHCCCCCCCEEEECC	47.88	-
358	Phosphorylation	KFVEFFGSGVSQLSI HHHHHHCCCCCEEEE	30.75	29255136
361	Phosphorylation	EFFGSGVSQLSIVDR HHHCCCCCEEEEECH	29.00	29255136
364	Phosphorylation	GSGVSQLSIVDRTTI CCCCCEEEEECHHHH	16.96	29255136
402	Ubiquitination	LEHTGFSKAKLESME EECCCCCHHHHHHHH	47.48	-
404	Ubiquitination	HTGFSKAKLESMETY CCCCCHHHHHHHHHH	57.43	21890473
413	Ubiquitination	ESMETYLKAVKLFRN HHHHHHHHHHHHHHC	40.49	21890473
416	Ubiquitination	ETYLKAVKLFRNDQN HHHHHHHHHHHCCCC	46.93	-
425	Phosphorylation	FRNDQNSSGEPEYSQ HHCCCCCCCCCCCEE	55.51	-
449	Ubiquitination	VPSVSGPKRPQDRVA CCCCCCCCCCCCCEE	79.02	21890473
461	Ubiquitination	RVAVTDMKSDFQACL CEEEEECHHHHHHHH	50.08	-
471	Ubiquitination	FQACLNEKVGFKGFQ HHHHHHCCCCCCCEE	46.73	-
475	Ubiquitination	LNEKVGFKGFQIAAE HHCCCCCCCEEEEEH	53.54	21890473
483	Ubiquitination	GFQIAAEKQKDIVSI CEEEEEHHHCCEEEE	58.90	21890473
485	Ubiquitination	QIAAEKQKDIVSIHY EEEEHHHCCEEEEEE	61.56	-
489	Phosphorylation	EKQKDIVSIHYEGSE HHHCCEEEEEECCCE	12.18	29083192
492	Phosphorylation	KDIVSIHYEGSEYKL CCEEEEEECCCEEEE	21.95	29083192
495	Phosphorylation	VSIHYEGSEYKLSHG EEEEECCCEEEECCC	26.30	29083192
497	Phosphorylation	IHYEGSEYKLSHGSV EEECCCEEEECCCCE	20.94	29083192
541	Phosphorylation	AGLRVKPYIRTSLSP CCCCCCCEECCCCCC	9.41	30576142
544	Phosphorylation	RVKPYIRTSLSPGSG CCCCEECCCCCCCCC	25.18	30576142
545	Phosphorylation	VKPYIRTSLSPGSGM CCCEECCCCCCCCCH	19.59	30576142
611	Malonylation	CGILSGNKNFEGRLC EEECCCCCCCCCCCC	67.55	26320211
611	Ubiquitination	CGILSGNKNFEGRLC EEECCCCCCCCCCCC	67.55	-
682	Phosphorylation	EEEHVILSMFKALKD HHHHHHHHHHHHHHH	15.85	-
685	Ubiquitination	HVILSMFKALKDKIE HHHHHHHHHHHHHHH	44.14	-
696	Ubiquitination	DKIEMGNKRWNSLEA HHHHHCCCCCCCCCC	53.73	21890473
714	Ubiquitination	VLFPWDLKSTYIRCP EEECCCCCCCEEECH	37.97	21890473
726	Ubiquitination	RCPSFFDKLTKEPIA ECHHHHHHHCCCCCH	53.55	-
769	Ubiquitination	ARNSAAAKYLTNRGL HCHHHHHHHHHHCCC	35.75	21890473
777	Phosphorylation	YLTNRGLTPREFNSY HHHHCCCCHHHHHHH	24.11	24719451
784	Phosphorylation	TPREFNSYGARRGND CHHHHHHHCCCCCCC	18.86	-
803	Ubiquitination	RGTFANIKLFNKFIG CCCHHCHHHHHHHCC	47.00	21890473
807	Ubiquitination	ANIKLFNKFIGKPAP HCHHHHHHHCCCCCC	30.90	21890473
811	Ubiquitination	LFNKFIGKPAPKTIH HHHHHCCCCCCCEEE	32.94	-
815	Ubiquitination	FIGKPAPKTIHFPSG HCCCCCCCEEECCCC	63.32	-
836	Ubiquitination	EAAELYQKEGIPLII HHHHHHHHCCCCEEE	44.33	-
847	Ubiquitination	PLIILAGKKYGSGNS CEEEECCCCCCCCCC	36.90	21890473
848	Ubiquitination	LIILAGKKYGSGNSR EEEECCCCCCCCCCC	54.66	-
860	Ubiquitination	NSRDWAAKGPYLLGV CCCHHHHHCHHHHHH	53.31	21890473
868	Ubiquitination	GPYLLGVKAVLAESY CHHHHHHHHHHHHHH	30.86	21890473
877	Ubiquitination	VLAESYEKIHKDHLI HHHHHHHHHCHHCEE	41.71	21890473
880	Ubiquitination	ESYEKIHKDHLIGIG HHHHHHCHHCEEEEE	50.76	21890473
913	Phosphorylation	GRETFSLTFPEELSP CCCEEEEECCCHHCC	35.63	-

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
157	S	Phosphorylation	Kinase	CDK1	P06493	PSP
157	S	Phosphorylation	Kinase	CDK1	P06493	GPS
157	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RBCK1	Q9BYM8	PMID:16275334
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL5	Q9UKA1	PMID:19762596
-	K	Ubiquitination	E3 ubiquitin ligase	VHL	P40337	PMID:15777842

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IREB2_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 IREB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
YBOX1_HUMAN	YBX1	physical	12192037
FBXL5_HUMAN	FBXL5	physical	19762596
HOIL1_HUMAN	RBCK1	physical	17822790
A4_HUMAN	APP	physical	21832049
UBP53_HUMAN	USP53	physical	21988832
SAE2_HUMAN	UBA2	physical	22863883
HOIL1_HUMAN	RBCK1	physical	12629548
SF01_HUMAN	SF1	physical	26344197

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 IREB2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-157, AND MASSSPECTROMETRY.	18669648 [Abstract]