UniProt ID | I2BP2_HUMAN | |
---|---|---|
UniProt AC | Q7Z5L9 | |
Protein Name | Interferon regulatory factor 2-binding protein 2 | |
Gene Name | IRF2BP2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 587 | |
Subcellular Localization | Cytoplasm. Nucleus. | |
Protein Description | Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle.. | |
Protein Sequence | MAAAVAVAAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAHGCFPEGRSPPGAAASAAAKPPPLSAKDILLQQQQQLGHGGPEAAPRAPQALERYPLAAAAERPPRLGSDFGSSRPAASLAQPPTPQPPPVNGILVPNGFSKLEEPPELNRQSPNPRRGHAVPPTLVPLMNGSATPLPTALGLGGRAAASLAAVSGTAAASLGSAQPTDLGAHKRPASVSSSAAVEHEQREAAAKEKQPPPPAHRGPADSLSTAAGAAELSAEGAGKSRGSGEQDWVNRPKTVRDTLLALHQHGHSGPFESKFKKEPALTAGRLLGFEANGANGSKAVARTARKRKPSPEPEGEVGPPKINGEAQPWLSTSTEGLKIPMTPTSSFVSPPPPTASPHSNRTTPPEAAQNGQSPMAALILVADNAGGSHASKDANQVHSTTRRNSNSPPSPSSMNQRRLGPREVGGQGAGNTGGLEPVHPASLPDSSLATSAPLCCTLCHERLEDTHFVQCPSVPSHKFCFPCSRQSIKQQGASGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAAAVAVAA ------CHHHHHHHH | 12.25 | 22814378 | |
11 | Phosphorylation | AVAVAAASRRQSCYL HHHHHHHHHCCCEEE | 24.22 | 20068231 | |
15 | Phosphorylation | AAASRRQSCYLCDLP HHHHHCCCEEECCCC | 11.69 | 25849741 | |
17 | Phosphorylation | ASRRQSCYLCDLPRM HHHCCCEEECCCCCC | 18.66 | 28450419 | |
71 | Phosphorylation | GCFPEGRSPPGAAAS CCCCCCCCCCCHHHH | 46.43 | 23401153 | |
78 | Phosphorylation | SPPGAAASAAAKPPP CCCCHHHHHHCCCCC | 17.45 | 24702127 | |
87 | Phosphorylation | AAKPPPLSAKDILLQ HCCCCCCCHHHHHHH | 38.76 | 24702127 | |
89 | Ubiquitination | KPPPLSAKDILLQQQ CCCCCCHHHHHHHHH | 41.76 | 21890473 | |
89 (in isoform 1) | Ubiquitination | - | 41.76 | 21890473 | |
89 (in isoform 2) | Ubiquitination | - | 41.76 | 21890473 | |
109 | Methylation | GGPEAAPRAPQALER CCCCCCCCCCHHHHH | 54.92 | 115480507 | |
116 | Methylation | RAPQALERYPLAAAA CCCHHHHHCCCHHHH | 38.94 | 80702545 | |
125 | Methylation | PLAAAAERPPRLGSD CCHHHHCCCCCCCCC | 41.62 | 115480499 | |
131 | Phosphorylation | ERPPRLGSDFGSSRP CCCCCCCCCCCCCCC | 34.07 | 23401153 | |
135 | Phosphorylation | RLGSDFGSSRPAASL CCCCCCCCCCCCHHH | 24.14 | 23312004 | |
136 | Phosphorylation | LGSDFGSSRPAASLA CCCCCCCCCCCHHHC | 42.54 | 27794612 | |
141 | Phosphorylation | GSSRPAASLAQPPTP CCCCCCHHHCCCCCC | 26.75 | 28450419 | |
147 | Phosphorylation | ASLAQPPTPQPPPVN HHHCCCCCCCCCCCC | 41.04 | 28450419 | |
163 | Phosphorylation | ILVPNGFSKLEEPPE EECCCCCCCCCCCCC | 37.42 | 22210691 | |
175 | Phosphorylation | PPELNRQSPNPRRGH CCCCCCCCCCCCCCC | 24.33 | 29255136 | |
195 | Phosphorylation | LVPLMNGSATPLPTA CCCCCCCCCCCCCCH | 24.78 | 21712546 | |
197 | Phosphorylation | PLMNGSATPLPTALG CCCCCCCCCCCCHHC | 27.36 | 25159151 | |
212 | O-linked_Glycosylation | LGGRAAASLAAVSGT CCHHHHHHHHHHHCC | 17.51 | 30059200 | |
212 | Phosphorylation | LGGRAAASLAAVSGT CCHHHHHHHHHHHCC | 17.51 | 28555341 | |
217 | O-linked_Glycosylation | AASLAAVSGTAAASL HHHHHHHHCCHHHHC | 26.21 | 30059200 | |
217 | Phosphorylation | AASLAAVSGTAAASL HHHHHHHHCCHHHHC | 26.21 | 28555341 | |
219 | O-linked_Glycosylation | SLAAVSGTAAASLGS HHHHHHCCHHHHCCC | 12.96 | 30059200 | |
223 | O-linked_Glycosylation | VSGTAAASLGSAQPT HHCCHHHHCCCCCCC | 28.65 | 30059200 | |
223 | Phosphorylation | VSGTAAASLGSAQPT HHCCHHHHCCCCCCC | 28.65 | 22210691 | |
226 | O-linked_Glycosylation | TAAASLGSAQPTDLG CHHHHCCCCCCCCCC | 29.08 | 30059200 | |
226 | Phosphorylation | TAAASLGSAQPTDLG CHHHHCCCCCCCCCC | 29.08 | 22210691 | |
230 | O-linked_Glycosylation | SLGSAQPTDLGAHKR HCCCCCCCCCCCCCC | 31.60 | 30059200 | |
230 | Phosphorylation | SLGSAQPTDLGAHKR HCCCCCCCCCCCCCC | 31.60 | 22210691 | |
236 | Acetylation | PTDLGAHKRPASVSS CCCCCCCCCCCCCCH | 60.59 | 25953088 | |
240 | O-linked_Glycosylation | GAHKRPASVSSSAAV CCCCCCCCCCHHHHH | 25.80 | 30059200 | |
240 | Phosphorylation | GAHKRPASVSSSAAV CCCCCCCCCCHHHHH | 25.80 | 29255136 | |
242 | O-linked_Glycosylation | HKRPASVSSSAAVEH CCCCCCCCHHHHHHH | 18.97 | 30059200 | |
242 | Phosphorylation | HKRPASVSSSAAVEH CCCCCCCCHHHHHHH | 18.97 | 29255136 | |
243 | Phosphorylation | KRPASVSSSAAVEHE CCCCCCCHHHHHHHH | 23.11 | 29255136 | |
244 | Phosphorylation | RPASVSSSAAVEHEQ CCCCCCHHHHHHHHH | 16.85 | 30278072 | |
272 | Phosphorylation | AHRGPADSLSTAAGA CCCCCCCHHHHHHHH | 26.73 | 28555341 | |
274 | Phosphorylation | RGPADSLSTAAGAAE CCCCCHHHHHHHHHH | 21.69 | 21601212 | |
275 | Phosphorylation | GPADSLSTAAGAAEL CCCCHHHHHHHHHHH | 26.31 | 23312004 | |
283 | Phosphorylation | AAGAAELSAEGAGKS HHHHHHHHHCCCCCC | 18.77 | 23312004 | |
289 | Acetylation | LSAEGAGKSRGSGEQ HHHCCCCCCCCCCCC | 36.12 | 25953088 | |
289 | Sumoylation | LSAEGAGKSRGSGEQ HHHCCCCCCCCCCCC | 36.12 | 28112733 | |
289 | Ubiquitination | LSAEGAGKSRGSGEQ HHHCCCCCCCCCCCC | 36.12 | 32015554 | |
290 | Phosphorylation | SAEGAGKSRGSGEQD HHCCCCCCCCCCCCC | 40.74 | 25159151 | |
291 | Methylation | AEGAGKSRGSGEQDW HCCCCCCCCCCCCCC | 46.94 | 115480511 | |
293 | Phosphorylation | GAGKSRGSGEQDWVN CCCCCCCCCCCCCCC | 37.74 | 25159151 | |
303 | Sumoylation | QDWVNRPKTVRDTLL CCCCCCCHHHHHHHH | 57.31 | 28112733 | |
303 | Ubiquitination | QDWVNRPKTVRDTLL CCCCCCCHHHHHHHH | 57.31 | 29967540 | |
308 | Phosphorylation | RPKTVRDTLLALHQH CCHHHHHHHHHHHHH | 17.07 | 22210691 | |
318 | Phosphorylation | ALHQHGHSGPFESKF HHHHHCCCCCCHHHC | 53.40 | 23401153 | |
323 | Phosphorylation | GHSGPFESKFKKEPA CCCCCCHHHCCCCCC | 43.71 | 23401153 | |
324 | Sumoylation | HSGPFESKFKKEPAL CCCCCHHHCCCCCCC | 54.74 | 28112733 | |
324 | Ubiquitination | HSGPFESKFKKEPAL CCCCCHHHCCCCCCC | 54.74 | 32015554 | |
326 | Sumoylation | GPFESKFKKEPALTA CCCHHHCCCCCCCCH | 61.02 | 28112733 | |
326 | Ubiquitination | GPFESKFKKEPALTA CCCHHHCCCCCCCCH | 61.02 | 29967540 | |
327 | Ubiquitination | PFESKFKKEPALTAG CCHHHCCCCCCCCHH | 72.55 | 29967540 | |
344 | Phosphorylation | LGFEANGANGSKAVA HCCCCCCCCCHHHHH | 19.61 | 32142685 | |
344 (in isoform 2) | Phosphorylation | - | 19.61 | 25849741 | |
347 | Phosphorylation | EANGANGSKAVARTA CCCCCCCHHHHHHHH | 19.76 | 26074081 | |
348 | Acetylation | ANGANGSKAVARTAR CCCCCCHHHHHHHHH | 48.56 | 25953088 | |
348 | Sumoylation | ANGANGSKAVARTAR CCCCCCHHHHHHHHH | 48.56 | 28112733 | |
348 | Ubiquitination | ANGANGSKAVARTAR CCCCCCHHHHHHHHH | 48.56 | 33845483 | |
353 | Phosphorylation | GSKAVARTARKRKPS CHHHHHHHHHHCCCC | 22.52 | 26074081 | |
360 | Phosphorylation | TARKRKPSPEPEGEV HHHHCCCCCCCCCCC | 44.95 | 29255136 | |
380 | Phosphorylation | NGEAQPWLSTSTEGL CCCCCCCCCCCCCCC | 5.21 | 32142685 | |
381 | O-linked_Glycosylation | GEAQPWLSTSTEGLK CCCCCCCCCCCCCCC | 19.22 | 30059200 | |
381 | Phosphorylation | GEAQPWLSTSTEGLK CCCCCCCCCCCCCCC | 19.22 | 28450419 | |
382 | O-linked_Glycosylation | EAQPWLSTSTEGLKI CCCCCCCCCCCCCCC | 37.18 | 30059200 | |
382 | Phosphorylation | EAQPWLSTSTEGLKI CCCCCCCCCCCCCCC | 37.18 | 28450419 | |
383 | O-linked_Glycosylation | AQPWLSTSTEGLKIP CCCCCCCCCCCCCCC | 22.53 | 30059200 | |
383 | Phosphorylation | AQPWLSTSTEGLKIP CCCCCCCCCCCCCCC | 22.53 | 21815630 | |
384 | Phosphorylation | QPWLSTSTEGLKIPM CCCCCCCCCCCCCCC | 33.87 | 28450419 | |
392 | O-linked_Glycosylation | EGLKIPMTPTSSFVS CCCCCCCCCCCCCCC | 20.33 | 30059200 | |
392 | Phosphorylation | EGLKIPMTPTSSFVS CCCCCCCCCCCCCCC | 20.33 | 23927012 | |
394 | Phosphorylation | LKIPMTPTSSFVSPP CCCCCCCCCCCCCCC | 28.03 | 23927012 | |
395 | O-linked_Glycosylation | KIPMTPTSSFVSPPP CCCCCCCCCCCCCCC | 24.00 | 30059200 | |
395 | Phosphorylation | KIPMTPTSSFVSPPP CCCCCCCCCCCCCCC | 24.00 | 23927012 | |
396 | Phosphorylation | IPMTPTSSFVSPPPP CCCCCCCCCCCCCCC | 31.95 | 30266825 | |
399 | Phosphorylation | TPTSSFVSPPPPTAS CCCCCCCCCCCCCCC | 29.67 | 30266825 | |
404 | Phosphorylation | FVSPPPPTASPHSNR CCCCCCCCCCCCCCC | 45.61 | 29255136 | |
406 | Phosphorylation | SPPPPTASPHSNRTT CCCCCCCCCCCCCCC | 26.14 | 29255136 | |
409 | Phosphorylation | PPTASPHSNRTTPPE CCCCCCCCCCCCCHH | 31.24 | 30266825 | |
412 | Phosphorylation | ASPHSNRTTPPEAAQ CCCCCCCCCCHHHHH | 48.15 | 30278072 | |
413 | Phosphorylation | SPHSNRTTPPEAAQN CCCCCCCCCHHHHHC | 33.34 | 30278072 | |
423 | Phosphorylation | EAAQNGQSPMAALIL HHHHCCCCCCEEEEE | 20.31 | 23401153 | |
438 | Phosphorylation | VADNAGGSHASKDAN EEECCCCCCCCCCHH | 18.24 | 23927012 | |
441 | Phosphorylation | NAGGSHASKDANQVH CCCCCCCCCCHHHHC | 26.16 | 20068231 | |
444 | Phosphorylation | GSHASKDANQVHSTT CCCCCCCHHHHCCCC | 16.46 | 32645325 | |
446 | Phosphorylation | HASKDANQVHSTTRR CCCCCHHHHCCCCCC | 35.70 | 33259812 | |
449 | Phosphorylation | KDANQVHSTTRRNSN CCHHHHCCCCCCCCC | 32.39 | 29514088 | |
450 | Phosphorylation | DANQVHSTTRRNSNS CHHHHCCCCCCCCCC | 14.94 | 29514088 | |
451 | Phosphorylation | ANQVHSTTRRNSNSP HHHHCCCCCCCCCCC | 30.55 | 29514088 | |
455 | Phosphorylation | HSTTRRNSNSPPSPS CCCCCCCCCCCCCCC | 36.55 | 29255136 | |
457 | Phosphorylation | TTRRNSNSPPSPSSM CCCCCCCCCCCCCHH | 37.70 | 29255136 | |
460 | Phosphorylation | RNSNSPPSPSSMNQR CCCCCCCCCCHHHCC | 40.58 | 29255136 | |
462 | Phosphorylation | SNSPPSPSSMNQRRL CCCCCCCCHHHCCCC | 46.70 | 29255136 | |
463 | Phosphorylation | NSPPSPSSMNQRRLG CCCCCCCHHHCCCCC | 25.74 | 29255136 | |
492 | Phosphorylation | LEPVHPASLPDSSLA CCCCCCCCCCCCHHC | 44.90 | 22817901 | |
496 | Phosphorylation | HPASLPDSSLATSAP CCCCCCCCHHCCCCC | 25.88 | 22210691 | |
497 | Phosphorylation | PASLPDSSLATSAPL CCCCCCCHHCCCCCE | 29.42 | 27080861 | |
500 | Phosphorylation | LPDSSLATSAPLCCT CCCCHHCCCCCEEHH | 30.62 | 27080861 | |
523 | Neddylation | THFVQCPSVPSHKFC CCCCCCCCCCCCCCE | 55.04 | 32015554 | |
523 | Ubiquitination | THFVQCPSVPSHKFC CCCCCCCCCCCCCCE | 55.04 | 32015554 | |
539 | Neddylation | PCSRQSIKQQGASGE ECCHHHHHHCCCCCE | 41.64 | 32015554 | |
539 | Ubiquitination | PCSRQSIKQQGASGE ECCHHHHHHCCCCCE | 41.64 | 32015554 | |
587 | Phosphorylation | KVKKERDS------- EEECCCCC------- | 48.63 | 26074081 |
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 I2BP2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
360 | S | Phosphorylation |
| 17081983 |
* 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 I2BP2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
IRF2_HUMAN | IRF2 | physical | 12799427 | |
NFAC2_HUMAN | NFATC2 | physical | 21576369 | |
VGLL4_HUMAN | VGLL4 | physical | 20702774 | |
IF4H_HUMAN | EIF4H | physical | 26344197 |
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. |
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Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-455; SER-457; SER-460 AND SER-462, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Identification of a phosphorylation-dependent nuclear localizationmotif in interferon regulatory factor 2 binding protein 2."; Teng A.C., Al-Montashiri N.A., Cheng B.L., Lou P., Ozmizrak P.,Chen H.H., Stewart A.F.; PLoS ONE 6:E24100-E24100(2011). Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND PHOSPHORYLATIONAT SER-360. | |
"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-360; THR-392 ANDSER-457, AND MASS SPECTROMETRY. | |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASSSPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-455; SER-457; SER-460 AND SER-462, AND MASSSPECTROMETRY. | |
"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-175; SER-360; SER-455;SER-457 AND SER-460, AND MASS SPECTROMETRY. |