| UniProt ID | GFI1B_HUMAN | |
|---|---|---|
| UniProt AC | Q5VTD9 | |
| Protein Name | Zinc finger protein Gfi-1b | |
| Gene Name | GFI1B | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 330 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. Transcriptional repressor or activator depending on both promoter and cell type context; represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down-regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription; as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma-satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation.. | |
| Protein Sequence | MPRSFLVKSKKAHTYHQPRVQEDEPLWPPALTPVPRDQAPSNSPVLSTLFPNQCLDWTNLKREPELEQDQNLARMAPAPEGPIVLSRPQDGDSPLSDSPPFYKPSFSWDTLATTYGHSYRQAPSTMQSAFLEHSVSLYGSPLVPSTEPALDFSLRYSPGMDAYHCVKCNKVFSTPHGLEVHVRRSHSGTRPFACDICGKTFGHAVSLEQHTHVHSQERSFECRMCGKAFKRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFSCELCTKGFQRKVDLRRHRESQHNLK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 8 | "N6,N6-dimethyllysine" | MPRSFLVKSKKAHTY CCCCEEEECCCCCCC | 59.72 | - | |
| 8 | Methylation | MPRSFLVKSKKAHTY CCCCEEEECCCCCCC | 59.72 | 22399799 | |
| 41 | Phosphorylation | VPRDQAPSNSPVLST CCCCCCCCCCCCHHH | 53.61 | 23401153 | |
| 43 | Phosphorylation | RDQAPSNSPVLSTLF CCCCCCCCCCHHHHC | 22.26 | 28165663 | |
| 47 | Phosphorylation | PSNSPVLSTLFPNQC CCCCCCHHHHCCCCC | 24.25 | 23898821 | |
| 48 | Phosphorylation | SNSPVLSTLFPNQCL CCCCCHHHHCCCCCC | 28.40 | 23898821 | |
| 156 | Phosphorylation | ALDFSLRYSPGMDAY CCCEECEECCCCCEE | 25.22 | 23186163 | |
| 157 | Phosphorylation | LDFSLRYSPGMDAYH CCEECEECCCCCEEE | 14.45 | 23401153 | |
| 187 | Phosphorylation | VHVRRSHSGTRPFAC EEEEECCCCCCCEEE | 43.01 | 23401153 | |
| 233 | Phosphorylation | GKAFKRSSTLSTHLL CCCHHCCCCCEEEEE | 37.08 | - | |
| 243 | Phosphorylation | STHLLIHSDTRPYPC EEEEEECCCCCCCCC | 33.41 | - | |
| 245 | Phosphorylation | HLLIHSDTRPYPCQF EEEECCCCCCCCCCC | 36.24 | - | |
| 261 | Phosphorylation | GKRFHQKSDMKKHTY CCCCCCCCCCCCCEE | 36.05 | 22817900 |
| 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 GFI1B_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 8 | K | Methylation |
| 22399799 |
* 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 GFI1B_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 187900 | Bleeding disorder, platelet-type 17 (BDPLT17) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY. | |
