GFI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GFI1_HUMAN
• UniProt AC: Q99684
• Protein Name: Zinc finger protein Gfi-1
• Gene Name: GFI1
• Organism: Homo sapiens (Human).
• Sequence Length: 422
• Subcellular Localization: Nucleus . Colocalizes with PIAS3 and RUNX1T1 in nuclear dots.
• Protein Description: Transcription repressor essential for hematopoiesis. Functions in a cell-context and development-specific manner. Binds to 5'-TAAATCAC[AT]GCA-3' in the promoter region of a large number of genes. Component of several complexes, including the EHMT2-GFI1-HDAC1, AJUBA-GFI1-HDAC1 and RCOR-GFI-KDM1A-HDAC complexes, that suppress, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Regulates neutrophil differentiation, promotes proliferation of lymphoid cells, and is required for granulocyte development. Mediates, together with U2AF1L4, the alternative splicing of CD45 and controls T-cell receptor signaling. Regulates the endotoxin-mediated Toll-like receptor (TLR) inflammatory response by antagonizing RELA. Cooperates with CBFA2T2 to regulate ITGB1-dependent neurite growth. Controls cell-cycle progression by repressing CDKNIA/p21 transcription in response to TGFB1 via recruitment of GFI1 by ZBTB17 to the CDKNIA/p21 and CDKNIB promoters. Required for the maintenance of inner ear hair cells..
• Protein Sequence: MPRSFLVKSKKAHSYHQPRSPGPDYSLRLENVPAPSRADSTSNAGGAKAEPRDRLSPESQLTEAPDRASASPDSCEGSVCERSSEFEDFWRPPSPSASPASEKSMCPSLDEAQPFPLPFKPYSWSGLAGSDLRHLVQSYRPCGALERGAGLGLFCEPAPEPGHPAALYGPKRAAGGAGAGAPGSCSAGAGATAGPGLGLYGDFGSAAAGLYERPTAAAGLLYPERGHGLHADKGAGVKVESELLCTRLLLGGGSYKCIKCSKVFSTPHGLEVHVRRSHSGTRPFACEMCGKTFGHAVSLEQHKAVHSQERSFDCKICGKSFKRSSTLSTHLLIHSDTRPYPCQYCGKRFHQKSDMKKHTFIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFGCDLCGKGFQRKVDLRRHRETQHGLK

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
4	Phosphorylation	----MPRSFLVKSKK ----CCCCEEECCCC	19.64	30576142
8	Methylation	MPRSFLVKSKKAHSY CCCCEEECCCCCCCC	59.72	-
14	Phosphorylation	VKSKKAHSYHQPRSP ECCCCCCCCCCCCCC	29.21	30576142
15	Phosphorylation	KSKKAHSYHQPRSPG CCCCCCCCCCCCCCC	8.46	-
20	Phosphorylation	HSYHQPRSPGPDYSL CCCCCCCCCCCCCEE	40.67	23401153
25	Phosphorylation	PRSPGPDYSLRLENV CCCCCCCCEEEEECC	16.85	28111955
26	Phosphorylation	RSPGPDYSLRLENVP CCCCCCCEEEEECCC	17.88	24719451
40	Phosphorylation	PAPSRADSTSNAGGA CCCCCCCCCCCCCCC	32.52	22210691
41	Phosphorylation	APSRADSTSNAGGAK CCCCCCCCCCCCCCC	26.92	22210691
42	Phosphorylation	PSRADSTSNAGGAKA CCCCCCCCCCCCCCC	28.74	-
56	Phosphorylation	AEPRDRLSPESQLTE CCCCCCCCHHHHHCC	27.75	23401153
59	Phosphorylation	RDRLSPESQLTEAPD CCCCCHHHHHCCCCC	33.60	30266825
62	Phosphorylation	LSPESQLTEAPDRAS CCHHHHHCCCCCHHC	23.59	28450419
69	Phosphorylation	TEAPDRASASPDSCE CCCCCHHCCCCCCCC	30.12	22468782
71	Phosphorylation	APDRASASPDSCEGS CCCHHCCCCCCCCCC	27.09	23401153
74	Phosphorylation	RASASPDSCEGSVCE HHCCCCCCCCCCCCC	19.90	28450419
78	Phosphorylation	SPDSCEGSVCERSSE CCCCCCCCCCCCCCC	10.99	22468782
83	Phosphorylation	EGSVCERSSEFEDFW CCCCCCCCCCCCCCC	16.36	27080861
84	Phosphorylation	GSVCERSSEFEDFWR CCCCCCCCCCCCCCC	53.15	27080861
94	Phosphorylation	EDFWRPPSPSASPAS CCCCCCCCCCCCCCC	33.88	23401153
96	Phosphorylation	FWRPPSPSASPASEK CCCCCCCCCCCCCCC	45.79	23401153
98	Phosphorylation	RPPSPSASPASEKSM CCCCCCCCCCCCCCC	25.90	23401153
101	Phosphorylation	SPSASPASEKSMCPS CCCCCCCCCCCCCCC	49.28	28450419
104	Phosphorylation	ASPASEKSMCPSLDE CCCCCCCCCCCCCCC	22.89	26074081
108	Phosphorylation	SEKSMCPSLDEAQPF CCCCCCCCCCCCCCC	43.45	26074081
171	Ubiquitination	PAALYGPKRAAGGAG CHHHHCCCCCCCCCC	50.75	-
205	Phosphorylation	GLYGDFGSAAAGLYE CCCCCCCHHHCCCCC	18.09	22210691
211	Phosphorylation	GSAAAGLYERPTAAA CHHHCCCCCCCCCCC	14.69	22210691
233	Ubiquitination	GHGLHADKGAGVKVE CCCCCCCCCCCCCCC	51.98	29967540
261	Phosphorylation	SYKCIKCSKVFSTPH CEEEEEECEEEECCC	27.18	-
303	Ubiquitination	AVSLEQHKAVHSQER EECHHHHHHHHHCCC	52.37	29967540
315	Ubiquitination	QERSFDCKICGKSFK CCCCCCCCCCCCCCC	42.76	-
335	Phosphorylation	STHLLIHSDTRPYPC CEEEEECCCCCCCCC	33.41	-
353	Phosphorylation	GKRFHQKSDMKKHTF CCCCCCCCCCCCCEE	36.05	17081983
363	Phosphorylation	KKHTFIHTGEKPHKC CCCEEEECCCCCCCC	42.07	-
366	Ubiquitination	TFIHTGEKPHKCQVC EEEECCCCCCCCCCC	54.49	29967540
391	Phosphorylation	ITHSRKHTGFKPFGC HHCCCCCCCCCCCCC	47.55	-

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
94	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
98	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	ARIH2	O95376	PMID:17646546

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GFI1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GFI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PIAS3_HUMAN	PIAS3	physical	11060035
ARI2_HUMAN	ARIH2	physical	17646546
EHMT2_HUMAN	EHMT2	physical	16287849
HDAC1_HUMAN	HDAC1	physical	16287849
PRDM5_HUMAN	PRDM5	physical	17636019
RCOR1_HUMAN	RCOR1	physical	17707228
KDM1A_HUMAN	KDM1A	physical	17707228
HDAC2_HUMAN	HDAC2	physical	17707228
PICK1_HUMAN	PICK1	physical	16713569
CAF1A_HUMAN	CHAF1A	physical	21570500
SPI1_HUMAN	SPI1	physical	17197705
TF65_HUMAN	RELA	physical	20547752
ZBT17_HUMAN	ZBTB17	physical	19164764

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 613107: Neutropenia, severe congenital 2, autosomal dominant (SCN2)
• 607847: Dominant nonimmune chronic idiopathic neutropenia of adults (NI-CINA)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-56, AND MASSSPECTROMETRY.
PubMed: 19369195