dbPTM

ZBT7B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZBT7B_HUMAN
UniProt AC	O15156
Protein Name	Zinc finger and BTB domain-containing protein 7B {ECO:0000305}
Gene Name	ZBTB7B {ECO:0000312\|HGNC:HGNC:18668}
Organism	Homo sapiens (Human).
Sequence Length	539
Subcellular Localization	Nucleus .
Protein Description	Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Exerts distinct biological functions in the mammary epithelial cells and T cells in a tissue-specific manner. Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitment. Development of immature T-cell precursors (thymocytes) to either the CD4 helper or CD8 killer T-cell lineages correlates precisely with their T-cell receptor specificity for major histocompatibility complex class II or class I molecules, respectively. Cross-antagonism between ZBTB7B and CBF complexes are determinative to CD4 versus CD8 cell fate decision. Suppresses RUNX3 expression and imposes CD4+ lineage fate by inducing the SOCS suppressors of cytokine signaling. induces, as a transcriptional activator, SOCS genes expression which represses RUNX3 expression and promotes the CD4+ lineage fate. During CD4 lineage commitment, associates with multiple sites at the CD8 locus, acting as a negative regulator of the CD8 promoter and enhancers by epigenetic silencing through the recruitment of class II histone deacetylases, such as HDAC4 and HDAC5, to these loci. Regulates the development of IL17-producing CD1d-restricted naural killer (NK) T cells. Also functions as an important metabolic regulator in the lactating mammary glands. Critical feed-forward regulator of insulin signaling in mammary gland lactation, directly regulates expression of insulin receptor substrate-1 (IRS-1) and insulin-induced Akt-mTOR-SREBP signaling (By similarity). Transcriptional repressor of the collagen COL1A1 and COL1A2 genes. May also function as a repressor of fibronectin and possibly other extracellular matrix genes. [PubMed: 9370309 Potent driver of brown fat development, thermogenesis and cold-induced beige fat formation. Recruits the brown fat lncRNA 1 (Blnc1):HNRNPU ribonucleoprotein complex to activate thermogenic gene expression in brown and beige adipocytes (By similarity]
Protein Sequence	MGSPEDDLIGIPFPDHSSELLSCLNEQRQLGHLCDLTIRTQGLEYRTHRAVLAACSHYFKKLFTEGGGGAVMGAGGSGTATGGAGAGVCELDFVGPEALGALLEFAYTATLTTSSANMPAVLQAARLLEIPCVIAACMEILQGSGLEAPSPDEDDCERARQYLEAFATATASGVPNGEDSPPQVPLPPPPPPPPRPVARRSRKPRKAFLQTKGARANHLVPEVPTVPAHPLTYEEEEVAGRVGSSGGSGPGDSYSPPTGTASPPEGPQSYEPYEGEEEEEELVYPPAYGLAQGGGPPLSPEELGSDEDAIDPDLMAYLSSLHQDNLAPGLDSQDKLVRKRRSQMPQECPVCHKIIHGAGKLPRHMRTHTGEKPFACEVCGVRFTRNDKLKIHMRKHTGERPYSCPHCPARFLHSYDLKNHMHLHTGDRPYECHLCHKAFAKEDHLQRHLKGQNCLEVRTRRRRKDDAPPHYPPPSTAAASPAGLDLSNGHLDTFRLSLARFWEQSAPTGPPVSTPGPPDDDEEEGAPTTPQAEGAMESS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MGSPEDDLIG -----CCCCHHHCCC	24.66	27499020
10 (in isoform 2)	Phosphorylation	-	28.90	28348404
10	Phosphorylation	SPEDDLIGIPFPDHS CCHHHCCCCCCCCCH	28.90	27251275
17	Phosphorylation	GIPFPDHSSELLSCL CCCCCCCHHHHHHHH	32.65	20068231
18	Phosphorylation	IPFPDHSSELLSCLN CCCCCCHHHHHHHHH	28.92	20068231
22	Phosphorylation	DHSSELLSCLNEQRQ CCHHHHHHHHHHHHH	29.23	20068231
144	Phosphorylation	CMEILQGSGLEAPSP HHHHHHCCCCCCCCC	27.52	20873877
150	Phosphorylation	GSGLEAPSPDEDDCE CCCCCCCCCCHHHHH	52.62	20873877
162	Phosphorylation	DCERARQYLEAFATA HHHHHHHHHHHHHHH	10.85	27080861
168	Phosphorylation	QYLEAFATATASGVP HHHHHHHHHHHCCCC	20.35	27080861
170	Phosphorylation	LEAFATATASGVPNG HHHHHHHHHCCCCCC	19.59	20068231
172	Phosphorylation	AFATATASGVPNGED HHHHHHHCCCCCCCC	35.65	20068231
180	Phosphorylation	GVPNGEDSPPQVPLP CCCCCCCCCCCCCCC	33.89	25849741
184	Phosphorylation	GEDSPPQVPLPPPPP CCCCCCCCCCCCCCC	6.92	27251275
206	Acetylation	RRSRKPRKAFLQTKG CCCCCCCHHHHHCCC	52.60	-
206	Methylation	RRSRKPRKAFLQTKG CCCCCCCHHHHHCCC	52.60	83136443
212	Acetylation	RKAFLQTKGARANHL CHHHHHCCCHHHCCC	37.30	-
212	Ubiquitination	RKAFLQTKGARANHL CHHHHHCCCHHHCCC	37.30	27667366
214	Phosphorylation	AFLQTKGARANHLVP HHHHCCCHHHCCCCC	14.68	33259812
246	Ubiquitination	AGRVGSSGGSGPGDS HCCCCCCCCCCCCCC	35.66	27667366
303	Ubiquitination	PPLSPEELGSDEDAI CCCCHHHHCCCCCCC	8.30	27667366
335	Acetylation	PGLDSQDKLVRKRRS CCCCHHHHHHHHHHH	41.04	-
342	Phosphorylation	KLVRKRRSQMPQECP HHHHHHHHCCCCCCH	34.56	28985074
360	Acetylation	KIIHGAGKLPRHMRT HHHCCCCCCCCHHCC	55.58	62154807
367	Phosphorylation	KLPRHMRTHTGEKPF CCCCHHCCCCCCCCE	19.06	23927012
369	Phosphorylation	PRHMRTHTGEKPFAC CCHHCCCCCCCCEEE	46.56	23927012
397	Phosphorylation	KIHMRKHTGERPYSC EEEEECCCCCCCCCC	43.71	29214152
403	Phosphorylation	HTGERPYSCPHCPAR CCCCCCCCCCCCCHH	24.69	29449344
414	Phosphorylation	CPARFLHSYDLKNHM CCHHHCCCCCCCCCC	23.61	28674419
425	Phosphorylation	KNHMHLHTGDRPYEC CCCCEEECCCCCCCC	47.33	24719451
431	Phosphorylation	HTGDRPYECHLCHKA ECCCCCCCCCCCCHH	20.38	27251275
448	Phosphorylation	KEDHLQRHLKGQNCL CHHHHHHHHCCCCCH	20.94	27251275
450	Acetylation	DHLQRHLKGQNCLEV HHHHHHHCCCCCHHH	52.94	20167786
450	Ubiquitination	DHLQRHLKGQNCLEV HHHHHHHCCCCCHHH	52.94	33845483
471	Phosphorylation	KDDAPPHYPPPSTAA CCCCCCCCCCCCCCC	24.17	23927012
475	Phosphorylation	PPHYPPPSTAAASPA CCCCCCCCCCCCCCC	36.13	23927012
476	Phosphorylation	PHYPPPSTAAASPAG CCCCCCCCCCCCCCC	26.53	23927012
480	Phosphorylation	PPSTAAASPAGLDLS CCCCCCCCCCCCCCC	15.57	25159151
484	Ubiquitination	AAASPAGLDLSNGHL CCCCCCCCCCCCCCH	6.95	33845483
487	Phosphorylation	SPAGLDLSNGHLDTF CCCCCCCCCCCHHHH	40.19	28450419
493	Phosphorylation	LSNGHLDTFRLSLAR CCCCCHHHHHHHHHH	19.60	28450419
505	Phosphorylation	LARFWEQSAPTGPPV HHHHHHHCCCCCCCC	25.38	20068231
508	Phosphorylation	FWEQSAPTGPPVSTP HHHHCCCCCCCCCCC	63.14	20068231
513	Phosphorylation	APTGPPVSTPGPPDD CCCCCCCCCCCCCCC	34.36	20068231
514	Phosphorylation	PTGPPVSTPGPPDDD CCCCCCCCCCCCCCC	32.28	28348404
521	Phosphorylation	TPGPPDDDEEEGAPT CCCCCCCCCCCCCCC	73.00	27251275
528	Phosphorylation	DEEEGAPTTPQAEGA CCCCCCCCCHHHCCH	51.04	20068231
529	Phosphorylation	EEEGAPTTPQAEGAM CCCCCCCCHHHCCHH	16.61	30576142
538	Phosphorylation	QAEGAMESS------ HHCCHHCCC------	28.41	28348404
539	Phosphorylation	AEGAMESS------- HCCHHCCC-------	30.82	28348404
562	Phosphorylation	------------------------------ ------------------------------		27251275
563	Phosphorylation	------------------------------- -------------------------------		27251275
573	Phosphorylation	----------------------------------------- -----------------------------------------		27251275

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
Oops, there are no upstream regulatory protein records of ZBT7B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
206	K	Acetylation	20810990
Competes with acetylation on Lys-206, Lys-212 and Lys-335 (By similarity).
206	K	Acetylation	20810990
EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity).
206	K	ubiquitylation	20810990
EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity).
212	K	Acetylation	20810990
Competes with acetylation on Lys-206, Lys-212 and Lys-335 (By similarity).
212	K	Acetylation	20810990
EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity).
212	K	ubiquitylation	20810990
EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity).
335	K	Acetylation	20810990
Competes with acetylation on Lys-206, Lys-212 and Lys-335 (By similarity).
335	K	Acetylation	20810990
EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity).
335	K	ubiquitylation	20810990
EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity).

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 ZBT7B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SP1_HUMAN	SP1	physical	17698844
SP3_HUMAN	SP3	physical	17698844
EP300_HUMAN	EP300	physical	20810990
PRP8_HUMAN	PRPF8	physical	20810990
MBB1A_HUMAN	MYBBP1A	physical	20810990
CEBPZ_HUMAN	CEBPZ	physical	20810990
HS105_HUMAN	HSPH1	physical	20810990
ZBT7B_HUMAN	ZBTB7B	physical	20810990
HDAC4_HUMAN	HDAC4	physical	22730529
HDAC5_HUMAN	HDAC5	physical	22730529
KAT5_HUMAN	KAT5	physical	23609452
IMP4_HUMAN	IMP4	physical	25416956
SYTL4_HUMAN	SYTL4	physical	25416956
IMP4_HUMAN	IMP4	physical	21516116

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 ZBT7B_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 THR-369, AND MASSSPECTROMETRY.	18669648 [Abstract]

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