PEBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PEBB_HUMAN
• UniProt AC: Q13951
• Protein Name: Core-binding factor subunit beta
• Gene Name: CBFB
• Organism: Homo sapiens (Human).
• Sequence Length: 182
• Subcellular Localization: Nucleus .
• Protein Description: Forms the heterodimeric complex core-binding factor (CBF) with RUNX family proteins (RUNX1, RUNX2, and RUNX3). RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation..
• Protein Sequence: MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVATGTNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLQRLDGMGCLEFDEERAQQEDALAQQAFEEARRRTREFEDRDRSHREEMEVRVSQLLAVTGKKTTRP

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
11	Ubiquitination	VVPDQRSKFENEEFF CCCCCHHHCCCHHHH	59.91	19608861
11	Acetylation	VVPDQRSKFENEEFF CCCCCHHHCCCHHHH	59.91	23749302
19	Methylation	FENEEFFRKLSRECE CCCHHHHHHHHHHCC	44.31	-
25	S-nitrosylation	FRKLSRECEIKYTGF HHHHHHHCCCEECCC	6.78	24105792
28	Ubiquitination	LSRECEIKYTGFRDR HHHHCCCEECCCCCC	17.92	22053931
28	Acetylation	LSRECEIKYTGFRDR HHHHCCCEECCCCCC	17.92	23749302
80 (in isoform 2)	Phosphorylation	-	25.97	24719451
80	Phosphorylation	WQGEQRQTPSREYVD CCCCCCCCCCCCCCH	25.97	30108239
82	Phosphorylation	GEQRQTPSREYVDLE CCCCCCCCCCCCHHH	40.92	28796482
85	Phosphorylation	RQTPSREYVDLEREA CCCCCCCCCHHHHHC	9.73	28796482
94	Ubiquitination	DLEREAGKVYLKAPM HHHHHCCCEEEECCE	34.45	-
96	Phosphorylation	EREAGKVYLKAPMIL HHHCCCEEEECCEEE	13.13	29496907
122	Sulfoxidation	DLQRLDGMGCLEFDE EHHHCCCCCCEECCH	3.23	21406390
150	Phosphorylation	FEEARRRTREFEDRD HHHHHHHHHHHHHHC	32.51	28555341
150 (in isoform 2)	Phosphorylation	-	32.51	-
159	Phosphorylation	EFEDRDRSHREEMEV HHHHHCCHHHHHHHH	31.05	28985074
159 (in isoform 2)	Phosphorylation	-	31.05	22210691
169	Phosphorylation	EEMEVRVSQLLAVTG HHHHHHHHHHHHHHC	12.44	23312004
169	O-linked_Glycosylation	EEMEVRVSQLLAVTG HHHHHHHHHHHHHHC	12.44	28510447
173 (in isoform 2)	Phosphorylation	-	12.86	23927012
175	Phosphorylation	VSQLLAVTGKKTTRP HHHHHHHHCCCCCCC	37.36	28555341
176 (in isoform 2)	Phosphorylation	-	23.90	23927012
177	Ubiquitination	QLLAVTGKKTTRP-- HHHHHHCCCCCCC--	37.27	-
177	Acetylation	QLLAVTGKKTTRP-- HHHHHHCCCCCCC--	37.27	23749302
178	Ubiquitination	LLAVTGKKTTRP--- HHHHHCCCCCCC---	57.37	-
185 (in isoform 2)	Ubiquitination	-		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PEBB_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 PEBB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SCG1_HUMAN	CHGB	physical	16169070
MYOD1_HUMAN	MYOD1	physical	20195544
RUNX1_HUMAN	RUNX1	physical	20195544
RAB2A_HUMAN	RAB2A	physical	20195357
VIF_HV1B1	vif	physical	24390320
VIF_HV1BR	vif	physical	24390320
VIF_HV1H2	vif	physical	24390320
CUL5_HUMAN	CUL5	physical	24402281
VIF_HV1B1	vif	physical	22479405
VIF_HV1BR	vif	physical	22479405
VIF_HV1H2	vif	physical	22479405
VIF_HV1B1	vif	physical	23333304
VIF_HV1BR	vif	physical	23333304
VIF_HV1H2	vif	physical	23333304
ELOC_HUMAN	TCEB1	physical	23333304
ELOB_HUMAN	TCEB2	physical	23333304
RUNX1_HUMAN	RUNX1	physical	23333304
RUNX2_HUMAN	RUNX2	physical	23333304
RUNX3_HUMAN	RUNX3	physical	23333304
CRIP1_HUMAN	CRIP1	physical	26344197
GALK1_HUMAN	GALK1	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
SODC_HUMAN	SOD1	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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND MASS SPECTROMETRY.
PubMed: 19608861