TAL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TAL1_HUMAN
• UniProt AC: P17542
• Protein Name: T-cell acute lymphocytic leukemia protein 1
• Gene Name: TAL1
• Organism: Homo sapiens (Human).
• Sequence Length: 331
• Subcellular Localization: Nucleus .
• Protein Description: Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation (By similarity)..
• Protein Sequence: MTERPPSEAARSDPQLEGRDAAEASMAPPHLVLLNGVAKETSRAAAAEPPVIELGARGGPGGGPAGGGGAARDLKGRDAATAEARHRVPTTELCRPPGPAPAPAPASVTAELPGDGRMVQLSPPALAAPAAPGRALLYSLSQPLASLGSGFFGEPDAFPMFTTNNRVKRRPSPYEMEITDGPHTKVVRRIFTNSRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYINFLAKLLNDQEEEGTQRAKTGKDPVVGAGGGGGGGGGGAPPDDLLQDVLSPNSSCGSSLDGAASPDSYTEEPAPKHTARSLHPAMLPAADGAGPR

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
7	Phosphorylation	-MTERPPSEAARSDP -CCCCCHHHHHHCCC	42.42	23186163
12	Phosphorylation	PPSEAARSDPQLEGR CHHHHHHCCCCCCCH	49.25	23186163
62	Acetylation	GARGGPGGGPAGGGG CCCCCCCCCCCCCCH	41.88	11118214
63	Acetylation	ARGGPGGGPAGGGGA CCCCCCCCCCCCCHH	18.14	11118214
90	Phosphorylation	EARHRVPTTELCRPP HHHHCCCCCCCCCCC	30.00	19406989
91	Phosphorylation	ARHRVPTTELCRPPG HHHCCCCCCCCCCCC	22.38	-
107	Phosphorylation	APAPAPASVTAELPG CCCCCCCEEEEECCC	20.95	-
122	Phosphorylation	DGRMVQLSPPALAAP CCCEEECCCHHHHCC	16.25	23401153
138	Phosphorylation	APGRALLYSLSQPLA CCCHHHHHHCHHHHH	14.39	-
139	Phosphorylation	PGRALLYSLSQPLAS CCHHHHHHCHHHHHH	22.86	-
141	Phosphorylation	RALLYSLSQPLASLG HHHHHHCHHHHHHCC	24.66	-
146	Phosphorylation	SLSQPLASLGSGFFG HCHHHHHHCCCCCCC	40.73	-
149	Phosphorylation	QPLASLGSGFFGEPD HHHHHCCCCCCCCCC	37.41	-
172	Phosphorylation	NRVKRRPSPYEMEIT CCCCCCCCCCEEEEC	38.00	23401153
174	Phosphorylation	VKRRPSPYEMEITDG CCCCCCCCEEEECCC	32.04	23403867
179	Phosphorylation	SPYEMEITDGPHTKV CCCEEEECCCCCHHH	22.92	29083192
184	Phosphorylation	EITDGPHTKVVRRIF EECCCCCHHHHHHHH	28.77	29083192
212	Acetylation	GAFAELRKLIPTHPP HHHHHHHHHCCCCCC	64.49	30582467
216	Phosphorylation	ELRKLIPTHPPDKKL HHHHHCCCCCCCCCC	39.77	-
221	Acetylation	IPTHPPDKKLSKNEI CCCCCCCCCCCHHHH	62.48	11118214
222	Ubiquitination	PTHPPDKKLSKNEIL CCCCCCCCCCHHHHH	66.43	11118214
222	Acetylation	PTHPPDKKLSKNEIL CCCCCCCCCCHHHHH	66.43	20167786
224	Phosphorylation	HPPDKKLSKNEILRL CCCCCCCCHHHHHHH	42.17	23403867
225	Ubiquitination	PPDKKLSKNEILRLA CCCCCCCHHHHHHHH	69.87	-
225	Acetylation	PPDKKLSKNEILRLA CCCCCCCHHHHHHHH	69.87	20167786
234	Acetylation	EILRLAMKYINFLAK HHHHHHHHHHHHHHH	37.05	25953088
241	Ubiquitination	KYINFLAKLLNDQEE HHHHHHHHHHCCCHH	56.50	-
251	Phosphorylation	NDQEEEGTQRAKTGK CCCHHHHCHHHHCCC	20.40	30622161
256	Phosphorylation	EGTQRAKTGKDPVVG HHCHHHHCCCCCCCC	48.78	30622161
300	Phosphorylation	SSLDGAASPDSYTEE CCCCCCCCCCCCCCC	28.80	26074081
303	Phosphorylation	DGAASPDSYTEEPAP CCCCCCCCCCCCCCC	37.02	26074081
304	Phosphorylation	GAASPDSYTEEPAPK CCCCCCCCCCCCCCC	26.08	26074081
305	Phosphorylation	AASPDSYTEEPAPKH CCCCCCCCCCCCCCC	37.51	26074081
313	Phosphorylation	EEPAPKHTARSLHPA CCCCCCCCHHHCCHH	29.86	26074081
316	Phosphorylation	APKHTARSLHPAMLP CCCCCHHHCCHHHHC	28.68	26074081

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
90	T	Phosphorylation	Kinase	AKT1	P31749	PSP
90	T	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
122	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
122	S	Phosphorylation	Kinase	MAP2K1	Q02750	GPS
172	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
172	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
172	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:17962192
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:17962192

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
122	S	Phosphorylation	Phosphorylation of Ser-122 is strongly stimulated by hypoxia (By similarity).	19690332
122	S	Phosphorylation	Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system.	19690332
122	S	ubiquitylation	Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system.	19690332

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TAL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBTN2_HUMAN	LMO2	physical	7957052
CNDG2_HUMAN	NCAPG2	physical	14729962
EP300_HUMAN	EP300	physical	10490830
ITF2_HUMAN	TCF4	physical	8576241
TFE2_HUMAN	TCF3	physical	16407974
HTF4_HUMAN	TCF12	physical	16407974
ITF2_HUMAN	TCF4	physical	16407974
RBTN2_HUMAN	LMO2	physical	16407974
GATA1_HUMAN	GATA1	physical	16407974
SSBP_HUMAN	SSBP1	physical	16407974
SSBP2_HUMAN	SSBP2	physical	16407974
SSBP3_HUMAN	SSBP3	physical	16407974
MTG16_HUMAN	CBFA2T3	physical	16407974
MTG8R_HUMAN	CBFA2T2	physical	16407974
HDAC1_HUMAN	HDAC1	physical	16407974
HDAC2_HUMAN	HDAC2	physical	16407974
TRRAP_HUMAN	TRRAP	physical	16407974
BRD1_HUMAN	BRD1	physical	16407974
RCC1_HUMAN	RCC1	physical	16407974
XRCC6_HUMAN	XRCC6	physical	16407974
TOP1_HUMAN	TOP1	physical	16407974
PARP1_HUMAN	PARP1	physical	16407974
LDB1_HUMAN	LDB1	physical	16407974
RBTN2_HUMAN	LMO2	physical	7568177
GATA1_HUMAN	GATA1	physical	7568177
GATA2_HUMAN	GATA2	physical	7568177
SIN3A_HUMAN	SIN3A	physical	10688671
RBTN1_HUMAN	LMO1	physical	7957052
TFE2_HUMAN	TCF3	physical	8159721
CHIP_HUMAN	STUB1	physical	17962192
SUV91_HUMAN	SUV39H1	physical	15677454
SATB1_HUMAN	SATB1	physical	15677454
TRI33_HUMAN	TRIM33	physical	20603019
TAL1_HUMAN	TAL1	physical	20603019
SP16H_HUMAN	SUPT16H	physical	20603019
CDK9_HUMAN	CDK9	physical	20603019
KDM1A_HUMAN	KDM1A	physical	19497860
HTF4_HUMAN	TCF12	physical	19497860
TFE2_HUMAN	TCF3	physical	19497860
MTG16_HUMAN	CBFA2T3	physical	19497860
HDAC1_HUMAN	HDAC1	physical	19497860
HDAC2_HUMAN	HDAC2	physical	19497860
RCOR1_HUMAN	RCOR1	physical	19497860
LDB1_HUMAN	LDB1	physical	19497860
SSBP3_HUMAN	SSBP3	physical	19497860
SSBP2_HUMAN	SSBP2	physical	19497860
RBBP7_HUMAN	RBBP7	physical	19497860
CHD4_HUMAN	CHD4	physical	19497860
CHD3_HUMAN	CHD3	physical	19497860
RB_HUMAN	RB1	physical	19497860
RUNX1_HUMAN	RUNX1	physical	19497860
LYL1_HUMAN	LYL1	physical	19497860
RB_HUMAN	RB1	physical	10866689
CHIP_HUMAN	STUB1	physical	19406989
ZHX1_HUMAN	ZHX1	physical	15383276
DRG1_HUMAN	DRG1	physical	9824680
KAT2B_HUMAN	KAT2B	physical	11118214
ESPB1_HUMAN	ELSPBP1	physical	11118214
EP300_HUMAN	EP300	physical	11118214
SIN3A_HUMAN	SIN3A	physical	11118214
EP300_HUMAN	EP300	physical	11756538

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.