dbPTM

ABT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ABT1_HUMAN
UniProt AC	Q9ULW3
Protein Name	Activator of basal transcription 1
Gene Name	ABT1
Organism	Homo sapiens (Human).
Sequence Length	272
Subcellular Localization	Nucleus. Nucleus, nucleolus.
Protein Description	Could be a novel TATA-binding protein (TBP) which can function as a basal transcription activator. Can act as a regulator of basal transcription for class II genes (By similarity)..
Protein Sequence	MEAEESEKAATEQEPLEGTEQTLDAEEEQEESEEAACGSKKRVVPGIVYLGHIPPRFRPLHVRNLLSAYGEVGRVFFQAEDRFVRRKKKAAAAAGGKKRSYTKDYTEGWVEFRDKRIAKRVAASLHNTPMGARRRSPFRYDLWNLKYLHRFTWSHLSEHLAFERQVRRQRLRAEVAQAKRETDFYLQSVERGQRFLAADGDPARPDGSWTFAQRPTEQELRARKAARPGGRERARLATAQDKARSNKGLLARIFGAPPPSESMEGPSLVRDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEAEESEK -------CCHHHHHH	11.26	19413330
11	Phosphorylation	EESEKAATEQEPLEG HHHHHHCCCCCCCCC	42.96	28634120
19	Phosphorylation	EQEPLEGTEQTLDAE CCCCCCCCCCCCCHH	18.62	28111955
22	Phosphorylation	PLEGTEQTLDAEEEQ CCCCCCCCCCHHHHH	22.00	30576142
32	Phosphorylation	AEEEQEESEEAACGS HHHHHHHHHHHHHCC	39.73	25159151
39	Phosphorylation	SEEAACGSKKRVVPG HHHHHHCCCCCEECC	34.58	28450419
40	Acetylation	EEAACGSKKRVVPGI HHHHHCCCCCEECCE	29.86	26051181
49	Phosphorylation	RVVPGIVYLGHIPPR CEECCEEEECCCCCC	12.68	50558879
67	Phosphorylation	LHVRNLLSAYGEVGR HHHHHHHHHHCCHHH	23.70	110760385
69	Phosphorylation	VRNLLSAYGEVGRVF HHHHHHHHCCHHHHE	15.50	23612710
82	Methylation	VFFQAEDRFVRRKKK HEEEHHHHHHHHHHH	24.38	-
87	Ubiquitination	EDRFVRRKKKAAAAA HHHHHHHHHHHHHHC	48.32	-
88	Ubiquitination	DRFVRRKKKAAAAAG HHHHHHHHHHHHHCC	45.92	-
88	Acetylation	DRFVRRKKKAAAAAG HHHHHHHHHHHHHCC	45.92	132703
89	Ubiquitination	RFVRRKKKAAAAAGG HHHHHHHHHHHHCCC	46.42	-
98	Acetylation	AAAAGGKKRSYTKDY HHHCCCCCCCCCCCC	50.26	7708571
100	Phosphorylation	AAGGKKRSYTKDYTE HCCCCCCCCCCCCCC	46.14	20860994
105	Phosphorylation	KRSYTKDYTEGWVEF CCCCCCCCCCCCEEC	14.30	113334077
106	Phosphorylation	RSYTKDYTEGWVEFR CCCCCCCCCCCEECC	37.85	113334083
128	Phosphorylation	VAASLHNTPMGARRR HHHHHHCCCCCCCCC	12.14	27067055
133	Methylation	HNTPMGARRRSPFRY HCCCCCCCCCCCCHH	28.90	-
136	Phosphorylation	PMGARRRSPFRYDLW CCCCCCCCCCHHHCC	26.95	46157319
146	Ubiquitination	RYDLWNLKYLHRFTW HHHCCCHHHHHHHCH	42.42	21890473
179	Ubiquitination	RAEVAQAKRETDFYL HHHHHHHHHHCCCHH	38.39	-
179	2-Hydroxyisobutyrylation	RAEVAQAKRETDFYL HHHHHHHHHHCCCHH	38.39	-
188	Phosphorylation	ETDFYLQSVERGQRF HCCCHHHHHHHCCCE	24.29	25159151
242	Ubiquitination	RLATAQDKARSNKGL HHHHHHHHHHCCCCH	33.35	-
260	Phosphorylation	IFGAPPPSESMEGPS HHCCCCCCHHCCCCC	48.34	46157325
262	Phosphorylation	GAPPPSESMEGPSLV CCCCCCHHCCCCCCC	26.86	46157331
267	Phosphorylation	SESMEGPSLVRDS-- CHHCCCCCCCCCC--	50.80	46157337
272	Phosphorylation	GPSLVRDS------- CCCCCCCC-------	31.40	30624053

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 ABT1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ABT1_HUMAN !!

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 ABT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDA7L_HUMAN	CDCA7L	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
SYNE4_HUMAN	SYNE4	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956

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 ABT1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]