dbPTM

SAT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAT1_HUMAN
UniProt AC	P21673
Protein Name	Diamine acetyltransferase 1
Gene Name	SAT1
Organism	Homo sapiens (Human).
Sequence Length	171
Subcellular Localization	Cytoplasm.
Protein Description	Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine..
Protein Sequence	MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVPKEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MAKFVIRPAT -----CCCEEECCCC	38.57	21890473
10	Phosphorylation	KFVIRPATAADCSDI CEEECCCCCCCHHHH	25.68	8954982
22	Ubiquitination	SDILRLIKELAKYEY HHHHHHHHHHHCHHH	51.79	-
26	Acetylation	RLIKELAKYEYMEEQ HHHHHHHCHHHHHHH	51.76	23954790
27	Phosphorylation	LIKELAKYEYMEEQV HHHHHHCHHHHHHHE	13.49	29978859
29	Phosphorylation	KELAKYEYMEEQVIL HHHHCHHHHHHHEEE	13.51	29978859
37	Phosphorylation	MEEQVILTEKDLLED HHHHEEEEHHHHHHC	29.84	29978859
77	Phosphorylation	SIVGFAMYYFTYDPW CCCEEEEEEECCCCC	7.62	-
78	Phosphorylation	IVGFAMYYFTYDPWI CCEEEEEEECCCCCH	4.03	-
87	Ubiquitination	TYDPWIGKLLYLEDF CCCCCHHHHHHHHCE	26.62	11485561
90	Phosphorylation	PWIGKLLYLEDFFVM CCHHHHHHHHCEEEC	20.62	-
111	Ubiquitination	GIGSEILKNLSQVAM CCCHHHHHCHHHHHH	62.60	21890473
146	Phosphorylation	FYKRRGASDLSSEEG CHHHCCCCCCCCHHC	41.74	8954982
149	Phosphorylation	RRGASDLSSEEGWRL HCCCCCCCCHHCCEE	40.47	8954982
158	Ubiquitination	EEGWRLFKIDKEYLL HHCCEEEEECHHHHH	55.37	21890473
161	Ubiquitination	WRLFKIDKEYLLKMA CEEEEECHHHHHHHH	52.29	21890473
163	Phosphorylation	LFKIDKEYLLKMATE EEEECHHHHHHHHCC	24.07	24505115
166	Ubiquitination	IDKEYLLKMATEE-- ECHHHHHHHHCCC--	24.72	21890473

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
10	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
10	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
146	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
146	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
146	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
149	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
149	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
149	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SAT1_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 SAT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPF45_HUMAN	RBM17	physical	16189514
SPB1_HUMAN	FTSJ3	physical	16189514
TCF25_HUMAN	TCF25	physical	16189514
T22D4_HUMAN	TSC22D4	physical	16189514
TACO1_HUMAN	TACO1	physical	16189514
DNPEP_HUMAN	DNPEP	physical	16189514
SAT2_HUMAN	SAT2	physical	16189514
LNX1_HUMAN	LNX1	physical	16189514
FA86C_HUMAN	FAM86C1	physical	16189514
SAT1_HUMAN	SAT1	physical	16189514
ABCB8_HUMAN	ABCB8	physical	16169070
EVA1A_HUMAN	EVA1A	physical	16169070
NRK2_HUMAN	NMRK2	physical	16169070
IN80C_HUMAN	INO80C	physical	16169070
SARAF_HUMAN	SARAF	physical	16169070
B4GT3_HUMAN	B4GALT3	physical	16169070
PLRKT_HUMAN	PLGRKT	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
DGKZ_HUMAN	DGKZ	physical	16169070
GBP2_HUMAN	GBP2	physical	16169070
GDF9_HUMAN	GDF9	physical	16169070
FUND2_HUMAN	FUNDC2	physical	16169070
LC7L2_HUMAN	LUC7L2	physical	16169070
CC90B_HUMAN	CCDC90B	physical	16169070
SPS1_HUMAN	SEPHS1	physical	16169070
APLP1_HUMAN	APLP1	physical	16169070
MED31_HUMAN	MED31	physical	16169070
CSN6_HUMAN	COPS6	physical	16169070
EPHB6_HUMAN	EPHB6	physical	16169070
KCNA4_HUMAN	KCNA4	physical	16169070
KAT7_HUMAN	KAT7	physical	16169070
PTN_HUMAN	PTN	physical	16169070
UT14A_HUMAN	UTP14A	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
TBB2A_HUMAN	TUBB2A	physical	16169070
ZHX1_HUMAN	ZHX1	physical	16169070
ERG28_HUMAN	C14orf1	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
RBM48_HUMAN	RBM48	physical	16169070
CH10_HUMAN	HSPE1	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
P53_HUMAN	TP53	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
RLA1_HUMAN	RPLP1	physical	16169070
TLE1_HUMAN	TLE1	physical	16169070
SAT1_HUMAN	SAT1	physical	25416956
SNAI2_HUMAN	SNAI2	physical	25416956
EIF3D_HUMAN	EIF3D	physical	25416956
MTA1_HUMAN	MTA1	physical	25416956
DX39A_HUMAN	DDX39A	physical	25416956
TCF25_HUMAN	TCF25	physical	25416956
FA156_HUMAN	FAM156A	physical	25416956
CCHCR_HUMAN	CCHCR1	physical	25416956
DMRT3_HUMAN	DMRT3	physical	25416956
LNX1_HUMAN	LNX1	physical	25416956
SPF45_HUMAN	RBM17	physical	25416956
CC148_HUMAN	CCDC148	physical	25416956
FA69B_HUMAN	FAM69B	physical	25416956
CS025_HUMAN	C19orf25	physical	25416956
SPF45_HUMAN	RBM17	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
308800	Keratosis follicularis spinulosa decalvans X-linked (KFSDX)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00127	Spermine

Regulatory Network of SAT1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-26, AND MASS SPECTROMETRY.	19608861 [Abstract]