dbPTM

SGF29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SGF29_HUMAN
UniProt AC	Q96ES7
Protein Name	SAGA-associated factor 29 {ECO:0000305}
Gene Name	SGF29 {ECO:0000312\|HGNC:HGNC:25156}
Organism	Homo sapiens (Human).
Sequence Length	293
Subcellular Localization	Nucleus .
Protein Description	Chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. [PubMed: 19103755]
Protein Sequence	MALVSADSRIAELLTELHQLIKQTQEERSRSEHNLVNIQKTHERMQTENKISPYYRTKLRGLYTTAKADAEAECNILRKALDKIAEIKSLLEERRIAAKIAGLYNDSEPPRKTMRRGVLMTLLQQSAMTLPLWIGKPGDKPPPLCGAIPASGDYVARPGDKVAARVKAVDGDEQWILAEVVSYSHATNKYEVDDIDEEGKERHTLSRRRVIPLPQWKANPETDPEALFQKEQLVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVACKEPKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALVSADSR ------CCCCCHHHH	19.37	-
5	Phosphorylation	---MALVSADSRIAE ---CCCCCHHHHHHH	27.49	25262027
8	Phosphorylation	MALVSADSRIAELLT CCCCCHHHHHHHHHH	25.88	25262027
15	Phosphorylation	SRIAELLTELHQLIK HHHHHHHHHHHHHHH	49.47	20068231
40	Ubiquitination	HNLVNIQKTHERMQT HHHHHHHHHHHHHHH	48.31	29967540
50	Ubiquitination	ERMQTENKISPYYRT HHHHHCCCCCHHHHH	38.03	29967540
52	Phosphorylation	MQTENKISPYYRTKL HHHCCCCCHHHHHHH	14.41	25159151
55	Phosphorylation	ENKISPYYRTKLRGL CCCCCHHHHHHHHHH	18.39	-
63	Phosphorylation	RTKLRGLYTTAKADA HHHHHHHHHHHHHHH	12.60	-
64	Phosphorylation	TKLRGLYTTAKADAE HHHHHHHHHHHHHHH	25.89	-
65	Phosphorylation	KLRGLYTTAKADAEA HHHHHHHHHHHHHHH	16.77	-
67	Ubiquitination	RGLYTTAKADAEAEC HHHHHHHHHHHHHHH	44.71	29967540
88	Ubiquitination	LDKIAEIKSLLEERR HHHHHHHHHHHHHHH	26.93	29967540
89	Phosphorylation	DKIAEIKSLLEERRI HHHHHHHHHHHHHHH	43.79	29514088
99	Acetylation	EERRIAAKIAGLYND HHHHHHHHHHCCCCC	24.86	23236377
99	Ubiquitination	EERRIAAKIAGLYND HHHHHHHHHHCCCCC	24.86	29967540
113	Phosphorylation	DSEPPRKTMRRGVLM CCCCCCHHHHHHHHH	19.72	-
206	Phosphorylation	GKERHTLSRRRVIPL CHHHHCCCCCCEECC	25.54	-
217	Ubiquitination	VIPLPQWKANPETDP EECCCHHCCCCCCCH	32.79	29967540
288	Acetylation	QRYVVACKEPKKK-- HHHHHCCCCCCCC--	68.28	19608861
293	Ubiquitination	ACKEPKKK------- CCCCCCCC-------	72.24	24816145

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 SGF29_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SGF29_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 SGF29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD158_HUMAN	CCDC158	physical	16189514
H3_YEAST	HHT1	physical	21685874
TADA3_HUMAN	TADA3	physical	22939629
CLHC1_HUMAN	CLHC1	physical	25416956
ZZZ3_HUMAN	ZZZ3	physical	20850016
NC2B_HUMAN	DR1	physical	20850016
YETS2_HUMAN	YEATS2	physical	20850016
TADA3_HUMAN	TADA3	physical	20850016
TAF5L_HUMAN	TAF5L	physical	20850016
KAT2A_HUMAN	KAT2A	physical	20850016
CSR2B_HUMAN	CSRP2BP	physical	20850016
MBIP1_HUMAN	MBIP	physical	20850016
TADA1_HUMAN	TADA1	physical	20850016
TAF10_HUMAN	TAF10	physical	20850016
UBP22_HUMAN	USP22	physical	20850016
ATX7_HUMAN	ATXN7	physical	20850016
ST65G_HUMAN	SUPT7L	physical	20850016
AT7L2_HUMAN	ATXN7L2	physical	20850016
SF3B3_HUMAN	SF3B3	physical	20850016
ENY2_HUMAN	ENY2	physical	20850016
TRRAP_HUMAN	TRRAP	physical	20850016
SP20H_HUMAN	SUPT20H	physical	20850016
AT7L3_HUMAN	ATXN7L3	physical	20850016
KAT2B_HUMAN	KAT2B	physical	20850016
TAF12_HUMAN	TAF12	physical	20850016
SF3B5_HUMAN	SF3B5	physical	20850016
WDR5_HUMAN	WDR5	physical	20850016
TAD2B_HUMAN	TADA2B	physical	20850016
ACTG_HUMAN	ACTG1	physical	20850016
ASPP2_HUMAN	TP53BP2	physical	26186194
YETS2_HUMAN	YEATS2	physical	26186194
TAD2B_HUMAN	TADA2B	physical	26186194
ZZZ3_HUMAN	ZZZ3	physical	26186194
DTNA_HUMAN	DTNA	physical	26186194
DTNB_HUMAN	DTNB	physical	26186194
CA122_HUMAN	C1orf122	physical	26186194
HTF4_HUMAN	TCF12	physical	26186194
ITF2_HUMAN	TCF4	physical	26186194
EDC4_HUMAN	EDC4	physical	26186194
RBG10_HUMAN	RABGAP1L	physical	26186194
RBG1L_HUMAN	RABGAP1L	physical	26186194
CP250_HUMAN	CEP250	physical	26186194
CSR2B_HUMAN	CSRP2BP	physical	26186194
TAF9B_HUMAN	TAF9B	physical	26186194
KIF2C_HUMAN	KIF2C	physical	26186194
SH3G1_HUMAN	SH3GL1	physical	26186194
TADA3_HUMAN	TADA3	physical	26186194
TAF12_HUMAN	TAF12	physical	26186194
MPRIP_HUMAN	MPRIP	physical	26186194
KAT2B_HUMAN	KAT2B	physical	26186194
KAT2A_HUMAN	KAT2A	physical	26186194
FP100_HUMAN	C17orf70	physical	26186194
KINH_HUMAN	KIF5B	physical	26186194
REPS1_HUMAN	REPS1	physical	26186194
BANP_HUMAN	BANP	physical	26186194
TAF5L_HUMAN	TAF5L	physical	26186194
WDR5_HUMAN	WDR5	physical	26186194
RFIP5_HUMAN	RAB11FIP5	physical	26186194
SUPT3_HUMAN	SUPT3H	physical	26186194
SKAP_HUMAN	KNSTRN	physical	26186194
FYCO1_HUMAN	FYCO1	physical	26186194
TAD2A_HUMAN	TADA2A	physical	26186194
WDR37_HUMAN	WDR37	physical	26186194
MBIP1_HUMAN	MBIP	physical	26186194
TADA1_HUMAN	TADA1	physical	26186194
SP20H_HUMAN	SUPT20H	physical	26186194
TFPT_HUMAN	TFPT	physical	26186194
ST65G_HUMAN	SUPT7L	physical	26186194
K1C15_HUMAN	KRT15	physical	21516116
KAT2A_HUMAN	KAT2A	physical	26496610
TAD2A_HUMAN	TADA2A	physical	26496610
TRRAP_HUMAN	TRRAP	physical	26496610
SUPT3_HUMAN	SUPT3H	physical	26496610
ST65G_HUMAN	SUPT7L	physical	26496610
TADA3_HUMAN	TADA3	physical	26496610
TAF6L_HUMAN	TAF6L	physical	26496610
EDC4_HUMAN	EDC4	physical	26496610
ZZZ3_HUMAN	ZZZ3	physical	26496610
TAF5L_HUMAN	TAF5L	physical	26496610
MBIP1_HUMAN	MBIP	physical	26496610
SP20H_HUMAN	SUPT20H	physical	26496610
YETS2_HUMAN	YEATS2	physical	26496610
CCD82_HUMAN	CCDC82	physical	26496610
TAD2B_HUMAN	TADA2B	physical	26496610
TADA1_HUMAN	TADA1	physical	26496610
TADA3_HUMAN	TADA3	physical	28514442
TAD2B_HUMAN	TADA2B	physical	28514442
MBIP1_HUMAN	MBIP	physical	28514442
RBG10_HUMAN	RABGAP1L	physical	28514442
RBG1L_HUMAN	RABGAP1L	physical	28514442
RFIP5_HUMAN	RAB11FIP5	physical	28514442
TAD2A_HUMAN	TADA2A	physical	28514442
KAT2B_HUMAN	KAT2B	physical	28514442
KIF2C_HUMAN	KIF2C	physical	28514442
EDC4_HUMAN	EDC4	physical	28514442
TADA1_HUMAN	TADA1	physical	28514442
TFPT_HUMAN	TFPT	physical	28514442
KAT2A_HUMAN	KAT2A	physical	28514442
FP100_HUMAN	C17orf70	physical	28514442
HTF4_HUMAN	TCF12	physical	28514442
YETS2_HUMAN	YEATS2	physical	28514442
ST65G_HUMAN	SUPT7L	physical	28514442
TAF5L_HUMAN	TAF5L	physical	28514442
ASPP2_HUMAN	TP53BP2	physical	28514442
SP20H_HUMAN	SUPT20H	physical	28514442
SKAP_HUMAN	KNSTRN	physical	28514442
CA122_HUMAN	C1orf122	physical	28514442
FYCO1_HUMAN	FYCO1	physical	28514442
ZZZ3_HUMAN	ZZZ3	physical	28514442
DTNB_HUMAN	DTNB	physical	28514442
REPS1_HUMAN	REPS1	physical	28514442
CSR2B_HUMAN	CSRP2BP	physical	28514442
TAF12_HUMAN	TAF12	physical	28514442
DTNA_HUMAN	DTNA	physical	28514442
WDR37_HUMAN	WDR37	physical	28514442
TAF9B_HUMAN	TAF9B	physical	28514442
BANP_HUMAN	BANP	physical	28514442
WDR5_HUMAN	WDR5	physical	28514442
MPRIP_HUMAN	MPRIP	physical	28514442
SUPT3_HUMAN	SUPT3H	physical	28514442
TAF6L_HUMAN	TAF6L	physical	28514442
CP250_HUMAN	CEP250	physical	28514442
SH3G1_HUMAN	SH3GL1	physical	28514442
TPM3_HUMAN	TPM3	physical	28514442
KINH_HUMAN	KIF5B	physical	28514442

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 SGF29_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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-288, AND MASS SPECTROMETRY.	19608861 [Abstract]