TAF5L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TAF5L_HUMAN
• UniProt AC: O75529
• Protein Name: TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L
• Gene Name: TAF5L
• Organism: Homo sapiens (Human).
• Sequence Length: 589
• Subcellular Localization: Nucleus .
• Protein Description: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex..
• Protein Sequence: MKRVRTEQIQMAVSCYLKRRQYVDSDGPLKQGLRLSQTAEEMAANLTVQSESGCANIVSAAPCQAEPQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLQNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQPAKRTDYQLYASGSSSRSENNGLEPPDMPSPILQNEAALEVLQESIKRVKDGPPSLTTICFYAFYNTEQLLNTAEISPDSKLLAAGFDNSCIKLWSLRSKKLKSEPHQVDVSRIHLACDILEEEDDEDDNAGTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNTYCSAPADGSSSELVGVYTGQMSNVLSVQFMACNLLLVTGITQENQEH

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
6	Phosphorylation	--MKRVRTEQIQMAV --CCCCCHHHHHHHH	29.41	29083192
18	Acetylation	MAVSCYLKRRQYVDS HHHHHHHHCCCCCCC	21.04	26051181
25	Phosphorylation	KRRQYVDSDGPLKQG HCCCCCCCCCCHHHC	34.13	-
30	Ubiquitination	VDSDGPLKQGLRLSQ CCCCCCHHHCCCHHH	45.51	-
102	Phosphorylation	LLYPLFVYLHLNLVQ HHHHHHHHHHHHHHC	4.89	32142685
111	Phosphorylation	HLNLVQNSPKSTVES HHHHHCCCCCHHHHH	19.33	32142685
230	Phosphorylation	LEPPDMPSPILQNEA CCCCCCCCHHHCCHH	20.24	28102081
245	Phosphorylation	ALEVLQESIKRVKDG HHHHHHHHHHHHCCC	22.05	28102081
247	Ubiquitination	EVLQESIKRVKDGPP HHHHHHHHHHCCCCC	61.49	-
296	Phosphorylation	NSCIKLWSLRSKKLK CHHHHHHHHCCCCCC	25.09	24719451
303	Ubiquitination	SLRSKKLKSEPHQVD HHCCCCCCCCCCCCC	62.75	29967540
389	Ubiquitination	GHAYPVWDLDISPYS CCCCCEECCCCCCCE	34.40	23000965
410	Ubiquitination	SHDRTARLWSFDRTY CCCCCEEEEEECCCC	4.10	23000965
422	Phosphorylation	RTYPLRIYAGHLADV CCCCEEEECCCCCCC	10.49	-
433	Acetylation	LADVDCVKFHPNSNY CCCCEEEECCCCCCC	44.26	26051181
443	Phosphorylation	PNSNYLATGSTDKTV CCCCCCCCCCCCCCE	29.12	-
448	Acetylation	LATGSTDKTVRLWSA CCCCCCCCCEEEEEC	49.35	12431213
449	Phosphorylation	ATGSTDKTVRLWSAQ CCCCCCCCEEEEECC	17.42	-
454	Phosphorylation	DKTVRLWSAQQGNSV CCCEEEEECCCCCEE	22.31	-
460	Phosphorylation	WSAQQGNSVRLFTGH EECCCCCEEEEEECC	18.55	-
477	Phosphorylation	PVLSLAFSPNGKYLA CEEEEEECCCCCEEE	16.31	-
481	Ubiquitination	LAFSPNGKYLASAGE EEECCCCCEEECCCC	43.67	23000965
481 (in isoform 1)	Ubiquitination	-	43.67	21890473
482	Phosphorylation	AFSPNGKYLASAGED EECCCCCEEECCCCC	14.65	27642862
504	Ubiquitination	LASGTLYKELRGHTD HCCCCHHHHHCCCCC	54.08	-

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

Oops, there are no upstream regulatory protein records of TAF5L_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TAF5L_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 TAF5L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBB8_HUMAN	TUBB8	physical	26186194
TAD2B_HUMAN	TADA2B	physical	26186194
TAF9B_HUMAN	TAF9B	physical	26186194
SUPT3_HUMAN	SUPT3H	physical	26186194
TAD2B_HUMAN	TADA2B	physical	28514442
TAF6L_HUMAN	TAF6L	physical	28514442
TAF9B_HUMAN	TAF9B	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
TBB8_HUMAN	TUBB8	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.