FKBPL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FKBPL_HUMAN
• UniProt AC: Q9UIM3
• Protein Name: FK506-binding protein-like
• Gene Name: FKBPL
• Organism: Homo sapiens (Human).
• Sequence Length: 349
• Protein Description: May be involved in response to X-ray. Regulates p21 protein stability by binding to Hsp90 and p21..
• Protein Sequence: METPPVNTIGEKDTSQPQQEWEKNLRENLDSVIQIRQQPRDPPTETLELEVSPDPASQILEHTQGAEKLVAELEGDSHKSHGSTSQMPEALQASDLWYCPDGSFVKKIVIRGHGLDKPKLGSCCRVLALGFPFGSGPPEGWTELTMGVGPWREETWGELIEKCLESMCQGEEAELQLPGHSGPPVRLTLASFTQGRDSWELETSEKEALAREERARGTELFRAGNPEGAARCYGRALRLLLTLPPPGPPERTVLHANLAACQLLLGQPQLAAQSCDRVLEREPGHLKALYRRGVAQAALGNLEKATADLKKVLAIDPKNRAAQEELGKVVIQGKNQDAGLAQGLRKMFG

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
3	Phosphorylation	-----METPPVNTIG -----CCCCCCCCCC	31.43	23401153
23	Ubiquitination	QPQQEWEKNLRENLD CHHHHHHHHHHHHHH	63.46	-
31	Phosphorylation	NLRENLDSVIQIRQQ HHHHHHHHHHHHHCC	25.04	28555341
80	Phosphorylation	LEGDSHKSHGSTSQM HHCCCCCCCCCHHHC	27.88	25693802
83	Phosphorylation	DSHKSHGSTSQMPEA CCCCCCCCHHHCCHH	21.33	25693802
84	Phosphorylation	SHKSHGSTSQMPEAL CCCCCCCHHHCCHHH	27.80	25693802
85	Phosphorylation	HKSHGSTSQMPEALQ CCCCCCHHHCCHHHH	26.61	25693802
94	Phosphorylation	MPEALQASDLWYCPD CCHHHHHCCCEECCC	21.92	25693802
106	Ubiquitination	CPDGSFVKKIVIRGH CCCCCCEEEEEEECC	34.47	-
107	Ubiquitination	PDGSFVKKIVIRGHG CCCCCEEEEEEECCC	36.58	-
193	Phosphorylation	RLTLASFTQGRDSWE EEEEEEECCCCCCEE	27.84	17525332
287	Ubiquitination	EREPGHLKALYRRGV HCCCCHHHHHHHHHH	30.58	-
311	Ubiquitination	KATADLKKVLAIDPK HHHCCHHHHHCCCCC	50.18	-
318	Ubiquitination	KVLAIDPKNRAAQEE HHHCCCCCCHHHHHH	56.15	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FKBPL_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 FKBPL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U119A_HUMAN	UNC119	physical	16169070
CDN1A_HUMAN	CDKN1A	physical	15664193
HS90A_HUMAN	HSP90AA1	physical	15664193
A4_HUMAN	APP	physical	21832049
HOIL1_HUMAN	RBCK1	physical	23912458
UBC_HUMAN	UBC	physical	23912458
HS90A_HUMAN	HSP90AA1	physical	23912458
ESR1_HUMAN	ESR1	physical	23912458
ANR49_HUMAN	ANKRD49	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	25036637
UBP19_HUMAN	USP19	physical	25036637
CDC37_HUMAN	CDC37	physical	25036637
HS90A_HUMAN	HSP90AA1	physical	25036637
TBA1B_HUMAN	TUBA1B	physical	25036637
SYTM_HUMAN	TARS2	physical	25036637
AHSA1_HUMAN	AHSA1	physical	25036637
NADE_HUMAN	NADSYN1	physical	28514442
HOIL1_HUMAN	RBCK1	physical	28514442
BRAF_HUMAN	BRAF	physical	28514442
RNF31_HUMAN	RNF31	physical	28514442
KC1E_HUMAN	CSNK1E	physical	28514442
PLSI_HUMAN	PLS1	physical	28514442
EDRF1_HUMAN	EDRF1	physical	28514442
CTU1_HUMAN	CTU1	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193, AND MASSSPECTROMETRY.
PubMed: 17525332