dbPTM

FNTB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FNTB_HUMAN
UniProt AC	P49356
Protein Name	Protein farnesyltransferase subunit beta
Gene Name	FNTB
Organism	Homo sapiens (Human).
Sequence Length	437
Subcellular Localization
Protein Description	Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X..
Protein Sequence	MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASPSSFTYY -----CCCCCCCCEE	24.82	23401153
5	Phosphorylation	---MASPSSFTYYCP ---CCCCCCCCEECC	35.27	25159151
6	Phosphorylation	--MASPSSFTYYCPP --CCCCCCCCEECCC	25.62	25159151
8	Phosphorylation	MASPSSFTYYCPPSS CCCCCCCCEECCCCC	18.61	24043423
9	Phosphorylation	ASPSSFTYYCPPSSS CCCCCCCEECCCCCC	10.89	23663014
10	Phosphorylation	SPSSFTYYCPPSSSP CCCCCCEECCCCCCC	8.74	23663014
14	Phosphorylation	FTYYCPPSSSPVWSE CCEECCCCCCCCCCC	28.70	23663014
15	Phosphorylation	TYYCPPSSSPVWSEP CEECCCCCCCCCCCC	44.42	23663014
16	Phosphorylation	YYCPPSSSPVWSEPL EECCCCCCCCCCCCC	28.01	23663014
17	Ubiquitination	YCPPSSSPVWSEPLY ECCCCCCCCCCCCCH	33.28	21890473
20	Phosphorylation	PSSSPVWSEPLYSLR CCCCCCCCCCCHHCC	29.57	28450419
24	Phosphorylation	PVWSEPLYSLRPEHA CCCCCCCHHCCHHHH	19.17	26074081
25	Phosphorylation	VWSEPLYSLRPEHAR CCCCCCHHCCHHHHH	26.11	26074081
39	Phosphorylation	RERLQDDSVETVTSI HHHHCCCCCCCCHHH	30.09	-
42	Phosphorylation	LQDDSVETVTSIEQA HCCCCCCCCHHHHHH	27.25	-
50	Ubiquitination	VTSIEQAKVEEKIQE CHHHHHHHHHHHHHH	50.28	21890473
54	Ubiquitination	EQAKVEEKIQEVFSS HHHHHHHHHHHHHHH	35.86	-
63	Ubiquitination	QEVFSSYKFNHLVPR HHHHHHHCHHCHHHH	41.45	21890473
63	Ubiquitination	QEVFSSYKFNHLVPR HHHHHHHCHHCHHHH	41.45	21890473
63	Ubiquitination	QEVFSSYKFNHLVPR HHHHHHHCHHCHHHH	41.45	21890473
89	Ubiquitination	LKRGLRQLTDAYECL HHHHHHHHHHHHHHH	3.65	33845483
124	Ubiquitination	PIPQIVATDVCQFLE CCCHHHHHHHHHHHH	20.33	21890473
130	Ubiquitination	ATDVCQFLELCQSPE HHHHHHHHHHHCCCC	1.71	22817900
176	Ubiquitination	YDIINREKLLQYLYS HHHCCHHHHHHHHHH	51.78	21890473
180	Phosphorylation	NREKLLQYLYSLKQP CHHHHHHHHHHCCCC	13.94	22817900
183	Phosphorylation	KLLQYLYSLKQPDGS HHHHHHHHCCCCCCC	26.88	24719451
237	Ubiquitination	ARCQNWEGGIGGVPG HHCCCCCCCCCCCCC	25.32	22817900
300	Phosphorylation	NKLVDGCYSFWQAGL HHHHHHHHHHHHHCH	16.66	20090780
372	Ubiquitination	YCLSGLSIAQHFGSG HHCCCCHHHHHHCCC	5.27	22817900
418	Ubiquitination	ATTYFLQKPVPGFEE HHHHHHCCCCCCHHH	50.56	2190698
430	Phosphorylation	FEELKDETSAEPATD HHHHCCCCCCCCCCC	43.29	20068231
431	Phosphorylation	EELKDETSAEPATD- HHHCCCCCCCCCCC-	28.70	20068231
436	Phosphorylation	ETSAEPATD------ CCCCCCCCC------	53.62	25850435
479	Ubiquitination	------------------------------------------------- -------------------------------------------------		22817900

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 FNTB_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPL4_HUMAN	NPLOC4	physical	22863883
RPR1A_HUMAN	RPRD1A	physical	22863883
UBB_HUMAN	UBB	physical	26186194
SPDLY_HUMAN	SPDL1	physical	26186194
YKT6_HUMAN	YKT6	physical	26186194
HOOK3_HUMAN	HOOK3	physical	26186194
LMNB2_HUMAN	LMNB2	physical	26186194
CENPF_HUMAN	CENPF	physical	26186194
DYR1A_HUMAN	DYRK1A	physical	26186194
FNTA_HUMAN	FNTA	physical	26186194
CAN1_HUMAN	CAPN1	physical	26186194
GRIP1_HUMAN	GRIP1	physical	26186194
DHX57_HUMAN	DHX57	physical	26186194
ENPP1_HUMAN	ENPP1	physical	26186194
ICAL_HUMAN	CAST	physical	26186194
RRAS2_HUMAN	RRAS2	physical	26186194
UH1BL_HUMAN	UHRF1BP1L	physical	26186194
PITH1_HUMAN	PITHD1	physical	26186194
PPM1B_HUMAN	PPM1B	physical	26186194
NDUF7_HUMAN	NDUFAF7	physical	26186194
CPNS1_HUMAN	CAPNS1	physical	26186194
TP4A1_HUMAN	PTP4A1	physical	26186194
F117B_HUMAN	FAM117B	physical	26186194
NSMA_HUMAN	SMPD2	physical	26186194
HOOK2_HUMAN	HOOK2	physical	26186194
TROAP_HUMAN	TROAP	physical	26186194
GRIP1_HUMAN	GRIP1	physical	28514442
FNTA_HUMAN	FNTA	physical	28514442
SPDLY_HUMAN	SPDL1	physical	28514442
CENPF_HUMAN	CENPF	physical	28514442
DYR1A_HUMAN	DYRK1A	physical	28514442
HOOK3_HUMAN	HOOK3	physical	28514442
ICAL_HUMAN	CAST	physical	28514442
TROAP_HUMAN	TROAP	physical	28514442
YKT6_HUMAN	YKT6	physical	28514442
UH1BL_HUMAN	UHRF1BP1L	physical	28514442
NSMA_HUMAN	SMPD2	physical	28514442
DHX57_HUMAN	DHX57	physical	28514442
UBB_HUMAN	UBB	physical	28514442
HOOK2_HUMAN	HOOK2	physical	28514442
LMNB2_HUMAN	LMNB2	physical	28514442
NDUF7_HUMAN	NDUFAF7	physical	28514442
ENPP1_HUMAN	ENPP1	physical	28514442
PITH1_HUMAN	PITHD1	physical	28514442
TP4A1_HUMAN	PTP4A1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FNTB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300, AND MASSSPECTROMETRY.	15592455 [Abstract]