P14324: Farnesyl pyrophosphate synthase

General Information

Protein names	- Farnesyl pyrophosphate synthase - FPP synthase - FPS - 2.5.1.10 - (2E,6E)-farnesyl diphosphate synthase - Dimethylallyltranstransferase - 2.5.1.1 - Farnesyl diphosphate synthase - Geranyltranstransferase
Gene names	FDPS
Organism	Homo sapiens
Protease Family
Protease ID
Chromosome location
UniProt ID	P14324

5 N-termini

2 C-termini

1 Cleavages

0 Substrates

Sequence

        10         20         30         40         50         60
MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW CQAWTEEPRA
        70         80         90        100        110        120
LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG HPEIGDAIAR LKEVLEYNAI
       130        140        150        160        170        180
GGKYNRGLTV VVAFRELVEP RKQDADSLQR AWTVGWCVEL LQAFFLVADD IMDSSLTRRG
       190        200        210        220        230        240
QICWYQKPGV GLDAINDANL LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD
       250        260        270        280        290        300
LLTAPQGNVD LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE
       310        320        330        340        350        360
MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ ILKENYGQKE
       370        380        390        400        410
AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA PLPPAVFLGL ARKIYKRRK

Isoforms

- Isoform 2 of Farnesyl pyrophosphate synthase

Sequence View

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Directness:

Physiological Relevance:

Evidence Codes:

Methodology:

Perturbation of System:

Biological System:

Protease Assignment Confidence:

Evidence Names:

Database:

Lab:

Protein Neighborhood

Domains & Features

5 N-termini - 2 C-termini - 1 Cleavages - 0 Substrates

N-termini

Name	Sequence	Position	Modification	Evidence type	Method	Source (database)	Source (Lab)	Evidence name
P14324-1-unknown	MPLSRW...	1		inferred from electronic annotation	electronic annotation	UniProtKB		inferred from uniprot
P14324-1-acetylation	MPLSRW...	1	acetylation-		other		CNRS/ISV	Large_scale_NTA_Human
P14324-67-acetylation	MNGDQN...	67	acetylation-		N-TAILS		Overall Laboratory	Lange_Huesgen_et_al-RBC
P14324-67-acetylation	MNGDQN...	67	acetylation-	inferred from isoform by sequence similarity	unknown	TopFIND		inferred from TNt181821
P14324-67-unknown	MNGDQN...	67		inferred from isoform by sequence similarity	unknown	TopFIND		inferred from TNt75433
P14324-67-unknown	MNGDQN...	67		inferred from electronic annotation	unknown	TISdb		inferred from TISdb
P14324-194-unknown	AINDAN...	194		inferred from cleavage	unknown	TopFIND		Inferred from cleavage TC11215
P14324-194-unknown	AINDAN...	194		inferred from isoform by sequence similarity	unknown	TopFIND		inferred from TNt143824

C-termini

Sequence	Position	Evidence type	Method	Source (database)	Evidence name
...GVGLDA	193	inferred from cleavage	unknown	TopFIND	Inferred from cleavage TC11215
...GVGLDA	193	inferred from isoform by sequence similarity	unknown	TopFIND	inferred from TCt127067
...YKRRK	419	inferred from electronic annotation	electronic annotation	UniProtKB	inferred from uniprot
...YKRRK	419	inferred from isoform by sequence similarity	unknown	TopFIND	inferred from TCt71051

Cleavages

Protease	Position	Sequence	Evidence type	Method	Source (database)	Source (Lab)	Evidence name	Publications (PMIDs)
GRAB_HUMAN	193	GLDA.\|.AIND	inferred from experiment	unknown	MEROPS	Gevaert K	Van Damme P et al.:Complementary positional proteo... (M14.017)	20526345,

Substrates

Substrate	Position	Sequence	Evidence type	Method	Source (database)	Source (Lab)	Evidence name	Publications (PMIDs)