HslV protein (Plasmodium falciparum)

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protein of unknown 3D structure

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some 3D structure is known or predicted

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query proteins and first shell of interactors

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second shell of interactors

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Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

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textmining

co-expression

protein homology

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[Homology]

Score

HslV

Heat shock protein hslv (207 aa)

Predicted Functional Partners:

PFI0355c

0.999

PFC0310c

0.885

PF14_0417

0.830

PF14_0147

0.818

MAL8P1.99

0.797

PF08_0063

0.788

PF10_0111

0.699

PF10_0123

0.684

PF07_0029

0.683

PFL1595w

0.674

Your Current Organism:

Plasmodium falciparum

NCBI taxonomy Id: 5833
Other names: Laverania, P. (Laverania), P. falciparum, Plasmodium (Laverania), Plasmodium (Laverania) falciparum, Plasmodium falciparum, malaria parasite P. falciparum

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
HslV	MAL8P1.99	PFL1465c	MAL8P1.99	Heat shock protein hslv	GTPase, putative	0.797
HslV	PF07_0029	PFL1465c	PF07_0029	Heat shock protein hslv	Heat shock protein 86; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity)	0.683
HslV	PF08_0063	PFL1465c	PF08_0063	Heat shock protein hslv	ClpB protein, putative	0.788
HslV	PF10_0111	PFL1465c	PF10_0111	Heat shock protein hslv	Proteasome subunit beta type; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity)	0.699
HslV	PF10_0123	PFL1465c	PF10_0123	Heat shock protein hslv	GMP synthetase	0.684
HslV	PF14_0147	PFL1465c	PF14_0147	Heat shock protein hslv	ATP-dependent protease, putative	0.818
HslV	PF14_0417	PFL1465c	PF14_0417	Heat shock protein hslv	HSP90	0.830
HslV	PFC0310c	PFL1465c	PFC0310c	Heat shock protein hslv	ATP-dependent Clp protease proteolytic subunit	0.885
HslV	PFI0355c	PFL1465c	PFI0355c	Heat shock protein hslv	ATP-dependent heat shock protein, putative	0.999
HslV	PFL1595w	PFL1465c	PFL1595w	Heat shock protein hslv	Conserved protein	0.674
MAL8P1.99	HslV	MAL8P1.99	PFL1465c	GTPase, putative	Heat shock protein hslv	0.797
MAL8P1.99	PF08_0063	MAL8P1.99	PF08_0063	GTPase, putative	ClpB protein, putative	0.654
MAL8P1.99	PF10_0123	MAL8P1.99	PF10_0123	GTPase, putative	GMP synthetase	0.795
MAL8P1.99	PF14_0147	MAL8P1.99	PF14_0147	GTPase, putative	ATP-dependent protease, putative	0.881
MAL8P1.99	PF14_0417	MAL8P1.99	PF14_0417	GTPase, putative	HSP90	0.509
MAL8P1.99	PFC0310c	MAL8P1.99	PFC0310c	GTPase, putative	ATP-dependent Clp protease proteolytic subunit	0.863
MAL8P1.99	PFI0355c	MAL8P1.99	PFI0355c	GTPase, putative	ATP-dependent heat shock protein, putative	0.745
PF07_0029	HslV	PF07_0029	PFL1465c	Heat shock protein 86; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity)	Heat shock protein hslv	0.683
PF07_0029	PF08_0063	PF07_0029	PF08_0063	Heat shock protein 86; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity)	ClpB protein, putative	0.966
PF07_0029	PF10_0123	PF07_0029	PF10_0123	Heat shock protein 86; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity)	GMP synthetase	0.632

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Experiments

Neighborhood

Textmining

Fusion

Coexpression

Cooccurrence

Databases