TBC1D8 protein (human) - STRING database

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TBC1D8

TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing (1140 aa)

Predicted Functional Partners:

RNF149

0.748

LONRF3

0.694

TBC1D22B

0.691

IL1RAPL1

0.627

TTYH3

0.595

RPL31

0.589

SGSM2

0.587

IL1R2

0.567

LONRF2

0.550

TBC1D20

0.547

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
IL1R2	LONRF2	ENSP00000330959	ENSP00000377086	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	LON peptidase N-terminal domain and ring finger 2	0.445
IL1R2	LONRF3	ENSP00000330959	ENSP00000360690	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	LON peptidase N-terminal domain and ring finger 3	0.496
IL1R2	RNF149	ENSP00000330959	ENSP00000295317	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	0.586
IL1R2	TBC1D8	ENSP00000330959	ENSP00000366036	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing	0.567
IL1RAPL1	LONRF2	ENSP00000368278	ENSP00000377086	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	LON peptidase N-terminal domain and ring finger 2	0.600
IL1RAPL1	LONRF3	ENSP00000368278	ENSP00000360690	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	LON peptidase N-terminal domain and ring finger 3	0.553
IL1RAPL1	RNF149	ENSP00000368278	ENSP00000295317	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	0.627
IL1RAPL1	TBC1D8	ENSP00000368278	ENSP00000366036	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing	0.627
LONRF2	IL1R2	ENSP00000377086	ENSP00000330959	LON peptidase N-terminal domain and ring finger 2	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	0.445
LONRF2	IL1RAPL1	ENSP00000377086	ENSP00000368278	LON peptidase N-terminal domain and ring finger 2	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	0.600
LONRF2	RNF149	ENSP00000377086	ENSP00000295317	LON peptidase N-terminal domain and ring finger 2	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	0.537
LONRF2	TBC1D8	ENSP00000377086	ENSP00000366036	LON peptidase N-terminal domain and ring finger 2	TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing	0.550
LONRF3	IL1R2	ENSP00000360690	ENSP00000330959	LON peptidase N-terminal domain and ring finger 3	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	0.496
LONRF3	IL1RAPL1	ENSP00000360690	ENSP00000368278	LON peptidase N-terminal domain and ring finger 3	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	0.553
LONRF3	RNF149	ENSP00000360690	ENSP00000295317	LON peptidase N-terminal domain and ring finger 3	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	0.681
LONRF3	TBC1D8	ENSP00000360690	ENSP00000366036	LON peptidase N-terminal domain and ring finger 3	TBC1 domain family member 8; May act as a GTPase-activating protein for Rab family protein(s); GRAM domain containing	0.694
RNF149	IL1R2	ENSP00000295317	ENSP00000330959	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	Interleukin-1 receptor type 2; Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competetive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors; CD molecules	0.586
RNF149	IL1RAPL1	ENSP00000295317	ENSP00000368278	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	Interleukin-1 receptor accessory protein-like 1; May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans- synaptically binding to PTPRD (By similarity); Belongs to the interleukin-1 receptor family	0.627
RNF149	LONRF2	ENSP00000295317	ENSP00000377086	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	LON peptidase N-terminal domain and ring finger 2	0.537
RNF149	LONRF3	ENSP00000295317	ENSP00000360690	E3 ubiquitin-protein ligase RNF149; E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation; Ring finger proteins	LON peptidase N-terminal domain and ring finger 3	0.681

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