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Protein Page:
TNIP1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TNIP1 Interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal; however, binding to A20/TNFAIP3 seems not to be required for this function. Inhibits NF-kappa-B activation by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcricption. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflamation; this function is mediated by association with SELPLG and dependent on phosohorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection. Interacts with TNFAIP3 and IKBKG; facilitates TNFAIP3- mediated de-ubiquitination of NEMO/IKBKG. Interacts with HIV-1 matrix protein. Interacts with Shigella flexneri ipah9.8; the interaction promotes polyubiquitination of IKBKG. Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts with IKBKG (polyubiquitinated). Interacts with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction is indicative for participation in an activated TLR-signaling complex. Ubiquitous. Strongly expressed in peripheral blood lymphocytes, spleen and skeletal muscle, and is weakly expressed in the brain. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transcription regulation
Chromosomal Location of Human Ortholog: 5q32-q33.1
Cellular Component: cytoplasm; intracellular; nucleus
Molecular Function: protein binding; ubiquitin-specific protease activity; mitogen-activated protein kinase binding
Biological Process: MyD88-dependent toll-like receptor signaling pathway; leukocyte adhesion; negative regulation of viral genome replication; glycoprotein biosynthetic process; translation; defense response; positive regulation of transcription from RNA polymerase II promoter; negative regulation of I-kappaB kinase/NF-kappaB cascade; inflammatory response; positive regulation of inflammatory response
Reference #:  Q15025 (UniProtKB)
Alt. Names/Synonyms: ABIN-1; HIV-1 Nef-interacting protein; hVAN; KIAA0113; NAF1; Nef-associated factor 1; Nef-associated factor 1 SNP; Nip40-1; TNFAIP3 interacting protein 1; TNFAIP3-interacting protein 1; TNIP1; VAN; Virion-associated nuclear shuttling protein; virion-associated nuclear-shuttling protein
Gene Symbols: TNIP1
Molecular weight: 71,864 Da
Basal Isoelectric point: 6.23  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TNIP1

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, induced: Y552‑p
molecular association, regulation: Y552‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 L73 LVKDNELLPPPsPSL
0 2 S77-p NELLPPPsPSLGSFD
0 2 S99-p KDSNVTAsPTAPACP
0 1 T101 SNVTAsPTAPACPSD
0 1 - gap
0 1 S107 PTAPACPSDKPAPVQ
0 1 K223-ub RKENEALkAKLDKGL
0 3 K257-ac LLMSNGNkEGASGRP
0 1 G265 EGASGRPGsPKMEGT
0 3 S266-p GASGRPGsPKMEGTG
0 1 S284-p VAGQQQAsVTAGKVP
0 1 K301-ub VALGAAEkKVKMLEQ
0 1 T336-p QQYEQKItELRQKLA
0 2 T350-p ADLQKQVtDLEAERE
0 1 T385-p ETDKEQLtAEAKELR
0 10 S403-p KYLQDQLsPLTRQRE
0 1 S428 KALEEALSIQtPPss
0 3 T431-p EEALSIQtPPssPPt
0 1 P432 EALSIQtPPssPPtA
0 2 S434-p LSIQtPPssPPtAFG
0 2 S435-p SIQtPPssPPtAFGs
0 3 T438-p tPPssPPtAFGsPEG
0 4 S442-p sPPtAFGsPEGAGAL
0 2 K463-ac VTQNELLkQQVkIFE
0 2 K467-ac ELLkQQVkIFEEDFQ
0 6 K496-ub ELKKQVEkLQAQVTL
1 0 Y552-p CGAYPYAyPPMPAMV
0 1 S568-p HHGFEDWsQIRYPPP
0 1 R571 FEDWsQIRYPPPPMA
0 1 Y596-p RLFHLPEyTWrLPCG
0 1 R599-m1 HLPEyTWrLPCGGVR
0 2 R599-m2 HLPEyTWrLPCGGVR
0 2 S627-p ARPTEPEsPKNDREG
  mouse

 
S73-p LVKDSELsPPTSAPS
S77 SELsPPTSAPSLVSF
H100 QDTKVQVHPAtSTAA
T103-gl KVQVHPAtSTAAtTT
T108-p PAtSTAAtTTATATT
S118-p ATATTGNsMEKPEPA
K236 RQENEALKAKLDKGL
K270 LLMNSSCKEGLCGQP
S278-p EGLCGQPssPKPEGA
S279-p GLCGQPssPKPEGAG
S297 VAGQQQASVMASKVP
K314 GAFGAAEKKVKLLEQ
T349 QQYEQKITELRQKLV
T363-p VDLQKQVtELEAERE
T398 ETDKEQLTAEAKELR
S416-p RYLQDQLsPLTRQRE
S441-p KALEEALsIQAsPSs
A444 EEALsIQAsPSsPPA
S445-p EALsIQAsPSsPPAA
S447 LsIQAsPSsPPAAFG
S448-p sIQAsPSsPPAAFGs
A451 AsPSsPPAAFGsPEG
S455-p sPPAAFGsPEGVGGH
K476 VTQNELLKQQVKIFE
K480 ELLKQQVKIFEEDFQ
K509 ELKKQVEKLQAQVTL
Y565 CGAYPYAYPPMPAMV
S581 HHAYKDWSQIrYPPP
R584-m2 YKDWSQIrYPPPPVP
Y609 RLFHLPEYTWRPPCA
R612 HLPEYTWRPPCAGIR
R612 HLPEYTWRPPCAGIR
S638 DRPAEPESADNDCDG
  rat

 
P74 LVRDSELPPPPPAPS
P78 SELPPPPPAPSLVSF
H101 QDTKVQAHPTTTTTT
T104 KVQAHPTTTTTTTTT
T109 PTTTTTTTTTTTTTT
S120 TTTTIGNSMEKSVSA
K238 RQENEALKAKLDKSL
K272 LLMNSNCKEGLCGQP
S280 EGLCGQPSSPKTEGA
S281 GLCGQPSSPKTEGAG
S299 VAGQQQASMTASKVP
K316 GAFGTAEKKVKLLEQ
T351 QQYEQKITELRQKLV
T365 VDLQKQVTELEAERE
T400 ETDKEQLTTEAKELR
S418 KYLQDQLSPLMRQRE
S443 KALEEALSIQASPSS
A446 EEALSIQASPSSPPA
S447 EALSIQASPSSPPAA
S449 LSIQASPSSPPAAFG
S450 SIQASPSSPPAAFGS
A453 ASPSSPPAAFGSPEG
S457 SPPAAFGSPEGVGGH
K478 VTQNELLKQQVKIFE
K482 ELLKQQVKIFEEDFQ
K511 ELKKQVEKLQAQVTL
Y567 CGAYPYAYPPMPAMV
S583 HHAYKDWSQIRYPPP
R586 YKDWSQIRYPPPPVP
Y611 RLFHLPEYTWRPPCA
R614 HLPEYTWRPPCAGIR
R614 HLPEYTWRPPCAGIR
S640 DRPAEPESADNDCDG
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