TNIP1
entrez
10318
canonical
uniprot
Q15025
canonical
ensembl
ENSG00000145901
resolver
ensp
ENSP00000317891
resolver
ensp
ENSP00000374029
resolver
ensp
ENSP00000427854
resolver
ensp
ENSP00000428187
resolver
ensp
ENSP00000428243
resolver
ensp
ENSP00000428487
resolver
ensp
ENSP00000429891
resolver
ensp
ENSP00000429912
resolver
ensp
ENSP00000430279
resolver
ensp
ENSP00000430760
resolver
ensp
ENSP00000430971
resolver
ensp
ENSP00000431105
resolver
ensp
ENSP00000483944
resolver
ensp
ENSP00000548074
resolver
ensp
ENSP00000548080
resolver
ensp
ENSP00000670765
resolver
ensp
ENSP00000670767
resolver
ensp
ENSP00000670774
resolver
ensp
ENSP00000695509
resolver
ensp
ENSP00000695522
resolver
enst
ENST00000389378
resolver
genesymbol
TNIP1
resolver
genesymbol_syn
KIAA0113
resolver
genesymbol_syn
NAF1
resolver
hgnc
HGNC:16903
resolver
uniprot
A0A0A0MRZ4
resolver
uniprot
A4F1W8
resolver
uniprot
A4F1W9
resolver
uniprot
A4F1X2
resolver
uniprot
A4F1X4
resolver
uniprot
A4F1X5
resolver
uniprot
A4F1X6
resolver
uniprot
A4F1X7
resolver
uniprot
A4F1X9
resolver
uniprot
A8K4N4
resolver
uniprot
B7Z699
resolver
uniprot
B7Z8K2
resolver
uniprot
E7EPY1
resolver
uniprot
E7ET96
resolver
uniprot
O76008
resolver
uniprot
Q05KP3
resolver
uniprot
Q05KP4
resolver
uniprot
Q6N077
resolver
uniprot
Q96EL9
resolver
uniprot
Q99833
resolver
uniprot
Q9H1J3
resolver
uniprot_entry
A0A0A0MRZ4_HUMAN
resolver
uniprot_entry
A8K4N4_HUMAN
resolver
uniprot_entry
B7Z8K2_HUMAN
resolver
uniprot_entry
TNIP1_HUMAN
resolver
uniprot_sec
A4F1W8
resolver
uniprot_sec
A4F1W9
resolver
uniprot_sec
A4F1X2
resolver
uniprot_sec
A4F1X4
resolver
uniprot_sec
A4F1X5
resolver
uniprot_sec
A4F1X6
resolver
uniprot_sec
A4F1X7
resolver
uniprot_sec
A4F1X9
resolver
uniprot_sec
B7Z699
resolver
uniprot_sec
E7EPY1
resolver
uniprot_sec
E7ET96
resolver
uniprot_sec
O76008
resolver
uniprot_sec
Q05KP3
resolver
uniprot_sec
Q05KP4
resolver
uniprot_sec
Q6N077
resolver
uniprot_sec
Q96EL9
resolver
uniprot_sec
Q99833
resolver
uniprot_sec
Q9H1J3
resolver
amino_acid_sequence
MEGRGPYRIYDPGGSVPSGEASAAFERLVKENSRLKEKMQGIKMLGELLEESQMEATRLRQKAEELVKDNELLPPPSPSLGSFDPLAELTGKDSNVTASPTAPACPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDHGQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVEPHPEHLCGAYPYAYPPMPAMVPHHGFEDWSQIRYPPPPMAMEHPPPLPNSRLFHLPEYTWRLPCGGVRNPNQSSQVMDPPTARPTEPESPKNDREGPQ
uniprot
proteins
function
FUNCTION: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating TAX1BP1 and A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG (PubMed:21885437). Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. 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 inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation 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. {ECO:0000269|PubMed:12220502, ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:17016622, ECO:0000269|PubMed:17632516, ECO:0000269|PubMed:20010814, ECO:0000269|PubMed:21885437}.
uniprot
proteins
mass_dalton
71864
uniprot
proteins
mutagenesis
MUTAGEN 472; /note="D->N: Abolishes binding to polyubiquitin ('K-63'-linked and linear)."; /evidence="ECO:0000269|PubMed:21606507"; MUTAGEN 552; /note="Y->F: Abolishes interaction with PI3K p85 regulatory subunit and abolishes interaction between SELPLG and PI3K p85 regulatory subunit."; /evidence="ECO:0000269|PubMed:17632516
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Tyr-552 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation. {ECO:0000269|PubMed:17632516}.
uniprot
proteins
pubmed
11090181
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12220502
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16684768
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17016622
uniprot
proteins
pubmed
17632516
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20010814
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21266526
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21606507
uniprot
proteins
pubmed
21885437
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
7788527
uniprot
proteins
pubmed
8681136
uniprot
proteins
pubmed
9923610
uniprot
proteins
sequence_length
636
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.
uniprot
proteins