TNIP1_HUMAN - dbPTM
TNIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNIP1_HUMAN
UniProt AC Q15025
Protein Name TNFAIP3-interacting protein 1
Gene Name TNIP1
Organism Homo sapiens (Human).
Sequence Length 636
Subcellular Localization Cytoplasm. Nucleus. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.
Protein Description Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression 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 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..
Protein Sequence MEGRGPYRIYDPGGSVPSGEASAAFERLVKENSRLKEKMQGIKMLGELLEESQMEATRLRQKAEELVKDNELLPPPSPSLGSFDPLAELTGKDSNVTASPTAPACPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDHGQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVEPHPEHLCGAYPYAYPPMPAMVPHHGFEDWSQIRYPPPPMAMEHPPPLPNSRLFHLPEYTWRLPCGGVRNPNQSSQVMDPPTARPTEPESPKNDREGPQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationGRGPYRIYDPGGSVP
CCCCCEEECCCCCCC		13.6927642862
15PhosphorylationRIYDPGGSVPSGEAS
EEECCCCCCCCHHHH		36.4530108239
18PhosphorylationDPGGSVPSGEASAAF
CCCCCCCCHHHHHHH		47.3030108239
22PhosphorylationSVPSGEASAAFERLV
CCCCHHHHHHHHHHH		18.8130108239
77PhosphorylationNELLPPPSPSLGSFD
CCCCCCCCCCCCCCC		32.6628355574
79PhosphorylationLLPPPSPSLGSFDPL
CCCCCCCCCCCCCHH		50.1028176443
82PhosphorylationPPSPSLGSFDPLAEL
CCCCCCCCCCHHHHH		31.5930108239
90PhosphorylationFDPLAELTGKDSNVT
CCHHHHHHCCCCCCC		33.4230108239
97PhosphorylationTGKDSNVTASPTAPA
HCCCCCCCCCCCCCC		26.1825627689
99PhosphorylationKDSNVTASPTAPACP
CCCCCCCCCCCCCCC		17.2625849741
166PhosphorylationLHLQRLETTLSVCAE
EEHHHHHHHHHHHCC		37.3128122231
167PhosphorylationHLQRLETTLSVCAEE
EHHHHHHHHHHHCCC		13.9928122231
169PhosphorylationQRLETTLSVCAEEPD
HHHHHHHHHHCCCCC		17.0424247654
205PhosphorylationVHKNEQRTSILQTLC
HHHHHHHHHHHHHHH		21.5829514088
206PhosphorylationHKNEQRTSILQTLCE
HHHHHHHHHHHHHHH		24.4030108239
223UbiquitinationRKENEALKAKLDKGL
HHHHHHHHHHHHHHH		50.99-
228UbiquitinationALKAKLDKGLEQRDQ
HHHHHHHHHHHHHHH		75.68-
253PhosphorylationELKKLLMSNGNKEGA
HHHHHHHHCCCCCCC		41.3722210691
257AcetylationLLMSNGNKEGASGRP
HHHHCCCCCCCCCCC		59.9520167786
261PhosphorylationNGNKEGASGRPGSPK
CCCCCCCCCCCCCCC		46.3123401153
266PhosphorylationGASGRPGSPKMEGTG
CCCCCCCCCCCCCCC		24.8330266825
272PhosphorylationGSPKMEGTGKKAVAG
CCCCCCCCCCCCCCC		32.3022210691
284PhosphorylationVAGQQQASVTAGKVP
CCCCHHHHCCCCCCC		18.7030108239
286PhosphorylationGQQQASVTAGKVPEV
CCHHHHCCCCCCCHH		27.4830108239
301AcetylationVALGAAEKKVKMLEQ
HHHCHHHHHHHHHHH		59.1326051181
301UbiquitinationVALGAAEKKVKMLEQ
HHHCHHHHHHHHHHH		59.13-
326PhosphorylationQWDQHFRSMKQQYEQ
HHHHHHHHHHHHHHH		29.4128348404
331PhosphorylationFRSMKQQYEQKITEL
HHHHHHHHHHHHHHH		20.1730266825
336PhosphorylationQQYEQKITELRQKLA
HHHHHHHHHHHHHHH		35.6830266825
347UbiquitinationQKLADLQKQVTDLEA
HHHHHHHHHHHHHHH		54.77-
350PhosphorylationADLQKQVTDLEAERE
HHHHHHHHHHHHHHH		32.16-
379PhosphorylationSKIEMEETDKEQLTA
HHHCCCCCCHHHHHH		38.7823532336
385PhosphorylationETDKEQLTAEAKELR
CCCHHHHHHHHHHHH		23.3423532336
389UbiquitinationEQLTAEAKELRQKVK
HHHHHHHHHHHHHHH		49.11-
396UbiquitinationKELRQKVKYLQDQLS
HHHHHHHHHHHHHCC		47.48-
397PhosphorylationELRQKVKYLQDQLSP
HHHHHHHHHHHHCCH		16.7523403867
403PhosphorylationKYLQDQLSPLTRQRE
HHHHHHCCHHHHHHH		16.5419664994
406PhosphorylationQDQLSPLTRQREYQE
HHHCCHHHHHHHHHH		28.3030266825
428PhosphorylationKALEEALSIQTPPSS
HHHHHHHCCCCCCCC		21.5023927012
431PhosphorylationEEALSIQTPPSSPPT
HHHHCCCCCCCCCCC		35.1830278072
434PhosphorylationLSIQTPPSSPPTAFG
HCCCCCCCCCCCCCC		57.5930278072
435PhosphorylationSIQTPPSSPPTAFGS
CCCCCCCCCCCCCCC		40.4430278072
438PhosphorylationTPPSSPPTAFGSPEG
CCCCCCCCCCCCCCC		37.6930278072
442PhosphorylationSPPTAFGSPEGAGAL
CCCCCCCCCCCHHHH		17.2123927012
452UbiquitinationGAGALLRKQELVTQN
CHHHHHHHHHHHCHH		48.36-
463AcetylationVTQNELLKQQVKIFE
HCHHHHHHHHHHHHH		51.8419822173
467AcetylationELLKQQVKIFEEDFQ
HHHHHHHHHHHHHHH		37.0219822183
496 (in isoform 2)Ubiquitination-47.2221906983
496 (in isoform 1)Ubiquitination-47.2221906983
496UbiquitinationELKKQVEKLQAQVTL
HHHHHHHHHHHHHHH		47.222190698
496UbiquitinationELKKQVEKLQAQVTL
HHHHHHHHHHHHHHH		47.2221906983
509UbiquitinationTLSNAQLKAFKDEEK
HHCHHHHHHHCCHHH		39.43-
512UbiquitinationNAQLKAFKDEEKARE
HHHHHHHCCHHHHHH		69.92-
516UbiquitinationKAFKDEEKAREALRQ
HHHCCHHHHHHHHHH		51.17-
535 (in isoform 5)Phosphorylation-13.1030206219
540 (in isoform 5)Phosphorylation-27.2030206219
542 (in isoform 5)Phosphorylation-46.5930206219
552PhosphorylationCGAYPYAYPPMPAMV
CCCCCCCCCCCCCCC		11.3017632516
559 (in isoform 6)Phosphorylation-4.4222210691
568PhosphorylationHHGFEDWSQIRYPPP
CCCCCCHHHCCCCCC		28.2219581576
571MethylationFEDWSQIRYPPPPMA
CCCHHHCCCCCCCCC		30.2154549865
571Asymmetric dimethylarginineFEDWSQIRYPPPPMA
CCCHHHCCCCCCCCC		30.21-
596PhosphorylationRLFHLPEYTWRLPCG
CCCCCCCEEEECCCC		15.06-
599MethylationHLPEYTWRLPCGGVR
CCCCEEEECCCCCCC		22.4324129315
599Asymmetric dimethylarginineHLPEYTWRLPCGGVR
CCCCEEEECCCCCCC		22.43-
611PhosphorylationGVRNPNQSSQVMDPP
CCCCCCCCCCCCCCC		29.4023927012
612PhosphorylationVRNPNQSSQVMDPPT
CCCCCCCCCCCCCCC		19.6129978859
619PhosphorylationSQVMDPPTARPTEPE
CCCCCCCCCCCCCCC		40.4630108239
623PhosphorylationDPPTARPTEPESPKN
CCCCCCCCCCCCCCC		59.6330108239
623 (in isoform 2)Phosphorylation-59.6322210691
627PhosphorylationARPTEPESPKNDREG
CCCCCCCCCCCCCCC		52.4729255136
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TNIP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNIP1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TNIP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGBI_HUMANMAGEB18physical
16189514
MK01_HUMANMAPK1physical
12220502
UBC_HUMANUBCphysical
18212736
TAXB1_HUMANTAX1BP1physical
21885437
IKKE_HUMANIKBKEphysical
21885437
TBK1_HUMANTBK1physical
21885437
RARA_HUMANRARAphysical
19732752
RARG_HUMANRARGphysical
19732752
NFKB1_HUMANNFKB1physical
19695220
SELPL_HUMANSELPLGphysical
17632516
P85A_HUMANPIK3R1physical
17632516
PK3CD_HUMANPIK3CDphysical
17632516
GAG_HV1H2gagphysical
11090181
UBC_HUMANUBCphysical
23032186
TNIP1_HUMANTNIP1physical
21988832
TNIP1_HUMANTNIP1physical
25416956
NDC80_HUMANNDC80physical
25416956
ZNHI1_HUMANZNHIT1physical
25416956
RBP1_HUMANRALBP1physical
25416956
MO4L1_HUMANMORF4L1physical
25416956
PNKP_HUMANPNKPphysical
25416956
GBRL2_HUMANGABARAPL2physical
25416956
F168A_HUMANFAM168Aphysical
25416956
GBRL1_HUMANGABARAPL1physical
25416956
VP33B_HUMANVPS33Bphysical
25416956
MAGH1_HUMANMAGEH1physical
25416956
NDK7_HUMANNME7physical
25416956
CDIP1_HUMANCDIP1physical
25416956
SNIP1_HUMANSNIP1physical
25416956
TNIP3_HUMANTNIP3physical
25416956
MLP3B_HUMANMAP1LC3Bphysical
25416956
F161A_HUMANFAM161Aphysical
25416956
MK67I_HUMANNIFKphysical
25416956
MLP3A_HUMANMAP1LC3Aphysical
25416956
MOB1B_HUMANMOB1Bphysical
25416956
TEAN2_HUMANTCEANC2physical
25416956
SYT6_HUMANSYT6physical
25416956
MOB3C_HUMANMOB3Cphysical
25416956
CC112_HUMANCCDC112physical
25416956
TXLNA_HUMANTXLNAphysical
25416956
CFA53_HUMANCFAP53physical
25416956
MAGBI_HUMANMAGEB18physical
25416956
MESH1_HUMANHDDC3physical
25416956
MK01_HUMANMAPK1physical
26046540
NDK7_HUMANNME7physical
21516116
CDIP1_HUMANCDIP1physical
21516116
MCM10_HUMANMCM10physical
21516116
TCEA2_HUMANTCEA2physical
21516116
TYRO3_HUMANTYRO3physical
21516116
CC121_HUMANCCDC121physical
21516116
AB17A_HUMANABHD17Aphysical
21516116
CCNG1_HUMANCCNG1physical
21516116
OPTN_HUMANOPTNphysical
28514442
POTEF_HUMANPOTEFphysical
28514442
UBC_HUMANUBCphysical
28319114
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TNIP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, AND MASSSPECTROMETRY.
"P-selectin primes leukocyte integrin activation duringinflammation.";
Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y.,Zhu X., Plow E.F., Chen M., Geng J.G.;
Nat. Immunol. 8:882-892(2007).
Cited for: FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION ATTYR-552, AND MUTAGENESIS OF TYR-552.

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