TIF1A_MOUSE - dbPTM
TIF1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIF1A_MOUSE
UniProt AC Q64127
Protein Name Transcription intermediary factor 1-alpha
Gene Name Trim24
Organism Mus musculus (Mouse).
Sequence Length 1051
Subcellular Localization Nucleus. Cytoplasm. Detected in the cytoplasm of the zygote. Translocates into the pronucleus at the time of genome activation. Colocalizes with sites of active transcription.
Protein Description Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23' (H3K23ac) (By similarity). Has E3 protein-ubiquitin ligase activity. Promotes ubiquitination and proteasomal degradation of p53/TP53. Plays a role in the regulation of cell proliferation and apoptosis via its effects on p53/TP53 levels. Up-regulates ligand-dependent transcription activation by AR, GCR/NR3C1, thyroid hormone receptor (TR) and ESR1. Modulates transcription activation by retinoic acid (RA) receptors, such as RARA. Plays a role in regulating retinoic acid-dependent proliferation of hepatocytes. Required for normal transition from proliferating neonatal hepatocytes to quiescent adult hepatocytes..
Protein Sequence MEVAVEKAAAAAAPAGGPAAAAPSGENEAESRQGPDSESGGEASRLNLLDTCAVCHQNIQSRVPKLLPCLHSFCQRCLPAPQRYLMLTAPALGSAETPPPAPAPAPAPGSPAGGPSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKYTGNQIQNRIIEINQNQKQVEQDIKVAIFTLMVEINKKGKALLHQLESLAKDHRMKLMQQQQEVAGLSKQLEHVMHFSKWAVSSGSSTALLYSKRLITYRLRHLLRARCDASPVTNTTIQFHCDPSFWAQNIINLGSLVIEDKESQPQMPKQNPVVEQSSQPPGGLPSNQLSKFPTQISLAQLRLQHIQQQVMAQRQQVQRRPAPVGLPNPRMQGPIQQPSISHQHPPPRLINFQNHSPKPNGPVLPPYPQQLRYSPSQNVPRQTTIKPNPLQMAFLAQQAIKQWQISSVQAPPTTASSSSSTPSSPTITSAAGYDGKAFSSPMIDLSAPVGGSYNLPSLPDIDCSSTIMLDNIARKDTGVDHAQPRPPSNRTVQSPNSSVPSPGLAGPVTMTSVHPPIRSPSASSVGSRGSSGSSSKPAGADSTHKVPVVMLEPIRIKQENSGPPENYDFPVVIVKQESDEESRPQNTNYPRSILTSLLLNSSQSSASEETVLRSDAPDSTGDQPGLHQENSSNGKSEWSDASQKSPVHVGETRKEDDPNEDWCAVCQNGGELLCCEKCPKVFHLTCHVPTLTNFPSGEWICTFCRDLSKPEVDYDCDVPSHHSEKRKSEGLTKLTPIDKRKCERLLLFLYCHEMSLAFQDPVPLTVPDYYKIIKNPMDLSTIKKRLQEDYCMYTKPEDFVADFRLIFQNCAEFNEPDSEVANAGIKLESYFEELLKNLYPEKRFPKVEFRHEAEDCKFSDDSDDDFVQPRKKRLKSTEDRQLLK
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
37PhosphorylationESRQGPDSESGGEAS
HHCCCCCCCCCCHHH		36.4729514104
39PhosphorylationRQGPDSESGGEASRL
CCCCCCCCCCHHHHH		56.9322006019
72PhosphorylationKLLPCLHSFCQRCLP
HHHHHHHHHHHHHCC		18.1229899451
84PhosphorylationCLPAPQRYLMLTAPA
HCCCCCEEEEECCCC		7.3926643407
88PhosphorylationPQRYLMLTAPALGSA
CCEEEEECCCCCCCC		19.3426643407
94PhosphorylationLTAPALGSAETPPPA
ECCCCCCCCCCCCCC		24.6326643407
97PhosphorylationPALGSAETPPPAPAP
CCCCCCCCCCCCCCC		40.5926643407
110PhosphorylationAPAPAPGSPAGGPSP
CCCCCCCCCCCCCCC		15.5426643407
116PhosphorylationGSPAGGPSPFATQVG
CCCCCCCCCCCCEEE		35.6026643407
120PhosphorylationGGPSPFATQVGVIRC
CCCCCCCCEEEEEEC		24.9426643407
209PhosphorylationVRQKEEVSPEAVGVT
CCCCCCCCHHHCCCC		21.9428066266
469MethylationQISLAQLRLQHIQQQ
HHHHHHHHHHHHHHH		21.8824129315
539MethylationPPYPQQLRYSPSQNV
CCCCCCCCCCCCCCC		26.0830989569
540PhosphorylationPYPQQLRYSPSQNVP
CCCCCCCCCCCCCCC		33.2628066266
541PhosphorylationYPQQLRYSPSQNVPR
CCCCCCCCCCCCCCC		16.1928066266
543PhosphorylationQQLRYSPSQNVPRQT
CCCCCCCCCCCCCCC		28.5728066266
573PhosphorylationAIKQWQISSVQAPPT
HHHHCCCEECCCCCC		14.8925777480
574PhosphorylationIKQWQISSVQAPPTT
HHHCCCEECCCCCCC		21.6325777480
580PhosphorylationSSVQAPPTTASSSSS
EECCCCCCCCCCCCC		33.6625777480
581PhosphorylationSVQAPPTTASSSSST
ECCCCCCCCCCCCCC		30.2525777480
583PhosphorylationQAPPTTASSSSSTPS
CCCCCCCCCCCCCCC		28.7625777480
584PhosphorylationAPPTTASSSSSTPSS
CCCCCCCCCCCCCCC		31.6025777480
585PhosphorylationPPTTASSSSSTPSSP
CCCCCCCCCCCCCCC		26.3025777480
586PhosphorylationPTTASSSSSTPSSPT
CCCCCCCCCCCCCCC		39.9325777480
587PhosphorylationTTASSSSSTPSSPTI
CCCCCCCCCCCCCCC		46.4125777480
588PhosphorylationTASSSSSTPSSPTIT
CCCCCCCCCCCCCCC		29.1925777480
590PhosphorylationSSSSSTPSSPTITSA
CCCCCCCCCCCCCCC		49.3825777480
591PhosphorylationSSSSTPSSPTITSAA
CCCCCCCCCCCCCCC		27.5425777480
593PhosphorylationSSTPSSPTITSAAGY
CCCCCCCCCCCCCCC		38.5425777480
595PhosphorylationTPSSPTITSAAGYDG
CCCCCCCCCCCCCCC		18.1325777480
596PhosphorylationPSSPTITSAAGYDGK
CCCCCCCCCCCCCCC		16.5725777480
600PhosphorylationTITSAAGYDGKAFSS
CCCCCCCCCCCCCCC		19.4525777480
644PhosphorylationDNIARKDTGVDHAQP
HHHHCCCCCCCCCCC		41.9825195567
655PhosphorylationHAQPRPPSNRTVQSP
CCCCCCCCCCCCCCC		41.4426824392
658PhosphorylationPRPPSNRTVQSPNSS
CCCCCCCCCCCCCCC		27.4426643407
661PhosphorylationPSNRTVQSPNSSVPS
CCCCCCCCCCCCCCC		23.0121082442
664PhosphorylationRTVQSPNSSVPSPGL
CCCCCCCCCCCCCCC		35.7825293948
665PhosphorylationTVQSPNSSVPSPGLA
CCCCCCCCCCCCCCC		44.6926643407
668PhosphorylationSPNSSVPSPGLAGPV
CCCCCCCCCCCCCCE		29.4621082442
676PhosphorylationPGLAGPVTMTSVHPP
CCCCCCEEEEECCCC		20.1925293948
678PhosphorylationLAGPVTMTSVHPPIR
CCCCEEEEECCCCCC		20.4525293948
679PhosphorylationAGPVTMTSVHPPIRS
CCCEEEEECCCCCCC		13.9625293948
686PhosphorylationSVHPPIRSPSASSVG
ECCCCCCCCCCCCCC		24.7525293948
688PhosphorylationHPPIRSPSASSVGSR
CCCCCCCCCCCCCCC		41.8728066266
690PhosphorylationPIRSPSASSVGSRGS
CCCCCCCCCCCCCCC		29.8728066266
691PhosphorylationIRSPSASSVGSRGSS
CCCCCCCCCCCCCCC		30.1628066266
694PhosphorylationPSASSVGSRGSSGSS
CCCCCCCCCCCCCCC		31.1728066266
700PhosphorylationGSRGSSGSSSKPAGA
CCCCCCCCCCCCCCC		33.1327149854
724SumoylationMLEPIRIKQENSGPP
EEEEEEEECCCCCCC		41.53-
742SumoylationDFPVVIVKQESDEES
CCCEEEEECCCCCCC		36.90-
745PhosphorylationVVIVKQESDEESRPQ
EEEEECCCCCCCCCC		48.0724899341
749PhosphorylationKQESDEESRPQNTNY
ECCCCCCCCCCCCCC		47.4128066266
768PhosphorylationLTSLLLNSSQSSASE
HHHHHHCCCCCCCCC		29.7122006019
769PhosphorylationTSLLLNSSQSSASEE
HHHHHCCCCCCCCCC		32.77-
771PhosphorylationLLLNSSQSSASEETV
HHHCCCCCCCCCCEE		29.8029895711
772PhosphorylationLLNSSQSSASEETVL
HHCCCCCCCCCCEEE		28.3322006019
803PhosphorylationENSSNGKSEWSDASQ
CCCCCCCCCCCCCCC		45.7725619855
806PhosphorylationSNGKSEWSDASQKSP
CCCCCCCCCCCCCCC		21.1725619855
809PhosphorylationKSEWSDASQKSPVHV
CCCCCCCCCCCCCCC		43.0325619855
812PhosphorylationWSDASQKSPVHVGET
CCCCCCCCCCCCCCC		25.2325521595
819PhosphorylationSPVHVGETRKEDDPN
CCCCCCCCCCCCCCC		40.9025619855
1003UbiquitinationSYFEELLKNLYPEKR
HHHHHHHHHHCCCCC		58.49-
1026PhosphorylationEAEDCKFSDDSDDDF
CHHCCCCCCCCCCCC		26.4625521595
1029PhosphorylationDCKFSDDSDDDFVQP
CCCCCCCCCCCCCCH		48.1825521595
1043PhosphorylationPRKKRLKSTEDRQLL
HHHHHCCCHHHHHHC		41.4429895711
1044PhosphorylationRKKRLKSTEDRQLLK
HHHHCCCHHHHHHCC		40.0825266776
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 TIF1A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIF1A_MOUSE !!
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 TIF1A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBX5_MOUSECbx5physical
10562550
CBX1_MOUSECbx1physical
10562550
TIF1A_MOUSETrim24physical
10562550
ESR1_HUMANESR1physical
10022127
ZNF10_HUMANZNF10physical
10022127
TIF1B_HUMANTRIM28physical
10022127
TRI33_HUMANTRIM33physical
10022127
SRTD1_MOUSESertad1physical
11331592
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIF1A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-812; SER-1026 ANDSER-1029, AND MASS SPECTROMETRY.

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