LRIF1_HUMAN - dbPTM
LRIF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRIF1_HUMAN
UniProt AC Q5T3J3
Protein Name Ligand-dependent nuclear receptor-interacting factor 1
Gene Name LRIF1
Organism Homo sapiens (Human).
Sequence Length 769
Subcellular Localization Nucleus matrix .
Protein Description Represses the ligand-induced transcriptional activity of retinoic acid receptor alpha (RARA). This repression may occur through direct recruitment of histone deacetylases..
Protein Sequence MSNNLRRVFLKPAEENSGNASRCVSGCMYQVVQTIGSDGKNLLQLLPIPKSSGNLIPLVQSSVMSDALKGNTGKPVQVTFQTQISSSSTSASVQLPIFQPASSSNYFLTRTVDTSEKGRVTSVGTGNFSSSVSKVQSHGVKIDGLTMQTFAVPPSTQKDSSFIVVNTQSLPVTVKSPVLPSGHHLQIPAHAEVKSVPASSLPPSVQQKILATATTSTSGMVEASQMPTVIYVSPVNTVKNVVTKNFQNIYPKPVTEIAKPVILNTTQIPKNVATETQLKGGQHSQAAPVKWIFQDNLQPFTPSLVPVKSSNNVASKILKTFVDRKNLGDNTINMPPLSTIDPSGTRSKNMPIKDNALVMFNGKVYLLAKKGTDVLPSQIDQQNSVSPDTPVRKDTLQTVSSSPVTEISREVVNIVLAKSKSSQMETKSLSNTQLASMANLRAEKNKVEKPSPSTTNPHMNQSSNYLKQSKTLFTNPIFPVGFSTGHNAPRKVTAVIYARKGSVLQSIEKISSSVDATTVTSQQCVFRDQEPKIHNEMASTSDKGAQGRNDKKDSQGRSNKALHLKSDAEFKKIFGLTKDLRVCLTRIPDHLTSGEGFDSFSSLVKSGTYKETEFMVKEGERKQQNFDKKRKAKTNKKMDHIKKRKTENAYNAIINGEANVTGSQLLSSILPTSDVSQHNILTSHSKTRQEKRTEMEYYTHEKQEKGTLNSNAAYEQSHFFNKNYTEDIFPVTPPELEETIRDEKIRRLKQVLREKEAALEEMRKKMHQK
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
2Phosphorylation------MSNNLRRVF
------CCCCCCEEE
34.1329978859
7Ubiquitination-MSNNLRRVFLKPAE
-CCCCCCEEECCCCC
27.0622817900
11SumoylationNLRRVFLKPAEENSG
CCCEEECCCCCCCCC
30.62-
11AcetylationNLRRVFLKPAEENSG
CCCEEECCCCCCCCC
30.6226051181
11SumoylationNLRRVFLKPAEENSG
CCCEEECCCCCCCCC
30.62-
11UbiquitinationNLRRVFLKPAEENSG
CCCEEECCCCCCCCC
30.6221906983
11 (in isoform 1)Ubiquitination-30.6221906983
17PhosphorylationLKPAEENSGNASRCV
CCCCCCCCCCHHHHH
36.3825262027
21PhosphorylationEENSGNASRCVSGCM
CCCCCCHHHHHHHHH
30.1625262027
29UbiquitinationRCVSGCMYQVVQTIG
HHHHHHHHHHHHHHC
11.3929967540
50UbiquitinationLQLLPIPKSSGNLIP
HHHEECCCCCCCCHH
58.95-
51O-linked_GlycosylationQLLPIPKSSGNLIPL
HHEECCCCCCCCHHH
37.8230059200
52O-linked_GlycosylationLLPIPKSSGNLIPLV
HEECCCCCCCCHHHH
37.5130059200
65O-linked_GlycosylationLVQSSVMSDALKGNT
HHHHHHHHHHHCCCC
19.9930059200
65PhosphorylationLVQSSVMSDALKGNT
HHHHHHHHHHHCCCC
19.9918669648
69UbiquitinationSVMSDALKGNTGKPV
HHHHHHHCCCCCCCE
52.4121963094
69 (in isoform 2)Ubiquitination-52.4121906983
72O-linked_GlycosylationSDALKGNTGKPVQVT
HHHHCCCCCCCEEEE
56.0830059200
74UbiquitinationALKGNTGKPVQVTFQ
HHCCCCCCCEEEEEE
39.7222817900
85O-linked_GlycosylationVTFQTQISSSSTSAS
EEEEEEECCCCCCCE
17.8530059200
89O-linked_GlycosylationTQISSSSTSASVQLP
EEECCCCCCCEEEEE
30.2030059200
90O-linked_GlycosylationQISSSSTSASVQLPI
EECCCCCCCEEEEEE
22.0930059200
107UbiquitinationPASSSNYFLTRTVDT
CCCCCCEEEEEEEEC
7.0322505724
122PhosphorylationSEKGRVTSVGTGNFS
CCCCCEEEEECCCCC
18.72-
134UbiquitinationNFSSSVSKVQSHGVK
CCCCCCHHHHHCCEE
41.9822505724
160PhosphorylationPPSTQKDSSFIVVNT
CCCCCCCCCEEEEEC
33.9027690223
161PhosphorylationPSTQKDSSFIVVNTQ
CCCCCCCCEEEEECC
29.1727690223
166UbiquitinationDSSFIVVNTQSLPVT
CCCEEEEECCCCCEE
22.8529967540
175UbiquitinationQSLPVTVKSPVLPSG
CCCCEEEECCCCCCC
39.41-
176PhosphorylationSLPVTVKSPVLPSGH
CCCEEEECCCCCCCC
18.8625849741
186UbiquitinationLPSGHHLQIPAHAEV
CCCCCCCCCCCCEEE
34.9529967540
194UbiquitinationIPAHAEVKSVPASSL
CCCCEEECCCCHHHC
36.9229967540
208UbiquitinationLPPSVQQKILATATT
CCHHHHHHHHHHEEC
23.6929967540
214PhosphorylationQKILATATTSTSGMV
HHHHHHEECCCCCCC
19.54-
215PhosphorylationKILATATTSTSGMVE
HHHHHEECCCCCCCC
27.78-
219UbiquitinationTATTSTSGMVEASQM
HEECCCCCCCCHHHC
25.0130230243
244SumoylationTVKNVVTKNFQNIYP
CHHHHHCCCCCCCCC
44.12-
244SumoylationTVKNVVTKNFQNIYP
CHHHHHCCCCCCCCC
44.12-
244UbiquitinationTVKNVVTKNFQNIYP
CHHHHHCCCCCCCCC
44.1229967540
250PhosphorylationTKNFQNIYPKPVTEI
CCCCCCCCCCCHHHC
16.8630622161
252UbiquitinationNFQNIYPKPVTEIAK
CCCCCCCCCHHHCCC
34.8421963094
255PhosphorylationNIYPKPVTEIAKPVI
CCCCCCHHHCCCCEE
30.1530622161
259SumoylationKPVTEIAKPVILNTT
CCHHHCCCCEEECCC
45.54-
259SumoylationKPVTEIAKPVILNTT
CCHHHCCCCEEECCC
45.5428112733
259UbiquitinationKPVTEIAKPVILNTT
CCHHHCCCCEEECCC
45.5429967540
263UbiquitinationEIAKPVILNTTQIPK
HCCCCEEECCCCCCC
4.7922505724
270SumoylationLNTTQIPKNVATETQ
ECCCCCCCCCCCCCC
66.73-
270SumoylationLNTTQIPKNVATETQ
ECCCCCCCCCCCCCC
66.73-
279SumoylationVATETQLKGGQHSQA
CCCCCCCCCCCCCCC
51.70-
279MethylationVATETQLKGGQHSQA
CCCCCCCCCCCCCCC
51.7042341213
279SumoylationVATETQLKGGQHSQA
CCCCCCCCCCCCCCC
51.7028112733
279UbiquitinationVATETQLKGGQHSQA
CCCCCCCCCCCCCCC
51.7021906983
279 (in isoform 1)Ubiquitination-51.7021906983
281UbiquitinationTETQLKGGQHSQAAP
CCCCCCCCCCCCCCC
22.0521963094
290SumoylationHSQAAPVKWIFQDNL
CCCCCCCEEEECCCC
33.25-
290AcetylationHSQAAPVKWIFQDNL
CCCCCCCEEEECCCC
33.2519608861
290SumoylationHSQAAPVKWIFQDNL
CCCCCCCEEEECCCC
33.2519608861
290UbiquitinationHSQAAPVKWIFQDNL
CCCCCCCEEEECCCC
33.2529967540
298UbiquitinationWIFQDNLQPFTPSLV
EEECCCCCCCCCCCC
37.0022505724
308SumoylationTPSLVPVKSSNNVAS
CCCCCCCCCCCCHHH
41.94-
308SumoylationTPSLVPVKSSNNVAS
CCCCCCCCCCCCHHH
41.94-
308UbiquitinationTPSLVPVKSSNNVAS
CCCCCCCCCCCCHHH
41.9421963094
316SumoylationSSNNVASKILKTFVD
CCCCHHHHHHHHHHH
42.17-
316AcetylationSSNNVASKILKTFVD
CCCCHHHHHHHHHHH
42.1725953088
316SumoylationSSNNVASKILKTFVD
CCCCHHHHHHHHHHH
42.17-
316UbiquitinationSSNNVASKILKTFVD
CCCCHHHHHHHHHHH
42.1729967540
319SumoylationNVASKILKTFVDRKN
CHHHHHHHHHHHHCC
43.31-
319SumoylationNVASKILKTFVDRKN
CHHHHHHHHHHHHCC
43.31-
319UbiquitinationNVASKILKTFVDRKN
CHHHHHHHHHHHHCC
43.3129967540
325TrimethylationLKTFVDRKNLGDNTI
HHHHHHHCCCCCCCC
52.65-
325MethylationLKTFVDRKNLGDNTI
HHHHHHHCCCCCCCC
52.65-
325UbiquitinationLKTFVDRKNLGDNTI
HHHHHHHCCCCCCCC
52.6522505724
342UbiquitinationPPLSTIDPSGTRSKN
CCCCCCCCCCCCCCC
30.7021963094
343UbiquitinationPLSTIDPSGTRSKNM
CCCCCCCCCCCCCCC
49.3922817900
348UbiquitinationDPSGTRSKNMPIKDN
CCCCCCCCCCCCCCC
54.7129967540
353SumoylationRSKNMPIKDNALVMF
CCCCCCCCCCEEEEE
38.77-
353SumoylationRSKNMPIKDNALVMF
CCCCCCCCCCEEEEE
38.77-
353UbiquitinationRSKNMPIKDNALVMF
CCCCCCCCCCEEEEE
38.7729967540
366UbiquitinationMFNGKVYLLAKKGTD
EECCEEEEEEECCCC
4.1422505724
369UbiquitinationGKVYLLAKKGTDVLP
CEEEEEEECCCCCCC
52.2721963094
370SumoylationKVYLLAKKGTDVLPS
EEEEEEECCCCCCCH
62.53-
370SumoylationKVYLLAKKGTDVLPS
EEEEEEECCCCCCCH
62.53-
370UbiquitinationKVYLLAKKGTDVLPS
EEEEEEECCCCCCCH
62.5322817900
384PhosphorylationSQIDQQNSVSPDTPV
HHHCCCCCCCCCCCC
21.4525850435
386PhosphorylationIDQQNSVSPDTPVRK
HCCCCCCCCCCCCCH
19.5130576142
389PhosphorylationQNSVSPDTPVRKDTL
CCCCCCCCCCCHHHH
27.3721815630
393UbiquitinationSPDTPVRKDTLQTVS
CCCCCCCHHHHHHHC
56.1322505724
398PhosphorylationVRKDTLQTVSSSPVT
CCHHHHHHHCCCCCH
26.0127174698
400PhosphorylationKDTLQTVSSSPVTEI
HHHHHHHCCCCCHHH
28.6125159151
401PhosphorylationDTLQTVSSSPVTEIS
HHHHHHCCCCCHHHH
34.0329255136
402PhosphorylationTLQTVSSSPVTEISR
HHHHHCCCCCHHHHH
18.8429255136
405PhosphorylationTVSSSPVTEISREVV
HHCCCCCHHHHHHHH
30.8729255136
408PhosphorylationSSPVTEISREVVNIV
CCCCHHHHHHHHHHH
19.0224732914
417UbiquitinationEVVNIVLAKSKSSQM
HHHHHHHCCCCCCCC
11.8122817900
418SumoylationVVNIVLAKSKSSQME
HHHHHHCCCCCCCCC
55.01-
418SumoylationVVNIVLAKSKSSQME
HHHHHHCCCCCCCCC
55.01-
418UbiquitinationVVNIVLAKSKSSQME
HHHHHHCCCCCCCCC
55.0129967540
419UbiquitinationVNIVLAKSKSSQMET
HHHHHCCCCCCCCCC
31.9621963094
422PhosphorylationVLAKSKSSQMETKSL
HHCCCCCCCCCCCCC
36.9620860994
422UbiquitinationVLAKSKSSQMETKSL
HHCCCCCCCCCCCCC
36.9622817900
427SumoylationKSSQMETKSLSNTQL
CCCCCCCCCCCHHHH
35.77-
427SumoylationKSSQMETKSLSNTQL
CCCCCCCCCCCHHHH
35.77-
427UbiquitinationKSSQMETKSLSNTQL
CCCCCCCCCCCHHHH
35.7729967540
428PhosphorylationSSQMETKSLSNTQLA
CCCCCCCCCCHHHHH
44.4423186163
430PhosphorylationQMETKSLSNTQLASM
CCCCCCCCHHHHHHH
44.9423917254
432PhosphorylationETKSLSNTQLASMAN
CCCCCCHHHHHHHHH
22.9123186163
436PhosphorylationLSNTQLASMANLRAE
CCHHHHHHHHHHHHH
27.3323917254
440UbiquitinationQLASMANLRAEKNKV
HHHHHHHHHHHHCCC
3.8922817900
443UbiquitinationSMANLRAEKNKVEKP
HHHHHHHHHCCCCCC
51.2121963094
444UbiquitinationMANLRAEKNKVEKPS
HHHHHHHHCCCCCCC
62.1722817900
446SumoylationNLRAEKNKVEKPSPS
HHHHHHCCCCCCCCC
63.9428112733
446UbiquitinationNLRAEKNKVEKPSPS
HHHHHHCCCCCCCCC
63.9421963094
449UbiquitinationAEKNKVEKPSPSTTN
HHHCCCCCCCCCCCC
54.5022817900
451PhosphorylationKNKVEKPSPSTTNPH
HCCCCCCCCCCCCCC
42.4225159151
467MethylationNQSSNYLKQSKTLFT
CCCCHHHHHCCCCCC
42.01115972601
467UbiquitinationNQSSNYLKQSKTLFT
CCCCHHHHHCCCCCC
42.0122817900
470UbiquitinationSNYLKQSKTLFTNPI
CHHHHHCCCCCCCCC
46.9121963094
491SumoylationTGHNAPRKVTAVIYA
CCCCCCCEEEEEEEE
42.76-
491SumoylationTGHNAPRKVTAVIYA
CCCCCCCEEEEEEEE
42.76-
491UbiquitinationTGHNAPRKVTAVIYA
CCCCCCCEEEEEEEE
42.76-
493PhosphorylationHNAPRKVTAVIYARK
CCCCCEEEEEEEECC
20.45-
500SumoylationTAVIYARKGSVLQSI
EEEEEECCCCHHHHH
47.57-
500SumoylationTAVIYARKGSVLQSI
EEEEEECCCCHHHHH
47.57-
500UbiquitinationTAVIYARKGSVLQSI
EEEEEECCCCHHHHH
47.5729967540
502PhosphorylationVIYARKGSVLQSIEK
EEEECCCCHHHHHHH
23.7723401153
506PhosphorylationRKGSVLQSIEKISSS
CCCCHHHHHHHHHCC
28.6726074081
509UbiquitinationSVLQSIEKISSSVDA
CHHHHHHHHHCCCCC
46.3329967540
516UbiquitinationKISSSVDATTVTSQQ
HHHCCCCCCEECCEE
11.7421963094
532UbiquitinationVFRDQEPKIHNEMAS
EECCCCCCCCCHHCC
56.71-
539PhosphorylationKIHNEMASTSDKGAQ
CCCCHHCCCCCCCCC
27.4221406692
540PhosphorylationIHNEMASTSDKGAQG
CCCHHCCCCCCCCCC
31.2621406692
541PhosphorylationHNEMASTSDKGAQGR
CCHHCCCCCCCCCCC
34.5321406692
543AcetylationEMASTSDKGAQGRND
HHCCCCCCCCCCCCC
56.7825953088
543UbiquitinationEMASTSDKGAQGRND
HHCCCCCCCCCCCCC
56.7821906983
543 (in isoform 1)Ubiquitination-56.7821906983
554PhosphorylationGRNDKKDSQGRSNKA
CCCCCCCCCCCCCCH
43.3320068231
558PhosphorylationKKDSQGRSNKALHLK
CCCCCCCCCCHHHCC
49.8920068231
565SumoylationSNKALHLKSDAEFKK
CCCHHHCCCHHHHHH
35.23-
565SumoylationSNKALHLKSDAEFKK
CCCHHHCCCHHHHHH
35.23-
565UbiquitinationSNKALHLKSDAEFKK
CCCHHHCCCHHHHHH
35.2329967540
578UbiquitinationKKIFGLTKDLRVCLT
HHHHCCCCCHHHHHH
60.8621963094
583UbiquitinationLTKDLRVCLTRIPDH
CCCCHHHHHHCCCCC
2.3122817900
599PhosphorylationTSGEGFDSFSSLVKS
CCCCCHHHHHHHHHC
25.4325159151
601PhosphorylationGEGFDSFSSLVKSGT
CCCHHHHHHHHHCCC
27.0618669648
602PhosphorylationEGFDSFSSLVKSGTY
CCHHHHHHHHHCCCC
34.8623186163
605SumoylationDSFSSLVKSGTYKET
HHHHHHHHCCCCCCE
48.7628112733
605UbiquitinationDSFSSLVKSGTYKET
HHHHHHHHCCCCCCE
48.7621963094
605 (in isoform 1)Ubiquitination-48.7621906983
609PhosphorylationSLVKSGTYKETEFMV
HHHHCCCCCCEEEEC
15.4522817900
610UbiquitinationLVKSGTYKETEFMVK
HHHCCCCCCEEEECC
58.9822817900
617UbiquitinationKETEFMVKEGERKQQ
CCEEEECCCCHHHHH
48.49-
697PhosphorylationEKRTEMEYYTHEKQE
HHHHHHHHHCHHCCC
16.6227642862
698PhosphorylationKRTEMEYYTHEKQEK
HHHHHHHHCHHCCCC
6.5723403867
699PhosphorylationRTEMEYYTHEKQEKG
HHHHHHHCHHCCCCC
23.7427642862
702SumoylationMEYYTHEKQEKGTLN
HHHHCHHCCCCCCCC
57.03-
702PhosphorylationMEYYTHEKQEKGTLN
HHHHCHHCCCCCCCC
57.0319081932
702SumoylationMEYYTHEKQEKGTLN
HHHHCHHCCCCCCCC
57.0325218447
702UbiquitinationMEYYTHEKQEKGTLN
HHHHCHHCCCCCCCC
57.0329967540
705UbiquitinationYTHEKQEKGTLNSNA
HCHHCCCCCCCCCCH
55.49-
707PhosphorylationHEKQEKGTLNSNAAY
HHCCCCCCCCCCHHH
33.5628555341
710PhosphorylationQEKGTLNSNAAYEQS
CCCCCCCCCHHHHHH
30.8425627689
714PhosphorylationTLNSNAAYEQSHFFN
CCCCCHHHHHHHCCC
16.4625394399
722UbiquitinationEQSHFFNKNYTEDIF
HHHHCCCCCCCCCCC
46.2929967540
732PhosphorylationTEDIFPVTPPELEET
CCCCCCCCCHHHHHH
33.1117455211
739PhosphorylationTPPELEETIRDEKIR
CCHHHHHHHCHHHHH
16.3722199227
744UbiquitinationEETIRDEKIRRLKQV
HHHHCHHHHHHHHHH
45.8929967540
755UbiquitinationLKQVLREKEAALEEM
HHHHHHHHHHHHHHH
46.3430230243

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 LRIF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRIF1_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 LRIF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RARA_HUMANRARAphysical
17455211
ESR1_HUMANESR1physical
17455211
RORA_HUMANRORAphysical
17455211
PPARG_HUMANPPARGphysical
17455211
THB_HUMANTHRBphysical
17455211
GCR_HUMANNR3C1physical
17455211
KBTB7_HUMANKBTBD7physical
15383276
GASP2_HUMANGPRASP2physical
15383276
LRIF1_HUMANLRIF1physical
15383276
HAP1_HUMANHAP1physical
15383276
MVD1_HUMANMVDphysical
26496610
PPM1G_HUMANPPM1Gphysical
26496610
CAF1B_HUMANCHAF1Bphysical
26496610
DCTN3_HUMANDCTN3physical
26496610
DDX42_HUMANDDX42physical
26496610
DJC13_HUMANDNAJC13physical
26496610
SMHD1_HUMANSMCHD1physical
26496610
HAUS5_HUMANHAUS5physical
26496610
SPN90_HUMANNCKIPSDphysical
26496610
MTHSD_HUMANMTHFSDphysical
26496610
OSBL5_HUMANOSBPL5physical
26496610

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 LRIF1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-290, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-402; SER-599 ANDTHR-732, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND MASSSPECTROMETRY.

TOP