NRIP1_MOUSE - dbPTM
NRIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRIP1_MOUSE
UniProt AC Q8CBD1
Protein Name Nuclear receptor-interacting protein 1
Gene Name Nrip1 {ECO:0000312|MGI:MGI:1315213}
Organism Mus musculus (Mouse).
Sequence Length 1161
Subcellular Localization Nucleus .
Protein Description Modulates transcriptional repression by nuclear hormone receptors such as NR2C1, thyroid hormone receptor and retinoic acid receptor/RARA. Essential for cumulus expansion and follicle rupture during ovulation. Also controls the balance between fat accumulation and energy expenditure. Positive regulator of the circadian clock gene expression: stimulates transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a coactivator for RORA and RORC..
Protein Sequence MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAINKKSAGHKEEDQNFNLSGSAFPSCQSNGPTVSTQTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIVNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHESLKVEKDLRCYGVASSHLKTLLKKSKTKDQKSGPTLPDVTPNLIRDSFVESSHPAVGQSGTKVMSEPLSCAARLQAVASMVEKRASPAASPKPSVACSQLALLLSSEAHLQQYSREHALKTQNAHQVASERLAAMARLQENGQKDVGSSQLSKGVSGHLNGQARALPASKLVANKNNAATFQSPMGVVPSSPKNTSYKNSLERNNLKQAANNSLLLHLLKSQTIPTPMNGHSQNERASSFESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRIEKPEAERPVSLENLTQSLLNTWDPKIPGVDIKEDQDTSTNSKLNSHQKVTLLQLLLGHKSEETVERNASPQDIHSDGTKFSPQNYTRTSVIESPSTNRTTPVSTPPLYTASQAESPINLSQHSLVIKWNSPPYACSTPASKLTNTAPSHLMDLTKGKESQAEKPAPSEGAQNSATFSASKLLQNLAQCGLQSSGPGEEQRPCKQLLSGNPDKPLGLIDRLNSPLLSNKTNAAEESKAFSSQPAGPEPGLPGCEIENLLERRTVLQLLLGNSSKGKNEKKEKTPARDEAPQEHSERAANEQILMVKIKSEPCDDFQTHNTNLPLNHDAKSAPFLGVTPAIHRSTAALPVSEDFKSEPASPQDFSFSKNGLLSRLLRQNQESYPADEQDKSHRNSELPTLESKNICMVPKKRKLYTEPLENPFKKMKNTAVDTANHHSGPEVLYGSLLHQEELKFSRNELDYKYPAGHSSASDGDHRSWARESKSFNVLKQLLLSENCVRDLSPHRSDSVPDTKKKGHKNNAPGSKPEFGISSLNGLMYSSPQPGSCVTDHRTFSYPGMVKTPLSPPFPEHLGCVGSRPEPGLLNGCSVPGEKGPIKWVIADMDKNEYEKDSPRLTKTNPILYYMLQKGGGNSVTTQETQDKDIWREPASAESLSQVTVKEELLPAAETKASFFNLRSPYNSHMGNNASRPHSTNGEVYGLLGNALTIKKESE
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
102PhosphorylationAAKRKRLSDSIVNLN
HHHHHHCCHHHCCCC		33.0918628823
104PhosphorylationKRKRLSDSIVNLNVK
HHHHCCHHHCCCCCC		25.6716093479
111AcetylationSIVNLNVKKEALLAG
HHCCCCCCHHHHHHC		43.7715879431
158AcetylationQQIRQSLKEQGYALS
HHHHHHHHHCCCCCC		53.9215879431
202PhosphorylationKDQKSGPTLPDVTPN
CCCCCCCCCCCCCHH		55.2216093479
207PhosphorylationGPTLPDVTPNLIRDS
CCCCCCCCHHHHHHH		17.5316093479
218PhosphorylationIRDSFVESSHPAVGQ
HHHHHHHCCCCCCCC		28.75-
240MethylationEPLSCAARLQAVASM
CCCHHHHHHHHHHHH		14.604726609
253PhosphorylationSMVEKRASPAASPKP
HHHHHHCCCCCCCCH		21.0726643407
257PhosphorylationKRASPAASPKPSVAC
HHCCCCCCCCHHHHH		35.2526643407
261PhosphorylationPAASPKPSVACSQLA
CCCCCCHHHHHHHHH		28.5926643407
265PhosphorylationPKPSVACSQLALLLS
CCHHHHHHHHHHHHC		20.6326643407
287AcetylationYSREHALKTQNAHQV
HHHHHHHHHCCHHHH		49.1715879431
311AcetylationRLQENGQKDVGSSQL
HHHHCCCCCCCHHHH		56.6415879431
347PhosphorylationANKNNAATFQSPMGV
CCCCCCCCCCCCCCC		21.5726643407
350PhosphorylationNNAATFQSPMGVVPS
CCCCCCCCCCCCCCC		16.8026643407
357PhosphorylationSPMGVVPSSPKNTSY
CCCCCCCCCCCCCCC		47.8926745281
358PhosphorylationPMGVVPSSPKNTSYK
CCCCCCCCCCCCCCC		33.5526239621
364PhosphorylationSSPKNTSYKNSLERN
CCCCCCCCCCHHHHC		16.4922388040
380PhosphorylationLKQAANNSLLLHLLK
HHHHHHHHHHHHHHH		21.8716093479
418PhosphorylationTPTTIDEYSDNNPSF
CCCCHHHCCCCCCCC		19.9922388040
429PhosphorylationNPSFTDDSSGDESSY
CCCCCCCCCCCCCCC		38.74-
436PhosphorylationSSGDESSYSNCVPID
CCCCCCCCCCEEECC		17.1222388040
447AcetylationVPIDLSCKHRIEKPE
EECCCCCCCCCCCCC		32.3260283
482AcetylationKIPGVDIKEDQDTST
CCCCCCCCCCCCCCC		51.2615879431
488PhosphorylationIKEDQDTSTNSKLNS
CCCCCCCCCCHHCCH		33.6022817900
510PhosphorylationQLLLGHKSEETVERN
HHHHCCCCHHHHHCC		34.6819060867
519PhosphorylationETVERNASPQDIHSD
HHHHCCCCHHHCCCC		27.0023684622
525PhosphorylationASPQDIHSDGTKFSP
CCHHHCCCCCCCCCC		37.7626643407
528PhosphorylationQDIHSDGTKFSPQNY
HHCCCCCCCCCCCCC		33.6326643407
529AcetylationDIHSDGTKFSPQNYT
HCCCCCCCCCCCCCC		49.7415879431
531PhosphorylationHSDGTKFSPQNYTRT
CCCCCCCCCCCCCEE		27.4226643407
535PhosphorylationTKFSPQNYTRTSVIE
CCCCCCCCCEEEEEE		7.7326643407
536PhosphorylationKFSPQNYTRTSVIES
CCCCCCCCEEEEEEC		34.7126643407
538PhosphorylationSPQNYTRTSVIESPS
CCCCCCEEEEEECCC		21.3926643407
539PhosphorylationPQNYTRTSVIESPST
CCCCCEEEEEECCCC		20.1526643407
543PhosphorylationTRTSVIESPSTNRTT
CEEEEEECCCCCCCC		17.0226643407
545PhosphorylationTSVIESPSTNRTTPV
EEEEECCCCCCCCCC		47.8226643407
546PhosphorylationSVIESPSTNRTTPVS
EEEECCCCCCCCCCC		31.9126643407
549PhosphorylationESPSTNRTTPVSTPP
ECCCCCCCCCCCCCC		37.2126643407
550PhosphorylationSPSTNRTTPVSTPPL
CCCCCCCCCCCCCCC		20.6126643407
553PhosphorylationTNRTTPVSTPPLYTA
CCCCCCCCCCCCCCC		36.0826643407
554PhosphorylationNRTTPVSTPPLYTAS
CCCCCCCCCCCCCCC		29.2026643407
558PhosphorylationPVSTPPLYTASQAES
CCCCCCCCCCCCCCC		13.1626643407
559PhosphorylationVSTPPLYTASQAESP
CCCCCCCCCCCCCCC		27.7626643407
561PhosphorylationTPPLYTASQAESPIN
CCCCCCCCCCCCCCC		23.3226643407
565PhosphorylationYTASQAESPINLSQH
CCCCCCCCCCCCCCC		33.8126643407
570PhosphorylationAESPINLSQHSLVIK
CCCCCCCCCCEEEEE		22.7426643407
573PhosphorylationPINLSQHSLVIKWNS
CCCCCCCEEEEECCC		19.3926643407
580PhosphorylationSLVIKWNSPPYACST
EEEEECCCCCCCCCC		26.5726643407
586PhosphorylationNSPPYACSTPASKLT
CCCCCCCCCCHHHHC		29.2926643407
587PhosphorylationSPPYACSTPASKLTN
CCCCCCCCCHHHHCC		23.8226643407
591MethylationACSTPASKLTNTAPS
CCCCCHHHHCCCCCH		62.53-
595PhosphorylationPASKLTNTAPSHLMD
CHHHHCCCCCHHHHH		34.4129899451
598PhosphorylationKLTNTAPSHLMDLTK
HHCCCCCHHHHHHHC		27.1329899451
607AcetylationLMDLTKGKESQAEKP
HHHHHCCCHHCCCCC		56.6015879431
650MethylationSGPGEEQRPCKQLLS
CCCCCCCCCCHHHHC		41.694726605
653MethylationGEEQRPCKQLLSGNP
CCCCCCCHHHHCCCC		46.81-
672PhosphorylationGLIDRLNSPLLSNKT
CHHHHCCCHHHCCCC		22.8627180971
778MethylationLPLNHDAKSAPFLGV
CCCCCCHHCCCCCCC		53.89-
792PhosphorylationVTPAIHRSTAALPVS
CCHHHCCCCCCCCCC		14.2929472430
793PhosphorylationTPAIHRSTAALPVSE
CHHHCCCCCCCCCCC		18.8629472430
799PhosphorylationSTAALPVSEDFKSEP
CCCCCCCCCCCCCCC		29.5223984901
804PhosphorylationPVSEDFKSEPASPQD
CCCCCCCCCCCCCCC		49.1328833060
808PhosphorylationDFKSEPASPQDFSFS
CCCCCCCCCCCCCCC		33.5323684622
813PhosphorylationPASPQDFSFSKNGLL
CCCCCCCCCCHHCHH		36.5828833060
815PhosphorylationSPQDFSFSKNGLLSR
CCCCCCCCHHCHHHH		24.8223984901
863PhosphorylationVPKKRKLYTEPLENP
EECCCCCCCCCCCCH		16.46-
864PhosphorylationPKKRKLYTEPLENPF
ECCCCCCCCCCCCHH		41.38-
932AcetylationRSWARESKSFNVLKQ
HHHHHHCHHHHHHHH		55.0715879431
948MethylationLLSENCVRDLSPHRS
HHCCCCCHHCCCCCC		41.164726601
951PhosphorylationENCVRDLSPHRSDSV
CCCCHHCCCCCCCCC		23.9727681418
955PhosphorylationRDLSPHRSDSVPDTK
HHCCCCCCCCCCCHH		31.0729550500
957PhosphorylationLSPHRSDSVPDTKKK
CCCCCCCCCCCHHCC		36.4729550500
1003PhosphorylationVTDHRTFSYPGMVKT
CCCCCCCCCCCCCCC		29.7918628823
1010PhosphorylationSYPGMVKTPLSPPFP
CCCCCCCCCCCCCCC		20.3226643407
1013PhosphorylationGMVKTPLSPPFPEHL
CCCCCCCCCCCCCCC		31.5626643407
1025PhosphorylationEHLGCVGSRPEPGLL
CCCCCCCCCCCCCCC		25.0226643407
1060PhosphorylationKNEYEKDSPRLTKTN
CCCCCCCCCCCCCCC		24.0022871156
1064PhosphorylationEKDSPRLTKTNPILY
CCCCCCCCCCCHHHH		36.7822871156
1117PhosphorylationELLPAAETKASFFNL
HHHCHHHHHHHHCCC		27.4725367039
1120PhosphorylationPAAETKASFFNLRSP
CHHHHHHHHCCCCCC		31.7425367039
1126PhosphorylationASFFNLRSPYNSHMG
HHHCCCCCCCCCCCC		34.6025367039
1128PhosphorylationFFNLRSPYNSHMGNN
HCCCCCCCCCCCCCC		30.4625367039
1130PhosphorylationNLRSPYNSHMGNNAS
CCCCCCCCCCCCCCC		14.7025367039
1137PhosphorylationSHMGNNASRPHSTNG
CCCCCCCCCCCCCCC		48.7625367039
1141PhosphorylationNNASRPHSTNGEVYG
CCCCCCCCCCCCCEE		26.6725367039
1142PhosphorylationNASRPHSTNGEVYGL
CCCCCCCCCCCCEEE		44.1825367039
1147PhosphorylationHSTNGEVYGLLGNAL
CCCCCCCEEEECCEE		9.5825367039
1155PhosphorylationGLLGNALTIKKESE-
EEECCEEEEECCCC-		28.4825367039
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
102SPhosphorylationKinasePRKCEP16054
GPS
202TPhosphorylationKinaseMAPK1P28482
GPS
207TPhosphorylationKinaseMAPK1P28482
GPS
364YPhosphorylationKinaseSYKP43405
PSP
418YPhosphorylationKinaseSYKP43405
PSP
436YPhosphorylationKinaseSYKP43405
PSP
1003SPhosphorylationKinasePRKCEP16054
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRIP1_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 NRIP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBP1_HUMANCTBP1physical
11509661
HDAC3_HUMANHDAC3physical
11006275
HDAC1_HUMANHDAC1physical
11006275
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRIP1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Receptor interacting protein 140 as a thyroid hormone-dependent,negative co-regulator for the induction of cellular retinoic acidbinding protein I gene.";
Wei L.-N., Hu X.;
Mol. Cell. Endocrinol. 218:39-48(2004).
Cited for: FUNCTION.
"Post-translational modification of nuclear co-repressor receptor-interacting protein 140 by acetylation.";
Huq M.D.M., Wei L.-N.;
Mol. Cell. Proteomics 4:975-983(2005).
Cited for: PROTEIN SEQUENCE OF 101-112; 155-170; 283-298; 305-320; 476-492;517-537; 606-630 AND 930-938, MASS SPECTROMETRY, SUBCELLULAR LOCATION,AND ACETYLATION AT LYS-111; LYS-158; LYS-287; LYS-311; LYS-482;LYS-529; LYS-607 AND LYS-932.
Phosphorylation
ReferencePubMed
"Mapping of phosphorylation sites of nuclear corepressor receptorinteracting protein 140 by liquid chromatography-tandem massspectroscopy.";
Huq M.D.M., Khan S.A., Park S.W., Wei L.-N.;
Proteomics 5:2157-2166(2005).
Cited for: PROTEIN SEQUENCE OF 101-112; 199-212; 343-360; 375-387; 476-492;517-548; 670-678 AND 1001-1009, MASS SPECTROMETRY, AND PHOSPHORYLATIONAT SER-104; THR-207; SER-358; SER-380; SER-488; SER-519; SER-531;SER-543; SER-672 AND SER-1003.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory