Tag | Content |
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CPLM ID | CPLM-016776 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nuclear receptor-interacting protein 1 |
Protein Synonyms/Alias | Nuclear factor RIP140; Receptor-interacting protein 140 |
Gene Name | Nrip1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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111 | SIVNLNVKKEALLAG | acetylation | [1] | 158 | QQIRQSLKEQGYALS | acetylation | [1, 2] | 287 | YSREHALKTQNAHQV | acetylation | [1, 2] | 311 | RLQENGQKDVGSSQL | acetylation | [1] | 482 | KIPGVDIKEDQDTST | acetylation | [1] | 529 | DIHSDGTKFSPQNYT | acetylation | [1] | 607 | LMDLTKGKESQAEKP | acetylation | [1] | 932 | RSWARESKSFNVLKQ | acetylation | [1] |
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Reference | [1] Post-translational modification of nuclear co-repressor receptor-interacting protein 140 by acetylation. Huq MD, Wei LN. Mol Cell Proteomics. 2005 Jul;4(7):975-83. [ PMID: 15879431] [2] Modulation of lysine acetylation-stimulated repressive activity by Erk2-mediated phosphorylation of RIP140 in adipocyte differentiation. Ho PC, Gupta P, Tsui YC, Ha SG, Huq M, Wei LN. Cell Signal. 2008 Oct;20(10):1911-9. [ PMID: 18655826] |
Functional 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. |
Sequence Annotation | REGION 1 416 Interaction with ZNF366 (By similarity). REGION 78 335 Repression domain 1 (By similarity). REGION 411 701 Repression domain 2 (By similarity). REGION 432 473 Required for targeting to small nuclear REGION 736 886 Repression domain 3 (By similarity). REGION 754 1161 Interaction with ZNF366 (By similarity). REGION 1063 1076 Ligand-dependent nuclear receptor REGION 1121 1161 Repression domain 4 (By similarity). MOTIF 21 25 LXXLL motif 1. MOTIF 133 137 LXXLL motif 2. MOTIF 185 189 LXXLL motif 3. MOTIF 267 271 LXXLL motif 4. MOTIF 382 386 LXXLL motif 5. MOTIF 441 447 CTBP-binding; principal site (By MOTIF 501 505 LXXLL motif 6. MOTIF 566 570 CTBP-binding (By similarity). MOTIF 714 718 LXXLL motif 7. MOTIF 820 824 LXXLL motif 8. MOTIF 937 941 LXXLL motif 9. MOTIF 947 951 CTBP-binding (By similarity). MOD_RES 104 104 Phosphoserine. MOD_RES 111 111 N6-acetyllysine. MOD_RES 158 158 N6-acetyllysine. MOD_RES 207 207 Phosphothreonine. MOD_RES 287 287 N6-acetyllysine. MOD_RES 311 311 N6-acetyllysine. MOD_RES 358 358 Phosphoserine. MOD_RES 380 380 Phosphoserine. MOD_RES 447 447 N6-acetyllysine (By similarity). MOD_RES 482 482 N6-acetyllysine. MOD_RES 488 488 Phosphoserine. MOD_RES 519 519 Phosphoserine. MOD_RES 529 529 N6-acetyllysine. MOD_RES 531 531 Phosphoserine. MOD_RES 543 543 Phosphoserine. MOD_RES 607 607 N6-acetyllysine. MOD_RES 672 672 Phosphoserine. MOD_RES 932 932 N6-acetyllysine. MOD_RES 1003 1003 Phosphoserine. |
Keyword | Acetylation; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1161 AA |
Protein Sequence | MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAINKK SAGHKEEDQN FNLSGSAFPS 60 CQSNGPTVST QTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIVNLNV KKEALLAGMV 120 DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHESLK VEKDLRCYGV 180 ASSHLKTLLK KSKTKDQKSG PTLPDVTPNL IRDSFVESSH PAVGQSGTKV MSEPLSCAAR 240 LQAVASMVEK RASPAASPKP SVACSQLALL LSSEAHLQQY SREHALKTQN AHQVASERLA 300 AMARLQENGQ KDVGSSQLSK GVSGHLNGQA RALPASKLVA NKNNAATFQS PMGVVPSSPK 360 NTSYKNSLER NNLKQAANNS LLLHLLKSQT IPTPMNGHSQ NERASSFESS TPTTIDEYSD 420 NNPSFTDDSS GDESSYSNCV PIDLSCKHRI EKPEAERPVS LENLTQSLLN TWDPKIPGVD 480 IKEDQDTSTN SKLNSHQKVT LLQLLLGHKS EETVERNASP QDIHSDGTKF SPQNYTRTSV 540 IESPSTNRTT PVSTPPLYTA SQAESPINLS QHSLVIKWNS PPYACSTPAS KLTNTAPSHL 600 MDLTKGKESQ AEKPAPSEGA QNSATFSASK LLQNLAQCGL QSSGPGEEQR PCKQLLSGNP 660 DKPLGLIDRL NSPLLSNKTN AAEESKAFSS QPAGPEPGLP GCEIENLLER RTVLQLLLGN 720 SSKGKNEKKE KTPARDEAPQ EHSERAANEQ ILMVKIKSEP CDDFQTHNTN LPLNHDAKSA 780 PFLGVTPAIH RSTAALPVSE DFKSEPASPQ DFSFSKNGLL SRLLRQNQES YPADEQDKSH 840 RNSELPTLES KNICMVPKKR KLYTEPLENP FKKMKNTAVD TANHHSGPEV LYGSLLHQEE 900 LKFSRNELDY KYPAGHSSAS DGDHRSWARE SKSFNVLKQL LLSENCVRDL SPHRSDSVPD 960 TKKKGHKNNA PGSKPEFGIS SLNGLMYSSP QPGSCVTDHR TFSYPGMVKT PLSPPFPEHL 1020 GCVGSRPEPG LLNGCSVPGE KGPIKWVIAD MDKNEYEKDS PRLTKTNPIL YYMLQKGGGN 1080 SVTTQETQDK DIWREPASAE SLSQVTVKEE LLPAAETKAS FFNLRSPYNS HMGNNASRPH 1140 STNGEVYGLL GNALTIKKES E 1161 |
Gene Ontology | GO:0000118; C:histone deacetylase complex; IPI:UniProtKB. GO:0003713; F:transcription coactivator activity; IEA:Compara. GO:0003714; F:transcription corepressor activity; IDA:MGI. GO:0019915; P:lipid storage; IMP:UniProtKB. GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI. GO:0001543; P:ovarian follicle rupture; IMP:UniProtKB. GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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