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Q8CBD1 (NRIP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor-interacting protein 1
Alternative name(s):
Nuclear factor RIP140
Receptor-interacting protein 140
Gene names
Name:Nrip1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1161 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Subunit structure

Interacts with CTBP1, CTBP2, ERS1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH By similarity. Interacts with NR2C1 (sumoylated form and via the ligand-binding domain); the interaction results in promoting the repressor activity of NR2C1. Interacts with RARA and RXRB homodimers and RARA/RXRB heterodimers in the presence of ligand. Interacts with HDAC1 and HDAC3 via its N-terminal domain. Interacts with ZNF366 By similarity. Ref.1 Ref.6 Ref.7 Ref.9 Ref.10 Ref.14 Ref.15 UniProtKB P48552

Subcellular location

Nucleus Ref.4 Ref.11.

Tissue specificity

Expressed in the embryonic placenta. In the adult, expression is strong in the testis and brain. Also expressed at a high level in the white adipose tissue. Expressed constantly but at a weaker level in the adult heart, lung, stomach and kidney. Expressed moderately in the skeletal muscle. Expressed at a low level in the adult spleen, liver and brown adipose tissue. Expressed in the ovary at a high level in granulosa cells and at a lower level in the thecal and interstitial compartments. Ref.1 Ref.7 Ref.8 Ref.12

Domain

Contains at least 4 autonomous repression domains (RD1-4) By similarity.

Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have different affinities for nuclear receptors.

The Ligand-dependent nuclear receptor binding region is required for ligand-dependent interaction with RAAR and RXRB homo- and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB.

Post-translational modification

Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH By similarity. Acetylation regulates its nuclear translocation and corepressive activity. Ref.4 Ref.11 UniProtKB P48552

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
   Molecular functionReceptor
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlipid storage

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: MGI

ovarian follicle rupture

Inferred from mutant phenotype Ref.13. Source: UniProtKB

ovulation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19796622. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthistone deacetylase complex

Inferred from physical interaction Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionhistone deacetylase binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: IntAct

receptor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

retinoic acid receptor binding

Inferred from physical interaction Ref.6. Source: UniProtKB

retinoid X receptor binding

Inferred from physical interaction Ref.6. Source: UniProtKB

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HDAC3O153792EBI-1771626,EBI-607682From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11611161Nuclear receptor-interacting protein 1
PRO_0000057952

Regions

Region1 – 416416Interaction with ZNF366 By similarity
Region78 – 335258Repression domain 1 By similarity UniProtKB P48552
Region411 – 701291Repression domain 2 By similarity UniProtKB P48552
Region432 – 47342Required for targeting to small nuclear foci By similarity UniProtKB P48552
Region736 – 886151Repression domain 3 By similarity UniProtKB P48552
Region754 – 1161408Interaction with ZNF366 By similarity
Region1063 – 107614Ligand-dependent nuclear receptor binding
Region1121 – 116141Repression domain 4 By similarity UniProtKB P48552
Motif21 – 255LXXLL motif 1
Motif133 – 1375LXXLL motif 2
Motif185 – 1895LXXLL motif 3
Motif267 – 2715LXXLL motif 4
Motif382 – 3865LXXLL motif 5
Motif441 – 4477CTBP-binding; principal site By similarity UniProtKB P48552
Motif501 – 5055LXXLL motif 6
Motif566 – 5705CTBP-binding By similarity UniProtKB P48552
Motif714 – 7185LXXLL motif 7
Motif820 – 8245LXXLL motif 8
Motif937 – 9415LXXLL motif 9
Motif947 – 9515CTBP-binding By similarity UniProtKB P48552

Amino acid modifications

Modified residue1041Phosphoserine Ref.5
Modified residue1111N6-acetyllysine Ref.4 Ref.11
Modified residue1581N6-acetyllysine Ref.4 Ref.11
Modified residue2071Phosphothreonine Ref.5
Modified residue2871N6-acetyllysine Ref.4 Ref.11
Modified residue3111N6-acetyllysine Ref.4 Ref.11
Modified residue3581Phosphoserine Ref.5
Modified residue3801Phosphoserine Ref.5
Modified residue4471N6-acetyllysine By similarity
Modified residue4821N6-acetyllysine Ref.4 Ref.11
Modified residue4881Phosphoserine Ref.5
Modified residue5191Phosphoserine Ref.5
Modified residue5291N6-acetyllysine Ref.4 Ref.11
Modified residue5311Phosphoserine Ref.5
Modified residue5431Phosphoserine Ref.5
Modified residue6071N6-acetyllysine Ref.4 Ref.11
Modified residue6721Phosphoserine Ref.5
Modified residue9321N6-acetyllysine Ref.4 Ref.11
Modified residue10031Phosphoserine Ref.5

Experimental info

Mutagenesis10671N → G: Reduces binding to RAR, RXR and RAR/RXR. Ref.10
Mutagenesis10681P → A: Abolishes binding to RAR, RXR and RAR/RXR. Ref.10
Mutagenesis10731M → I: Reduces binding to RAR, RXR and RAR/RXR. Ref.10
Mutagenesis10731M → K: Abolishes binding to RAR, RXR and RAR/RXR. Ref.10
Mutagenesis10731M → L: Reduces binding to RAR, RXR and RAR/RXR. Ref.10
Sequence conflict1061V → N AA sequence Ref.4
Sequence conflict1071N → NN AA sequence Ref.5
Sequence conflict119 – 1202MV → IL in AAC69611. Ref.1
Sequence conflict1901K → R in AAC69611. Ref.1
Sequence conflict1971Q → E in AAC69611. Ref.1
Sequence conflict2001G → D in AAC69611. Ref.1
Sequence conflict5221D → V in AAC69611. Ref.1
Sequence conflict5961A → V in AAC69611. Ref.1
Sequence conflict6171S → N in AAC69611. Ref.1
Sequence conflict6291S → K AA sequence Ref.4
Sequence conflict6741L → Q in AAC69611. Ref.1
Sequence conflict8181G → F in AAC69611. Ref.1
Sequence conflict8551M → I in BAE33634. Ref.2
Sequence conflict8861S → R in AAC69611. Ref.1
Sequence conflict10491A → T in AAC69611. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8CBD1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 56ABD0C2A5AAC0A1

FASTA1,161126,337
        10         20         30         40         50         60 
MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAINKK SAGHKEEDQN FNLSGSAFPS 

        70         80         90        100        110        120 
CQSNGPTVST QTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIVNLNV KKEALLAGMV 

       130        140        150        160        170        180 
DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHESLK VEKDLRCYGV 

       190        200        210        220        230        240 
ASSHLKTLLK KSKTKDQKSG PTLPDVTPNL IRDSFVESSH PAVGQSGTKV MSEPLSCAAR 

       250        260        270        280        290        300 
LQAVASMVEK RASPAASPKP SVACSQLALL LSSEAHLQQY SREHALKTQN AHQVASERLA 

       310        320        330        340        350        360 
AMARLQENGQ KDVGSSQLSK GVSGHLNGQA RALPASKLVA NKNNAATFQS PMGVVPSSPK 

       370        380        390        400        410        420 
NTSYKNSLER NNLKQAANNS LLLHLLKSQT IPTPMNGHSQ NERASSFESS TPTTIDEYSD 

       430        440        450        460        470        480 
NNPSFTDDSS GDESSYSNCV PIDLSCKHRI EKPEAERPVS LENLTQSLLN TWDPKIPGVD 

       490        500        510        520        530        540 
IKEDQDTSTN SKLNSHQKVT LLQLLLGHKS EETVERNASP QDIHSDGTKF SPQNYTRTSV 

       550        560        570        580        590        600 
IESPSTNRTT PVSTPPLYTA SQAESPINLS QHSLVIKWNS PPYACSTPAS KLTNTAPSHL 

       610        620        630        640        650        660 
MDLTKGKESQ AEKPAPSEGA QNSATFSASK LLQNLAQCGL QSSGPGEEQR PCKQLLSGNP 

       670        680        690        700        710        720 
DKPLGLIDRL NSPLLSNKTN AAEESKAFSS QPAGPEPGLP GCEIENLLER RTVLQLLLGN 

       730        740        750        760        770        780 
SSKGKNEKKE KTPARDEAPQ EHSERAANEQ ILMVKIKSEP CDDFQTHNTN LPLNHDAKSA 

       790        800        810        820        830        840 
PFLGVTPAIH RSTAALPVSE DFKSEPASPQ DFSFSKNGLL SRLLRQNQES YPADEQDKSH 

       850        860        870        880        890        900 
RNSELPTLES KNICMVPKKR KLYTEPLENP FKKMKNTAVD TANHHSGPEV LYGSLLHQEE 

       910        920        930        940        950        960 
LKFSRNELDY KYPAGHSSAS DGDHRSWARE SKSFNVLKQL LLSENCVRDL SPHRSDSVPD 

       970        980        990       1000       1010       1020 
TKKKGHKNNA PGSKPEFGIS SLNGLMYSSP QPGSCVTDHR TFSYPGMVKT PLSPPFPEHL 

      1030       1040       1050       1060       1070       1080 
GCVGSRPEPG LLNGCSVPGE KGPIKWVIAD MDKNEYEKDS PRLTKTNPIL YYMLQKGGGN 

      1090       1100       1110       1120       1130       1140 
SVTTQETQDK DIWREPASAE SLSQVTVKEE LLPAAETKAS FFNLRSPYNS HMGNNASRPH 

      1150       1160 
STNGEVYGLL GNALTIKKES E 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2."
Lee C.-H., Chinpaisal C., Wei L.-N.
Mol. Cell. Biol. 18:6745-6755(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH NR2C1 AND RARA.
Strain: ICR.
Tissue: Embryo.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Cerebellum, Heart and Spleen.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 101-112; 155-170; 283-298; 305-320; 476-492; 517-537; 606-630 AND 930-938, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-111; LYS-158; LYS-287; LYS-311; LYS-482; LYS-529; LYS-607 AND LYS-932.
[5]"Mapping of phosphorylation sites of nuclear corepressor receptor interacting protein 140 by liquid chromatography-tandem mass spectroscopy."
Huq M.D.M., Khan S.A., Park S.W., Wei L.-N.
Proteomics 5:2157-2166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 101-112; 199-212; 343-360; 375-387; 476-492; 517-548; 670-678 AND 1001-1009, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-104; THR-207; SER-358; SER-380; SER-488; SER-519; SER-531; SER-543; SER-672 AND SER-1003.
[6]"Characterization of receptor-interacting protein 140 in retinoid receptor activities."
Lee C.-H., Wei L.-N.
J. Biol. Chem. 274:31320-31326(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RARA AND RXRB.
[7]"Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing."
Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.
J. Biol. Chem. 275:40782-40787(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1 AND HDAC3.
[8]"The nuclear receptor co-repressor Nrip1 (RIP140) is essential for female fertility."
White R., Leonardsson G., Rosewell I., Jacobs M.A., Milligan S., Parker M.G.
Nat. Med. 6:1368-1374(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"Ligand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of RIP140."
Wei L.-N., Farooqui M., Hu X.
J. Biol. Chem. 276:16107-16112(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RARA AND RXRB, IDENTIFICATION IN A COMPLEX WITH HDAC3.
[10]"Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity."
Farooqui M., Franco P.J., Thompson J., Kagechika H., Chandraratna R.A.S., Banaszak L., Wei L.-N.
Biochemistry 42:971-979(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RARA AND RXRB, MUTAGENESIS OF ASN-1067; PRO-1068 AND MET-1073.
[11]"Receptor interacting protein 140 as a thyroid hormone-dependent, negative co-regulator for the induction of cellular retinoic acid binding protein I gene."
Wei L.-N., Hu X.
Mol. Cell. Endocrinol. 218:39-48(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Nuclear receptor corepressor RIP140 regulates fat accumulation."
Leonardsson G., Steel J.H., Christian M., Pocock V., Milligan S., Bell J., So P.-W., Medina-Gomez G., Vidal-Puig A., White R., Parker M.G.
Proc. Natl. Acad. Sci. U.S.A. 101:8437-8442(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]"Multiple signaling defects in the absence of RIP140 impair both cumulus expansion and follicle rupture."
Tullet J.M.A., Pocock V., Steel J.H., White R., Milligan S., Parker M.G.
Endocrinology 146:4127-4137(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1.
[15]"Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression."
Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P., Wei L.N.
Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF053062 mRNA. Translation: AAC69611.1.
AK036273 mRNA. Translation: BAC29368.1.
AK084498 mRNA. Translation: BAC39197.1.
AK156233 mRNA. Translation: BAE33634.1.
BC060232 mRNA. Translation: AAH60232.1.
CCDSCCDS28274.1.
RefSeqNP_775616.1. NM_173440.2.
XP_006523113.1. XM_006523050.1.
XP_006523114.1. XM_006523051.1.
XP_006523115.1. XM_006523052.1.
XP_006523116.1. XM_006523053.1.
XP_006523117.1. XM_006523054.1.
UniGeneMm.455873.
Mm.74711.

3D structure databases

ProteinModelPortalQ8CBD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234576. 11 interactions.
DIPDIP-29280N.
IntActQ8CBD1. 4 interactions.
STRING10090.ENSMUSP00000112959.

PTM databases

PhosphoSiteQ8CBD1.

Proteomic databases

PRIDEQ8CBD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054178; ENSMUSP00000051726; ENSMUSG00000048490.
ENSMUST00000121927; ENSMUSP00000112959; ENSMUSG00000048490.
GeneID268903.
KEGGmmu:268903.
UCSCuc007zrx.1. mouse.

Organism-specific databases

CTD8204.
MGIMGI:1315213. Nrip1.

Phylogenomic databases

eggNOGNOG47583.
GeneTreeENSGT00390000007999.
HOGENOMHOG000236277.
HOVERGENHBG052667.
InParanoidQ8CBD1.
KOK17965.
OMAVEKDLRC.
OrthoDBEOG7H1JJQ.
PhylomeDBQ8CBD1.
TreeFamTF332210.

Gene expression databases

BgeeQ8CBD1.
CleanExMM_NRIP1.
GenevestigatorQ8CBD1.

Family and domain databases

InterProIPR026649. NRIP1.
[Graphical view]
PANTHERPTHR15088. PTHR15088. 1 hit.
ProtoNetSearch...

Other

NextBio392571.
PROQ8CBD1.
SOURCESearch...

Entry information

Entry nameNRIP1_MOUSE
AccessionPrimary (citable) accession number: Q8CBD1
Secondary accession number(s): Q3U166, Q8C3Y8, Q9Z2K2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot