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Protein

Nuclear receptor-binding protein

Gene

Nrbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases.By similarity

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-383280. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor-binding protein
Alternative name(s):
HLS7-interacting protein kinase
MLF1 adapter molecule
Gene namesi
Name:Nrbp1
Synonyms:Madm, Nrbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2183436. Nrbp1.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytosol Source: GO_Central
  • endomembrane system Source: MGI
  • lamellipodium Source: UniProtKB-SubCell
  • membrane Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 535534Nuclear receptor-binding proteinPRO_0000086451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei431 – 4311PhosphothreonineCombined sources
Modified residuei433 – 4331PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99J45.
MaxQBiQ99J45.
PaxDbiQ99J45.
PRIDEiQ99J45.

PTM databases

iPTMnetiQ99J45.
PhosphoSiteiQ99J45.

Expressioni

Gene expression databases

BgeeiQ99J45.
CleanExiMM_NRBP1.
ExpressionAtlasiQ99J45. baseline and differential.
GenevisibleiQ99J45. MM.

Interactioni

Subunit structurei

Homodimer. Binds to MLF1, recruiting a serine kinase which phosphorylates both itself and MLF1. Phosphorylated MLF1 binds to YWHAZ and is retained in the cytoplasm.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-767484,EBI-767484
Mlf1Q9QWV45EBI-767484,EBI-354765

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi228688. 5 interactions.
IntActiQ99J45. 4 interactions.
MINTiMINT-4123328.
STRINGi10090.ENSMUSP00000031034.

Structurei

3D structure databases

ProteinModelPortaliQ99J45.
SMRiQ99J45. Positions 81-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 327260Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1266. Eukaryota.
ENOG410XSIC. LUCA.
GeneTreeiENSGT00800000124049.
HOGENOMiHOG000267147.
HOVERGENiHBG057400.
InParanoidiQ99J45.
KOiK08875.
OMAiCLNPQPQ.
PhylomeDBiQ99J45.
TreeFamiTF315519.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99J45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGESQTVV SSGSDPKVES SSLAPGLTSV SPPVTSTTSA ASPEEEEESE
60 70 80 90 100
DESEILEESP CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ
110 120 130 140 150
FSERKNYKLQ EEKVRAVFDN LIQLEHLNIV KFHKYWADVK ENKARVIFIT
160 170 180 190 200
EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW CTQILSALSY LHSCDPPIIH
210 220 230 240 250
GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL HFFAPEYGEV
260 270 280 290 300
TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDSLQ
310 320 330 340 350
REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE
360 370 380 390 400
NALEEITKNM DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG
410 420 430 440 450
IYPLTAFGLP RPQQPQQEEV TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN
460 470 480 490 500
IESVEEGVKH HLTLLLKLED KLNRHLSCDL MPNESIPDLA AELVQLGFIS
510 520 530
EADQSRLTSL LEETLNKFNF TRNSTLNTAT VTVSS
Length:535
Mass (Da):59,866
Last modified:June 1, 2001 - v1
Checksum:i85DD5F6FC25C5AB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201S → SVFHRIFAN in BAC32612 (PubMed:16141072).Curated
Sequence conflicti494 – 4941V → G in BAC32612 (PubMed:16141072).Curated
Sequence conflicti508 – 5103TSL → SSV in BAC32612 (PubMed:16141072).Curated
Sequence conflicti521 – 5211T → S in BAC32612 (PubMed:16141072).Curated
Sequence conflicti535 – 5351S → VVELT in BAC32612 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302138 mRNA. Translation: AAK97260.1.
AF302139 Genomic DNA. Translation: AAK97261.1.
AK046142 mRNA. Translation: BAC32612.1.
BC004756 mRNA. Translation: AAH04756.1.
BC018463 mRNA. Translation: AAH18463.1.
CCDSiCCDS19180.1.
RefSeqiNP_671734.1. NM_147201.2.
UniGeneiMm.292040.

Genome annotation databases

EnsembliENSMUST00000031034; ENSMUSP00000031034; ENSMUSG00000029148.
GeneIDi192292.
KEGGimmu:192292.
UCSCiuc008wxt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302138 mRNA. Translation: AAK97260.1.
AF302139 Genomic DNA. Translation: AAK97261.1.
AK046142 mRNA. Translation: BAC32612.1.
BC004756 mRNA. Translation: AAH04756.1.
BC018463 mRNA. Translation: AAH18463.1.
CCDSiCCDS19180.1.
RefSeqiNP_671734.1. NM_147201.2.
UniGeneiMm.292040.

3D structure databases

ProteinModelPortaliQ99J45.
SMRiQ99J45. Positions 81-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228688. 5 interactions.
IntActiQ99J45. 4 interactions.
MINTiMINT-4123328.
STRINGi10090.ENSMUSP00000031034.

PTM databases

iPTMnetiQ99J45.
PhosphoSiteiQ99J45.

Proteomic databases

EPDiQ99J45.
MaxQBiQ99J45.
PaxDbiQ99J45.
PRIDEiQ99J45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031034; ENSMUSP00000031034; ENSMUSG00000029148.
GeneIDi192292.
KEGGimmu:192292.
UCSCiuc008wxt.1. mouse.

Organism-specific databases

CTDi29959.
MGIiMGI:2183436. Nrbp1.

Phylogenomic databases

eggNOGiKOG1266. Eukaryota.
ENOG410XSIC. LUCA.
GeneTreeiENSGT00800000124049.
HOGENOMiHOG000267147.
HOVERGENiHBG057400.
InParanoidiQ99J45.
KOiK08875.
OMAiCLNPQPQ.
PhylomeDBiQ99J45.
TreeFamiTF315519.

Enzyme and pathway databases

ReactomeiR-MMU-383280. Nuclear Receptor transcription pathway.

Miscellaneous databases

ChiTaRSiNrbp1. mouse.
PROiQ99J45.
SOURCEiSearch...

Gene expression databases

BgeeiQ99J45.
CleanExiMM_NRBP1.
ExpressionAtlasiQ99J45. baseline and differential.
GenevisibleiQ99J45. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MADM, a novel adaptor protein that mediates phosphorylation of the 14-3-3 binding site of myeloid leukemia factor 1."
    Lim R., Winteringham L.N., Williams J.H., McCulloch R.K., Ingley E., Tiao J.Y.-H., Lalonde J.-P., Tsai S., Tilbrook P.A., Sun Y., Wu X., Morris S.W., Klinken S.P.
    J. Biol. Chem. 277:40997-41008(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION, HOMODIMERIZATION, INTERACTION WITH MLF1.
    Strain: 129Imported and BDF1Imported.
  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.
    , 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.
    Tissue: Corpora quadrigemina.
  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: 129Imported and FVB/NImported.
    Tissue: Mammary glandImported.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-431 AND THR-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNRBP_MOUSE
AccessioniPrimary (citable) accession number: Q99J45
Secondary accession number(s): Q8BL77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.