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P31266 (SUH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Recombining binding protein suppressor of hairless
Alternative name(s):
J kappa-recombination signal-binding protein
RBP-J kappa
Gene names
Name:Rbpj
Synonyms:Igkjrb1, Igkrsbp, Rbpsuh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Ref.6

Subunit structure

Interacts with RITA1, leading to nuclear export, prevent the interaction between RBPJ and NICD product and subsequent down-regulation of the Notch signaling pathway By similarity. Interacts with activated NOTCH1, NOTCH2 and NOTCH3. Interacts with MINT/SHARP. This interaction may mediate the recruitment of large corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2, SAP30, FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A. Interacts with SNW1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Nucleus. Cytoplasm By similarity. Note: Mainly nuclear, upon interaction with RITA1, translocates to the cytoplasm, down-regulating the Notch signaling pathway By similarity.

Sequence similarities

Belongs to the Su(H) family.

Contains 1 IPT/TIG domain.

Caution

Despite some similarity with the "phage" integrase family, it has no recombinase activity.

Ontologies

Keywords
   Biological processNotch signaling pathway
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 11967543. Source: MGI

Clara cell differentiation

Inferred from mutant phenotype PubMed 22797898. Source: MGI

Notch signaling pathway

Inferred from mutant phenotype PubMed 14701881PubMed 19124651PubMed 19154718. Source: MGI

Notch signaling pathway involved in arterial endothelial cell fate commitment

Inferred by curator PubMed 15466160. Source: BHF-UCL

angiogenesis

Inferred from mutant phenotype PubMed 15466160. Source: MGI

arterial endothelial cell fate commitment

Inferred from mutant phenotype PubMed 15466160. Source: BHF-UCL

atrioventricular canal development

Inferred from mutant phenotype PubMed 14701881. Source: BHF-UCL

auditory receptor cell fate commitment

Inferred from mutant phenotype PubMed 19154718. Source: MGI

blood vessel endothelial cell fate specification

Inferred from genetic interaction PubMed 15466160. Source: BHF-UCL

blood vessel lumenization

Inferred from mutant phenotype PubMed 15466160. Source: BHF-UCL

blood vessel remodeling

Inferred from mutant phenotype PubMed 15466160. Source: BHF-UCL

cardiac left ventricle morphogenesis

Inferred from mutant phenotype PubMed 21493891. Source: BHF-UCL

cell fate commitment

Inferred from mutant phenotype PubMed 17015435. Source: MGI

defense response to bacterium

Inferred from mutant phenotype PubMed 11967543. Source: MGI

determination of heart left/right asymmetry

Traceable author statement PubMed 15466160. Source: BHF-UCL

dorsal aorta morphogenesis

Inferred from mutant phenotype PubMed 15466160. Source: BHF-UCL

endocardium development

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

endocardium morphogenesis

Inferred from mutant phenotype PubMed 14701881. Source: BHF-UCL

epidermal cell fate specification

Inferred from mutant phenotype PubMed 17079689. Source: MGI

epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 14701881. Source: MGI

epithelial to mesenchymal transition involved in endocardial cushion formation

Inferred from mutant phenotype PubMed 14701881. Source: BHF-UCL

hair follicle maturation

Inferred from mutant phenotype PubMed 17079689. Source: MGI

heart development

Inferred from mutant phenotype PubMed 14701881. Source: MGI

heart looping

Traceable author statement PubMed 15466160. Source: BHF-UCL

hemopoiesis

Inferred from mutant phenotype PubMed 15689374. Source: MGI

humoral immune response

Inferred from mutant phenotype PubMed 17658279. Source: MGI

inflammatory response to antigenic stimulus

Inferred from mutant phenotype PubMed 17658279. Source: MGI

interleukin-4 secretion

Inferred from mutant phenotype PubMed 17658279. Source: MGI

keratinocyte differentiation

Inferred from mutant phenotype PubMed 17079689. Source: MGI

labyrinthine layer blood vessel development

Inferred from mutant phenotype PubMed 15466160. Source: BHF-UCL

negative regulation of cell differentiation

Inferred from mutant phenotype PubMed 10476967PubMed 17015435. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 17079689. Source: MGI

negative regulation of ossification

Inferred from mutant phenotype PubMed 21493891. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 14701881PubMed 17336907PubMed 21311046. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9111338. Source: MGI

neuron differentiation

Inferred from mutant phenotype PubMed 9102301. Source: MGI

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 14701881. Source: BHF-UCL

pituitary gland development

Inferred from mutant phenotype PubMed 17015435. Source: MGI

positive regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

positive regulation of ERBB signaling pathway

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

positive regulation of Notch signaling pathway involved in heart induction

Traceable author statement PubMed 15466160. Source: BHF-UCL

positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment

Inferred from mutant phenotype PubMed 22711842. Source: MGI

positive regulation of cardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 15509736. Source: MGI

positive regulation of cell proliferation involved in heart morphogenesis

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

positive regulation of ephrin receptor signaling pathway

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

positive regulation of gene expression

Inferred from mutant phenotype PubMed 15466160. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12730124PubMed 16287852. Source: BHF-UCL

positive regulation of transcription of Notch receptor target

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence alignment PubMed 11741889. Source: MGI

regulation of cell adhesion involved in heart morphogenesis

Inferred by curator PubMed 14701881. Source: BHF-UCL

regulation of gene expression

Inferred from mutant phenotype PubMed 9102301. Source: MGI

regulation of timing of cell differentiation

Inferred from mutant phenotype PubMed 17015435. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15689374. Source: MGI

regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation

Inferred from mutant phenotype PubMed 21311046. Source: BHF-UCL

sebaceous gland development

Inferred from mutant phenotype PubMed 17079689. Source: MGI

secondary heart field specification

Inferred from mutant phenotype PubMed 22711842. Source: MGI

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 21402740. Source: MGI

somitogenesis

Traceable author statement PubMed 15466160. Source: BHF-UCL

ventricular trabecula myocardium morphogenesis

Inferred from mutant phenotype PubMed 17336907. Source: BHF-UCL

   Cellular_componentMAML1-RBP-Jkappa- ICN1 complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 17938243. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 9111338. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from sequence orthology PubMed 18663143. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 17658279. Source: MGI

RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 12730124PubMed 17336907. Source: BHF-UCL

chromatin binding

Inferred from direct assay PubMed 17015435PubMed 23639443. Source: MGI

protein N-terminus binding

Inferred from physical interaction PubMed 17283045. Source: MGI

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 17658278PubMed 17938243. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 17392792. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Notch1Q017056EBI-1392666,EBI-1392707

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P31266-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P31266-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-45: AHAPSA → MAPVVT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Recombining binding protein suppressor of hairless
PRO_0000208568

Regions

Domain381 – 47191IPT/TIG
DNA binding84 – 918 By similarity
DNA binding218 – 22710
DNA binding291 – 32333

Amino acid modifications

Modified residue2011N6-acetyllysine Ref.11

Natural variations

Alternative sequence1 – 3939Missing in isoform 2.
VSP_008392
Alternative sequence40 – 456AHAPSA → MAPVVT in isoform 2.
VSP_008393

Secondary structure

............................................................................. 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 8BF517CC24099E03

FASTA52658,537
        10         20         30         40         50         60 
MPSGFPQSPR TSPRARPKTR ITGALPMDYS EGLSAEERPA HAPSAGKFGE RPPPKRLTRE 

        70         80         90        100        110        120 
AMRNYLKERG DQTVLILHAK VAQKSYGNEK RFFCPPPCVY LMGSGWKKKK EQMERDGCSE 

       130        140        150        160        170        180 
QESQPCAFIG IGNSDQEMQQ LNLEGKNYCT AKTLYISDSD KRKHFMLSVK MFYGNSDDIG 

       190        200        210        220        230        240 
VFLSKRIKVI SKPSKKKQSL KNADLCIASG TKVALFNRLR SQTVSTRYLH VEGGNFHASS 

       250        260        270        280        290        300 
QQWGAFYIHL LDDDESEGEE FTVRDGYIHY GQTVKLVCSV TGMALPRLII RKVDKQTALL 

       310        320        330        340        350        360 
DADDPVSQLH KCAFYLKDTE RMYLCLSQER IIQFQATPCP KEQNKEMIND GASWTIISTD 

       370        380        390        400        410        420 
KAEYTFYEGM GPVLAPVTPV PVVESLQLNG GGDVAMLELT GQNFTPNLRV WFGDVEAETM 

       430        440        450        460        470        480 
YRCGESMLCV VPDISAFREG WRWVRQPVQV PVTLVRNDGV IYSTSLTFTY TPEPGPRPHC 

       490        500        510        520 
SAAGAILRAN SSQVPSNESN TNSEGNYTNA STNSTSVTSS TATVVS 

« Hide

Isoform 2 [UniParc].

Checksum: 88C0D1DCECACC9E2
Show »

FASTA48754,347

References

« Hide 'large scale' references
[1]"A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif."
Matsunami N., Hamaguchi Y., Yamamoto Y., Kuze K., Kangawa K., Matsuo H., Kawaichi M., Honjo T.
Nature 342:934-937(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"Genomic organization of mouse J kappa recombination signal binding protein (RBP-J kappa) gene."
Kawaichi M., Oka C., Shibayama S., Koromilas A.E., Matsunami N., Hamaguchi Y., Honjo T.
J. Biol. Chem. 267:4016-4022(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Liver.
[3]"Cloning and characterization of a protein binding to the J kappa recombination signal sequence of immunoglobulin genes."
Hamaguchi Y., Matsunami N., Yamamoto Y., Kuze K., Kangawa K., Matsuo H., Kawaichi M., Honjo T.
Adv. Exp. Med. Biol. 292:177-186(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"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] (ISOFORM 2).
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"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] OF 1-341 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Thymus.
[6]"Signalling downstream of activated mammalian Notch."
Jarriault S., Brou C., Logeat F., Schroeter E.H., Kopan R., Israel A.
Nature 377:355-358(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NOTCH1.
[7]"LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein."
Taniguchi Y., Furukawa T., Tun T., Han H., Honjo T.
Mol. Cell. Biol. 18:644-654(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FHL1.
[8]"p300 acts as a transcriptional coactivator for mammalian Notch-1."
Oswald F., Taeuber B., Dobner T., Bourteele S., Kostezka U., Adler G., Liptay S., Schmid R.M.
Mol. Cell. Biol. 21:7761-7774(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EP300.
[9]"p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular mediator of Notch signalling, and is expressed in the neural tube of early stage embryos."
Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C., Kawaichi M.
Genes Cells 6:345-360(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTF1A.
Strain: ICR.
Tissue: Embryo.
[10]"Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NCOR2 AND HDAC1.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S63463 mRNA. Translation: AAB20195.1.
X17459 mRNA. Translation: CAA35501.1.
X58337 Genomic DNA. No translation available.
M81867, M81865, M81866 Genomic DNA. Translation: AAA39018.1.
M81868 Genomic DNA. Translation: AAA39019.1.
M81870, M81869 Genomic DNA. Translation: AAA39020.1. Sequence problems.
M81873, M81872 Genomic DNA. Translation: AAA39021.1.
M81875, M81874 Genomic DNA. Translation: AAA39022.1.
M81876 Genomic DNA. Translation: AAA39023.1.
M81877 Genomic DNA. No translation available.
BC051387 mRNA. Translation: AAH51387.1.
AK080359 mRNA. Translation: BAC37889.1.
CCDSCCDS19292.1. [P31266-1]
CCDS51504.1. [P31266-2]
PIRA42267.
A43567.
RefSeqNP_001074396.1. NM_001080927.2. [P31266-2]
NP_033061.3. NM_009035.5. [P31266-1]
UniGeneMm.209292.
Mm.488709.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BRGX-ray2.20C53-474[»]
3IAGX-ray2.00C53-474[»]
4J2XX-ray2.85A/C53-474[»]
ProteinModelPortalP31266.
SMRP31266. Positions 53-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202832. 9 interactions.
DIPDIP-171N.
IntActP31266. 3 interactions.

PTM databases

PhosphoSiteP31266.

Proteomic databases

MaxQBP31266.
PaxDbP31266.
PRIDEP31266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037618; ENSMUSP00000040694; ENSMUSG00000039191. [P31266-1]
ENSMUST00000113865; ENSMUSP00000109496; ENSMUSG00000039191. [P31266-2]
GeneID19664.
KEGGmmu:19664.
UCSCuc008xli.1. mouse. [P31266-1]

Organism-specific databases

CTD3516.
MGIMGI:96522. Rbpj.

Phylogenomic databases

eggNOGNOG295376.
GeneTreeENSGT00390000005197.
HOGENOMHOG000253907.
HOVERGENHBG006618.
InParanoidP31266.
KOK06053.
OMAMGPVHAP.
PhylomeDBP31266.
TreeFamTF314117.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.

Gene expression databases

ArrayExpressP31266.
BgeeP31266.
GenevestigatorP31266.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProIPR015350. Beta-trefoil_DNA-bd_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR015351. LAG1_DNA-bd.
IPR008967. p53-like_TF_DNA-bd.
[Graphical view]
PfamPF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
SUPFAMSSF110217. SSF110217. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP31266.
NextBio296966.
PROP31266.
SOURCESearch...

Entry information

Entry nameSUH_MOUSE
AccessionPrimary (citable) accession number: P31266
Secondary accession number(s): Q80UN8, Q8C4Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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