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P68040 (GBLP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Guanine nucleotide-binding protein subunit beta-2-like 1
Alternative name(s):
12-3
Receptor for activated C kinase
Receptor of activated protein kinase C 1
Short name=RACK1
p205
Gene names
Name:Gnb2l1
Synonyms:Gnb2-rs1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Ref.1 Ref.11 Ref.12

Subunit structure

Component of the small (40S) ribosomal subunit. Interacts with LARP4B. Interacts with PKD2L1 By similarity. Exists as a monomer and also forms oligomers. Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of GNB2L1/RACK1. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation. Interacts with RHOA; this enhances RHOA activation and promotes cell migration. Interacts with CHRM2; the interaction regulates CHRM2 internalization. Interacts with TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. Interacts with HRAS. Ref.11 Ref.12 Ref.13

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeleton By similarity. Nucleus. Perikaryon. Cell projectiondendrite. Note: Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. PKC activation induces translocation from the perinuclear region to the cell periphery. In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei By similarity. Ref.10 Ref.12

Tissue specificity

Strongly and ubiquitously expressed in the embryonic and early postnatal brain. At E11.5, expressed in a high-dorsal to low-ventral gradient throughout the brain. At E13.5, most abundant in the telecephalon. At E18.5, expressed most abundantly in layers 1-4 of the cortex, striatum, hippocampus, dentate gyrus, and specific thalamic nuclei. This expression decreases during postnatal development and is localized in the dentate gyrus, habenula, piriform cortex, paraventricular nucleus of the hypothalamus and supraoptic nucleus of the adult brain. Ref.1 Ref.10

Developmental stage

Expressed throughout embryonic brain development with high levels detected at E11.5, E13.5 and E18.5. Also detected at high levels in the adult brain. Ref.10

Post-translational modification

Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC By similarity.

Sequence similarities

Belongs to the WD repeat G protein beta family.

Contains 7 WD repeats.

Sequence caution

The sequence AAG29506.1 differs from that shown. Reason: Frameshift at positions 232 and 239.

Ontologies

Keywords
   Biological processApoptosis
Biological rhythms
Cell cycle
Gastrulation
Growth regulation
Translation regulation
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   DomainRepeat
WD repeat
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

gastrulation

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from sequence alignment PubMed 11099474. Source: MGI

negative regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

negative regulation of translation

Inferred from electronic annotation. Source: Ensembl

positive regulation of GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of gastrulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein homooligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization

Inferred from sequence alignment PubMed 11099474. Source: MGI

regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

regulation of protein localization

Inferred from sequence or structural similarity. Source: UniProtKB

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12826667. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from direct assay Ref.10. Source: UniProtKB

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from direct assay Ref.10. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perikaryon

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic cup

Inferred from sequence or structural similarity. Source: UniProtKB

small ribosomal subunit

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

ion channel inhibitor activity

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11Ref.13. Source: UniProtKB

protein kinase C binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor activity

Inferred from sequence alignment PubMed 11099474. Source: MGI

receptor tyrosine kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IkbkbO883514EBI-296749,EBI-447960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Guanine nucleotide-binding protein subunit beta-2-like 1
PRO_0000424482
Initiator methionine11Removed; alternate Ref.8
Chain2 – 317316Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed
PRO_0000127732

Regions

Repeat13 – 4432WD 1
Repeat61 – 9131WD 2
Repeat103 – 13331WD 3
Repeat146 – 17833WD 4
Repeat190 – 22031WD 5
Repeat231 – 26030WD 6
Repeat281 – 31131WD 7

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed Ref.8
Modified residue521Phosphotyrosine; by ABL1 By similarity
Modified residue1301N6-acetyllysine Ref.14
Modified residue1831N6-acetyllysine Ref.14
Modified residue2281Phosphotyrosine By similarity

Experimental info

Sequence conflict91G → R in BAE40068. Ref.3
Sequence conflict91G → R in BAE40156. Ref.3
Sequence conflict1251R → Q in BAE40059. Ref.3
Sequence conflict1251R → Q in BAE40068. Ref.3
Sequence conflict1251R → Q in BAE40156. Ref.3
Sequence conflict2481L → P in BAE35378. Ref.3
Sequence conflict2661I → M in AAG29506. Ref.6
Sequence conflict2731E → A in BAA06185. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P68040 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 257F91E369ED2044

FASTA31735,077
        10         20         30         40         50         60 
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR 

        70         80         90        100        110        120 
GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI 

       130        140        150        160        170        180 
VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA 

       190        200        210        220        230        240 
NCKLKTNHIG HTGYLNTVTV SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC 

       250        260        270        280        290        300 
FSPNRYWLCA ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA 

       310 
GYTDNLVRVW QVTIGTR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a neural differentiation-associated gene, p205, in the embryonal carcinoma cell line P19 and in the developing mouse."
Imai Y., Suzuki Y., Tohyama M., Wanaka A., Takagi T.
Brain Res. Mol. Brain Res. 24:313-319(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Primary sequence of the mouse guanine nucleotide binding protein related gene."
Raj N.B.K., Su Y., Au W.C., Pitha P.M.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Spleen.
[3]"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: BALB/c, C57BL/6J and DBA/2.
Tissue: Blastocyst, Embryo, Embryonic head, Embryonic spinal ganglion, Embryonic stem cell, Head, Kidney, Mammary gland and Osteoclast.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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.
[7]"Genomic structure and expression of mouse receptor for activated C kinase (RACK1)."
Choi D., Messing R.O.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
Strain: 129/SvJ.
[8]Kanor S., Quadroni M., Bienvenut W.V.
Submitted (MAR-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11 AND 271-279, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6J.
Tissue: Skeletal muscle.
[9]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 226-317, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[10]"Localization of the scaffolding protein RACK1 in the developing and adult mouse brain."
Ashique A.M., Kharazia V., Yaka R., Phamluong K., Peterson A.S., Ron D.
Brain Res. 1069:31-38(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[11]"RACK1 inhibits TRPM6 activity via phosphorylation of the fused alpha-kinase domain."
Cao G., Thebault S., van der Wijst J., van der Kemp A., Lasonder E., Bindels R.J., Hoenderop J.G.
Curr. Biol. 18:168-176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TRPM6.
[12]"Identification of RACK1 and protein kinase Calpha as integral components of the mammalian circadian clock."
Robles M.S., Boyault C., Knutti D., Padmanabhan K., Weitz C.J.
Science 327:463-466(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BMAL1 AND PRKCA, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"Rack1 is required for Vangl2 membrane localization and planar cell polarity signaling while attenuating canonical Wnt activity."
Li S., Esterberg R., Lachance V., Ren D., Radde-Gallwitz K., Chi F., Parent J.L., Fritz A., Chen P.
Proc. Natl. Acad. Sci. U.S.A. 108:2264-2269(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VANGL2.
[14]"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-130 AND LYS-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D29802 mRNA. Translation: BAA06185.1.
X75313 mRNA. Translation: CAA53062.1.
AK002493 mRNA. Translation: BAB22141.1.
AK012242 mRNA. Translation: BAB28114.1.
AK017772 mRNA. Translation: BAB30920.1.
AK051226 mRNA. Translation: BAC34564.1.
AK159797 mRNA. Translation: BAE35378.1.
AK160528 mRNA. Translation: BAE35846.1.
AK160739 mRNA. Translation: BAE35980.1.
AK161234 mRNA. Translation: BAE36257.1.
AK166417 mRNA. Translation: BAE38762.1.
AK166786 mRNA. Translation: BAE39017.1.
AK166800 mRNA. Translation: BAE39028.1.
AK166889 mRNA. Translation: BAE39095.1.
AK166945 mRNA. Translation: BAE39133.1.
AK168086 mRNA. Translation: BAE40059.1.
AK168096 mRNA. Translation: BAE40068.1.
AK168196 mRNA. Translation: BAE40156.1.
AK168349 mRNA. Translation: BAE40286.1.
AL645849 Genomic DNA. Translation: CAI35106.1.
CH466575 Genomic DNA. Translation: EDL33791.1.
BC046760 mRNA. Translation: AAH46760.1.
AF295529 Genomic DNA. Translation: AAG29506.1. Frameshift.
CCDSCCDS24585.1.
PIRS38398.
RefSeqNP_032169.1. NM_008143.3.
UniGeneMm.5305.

3D structure databases

ProteinModelPortalP68040.
SMRP68040. Positions 2-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199978. 11 interactions.
IntActP68040. 18 interactions.
MINTMINT-248042.

2D gel databases

REPRODUCTION-2DPAGEP68040.
SWISS-2DPAGEP68040.

Proteomic databases

MaxQBP68040.
PaxDbP68040.
PRIDEP68040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020640; ENSMUSP00000020640; ENSMUSG00000020372.
GeneID14694.
KEGGmmu:14694.
UCSCuc007ipa.1. mouse.

Organism-specific databases

CTD10399.
MGIMGI:101849. Gnb2l1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00750000117670.
HOVERGENHBG000277.
InParanoidQ9CSQ0.
KOK14753.
OMAKSIIMWK.
OrthoDBEOG7BW0JV.
PhylomeDBP68040.
TreeFamTF300600.

Gene expression databases

BgeeP68040.
GenevestigatorP68040.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNB2L1. mouse.
NextBio286639.
PROP68040.
SOURCESearch...

Entry information

Entry nameGBLP_MOUSE
AccessionPrimary (citable) accession number: P68040
Secondary accession number(s): P25388 expand/collapse secondary AC list , P99049, Q3THP0, Q3THY7, Q3TKQ0, Q3TW88, Q5NCC5, Q5NCC6, Q9CSQ0, Q9ERM6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 3 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

MGD cross-references

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