Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P68040

- GBLP_MOUSE

UniProt

P68040 - GBLP_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Guanine nucleotide-binding protein subunit beta-2-like 1

Gene

Gnb2l1

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

Functioni

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.3 Publications

GO - Molecular functioni

  1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: Ensembl
  2. ion channel inhibitor activity Source: UniProtKB
  3. poly(A) RNA binding Source: Ensembl
  4. protein kinase C binding Source: UniProtKB
  5. protein tyrosine kinase inhibitor activity Source: UniProtKB
  6. receptor activity Source: MGI
  7. receptor tyrosine kinase binding Source: UniProtKB
  8. SH2 domain binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. gastrulation Source: UniProtKB-KW
  3. intracellular signal transduction Source: MGI
  4. negative regulation of cell growth Source: UniProtKB
  5. negative regulation of gene expression Source: Ensembl
  6. negative regulation of hydrogen peroxide-induced neuron death Source: ParkinsonsUK-UCL
  7. negative regulation of phagocytosis Source: UniProtKB
  8. negative regulation of protein kinase B signaling Source: Ensembl
  9. negative regulation of translation Source: Ensembl
  10. negative regulation of Wnt signaling pathway Source: UniProtKB
  11. positive regulation of apoptotic process Source: UniProtKB
  12. positive regulation of cAMP catabolic process Source: Ensembl
  13. positive regulation of cell migration Source: UniProtKB
  14. positive regulation of cyclic-nucleotide phosphodiesterase activity Source: Ensembl
  15. positive regulation of gastrulation Source: UniProtKB
  16. positive regulation of GTPase activity Source: UniProtKB
  17. positive regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  18. positive regulation of mitochondrial depolarization Source: Ensembl
  19. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  20. positive regulation of protein homooligomerization Source: UniProtKB
  21. positive regulation of protein phosphorylation Source: UniProtKB
  22. protein localization Source: MGI
  23. regulation of cell cycle Source: UniProtKB
  24. regulation of cell division Source: UniProtKB
  25. regulation of establishment of cell polarity Source: UniProtKB
  26. regulation of establishment of protein localization to plasma membrane Source: Ensembl
  27. regulation of protein localization Source: UniProtKB
  28. rhythmic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Biological rhythms, Cell cycle, Gastrulation, Growth regulation, Translation regulation

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following chain:
Gene namesi
Name:Gnb2l1
Synonyms:Gnb2-rs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:101849. Gnb2l1.

Subcellular locationi

Cell membrane By similarity; 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).By similarity

GO - Cellular componenti

  1. cell body Source: ParkinsonsUK-UCL
  2. cytoplasm Source: MGI
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: Ensembl
  5. dendrite Source: UniProtKB
  6. extracellular vesicular exosome Source: Ensembl
  7. midbody Source: UniProtKB
  8. mitochondrion Source: Ensembl
  9. neuronal cell body Source: MGI
  10. neuron projection Source: ParkinsonsUK-UCL
  11. nucleus Source: UniProtKB
  12. perinuclear region of cytoplasm Source: UniProtKB
  13. phagocytic cup Source: UniProtKB
  14. small ribosomal subunit Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Guanine nucleotide-binding protein subunit beta-2-like 1PRO_0000424482Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 317316Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processedPRO_0000127732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed1 Publication
Modified residuei52 – 521Phosphotyrosine; by ABL1By similarity
Modified residuei130 – 1301N6-acetyllysine1 Publication
Modified residuei183 – 1831N6-acetyllysine1 Publication
Modified residuei228 – 2281PhosphotyrosineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP68040.
PaxDbiP68040.
PRIDEiP68040.

2D gel databases

REPRODUCTION-2DPAGEP68040.
SWISS-2DPAGEP68040.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiP68040.
GenevestigatoriP68040.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IkbkbO883514EBI-296749,EBI-447960

Protein-protein interaction databases

BioGridi199978. 11 interactions.
IntActiP68040. 19 interactions.
MINTiMINT-248042.

Structurei

3D structure databases

ProteinModelPortaliP68040.
SMRiP68040. Positions 2-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati13 – 4432WD 1Add
BLAST
Repeati61 – 9131WD 2Add
BLAST
Repeati103 – 13331WD 3Add
BLAST
Repeati146 – 17833WD 4Add
BLAST
Repeati190 – 22031WD 5Add
BLAST
Repeati231 – 26030WD 6Add
BLAST
Repeati281 – 31131WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat G protein beta family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00770000120570.
HOVERGENiHBG000277.
InParanoidiP68040.
KOiK14753.
OMAiKSIIMWK.
OrthoDBiEOG7BW0JV.
PhylomeDBiP68040.
TreeFamiTF300600.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. 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]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P68040-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET
60 70 80 90 100
NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR
110 120 130 140 150
FVGHTKDVLS VAFSSDNRQI VSGSRDKTIK LWNTLGVCKY TVQDESHSEW
160 170 180 190 200
VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA NCKLKTNHIG HTGYLNTVTV
210 220 230 240 250
SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC FSPNRYWLCA
260 270 280 290 300
ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA
310
GYTDNLVRVW QVTIGTR
Length:317
Mass (Da):35,077
Last modified:January 23, 2007 - v3
Checksum:i257F91E369ED2044
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91G → R in BAE40068. (PubMed:16141072)Curated
Sequence conflicti9 – 91G → R in BAE40156. (PubMed:16141072)Curated
Sequence conflicti125 – 1251R → Q in BAE40059. (PubMed:16141072)Curated
Sequence conflicti125 – 1251R → Q in BAE40068. (PubMed:16141072)Curated
Sequence conflicti125 – 1251R → Q in BAE40156. (PubMed:16141072)Curated
Sequence conflicti248 – 2481L → P in BAE35378. (PubMed:16141072)Curated
Sequence conflicti266 – 2661I → M in AAG29506. (PubMed:15489334)Curated
Sequence conflicti273 – 2731E → A in BAA06185. (PubMed:7968370)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24585.1.
PIRiS38398.
RefSeqiNP_032169.1. NM_008143.3.
UniGeneiMm.5305.

Genome annotation databases

EnsembliENSMUST00000020640; ENSMUSP00000020640; ENSMUSG00000020372.
GeneIDi14694.
KEGGimmu:14694.
UCSCiuc007ipa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS24585.1.
PIRi S38398.
RefSeqi NP_032169.1. NM_008143.3.
UniGenei Mm.5305.

3D structure databases

ProteinModelPortali P68040.
SMRi P68040. Positions 2-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199978. 11 interactions.
IntActi P68040. 19 interactions.
MINTi MINT-248042.

2D gel databases

REPRODUCTION-2DPAGE P68040.
SWISS-2DPAGE P68040.

Proteomic databases

MaxQBi P68040.
PaxDbi P68040.
PRIDEi P68040.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020640 ; ENSMUSP00000020640 ; ENSMUSG00000020372 .
GeneIDi 14694.
KEGGi mmu:14694.
UCSCi uc007ipa.1. mouse.

Organism-specific databases

CTDi 10399.
MGIi MGI:101849. Gnb2l1.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00770000120570.
HOVERGENi HBG000277.
InParanoidi P68040.
KOi K14753.
OMAi KSIIMWK.
OrthoDBi EOG7BW0JV.
PhylomeDBi P68040.
TreeFami TF300600.

Miscellaneous databases

ChiTaRSi Gnb2l1. mouse.
NextBioi 286639.
PROi P68040.
SOURCEi Search...

Gene expression databases

Bgeei P68040.
Genevestigatori P68040.

Family and domain databases

Gene3Di 2.130.10.10. 2 hits.
InterProi IPR020472. 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 ]
Pfami PF00400. WD40. 7 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 7 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiGBLP_MOUSE
AccessioniPrimary (citable) accession number: P68040
Secondary accession number(s): P25388
, P99049, Q3THP0, Q3THY7, Q3TKQ0, Q3TW88, Q5NCC5, Q5NCC6, Q9CSQ0, Q9ERM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3