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P63244

- GBLP_HUMAN

UniProt

P63244 - GBLP_HUMAN

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Protein

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

Gene

GNB2L1

Organism
Homo sapiens (Human)
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. Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. Enhances phosphorylation of HIV-1 Nef by PKCs. Promotes migration of breast carcinoma cells by binding to and activating RHOA.19 Publications

GO - Molecular functioni

  1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  2. enzyme binding Source: BHF-UCL
  3. ion channel inhibitor activity Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. protein complex scaffold Source: BHF-UCL
  6. protein homodimerization activity Source: ParkinsonsUK-UCL
  7. protein kinase C binding Source: UniProtKB
  8. protein phosphatase binding Source: UniProtKB
  9. protein tyrosine kinase inhibitor activity Source: UniProtKB
  10. receptor binding Source: UniProtKB
  11. receptor tyrosine kinase binding Source: UniProtKB
  12. SH2 domain binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. cell cycle Source: UniProtKB-KW
  3. gastrulation Source: UniProtKB-KW
  4. negative regulation of cell growth Source: UniProtKB
  5. negative regulation of gene expression Source: UniProt
  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: UniProtKB
  9. negative regulation of protein tyrosine kinase activity Source: GOC
  10. negative regulation of translation Source: UniProtKB
  11. negative regulation of Wnt signaling pathway Source: UniProtKB
  12. positive regulation of apoptotic process Source: UniProtKB
  13. positive regulation of cAMP catabolic process Source: BHF-UCL
  14. positive regulation of cell migration Source: UniProtKB
  15. positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
  16. positive regulation of gastrulation Source: UniProtKB
  17. positive regulation of GTPase activity Source: UniProtKB
  18. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  19. positive regulation of mitochondrial depolarization Source: UniProtKB
  20. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  21. positive regulation of protein homooligomerization Source: UniProtKB
  22. positive regulation of protein phosphorylation Source: UniProtKB
  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
  29. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Biological rhythms, Cell cycle, Gastrulation, Growth regulation, Host-virus interaction, Translation regulation

Enzyme and pathway databases

SignaLinkiP63244.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit beta-2-like 1
Alternative name(s):
Cell proliferation-inducing gene 21 protein
Guanine nucleotide-binding protein subunit beta-like protein 12.3
Human lung cancer oncogene 7 protein
Short name:
HLC-7
Receptor for activated C kinase
Receptor of activated protein kinase C 1
Short name:
RACK1
Cleaved into the following chain:
Gene namesi
Name:GNB2L1
ORF Names:HLC7, PIG21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4399. GNB2L1.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasmperinuclear region. Cytoplasmcytoskeleton. Nucleus. Perikaryon By similarity. Cell projectiondendrite By similarity. Cell projectionphagocytic cup
Note: Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. 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. Localized to phagocytic cups following infection by Y.pestis.

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521Y → F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. 3 Publications
Mutagenesisi57 – 571R → A: Decreased binding to PTK2/FAK1; when associated with A-60. 1 Publication
Mutagenesisi60 – 601R → A: Decreased binding to PTK2/FAK1; when associated with A-57. 1 Publication
Mutagenesisi127 – 1271K → A: Decreased binding to PTK2/FAK1; when associated with A-130. 1 Publication
Mutagenesisi130 – 1301K → A: Decreased binding to PTK2/FAK1; when associated with A-127. 1 Publication
Mutagenesisi140 – 1401Y → F: No effect on binding to SRC. 2 Publications
Mutagenesisi194 – 1941Y → F: No effect on binding to SRC. 2 Publications
Mutagenesisi228 – 2281Y → F: No effect on binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-246 and F-302. 2 Publications
Mutagenesisi246 – 2461Y → F: Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302. 2 Publications
Mutagenesisi302 – 3021Y → F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246. 2 Publications

Organism-specific databases

PharmGKBiPA28779.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Guanine nucleotide-binding protein subunit beta-2-like 1PRO_0000424480Add
BLAST
Initiator methioninei1 – 11Removed; alternate4 Publications
Chaini2 – 317316Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processedPRO_0000127731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed5 Publications
Modified residuei52 – 521Phosphotyrosine; by ABL11 Publication
Modified residuei130 – 1301N6-acetyllysine1 Publication
Modified residuei183 – 1831N6-acetyllysineBy similarity
Modified residuei228 – 2281Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP63244.
PaxDbiP63244.
PRIDEiP63244.

2D gel databases

REPRODUCTION-2DPAGEIPI00848226.
P63244.

PTM databases

PhosphoSiteiP63244.

Expressioni

Tissue specificityi

In the liver, expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue.1 Publication

Gene expression databases

BgeeiP63244.
CleanExiHS_GNB2L1.
ExpressionAtlasiP63244. baseline and differential.
GenevestigatoriP63244.

Organism-specific databases

HPAiCAB004288.
HPA021676.

Interactioni

Subunit structurei

Component of the small (40S) ribosomal subunit (By similarity). Interacts with the 80S ribosome. 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 TBXA2R isoform 2. Interacts with HRAS. Interacts with LARP4B. Interacts with PKD2L1. Interacts with Y.pseudotuberculosis yopK. Interacts with a number of viral proteins including Epstein-Barr virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef phosphorylation by PKC.By similarity28 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACHEP223032EBI-296739,EBI-1637793
AGO2Q9UKV82EBI-296739,EBI-528269
BCL2L11O435212EBI-296739,EBI-526406
Bcl2l11O54918-12EBI-296739,EBI-526076From a different organism.
DYNLL1P631676EBI-296739,EBI-349105
IFNAR2P485514EBI-296739,EBI-958408
LRP12Q9Y5612EBI-296739,EBI-296693
LYNP079482EBI-296739,EBI-79452
PAG1Q9NWQ82EBI-296739,EBI-2828115
PARK7Q994974EBI-296739,EBI-1164361
PIAS2O759282EBI-296739,EBI-348555
PPIDQ087524EBI-296739,EBI-716596
VHLP403379EBI-296739,EBI-301246

Protein-protein interaction databases

BioGridi115671. 164 interactions.
DIPiDIP-46736N.
IntActiP63244. 73 interactions.
MINTiMINT-105673.
STRINGi9606.ENSP00000366013.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi18 – 236Combined sources
Beta strandi30 – 356Combined sources
Beta strandi40 – 456Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 598Combined sources
Beta strandi66 – 716Combined sources
Beta strandi75 – 828Combined sources
Beta strandi85 – 917Combined sources
Turni92 – 954Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi174 – 1785Combined sources
Turni179 – 1824Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi215 – 2206Combined sources
Turni221 – 2244Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi243 – 25210Combined sources
Beta strandi255 – 2606Combined sources
Turni261 – 2644Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi286 – 2916Combined sources
Beta strandi295 – 3028Combined sources
Beta strandi307 – 3137Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00g1-317[»]
4AOWX-ray2.45A/B/C1-317[»]
ProteinModelPortaliP63244.
SMRiP63244. 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.
InParanoidiP63244.
KOiK14753.
OMAiKSIIMWK.
PhylomeDBiP63244.
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.

P63244-1 [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 AAO21313.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAR24619.1 differs from that shown. Reason: Frameshift at position 94. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 11142Missing in BAG53102. (PubMed:14702039)CuratedAdd
BLAST
Sequence conflicti94 – 941T → TRK in AAR24619. 1 PublicationCurated
Sequence conflicti221 – 2211L → F in BAD96208. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24194 mRNA. Translation: AAA59626.1.
AY159316 mRNA. Translation: AAO21313.1. Different initiation.
AY336089 mRNA. Translation: AAR24619.1. Frameshift.
AK095666 mRNA. Translation: BAG53102.1.
CR456978 mRNA. Translation: CAG33259.1.
CR541909 mRNA. Translation: CAG46707.1.
AK222488 mRNA. Translation: BAD96208.1.
CH471165 Genomic DNA. Translation: EAW53692.1.
CH471165 Genomic DNA. Translation: EAW53702.1.
BC000214 mRNA. Translation: AAH00214.1.
BC000366 mRNA. Translation: AAH00366.1.
BC010119 mRNA. Translation: AAH10119.1.
BC014256 mRNA. Translation: AAH14256.1.
BC014788 mRNA. Translation: AAH14788.1.
BC017287 mRNA. Translation: AAH17287.1.
BC019093 mRNA. Translation: AAH19093.1.
BC019362 mRNA. Translation: AAH19362.1.
BC021993 mRNA. Translation: AAH21993.1.
BC032006 mRNA. Translation: AAH32006.1.
CCDSiCCDS34324.1.
PIRiB33928.
RefSeqiNP_006089.1. NM_006098.4.
UniGeneiHs.5662.

Genome annotation databases

EnsembliENST00000512805; ENSP00000426909; ENSG00000204628.
GeneIDi10399.
KEGGihsa:10399.
UCSCiuc003mni.1. human.

Polymorphism databases

DMDMi54037168.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24194 mRNA. Translation: AAA59626.1 .
AY159316 mRNA. Translation: AAO21313.1 . Different initiation.
AY336089 mRNA. Translation: AAR24619.1 . Frameshift.
AK095666 mRNA. Translation: BAG53102.1 .
CR456978 mRNA. Translation: CAG33259.1 .
CR541909 mRNA. Translation: CAG46707.1 .
AK222488 mRNA. Translation: BAD96208.1 .
CH471165 Genomic DNA. Translation: EAW53692.1 .
CH471165 Genomic DNA. Translation: EAW53702.1 .
BC000214 mRNA. Translation: AAH00214.1 .
BC000366 mRNA. Translation: AAH00366.1 .
BC010119 mRNA. Translation: AAH10119.1 .
BC014256 mRNA. Translation: AAH14256.1 .
BC014788 mRNA. Translation: AAH14788.1 .
BC017287 mRNA. Translation: AAH17287.1 .
BC019093 mRNA. Translation: AAH19093.1 .
BC019362 mRNA. Translation: AAH19362.1 .
BC021993 mRNA. Translation: AAH21993.1 .
BC032006 mRNA. Translation: AAH32006.1 .
CCDSi CCDS34324.1.
PIRi B33928.
RefSeqi NP_006089.1. NM_006098.4.
UniGenei Hs.5662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 g 1-317 [» ]
4AOW X-ray 2.45 A/B/C 1-317 [» ]
ProteinModelPortali P63244.
SMRi P63244. Positions 2-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115671. 164 interactions.
DIPi DIP-46736N.
IntActi P63244. 73 interactions.
MINTi MINT-105673.
STRINGi 9606.ENSP00000366013.

PTM databases

PhosphoSitei P63244.

Polymorphism databases

DMDMi 54037168.

2D gel databases

REPRODUCTION-2DPAGE IPI00848226.
P63244.

Proteomic databases

MaxQBi P63244.
PaxDbi P63244.
PRIDEi P63244.

Protocols and materials databases

DNASUi 10399.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000512805 ; ENSP00000426909 ; ENSG00000204628 .
GeneIDi 10399.
KEGGi hsa:10399.
UCSCi uc003mni.1. human.

Organism-specific databases

CTDi 10399.
GeneCardsi GC05M180663.
HGNCi HGNC:4399. GNB2L1.
HPAi CAB004288.
HPA021676.
MIMi 176981. gene.
neXtProti NX_P63244.
PharmGKBi PA28779.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00770000120570.
HOVERGENi HBG000277.
InParanoidi P63244.
KOi K14753.
OMAi KSIIMWK.
PhylomeDBi P63244.
TreeFami TF300600.

Enzyme and pathway databases

SignaLinki P63244.

Miscellaneous databases

ChiTaRSi GNB2L1. human.
GeneWikii GNB2L1.
GenomeRNAii 10399.
NextBioi 39404.
PROi P63244.
SOURCEi Search...

Gene expression databases

Bgeei P63244.
CleanExi HS_GNB2L1.
ExpressionAtlasi P63244. baseline and differential.
Genevestigatori P63244.

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. "Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex."
    Guillemot F., Billault A., Auffray C.
    Proc. Natl. Acad. Sci. U.S.A. 86:4594-4598(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of new tumor-related gene in human lung cancer."
    Kim J.W.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Identification of a proliferation-inducing gene."
    Kim J.W.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: B-cell, Brain, Cervix, Lung, Lymph, Ovary and Skin.
  9. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 48-57; 107-118; 258-280 AND 309-317, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and T-cell.
  10. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 48-57; 107-118; 140-155 AND 226-245, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  11. "RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells."
    Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.
    Mol. Cell. Biol. 18:3245-3256(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRC.
  12. "The PKC targeting protein RACK1 interacts with the Epstein-Barr virus activator protein BZLF1."
    Baumann M., Gires O., Kolch W., Mischak H., Zeidler R., Pich D., Hammerschmidt W.
    Eur. J. Biochem. 267:3891-3901(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1, SUBCELLULAR LOCATION.
  13. "The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1."
    Chang B.Y., Chiang M., Cartwright C.A.
    J. Biol. Chem. 276:20346-20356(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-228, MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; TYR-246 AND TYR-302.
  14. "Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor."
    Gallina A., Rossi F., Milanesi G.
    Virology 283:7-18(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIV-1 NEF, SUBCELLULAR LOCATION.
  15. "Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor."
    Liedtke C.M., Yun C.H.C., Kyle N., Wang D.
    J. Biol. Chem. 277:22925-22933(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1.
  16. "RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting protein, modulates IGF-I-dependent integrin signaling and promotes cell spreading and contact with extracellular matrix."
    Hermanto U., Zong C.S., Li W., Wang L.H.
    Mol. Cell. Biol. 22:2345-2365(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IGF1R.
  17. "RACK1: a novel substrate for the Src protein-tyrosine kinase."
    Chang B.Y., Harte R.A., Cartwright C.A.
    Oncogene 21:7619-7629(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; TYR-246 AND TYR-302.
  18. "Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus."
    Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C., Guinovart J.J., Bach-Elias M.
    Cancer Res. 63:5178-5187(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRAS.
  19. "The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway."
    Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.
    J. Biol. Chem. 278:46087-46093(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION.
  20. "RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic cell migration via its Src-binding site."
    Cox E.A., Bennin D., Doan A.T., O'Toole T., Huttenlocher A.
    Mol. Biol. Cell 14:658-669(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Muscle ring finger protein-1 inhibits PKC-epsilon activation and prevents cardiomyocyte hypertrophy."
    Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., Patterson C.
    J. Cell Biol. 167:1147-1159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM63 AND PRKCE.
  22. "Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate-activated protein kinase C."
    Nery F.C., Passos D.O., Garcia V.S., Kobarg J.
    J. Biol. Chem. 279:11444-11455(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HABP4.
  23. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine phosphorylation and function of the androgen receptor."
    Kraus S., Gioeli D., Vomastek T., Gordon V., Weber M.J.
    Cancer Res. 66:11047-11054(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AR.
  25. "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."
    Chuang N.N., Huang C.C.
    Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KRT1, SUBCELLULAR LOCATION.
  26. "RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha."
    Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L.
    Mol. Cell 25:207-217(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIF1A, IDENTIFICATION BY MASS SPECTROMETRY.
  27. "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.
  28. "RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis."
    Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., Theret N.
    J. Biol. Chem. 283:26000-26009(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADAM12, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  29. "RACK1 regulates the cell surface expression of the G protein-coupled receptor for thromboxane A(2)."
    Parent A., Laroche G., Hamelin E., Parent J.L.
    Traffic 9:394-407(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBXA2R, SUBCELLULAR LOCATION.
  30. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome degradation."
    Ruan Y., Guo L., Qiao Y., Hong Y., Zhou L., Sun L., Wang L., Zhu H., Wang L., Yun X., Xie J., Gu J.
    Biochem. Biophys. Res. Commun. 390:217-222(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLEC1B, SUBCELLULAR LOCATION.
  32. "Structural basis and specificity of human otubain 1-mediated deubiquitination."
    Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B., Fiebiger E., Dhe-Paganon S., Kessler B.M.
    Biochem. J. 418:379-390(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OTUB1.
  33. "Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase."
    Kiely P.A., Baillie G.S., Barrett R., Buckley D.A., Adams D.R., Houslay M.D., O'Connor R.
    J. Biol. Chem. 284:20263-20274(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION AT TYR-52, MUTAGENESIS OF TYR-52; ARG-57; ARG-60; LYS-127 AND LYS-130.
  34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "RACK1 promotes Bax oligomerization and dissociates the interaction of Bax and Bcl-XL."
    Wu Y., Wang Y., Sun Y., Zhang L., Wang D., Ren F., Chang D., Chang Z., Jia B.
    Cell. Signal. 22:1495-1501(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BAX.
  36. "RACK1 associates with muscarinic receptors and regulates M(2) receptor trafficking."
    Reiner C.L., McCullar J.S., Kow R.L., Le J.H., Goodlett D.R., Nathanson N.M.
    PLoS ONE 5:E13517-E13517(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHRM2, IDENTIFICATION BY MASS SPECTROMETRY.
  37. "A stimulatory role for the La-related protein 4B in translation."
    Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.
    RNA 16:1488-1499(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PABPC1 AND GNB2L1.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway."
    Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D., Liu X.P.
    Breast Cancer Res. Treat. 126:555-563(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
  40. "RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3-K/Akt pathway."
    Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.
    J. Biol. Chem. 286:9097-9106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FLT1.
  41. "The RACK1 signaling scaffold protein selectively interacts with Yersinia pseudotuberculosis virulence function."
    Thorslund S.E., Edgren T., Pettersson J., Nordfelth R., Sellin M.E., Ivanova E., Francis M.S., Isaksson E.L., Wolf-Watz H., Fallman M.
    PLoS ONE 6:E16784-E16784(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPK, SUBCELLULAR LOCATION.
  42. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. "Receptor for activated C kinase 1 (RACK1) inhibits function of transient receptor potential (TRP)-type channel Pkd2L1 through physical interaction."
    Yang J., Wang Q., Zheng W., Tuli J., Li Q., Wu Y., Hussein S., Dai X.Q., Shafiei S., Li X.G., Shen P.Y., Tu J.C., Chen X.Z.
    J. Biol. Chem. 287:6551-6561(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKD2L1.
  44. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  45. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  46. Cited for: X-RAY SCATTERING SOLUTION STRUCTURE, INTERACTION WITH HABP4.
  47. Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
  48. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S RIBOSOME, SUBUNIT.

Entry informationi

Entry nameiGBLP_HUMAN
AccessioniPrimary (citable) accession number: P63244
Secondary accession number(s): B3KTJ0
, D3DWS0, P25388, P99049, Q53HU2, Q5J8M6, Q5VLR4, Q6FH47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3