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Protein

Receptor of activated protein C kinase 1

Gene

RACK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). 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.20 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  • enzyme binding Source: BHF-UCL
  • ion channel inhibitor activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein complex scaffold Source: BHF-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • protein kinase C binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein tyrosine kinase inhibitor activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB
  • signaling adaptor activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • cell cycle Source: UniProtKB-KW
  • cellular response to glucose stimulus Source: ParkinsonsUK-UCL
  • cellular response to growth factor stimulus Source: UniProtKB
  • gastrulation Source: UniProtKB-KW
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of endoplasmic reticulum unfolded protein response Source: ParkinsonsUK-UCL
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of hydrogen peroxide-induced neuron death Source: ParkinsonsUK-UCL
  • negative regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • negative regulation of phagocytosis Source: UniProtKB
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • negative regulation of Wnt signaling pathway Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cAMP catabolic process Source: BHF-UCL
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of ceramide biosynthetic process Source: Reactome
  • positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
  • positive regulation of gastrulation Source: UniProtKB
  • positive regulation of Golgi to plasma membrane protein transport Source: UniProtKB
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of mitochondrial depolarization Source: UniProtKB
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • positive regulation of protein homooligomerization Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • regulation of cell division Source: UniProtKB
  • regulation of establishment of cell polarity Source: UniProtKB
  • regulation of protein localization Source: UniProtKB
  • regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
  • rhythmic process Source: UniProtKB-KW
  • 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

BioCyciZFISH:G66-31134-MONOMER.
ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5626978. TNFR1-mediated ceramide production.
SignaLinkiP63244.
SIGNORiP63244.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor of activated protein C kinase 1
Alternative name(s):
Cell proliferation-inducing gene 21 protein
Guanine nucleotide-binding protein subunit beta-2-like 1
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
Cleaved into the following chain:
Alternative name(s):
Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed
Gene namesi
Name:RACK1Imported
Synonyms:GNB2L1
ORF Names:HLC7, PIG21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:4399. RACK1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • dendrite Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • IRE1-RACK1-PP2A complex Source: ParkinsonsUK-UCL
  • midbody Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB
  • phagocytic cup Source: UniProtKB
  • small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52Y → F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. 3 Publications1
Mutagenesisi57R → A: Decreased binding to PTK2/FAK1; when associated with A-60. 1 Publication1
Mutagenesisi60R → A: Decreased binding to PTK2/FAK1; when associated with A-57. 1 Publication1
Mutagenesisi127K → A: Decreased binding to PTK2/FAK1; when associated with A-130. 1 Publication1
Mutagenesisi130K → A: Decreased binding to PTK2/FAK1; when associated with A-127. 1 Publication1
Mutagenesisi140Y → F: No effect on binding to SRC. 2 Publications1
Mutagenesisi194Y → F: No effect on binding to SRC. 2 Publications1
Mutagenesisi228Y → 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 Publications1
Mutagenesisi246Y → F: Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302. 2 Publications1
Mutagenesisi302Y → F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246. 2 Publications1

Organism-specific databases

DisGeNETi10399.
OpenTargetsiENSG00000204628.
PharmGKBiPA28779.

Polymorphism and mutation databases

BioMutaiGNB2L1.
DMDMi54037168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004244801 – 317Receptor of activated protein C kinase 1Add BLAST317
Initiator methionineiRemoved; alternateCombined sources1 Publication
ChainiPRO_00001277312 – 317Receptor of activated protein C kinase 1, N-terminally processedAdd BLAST316

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processedCombined sources1 Publication1
Modified residuei6PhosphothreonineCombined sources1
Modified residuei10PhosphothreonineCombined sources1
Modified residuei52Phosphotyrosine; by ABL11 Publication1
Modified residuei96PhosphothreonineCombined sources1
Modified residuei130N6-acetyllysineCombined sources1
Modified residuei183N6-acetyllysineBy similarity1
Modified residuei228Phosphotyrosine1 Publication1
Modified residuei276PhosphoserineCombined sources1
Modified residuei316PhosphothreonineBy similarity1

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

EPDiP63244.
MaxQBiP63244.
PaxDbiP63244.
PeptideAtlasiP63244.
PRIDEiP63244.
TopDownProteomicsiP63244.

2D gel databases

REPRODUCTION-2DPAGEIPI00848226.
P63244.

PTM databases

iPTMnetiP63244.
PhosphoSitePlusiP63244.
SwissPalmiP63244.

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

BgeeiENSG00000204628.
CleanExiHS_GNB2L1.
ExpressionAtlasiP63244. baseline and differential.
GenevisibleiP63244. HS.

Organism-specific databases

HPAiCAB004288.
HPA021676.

Interactioni

Subunit structurei

Interacts with CPNE3 (PubMed:20010870). May interact with ABCB4 (PubMed:19674157). 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 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 similarity30 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.
BZLF1P032065EBI-296739,EBI-2621186From 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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • protein complex scaffold Source: BHF-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • protein kinase C binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • receptor binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115671. 203 interactors.
DIPiDIP-46736N.
IntActiP63244. 89 interactors.
MINTiMINT-105673.
STRINGi9606.ENSP00000426909.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi18 – 23Combined sources6
Beta strandi30 – 35Combined sources6
Beta strandi40 – 45Combined sources6
Beta strandi48 – 50Combined sources3
Beta strandi52 – 59Combined sources8
Beta strandi66 – 71Combined sources6
Beta strandi75 – 82Combined sources8
Beta strandi85 – 91Combined sources7
Turni92 – 95Combined sources4
Beta strandi96 – 102Combined sources7
Beta strandi108 – 113Combined sources6
Beta strandi120 – 124Combined sources5
Beta strandi129 – 132Combined sources4
Beta strandi138 – 142Combined sources5
Beta strandi144 – 146Combined sources3
Beta strandi151 – 156Combined sources6
Beta strandi160 – 162Combined sources3
Beta strandi164 – 169Combined sources6
Beta strandi174 – 178Combined sources5
Turni179 – 182Combined sources4
Beta strandi183 – 188Combined sources6
Beta strandi195 – 200Combined sources6
Beta strandi204 – 211Combined sources8
Beta strandi215 – 220Combined sources6
Turni221 – 224Combined sources4
Beta strandi225 – 231Combined sources7
Beta strandi236 – 241Combined sources6
Beta strandi243 – 252Combined sources10
Beta strandi255 – 260Combined sources6
Turni261 – 264Combined sources4
Beta strandi265 – 270Combined sources6
Beta strandi286 – 291Combined sources6
Beta strandi295 – 302Combined sources8
Beta strandi307 – 313Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AOWX-ray2.45A/B/C1-317[»]
4UG0electron microscopy-Sg1-317[»]
4V6Xelectron microscopy5.00Ag1-317[»]
5A2Qelectron microscopy3.90g1-315[»]
5AJ0electron microscopy3.50Bg1-317[»]
5FLXelectron microscopy3.90g1-317[»]
ProteinModelPortaliP63244.
SMRiP63244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati13 – 44WD 1Add BLAST32
Repeati61 – 91WD 2Add BLAST31
Repeati103 – 133WD 3Add BLAST31
Repeati146 – 178WD 4Add BLAST33
Repeati190 – 220WD 5Add BLAST31
Repeati231 – 260WD 6Add BLAST30
Repeati281 – 311WD 7Add BLAST31

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

eggNOGiKOG0279. Eukaryota.
ENOG410XQGZ. LUCA.
GeneTreeiENSGT00840000129847.
HOVERGENiHBG000277.
InParanoidiP63244.
KOiK14753.
OMAiATSMENP.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAR24619 differs from that shown. Reason: Frameshift at position 94.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70 – 111Missing in BAG53102 (PubMed:14702039).CuratedAdd BLAST42
Sequence conflicti94T → TRK in AAR24619 (Ref. 3) Curated1
Sequence conflicti221L → F in BAD96208 (Ref. 6) Curated1

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.2. human.

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.
CCDSiCCDS34324.1.
PIRiB33928.
RefSeqiNP_006089.1. NM_006098.4.
UniGeneiHs.5662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AOWX-ray2.45A/B/C1-317[»]
4UG0electron microscopy-Sg1-317[»]
4V6Xelectron microscopy5.00Ag1-317[»]
5A2Qelectron microscopy3.90g1-315[»]
5AJ0electron microscopy3.50Bg1-317[»]
5FLXelectron microscopy3.90g1-317[»]
ProteinModelPortaliP63244.
SMRiP63244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115671. 203 interactors.
DIPiDIP-46736N.
IntActiP63244. 89 interactors.
MINTiMINT-105673.
STRINGi9606.ENSP00000426909.

PTM databases

iPTMnetiP63244.
PhosphoSitePlusiP63244.
SwissPalmiP63244.

Polymorphism and mutation databases

BioMutaiGNB2L1.
DMDMi54037168.

2D gel databases

REPRODUCTION-2DPAGEIPI00848226.
P63244.

Proteomic databases

EPDiP63244.
MaxQBiP63244.
PaxDbiP63244.
PeptideAtlasiP63244.
PRIDEiP63244.
TopDownProteomicsiP63244.

Protocols and materials databases

DNASUi10399.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000512805; ENSP00000426909; ENSG00000204628.
GeneIDi10399.
KEGGihsa:10399.
UCSCiuc003mni.2. human.

Organism-specific databases

CTDi10399.
DisGeNETi10399.
GeneCardsiGNB2L1.
HGNCiHGNC:4399. RACK1.
HPAiCAB004288.
HPA021676.
MIMi176981. gene.
neXtProtiNX_P63244.
OpenTargetsiENSG00000204628.
PharmGKBiPA28779.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0279. Eukaryota.
ENOG410XQGZ. LUCA.
GeneTreeiENSGT00840000129847.
HOVERGENiHBG000277.
InParanoidiP63244.
KOiK14753.
OMAiATSMENP.
PhylomeDBiP63244.
TreeFamiTF300600.

Enzyme and pathway databases

BioCyciZFISH:G66-31134-MONOMER.
ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5626978. TNFR1-mediated ceramide production.
SignaLinkiP63244.
SIGNORiP63244.

Miscellaneous databases

ChiTaRSiGNB2L1. human.
GeneWikiiGNB2L1.
GenomeRNAii10399.
PROiP63244.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204628.
CleanExiHS_GNB2L1.
ExpressionAtlasiP63244. baseline and differential.
GenevisibleiP63244. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiRACK1_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 30, 2016
This is version 135 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

Similar proteinsi

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