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O43566 (RGS14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 14

Short name=RGS14
Gene names
Name:RGS14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a regulator of G protein signaling (RGS). Modulates G protein alpha subunits nucleotide exchange and hydrolysis activities by functioning either as a GTPase-activating protein (GAP), thereby driving G protein alpha subunits into their inactive GDP-bound form, or as a GDP-dissociation inhibitor (GDI). Confers GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not G(o) alpha subunit GNAO1 and G(i) alpha subunit GNAI2. Confers GAP activity on G(o) alpha subunit GNAI0 and G(i) alpha subunits GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Probably required for the nerve growth factor (NGF)-mediated neurite outgrowth. May be involved in visual memory processing capacity and hippocampal-based learning and memory. Ref.7 Ref.8

Subunit structure

Interacts with GNAO1 and GNAI2. Interacts (via RGS and GoLoco domains) GNAI1; the interaction occurs in the centrosomes. Interacts with RABGEF1; the interactions is GTP-dependent. Interacts with RAP2A; the interactions is GTP-dependent and does not alter its function on G(i) alpha subunits either as GAP or as GDI. Associates with microtubules. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain) with HRAS (active GTP-bound form preferentially). Interacts (via RBD domains) with BRAF (via N-terminus); the interaction mediates the formation of a ternary complex with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the interaction mediates the formation of a ternary complex with BRAF. Interacts with KRAS (active GTP-bound form preferentially), MRAS (active GTP-bound form preferentially), NRAS (active GTP-bound form preferentially) and RRAS (active GTP-bound form preferentially). Interacts with GNAI1 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization. Interacts with GNAI2. Interacts with GNAI3 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization By similarity. Associates with microtubules.

Subcellular location

Nucleus By similarity. NucleusPML body By similarity. Cytoplasm. Membrane By similarity. Cell membrane By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Note: Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel-shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Relocalizes to the nucleus in PML nuclear bodies in response to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons. Localizes to spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes By similarity. Ref.7

Domain

The RGS domain is necessary for GTPase-activating protein (GAP) activity for G subunits and localization to the nucleus and centrosomes By similarity.

The GoLoco domain is necessary for GDP-dissociation inhibitor (GDI) activity, translocation out of the nucleus and interaction with G(i) alpha subunits GNAI1, GNAI2 and GNAI3 By similarity.

The RBD domains are necessary for localization to the nucleus and centrosomes By similarity.

Post-translational modification

Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1 By similarity.

Sequence similarities

Contains 1 GoLoco domain.

Contains 2 RBD (Ras-binding) domains.

Contains 1 RGS domain.

Sequence caution

The sequence AAB92614.1 differs from that shown. Reason: Frameshift at positions 337, 344, 348, 539 and 544.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Microtubule
Nucleus
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionGTPase activation
Signal transduction inhibitor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell division

Inferred from mutant phenotype Ref.8. Source: UniProtKB

chromosome segregation

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from sequence or structural similarity. Source: GOC

learning

Inferred from sequence or structural similarity. Source: UniProtKB

long-term memory

Inferred from sequence or structural similarity. Source: UniProtKB

long-term synaptic potentiation

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synaptic plasticity

Inferred from sequence or structural similarity. Source: UniProtKB

nucleocytoplasmic transport

Inferred from sequence or structural similarity. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of GTPase activity

Inferred from direct assay Ref.7. Source: GOC

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA-templated transcription in response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Traceable author statement PubMed 9168931. Source: ProtInc

response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

spindle organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

visual learning

Inferred from sequence or structural similarity. Source: UniProtKB

zygote asymmetric cell division

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

spindle

Inferred from direct assay Ref.7. Source: UniProtKB

spindle pole

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP-dissociation inhibitor activity

Inferred from direct assay Ref.7. Source: UniProtKB

GTPase activator activity

Inferred from direct assay Ref.7. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.7. Source: UniProtKB

receptor signaling complex scaffold activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor signaling protein activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43566-7)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: O43566-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     352-354: ALV → VGT
     355-566: Missing.
Isoform 3 (identifier: O43566-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     351-351: Q → QK
Isoform 4 (identifier: O43566-6)

The sequence of this isoform differs from the canonical sequence as follows:
     54-273: Missing.
     351-351: Q → QK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Regulator of G-protein signaling 14
PRO_0000204217

Regions

Domain67 – 184118RGS
Domain302 – 37372RBD 1
Domain375 – 44571RBD 2
Domain498 – 52124GoLoco
Region299 – 425127Necessary for interaction with RABGEF1 By similarity

Amino acid modifications

Modified residue201Phosphoserine Ref.9
Modified residue421Phosphoserine Ref.9
Modified residue451Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 153153Missing in isoform 2 and isoform 3.
VSP_027577
Alternative sequence54 – 273220Missing in isoform 4.
VSP_029426
Alternative sequence3511Q → QK in isoform 3 and isoform 4.
VSP_037959
Alternative sequence352 – 3543ALV → VGT in isoform 2.
VSP_027578
Alternative sequence355 – 566212Missing in isoform 2.
VSP_027579

Experimental info

Sequence conflict4071H → R in BAC85600. Ref.4
Sequence conflict4151V → A in AAY26402. Ref.1
Sequence conflict5021Missing in AAB92614. Ref.2

Secondary structure

.............................. 566
Helix Strand Turn

Details...

Sequences

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

Last modified September 1, 2009. Version 4.
Checksum: 811296228B479C3D

FASTA56661,447
        10         20         30         40         50         60 
MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP SSPFPTEEQP 

        70         80         90        100        110        120 
VASWALSFER LLQDPLGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TQQLAQEARN 

       130        140        150        160        170        180 
IYQEFLSSQA LSPVNIDRQA WLGEEVLAEP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY 

       190        200        210        220        230        240 
RECLLAEAEG RPLREPGSSR LGSPDATRKK PKLKPGKSLP LGVEELGQLP PVEGPGGRPL 

       250        260        270        280        290        300 
RKSFRRELGG TANAALRRES QGSLNSSASL DLGFLAFVSS KSESHRKSLG STEGESESRP 

       310        320        330        340        350        360 
GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP DIKVYLVGNE QALVLDQDCT 

       370        380        390        400        410        420 
VLADQEVRLE NRITFELELT ALERVVRISA KPTKRLQEAL QPILEKHGLS PLEVVLHRPG 

       430        440        450        460        470        480 
EKQPLDLGKL VSSVAAQRLV LDTLPGVKIS KARDKSPCRS QGCPPRTQDK ATHPPPASPS 

       490        500        510        520        530        540 
SLVKVPSSAT GKRQTCDIEG LVELLNRVQS SGAHDQRGLL RKEDLVLPEF LQLPAQGPSS 

       550        560 
EETPPQTKSA AQPIGGSLNS TTDSAL 

« Hide

Isoform 2 [UniParc].

Checksum: 3CBC0E128BC8346E
Show »

FASTA20121,781
Isoform 3 [UniParc].

Checksum: 9B2548AD3346AA00
Show »

FASTA41444,820
Isoform 4 [UniParc].

Checksum: FBB19202385063E6
Show »

FASTA34736,922

References

« Hide 'large scale' references
[1]"Localization of the GoLoco motif carrier regulator of G-protein signalling 12 and 14 proteins in monkey and rat brain."
Lopez-Aranda M.F., Acevedo M.J., Carballo F.J., Gutierrez A., Khan Z.U.
Eur. J. Neurosci. 23:2971-2982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Brain.
[2]Chatterjee T.K., Fisher R.A.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[3]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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. expand/collapse author list , 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] (ISOFORM 4).
Tissue: Caudate nucleus.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORM 1).
Tissue: Colon.
[7]"RGS14 is a microtubule-associated protein."
Martin-McCaffrey L., Willard F.S., Pajak A., Dagnino L., Siderovski D.P., D'Souza S.J.
Cell Cycle 4:953-960(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[8]"Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division."
Cho H., Kehrl J.H.
J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-42 AND SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Structure-based protocol for identifying mutations that enhance protein-protein binding affinities."
Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P., Kuhlman B.
J. Mol. Biol. 371:1392-1404(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 497-532.
[11]"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits."
Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J., Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A., Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 56-207.
[12]"Structural determinants of affinity enhancement between GoLoco motifs and G-protein alpha subunit mutants."
Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M., Kuhlman B., Willard F.S., Siderovski D.P.
J. Biol. Chem. 286:3351-3358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 497-532 IN COMPLEX WITH GNAI1 AND GDP.
+Additional computationally mapped references.

Web resources

Protein Spotlight

A balanced mind - Issue 132 of October 2011

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY987041 mRNA. Translation: AAY26402.1.
AF037194 mRNA. Translation: AAB92613.1.
AF037195 mRNA. Translation: AAB92614.1. Frameshift.
AF493936 mRNA. Translation: AAM12650.1.
AK123382 mRNA. Translation: BAC85600.1.
AC146507 Genomic DNA. No translation available.
BC014094 mRNA. Translation: AAH14094.1.
RefSeqNP_006471.2. NM_006480.4.
UniGeneHs.9347.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNUNMR-A56-207[»]
2OM2X-ray2.20B/D497-532[»]
2XNSX-ray3.41C/D497-520[»]
3ONWX-ray2.38C/D497-532[»]
3QI2X-ray2.80C/D497-532[»]
ProteinModelPortalO43566.
SMRO43566. Positions 56-189, 302-457, 497-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115880. 17 interactions.
DIPDIP-41167N.
IntActO43566. 6 interactions.
MINTMINT-236295.
STRING9606.ENSP00000386229.

PTM databases

PhosphoSiteO43566.

Proteomic databases

PaxDbO43566.
PRIDEO43566.

Protocols and materials databases

DNASU10636.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000408923; ENSP00000386229; ENSG00000169220. [O43566-7]
GeneID10636.
KEGGhsa:10636.
UCSCuc003mgf.3. human. [O43566-7]
uc003mgg.1. human. [O43566-4]

Organism-specific databases

CTD10636.
GeneCardsGC05P176784.
HGNCHGNC:9996. RGS14.
HPAHPA046847.
MIM602513. gene.
neXtProtNX_O43566.
PharmGKBPA34366.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253607.
HOGENOMHOG000049111.
HOVERGENHBG061568.
KOK17706.
OMAPPRTQDK.
OrthoDBEOG7XDBF0.
PhylomeDBO43566.
TreeFamTF328814.

Enzyme and pathway databases

SignaLinkO43566.

Gene expression databases

BgeeO43566.
CleanExHS_RGS14.
GenevestigatorO43566.

Family and domain databases

Gene3D1.10.196.10. 1 hit.
InterProIPR003109. GoLoco_motif.
IPR003116. Raf-like_ras-bd.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43566.
GeneWikiRGS14.
GenomeRNAi10636.
NextBio40425.
PROO43566.
SOURCESearch...

Entry information

Entry nameRGS14_HUMAN
AccessionPrimary (citable) accession number: O43566
Secondary accession number(s): O43565 expand/collapse secondary AC list , Q506M1, Q6ZWA4, Q8TD62
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM