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O43566

- RGS14_HUMAN

UniProt

O43566 - RGS14_HUMAN

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Protein

Regulator of G-protein signaling 14

Gene

RGS14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. GDP-dissociation inhibitor activity Source: UniProtKB
  2. GTPase activator activity Source: UniProtKB
  3. microtubule binding Source: UniProtKB
  4. receptor signaling complex scaffold activity Source: UniProtKB
  5. receptor signaling protein activity Source: UniProtKB

GO - Biological processi

  1. cell division Source: UniProtKB
  2. chromosome segregation Source: UniProtKB
  3. intracellular signal transduction Source: GOC
  4. learning Source: UniProtKB
  5. long-term memory Source: UniProtKB
  6. long-term synaptic potentiation Source: UniProtKB
  7. mitotic nuclear division Source: Ensembl
  8. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  9. negative regulation of MAP kinase activity Source: UniProtKB
  10. negative regulation of synaptic plasticity Source: UniProtKB
  11. nucleocytoplasmic transport Source: UniProtKB
  12. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  13. positive regulation of GTPase activity Source: GOC
  14. positive regulation of neurogenesis Source: UniProtKB
  15. regulation of DNA-templated transcription in response to stress Source: UniProtKB
  16. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  17. response to oxidative stress Source: UniProtKB
  18. spindle organization Source: UniProtKB
  19. termination of G-protein coupled receptor signaling pathway Source: InterPro
  20. visual learning Source: UniProtKB
  21. zygote asymmetric cell division Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Signal transduction inhibitor

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiREACT_19231. G alpha (i) signalling events.
SignaLinkiO43566.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 14
Short name:
RGS14
Gene namesi
Name:RGS14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9996. RGS14.

Subcellular locationi

Nucleus By similarity. NucleusPML body By similarity. Cytoplasm 1 Publication. Membrane By similarity. Cell membrane By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle 1 Publication. 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).By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. dendrite Source: UniProtKB
  5. dendritic spine Source: UniProtKB
  6. microtubule Source: UniProtKB-KW
  7. nuclear body Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. plasma membrane Source: UniProtKB
  10. postsynaptic density Source: UniProtKB
  11. postsynaptic membrane Source: UniProtKB-KW
  12. spindle Source: UniProtKB
  13. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34366.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566Regulator of G-protein signaling 14PRO_0000204217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43566.
PaxDbiO43566.
PRIDEiO43566.

PTM databases

PhosphoSiteiO43566.

Expressioni

Gene expression databases

BgeeiO43566.
CleanExiHS_RGS14.
GenevestigatoriO43566.

Organism-specific databases

HPAiHPA046847.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi115880. 17 interactions.
DIPiDIP-41167N.
IntActiO43566. 6 interactions.
MINTiMINT-236295.
STRINGi9606.ENSP00000386229.

Structurei

Secondary structure

1
566
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi61 – 655
Helixi68 – 736
Helixi75 – 8410
Beta strandi87 – 893
Helixi92 – 10514
Helixi111 – 12515
Helixi144 – 1485
Turni152 – 1554
Helixi156 – 16712
Helixi170 – 1745
Helixi180 – 1845
Helixi499 – 50911
Beta strandi517 – 5193
Turni522 – 5254
Helixi529 – 5313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JNUNMR-A56-207[»]
2OM2X-ray2.20B/D497-532[»]
2XNSX-ray3.41C/D497-517[»]
3ONWX-ray2.38C/D497-532[»]
3QI2X-ray2.80C/D497-532[»]
ProteinModelPortaliO43566.
SMRiO43566. Positions 56-189, 363-457, 497-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43566.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 184118RGSPROSITE-ProRule annotationAdd
BLAST
Domaini302 – 37372RBD 1PROSITE-ProRule annotationAdd
BLAST
Domaini375 – 44571RBD 2PROSITE-ProRule annotationAdd
BLAST
Domaini498 – 52124GoLocoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni299 – 425127Necessary for interaction with RABGEF1By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 GoLoco domain.PROSITE-ProRule annotation
Contains 2 RBD (Ras-binding) domains.PROSITE-ProRule annotation
Contains 1 RGS domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG253607.
GeneTreeiENSGT00760000119142.
HOGENOMiHOG000049111.
HOVERGENiHBG061568.
InParanoidiO43566.
KOiK17706.
OMAiPPRTQDK.
OrthoDBiEOG7XDBF0.
PhylomeDBiO43566.
TreeFamiTF328814.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR003109. GoLoco_motif.
IPR003116. Raf-like_ras-bd.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43566-7) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP
60 70 80 90 100
SSPFPTEEQP VASWALSFER LLQDPLGLAY FTEFLKKEFS AENVTFWKAC
110 120 130 140 150
ERFQQIPASD TQQLAQEARN IYQEFLSSQA LSPVNIDRQA WLGEEVLAEP
160 170 180 190 200
RPDMFRAQQL QIFNLMKFDS YARFVKSPLY RECLLAEAEG RPLREPGSSR
210 220 230 240 250
LGSPDATRKK PKLKPGKSLP LGVEELGQLP PVEGPGGRPL RKSFRRELGG
260 270 280 290 300
TANAALRRES QGSLNSSASL DLGFLAFVSS KSESHRKSLG STEGESESRP
310 320 330 340 350
GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP DIKVYLVGNE
360 370 380 390 400
QALVLDQDCT VLADQEVRLE NRITFELELT ALERVVRISA KPTKRLQEAL
410 420 430 440 450
QPILEKHGLS PLEVVLHRPG EKQPLDLGKL VSSVAAQRLV LDTLPGVKIS
460 470 480 490 500
KARDKSPCRS QGCPPRTQDK ATHPPPASPS SLVKVPSSAT GKRQTCDIEG
510 520 530 540 550
LVELLNRVQS SGAHDQRGLL RKEDLVLPEF LQLPAQGPSS EETPPQTKSA
560
AQPIGGSLNS TTDSAL

Note: No experimental confirmation available.

Length:566
Mass (Da):61,447
Last modified:September 1, 2009 - v4
Checksum:i811296228B479C3D
GO
Isoform 2 (identifier: O43566-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     352-354: ALV → VGT
     355-566: Missing.

Show »
Length:201
Mass (Da):21,781
Checksum:i3CBC0E128BC8346E
GO
Isoform 3 (identifier: O43566-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     351-351: Q → QK

Show »
Length:414
Mass (Da):44,820
Checksum:i9B2548AD3346AA00
GO
Isoform 4 (identifier: O43566-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-273: Missing.
     351-351: Q → QK

Note: No experimental confirmation available.

Show »
Length:347
Mass (Da):36,922
Checksum:iFBB19202385063E6
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti407 – 4071H → R in BAC85600. (PubMed:14702039)Curated
Sequence conflicti415 – 4151V → A in AAY26402. (PubMed:16819986)Curated
Sequence conflicti502 – 5021Missing in AAB92614. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 153153Missing in isoform 2 and isoform 3. 3 PublicationsVSP_027577Add
BLAST
Alternative sequencei54 – 273220Missing in isoform 4. 1 PublicationVSP_029426Add
BLAST
Alternative sequencei351 – 3511Q → QK in isoform 3 and isoform 4. 3 PublicationsVSP_037959
Alternative sequencei352 – 3543ALV → VGT in isoform 2. 2 PublicationsVSP_027578
Alternative sequencei355 – 566212Missing in isoform 2. 2 PublicationsVSP_027579Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43405.1. [O43566-7]
RefSeqiNP_006471.2. NM_006480.4. [O43566-7]
UniGeneiHs.9347.

Genome annotation databases

EnsembliENST00000408923; ENSP00000386229; ENSG00000169220. [O43566-7]
GeneIDi10636.
KEGGihsa:10636.
UCSCiuc003mgf.3. human. [O43566-7]
uc003mgg.1. human. [O43566-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

A balanced mind - Issue 132 of October 2011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43405.1. [O43566-7 ]
RefSeqi NP_006471.2. NM_006480.4. [O43566-7 ]
UniGenei Hs.9347.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JNU NMR - A 56-207 [» ]
2OM2 X-ray 2.20 B/D 497-532 [» ]
2XNS X-ray 3.41 C/D 497-517 [» ]
3ONW X-ray 2.38 C/D 497-532 [» ]
3QI2 X-ray 2.80 C/D 497-532 [» ]
ProteinModelPortali O43566.
SMRi O43566. Positions 56-189, 363-457, 497-532.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115880. 17 interactions.
DIPi DIP-41167N.
IntActi O43566. 6 interactions.
MINTi MINT-236295.
STRINGi 9606.ENSP00000386229.

PTM databases

PhosphoSitei O43566.

Proteomic databases

MaxQBi O43566.
PaxDbi O43566.
PRIDEi O43566.

Protocols and materials databases

DNASUi 10636.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000408923 ; ENSP00000386229 ; ENSG00000169220 . [O43566-7 ]
GeneIDi 10636.
KEGGi hsa:10636.
UCSCi uc003mgf.3. human. [O43566-7 ]
uc003mgg.1. human. [O43566-4 ]

Organism-specific databases

CTDi 10636.
GeneCardsi GC05P176784.
HGNCi HGNC:9996. RGS14.
HPAi HPA046847.
MIMi 602513. gene.
neXtProti NX_O43566.
PharmGKBi PA34366.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253607.
GeneTreei ENSGT00760000119142.
HOGENOMi HOG000049111.
HOVERGENi HBG061568.
InParanoidi O43566.
KOi K17706.
OMAi PPRTQDK.
OrthoDBi EOG7XDBF0.
PhylomeDBi O43566.
TreeFami TF328814.

Enzyme and pathway databases

Reactomei REACT_19231. G alpha (i) signalling events.
SignaLinki O43566.

Miscellaneous databases

EvolutionaryTracei O43566.
GeneWikii RGS14.
GenomeRNAii 10636.
NextBioi 40425.
PROi O43566.
SOURCEi Search...

Gene expression databases

Bgeei O43566.
CleanExi HS_RGS14.
Genevestigatori O43566.

Family and domain databases

Gene3Di 1.10.196.10. 1 hit.
InterProi IPR003109. GoLoco_motif.
IPR003116. Raf-like_ras-bd.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEi PS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiRGS14_HUMAN
AccessioniPrimary (citable) accession number: O43566
Secondary accession number(s): O43565
, Q506M1, Q6ZWA4, Q8TD62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 1, 2009
Last modified: October 29, 2014
This is version 138 of the entry and version 4 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, 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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