Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

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

O43566

- RGS14_HUMAN

UniProt

O43566 - RGS14_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 4 (01 Sep 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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. PML body Source: UniProtKB-SubCell
    11. postsynaptic density Source: UniProtKB
    12. postsynaptic membrane Source: UniProtKB-KW
    13. spindle Source: UniProtKB
    14. spindle pole Source: UniProtKB

    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.
    HOGENOMiHOG000049111.
    HOVERGENiHBG061568.
    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

    MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP    50
    SSPFPTEEQP VASWALSFER LLQDPLGLAY FTEFLKKEFS AENVTFWKAC 100
    ERFQQIPASD TQQLAQEARN IYQEFLSSQA LSPVNIDRQA WLGEEVLAEP 150
    RPDMFRAQQL QIFNLMKFDS YARFVKSPLY RECLLAEAEG RPLREPGSSR 200
    LGSPDATRKK PKLKPGKSLP LGVEELGQLP PVEGPGGRPL RKSFRRELGG 250
    TANAALRRES QGSLNSSASL DLGFLAFVSS KSESHRKSLG STEGESESRP 300
    GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP DIKVYLVGNE 350
    QALVLDQDCT VLADQEVRLE NRITFELELT ALERVVRISA KPTKRLQEAL 400
    QPILEKHGLS PLEVVLHRPG EKQPLDLGKL VSSVAAQRLV LDTLPGVKIS 450
    KARDKSPCRS QGCPPRTQDK ATHPPPASPS SLVKVPSSAT GKRQTCDIEG 500
    LVELLNRVQS SGAHDQRGLL RKEDLVLPEF LQLPAQGPSS EETPPQTKSA 550
    AQPIGGSLNS TTDSAL 566

    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.
    HOGENOMi HOG000049111.
    HOVERGENi HBG061568.
    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

    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 1, 2014
    This is version 137 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

    Dasty 3