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P19086

- GNAZ_HUMAN

UniProt

P19086 - GNAZ_HUMAN

Protein

Guanine nucleotide-binding protein G(z) subunit alpha

Gene

GNAZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471MagnesiumBy similarity
    Metal bindingi182 – 1821MagnesiumBy similarity
    Binding sitei327 – 3271GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi40 – 478GTPBy similarity
    Nucleotide bindingi176 – 1827GTPBy similarity
    Nucleotide bindingi201 – 2055GTPBy similarity
    Nucleotide bindingi270 – 2734GTPBy similarity

    GO - Molecular functioni

    1. G-protein beta/gamma-subunit complex binding Source: RefGenome
    2. G-protein coupled serotonin receptor binding Source: RefGenome
    3. GTPase activity Source: RefGenome
    4. GTP binding Source: UniProtKB-KW
    5. metal ion binding Source: UniProtKB-KW
    6. receptor signaling protein activity Source: ProtInc
    7. signal transducer activity Source: RefGenome

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: Ensembl
    2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
    3. G-protein coupled receptor signaling pathway Source: ProtInc
    4. intracellular signal transduction Source: GOC

    Keywords - Molecular functioni

    Transducer

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15426. PLC beta mediated events.
    REACT_15457. G-protein activation.
    REACT_19231. G alpha (i) signalling events.
    REACT_19327. G alpha (s) signalling events.
    REACT_19333. G alpha (z) signalling events.
    SignaLinkiP19086.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(z) subunit alpha
    Alternative name(s):
    G(x) alpha chain
    Gz-alpha
    Gene namesi
    Name:GNAZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4395. GNAZ.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum Source: ProtInc
    3. extracellular vesicular exosome Source: UniProt
    4. heterotrimeric G-protein complex Source: RefGenome
    5. nuclear envelope Source: ProtInc
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28775.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 355354Guanine nucleotide-binding protein G(z) subunit alphaPRO_0000203696Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Modified residuei179 – 1791ADP-ribosylarginine; by cholera toxinBy similarity

    Keywords - PTMi

    ADP-ribosylation, Lipoprotein, Myristate, Palmitate

    Proteomic databases

    MaxQBiP19086.
    PaxDbiP19086.
    PRIDEiP19086.

    PTM databases

    PhosphoSiteiP19086.

    Expressioni

    Gene expression databases

    BgeeiP19086.
    CleanExiHS_GNAZ.
    GenevestigatoriP19086.

    Organism-specific databases

    HPAiHPA003011.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.

    Protein-protein interaction databases

    BioGridi109043. 10 interactions.
    IntActiP19086. 11 interactions.
    MINTiMINT-139942.
    STRINGi9606.ENSP00000248996.

    Structurei

    3D structure databases

    ProteinModelPortaliP19086.
    SMRiP19086. Positions 6-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-alpha family. G(i/o/t/z) subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG282619.
    HOGENOMiHOG000038730.
    HOVERGENiHBG063184.
    InParanoidiP19086.
    KOiK04535.
    OMAiDYKGQNT.
    OrthoDBiEOG72C50B.
    PhylomeDBiP19086.
    TreeFamiTF300673.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR001408. Gprotein_alpha_I.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR00441. GPROTEINAI.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P19086-1 [UniParc]FASTAAdd to Basket

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    MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV    50
    KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR 100
    AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE 150
    DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV 200
    DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL 250
    FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA 300
    AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK 350
    YIGLC 355
    Length:355
    Mass (Da):40,924
    Last modified:January 23, 2007 - v3
    Checksum:iE868FAE7CD2873EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321W → Y(PubMed:1908722)Curated
    Sequence conflicti230 – 2301G → A in BAA14180. (PubMed:2115889)Curated
    Sequence conflicti273 – 2731D → N(PubMed:1908722)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03260 mRNA. Translation: AAA52580.1.
    D90150 Genomic DNA. Translation: BAA14180.1.
    AF493899 mRNA. Translation: AAM12613.1.
    CR456495 mRNA. Translation: CAG30381.1.
    AK312519 mRNA. Translation: BAG35418.1.
    CH471095 Genomic DNA. Translation: EAW59559.1.
    BC078163 mRNA. Translation: AAH78163.1.
    BC096828 mRNA. Translation: AAH96828.1.
    CCDSiCCDS13804.1.
    PIRiA36628. RGHUGX.
    RefSeqiNP_002064.1. NM_002073.2.
    UniGeneiHs.584760.

    Genome annotation databases

    EnsembliENST00000248996; ENSP00000248996; ENSG00000128266.
    GeneIDi2781.
    KEGGihsa:2781.
    UCSCiuc002zwu.1. human.

    Polymorphism databases

    DMDMi121005.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03260 mRNA. Translation: AAA52580.1 .
    D90150 Genomic DNA. Translation: BAA14180.1 .
    AF493899 mRNA. Translation: AAM12613.1 .
    CR456495 mRNA. Translation: CAG30381.1 .
    AK312519 mRNA. Translation: BAG35418.1 .
    CH471095 Genomic DNA. Translation: EAW59559.1 .
    BC078163 mRNA. Translation: AAH78163.1 .
    BC096828 mRNA. Translation: AAH96828.1 .
    CCDSi CCDS13804.1.
    PIRi A36628. RGHUGX.
    RefSeqi NP_002064.1. NM_002073.2.
    UniGenei Hs.584760.

    3D structure databases

    ProteinModelPortali P19086.
    SMRi P19086. Positions 6-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109043. 10 interactions.
    IntActi P19086. 11 interactions.
    MINTi MINT-139942.
    STRINGi 9606.ENSP00000248996.

    PTM databases

    PhosphoSitei P19086.

    Polymorphism databases

    DMDMi 121005.

    Proteomic databases

    MaxQBi P19086.
    PaxDbi P19086.
    PRIDEi P19086.

    Protocols and materials databases

    DNASUi 2781.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248996 ; ENSP00000248996 ; ENSG00000128266 .
    GeneIDi 2781.
    KEGGi hsa:2781.
    UCSCi uc002zwu.1. human.

    Organism-specific databases

    CTDi 2781.
    GeneCardsi GC22P023413.
    HGNCi HGNC:4395. GNAZ.
    HPAi HPA003011.
    MIMi 139160. gene.
    neXtProti NX_P19086.
    PharmGKBi PA28775.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282619.
    HOGENOMi HOG000038730.
    HOVERGENi HBG063184.
    InParanoidi P19086.
    KOi K04535.
    OMAi DYKGQNT.
    OrthoDBi EOG72C50B.
    PhylomeDBi P19086.
    TreeFami TF300673.

    Enzyme and pathway databases

    Reactomei REACT_15426. PLC beta mediated events.
    REACT_15457. G-protein activation.
    REACT_19231. G alpha (i) signalling events.
    REACT_19327. G alpha (s) signalling events.
    REACT_19333. G alpha (z) signalling events.
    SignaLinki P19086.

    Miscellaneous databases

    GeneWikii GNAZ.
    GenomeRNAii 2781.
    NextBioi 10955.
    PROi P19086.
    SOURCEi Search...

    Gene expression databases

    Bgeei P19086.
    CleanExi HS_GNAZ.
    Genevestigatori P19086.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR001408. Gprotein_alpha_I.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR00441. GPROTEINAI.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a GTP-binding protein alpha subunit that lacks an apparent ADP-ribosylation site for pertussis toxin."
      Fong H.K.W., Yoshimoto K.K., Eversole-Cire P., Simon M.I.
      Proc. Natl. Acad. Sci. U.S.A. 85:3066-3070(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of the human gene for Gx alpha, a pertussis toxin-insensitive regulatory GTP-binding protein."
      Matsuoka M., Itoh H., Kaziro Y.
      J. Biol. Chem. 265:13215-13220(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Identification of Gz alpha as a pertussis toxin-insensitive G protein in human platelets and megakaryocytes."
      Gagnon A.W., Manning D.R., Catani L., Gewirtz A., Poncz M., Brass L.F.
      Blood 78:1247-1253(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thalamus.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: PNS.

    Entry informationi

    Entry nameiGNAZ_HUMAN
    AccessioniPrimary (citable) accession number: P19086
    Secondary accession number(s): B2R6C1, Q4QRJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3