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Protein

Guanine nucleotide-binding protein G(z) subunit alpha

Gene

GNAZ

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

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:4395. GNAZ.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • heterotrimeric G-protein complex Source: GO_Central
  • nuclear envelope Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28775.

Polymorphism and mutation databases

BioMutaiGNAZ.
DMDMi121005.

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. 24 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.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP19086.
KOiK04535.
OMAiYDLRLYE.
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

« Hide

        10         20         30         40         50
MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV
60 70 80 90 100
KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR
110 120 130 140 150
AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE
160 170 180 190 200
DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV
210 220 230 240 250
DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL
260 270 280 290 300
FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA
310 320 330 340 350
AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK

YIGLC
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000615612; ENSP00000478892; ENSG00000128266.
GeneIDi2781.
KEGGihsa:2781.
UCSCiuc002zwu.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi109043. 24 interactions.
IntActiP19086. 11 interactions.
MINTiMINT-139942.
STRINGi9606.ENSP00000248996.

PTM databases

PhosphoSiteiP19086.

Polymorphism and mutation databases

BioMutaiGNAZ.
DMDMi121005.

Proteomic databases

MaxQBiP19086.
PaxDbiP19086.
PRIDEiP19086.

Protocols and materials databases

DNASUi2781.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000615612; ENSP00000478892; ENSG00000128266.
GeneIDi2781.
KEGGihsa:2781.
UCSCiuc002zwu.1. human.

Organism-specific databases

CTDi2781.
GeneCardsiGC22P023413.
HGNCiHGNC:4395. GNAZ.
HPAiHPA003011.
MIMi139160. gene.
neXtProtiNX_P19086.
PharmGKBiPA28775.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282619.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP19086.
KOiK04535.
OMAiYDLRLYE.
OrthoDBiEOG72C50B.
PhylomeDBiP19086.
TreeFamiTF300673.

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.

Miscellaneous databases

GeneWikiiGNAZ.
GenomeRNAii2781.
NextBioi10955.
PROiP19086.
SOURCEiSearch...

Gene expression databases

BgeeiP19086.
CleanExiHS_GNAZ.
GenevestigatoriP19086.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 158 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

Similar proteinsi

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