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P63096

- GNAI1_HUMAN

UniProt

P63096 - GNAI1_HUMAN

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Protein

Guanine nucleotide-binding protein G(i) subunit alpha-1

Gene

GNAI1

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

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi181 – 1811MagnesiumBy similarity
Binding sitei326 – 3261GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478GTP
Nucleotide bindingi175 – 1817GTPBy similarity
Nucleotide bindingi200 – 2045GTP
Nucleotide bindingi269 – 2724GTP

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: BHF-UCL
  5. metal ion binding Source: UniProtKB-KW
  6. signal transducer activity Source: RefGenome

GO - Biological processi

  1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: Reactome
  2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
  3. blood coagulation Source: Reactome
  4. cell cycle Source: UniProtKB-KW
  5. cell division Source: UniProtKB
  6. G-protein coupled receptor signaling pathway Source: BHF-UCL
  7. platelet activation Source: Reactome
  8. response to peptide hormone Source: BHF-UCL
  9. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_15333. Adenylate cyclase inhibitory pathway.
REACT_15426. PLC beta mediated events.
REACT_15457. G-protein activation.
REACT_18325. Regulation of insulin secretion.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_19231. G alpha (i) signalling events.
REACT_19327. G alpha (s) signalling events.
REACT_19333. G alpha (z) signalling events.
REACT_20653. ADP signalling through P2Y purinoceptor 12.
SignaLinkiP63096.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-1
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene namesi
Name:GNAI1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4384. GNAI1.

Subcellular locationi

Nucleus By similarity. Cytoplasm 1 Publication. Cell membrane 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane (By similarity). Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody.By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. heterotrimeric G-protein complex Source: RefGenome
  5. lysosomal membrane Source: UniProtKB
  6. midbody Source: UniProtKB
  7. nucleus Source: UniProtKB-KW
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161E → L: Enhances interaction (inactive GDP-bound) with RGS14. 2 Publications
Mutagenesisi147 – 1471Q → L: Enhances interaction (inactive GDP-bound) with RGS14. 2 Publications
Mutagenesisi245 – 2451E → L: Enhances interaction (inactive GDP-bound) with RGS14. 1 Publication

Organism-specific databases

PharmGKBiPA172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 354353Guanine nucleotide-binding protein G(i) subunit alpha-1PRO_0000203671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Lipidationi3 – 31S-palmitoyl cysteineBy similarity
Modified residuei178 – 1781ADP-ribosylarginine; by cholera toxinBy similarity
Modified residuei351 – 3511ADP-ribosylcysteine; by pertussis toxinBy similarity

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Myristate, Palmitate

Proteomic databases

MaxQBiP63096.
PaxDbiP63096.
PRIDEiP63096.

PTM databases

PhosphoSiteiP63096.

Expressioni

Gene expression databases

BgeeiP63096.
CleanExiHS_GNAI1.
ExpressionAtlasiP63096. baseline and differential.
GenevestigatoriP63096.

Organism-specific databases

HPAiCAB022449.

Interactioni

Subunit structurei

Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains); the interaction occurs in the centrosomes. Interacts (GDP-bound form) with RIC8A (via C-terminus) (By similarity). Interacts with DRD2. G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GPSM2P812743EBI-618639,EBI-618655
NUMA1Q149804EBI-618639,EBI-521611

Protein-protein interaction databases

BioGridi109032. 62 interactions.
IntActiP63096. 19 interactions.
MINTiMINT-2913925.
STRINGi9606.ENSP00000343027.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 168Combined sources
Helixi20 – 234Combined sources
Helixi27 – 293Combined sources
Beta strandi31 – 4111Combined sources
Helixi46 – 5712Combined sources
Helixi63 – 675Combined sources
Helixi70 – 9122Combined sources
Helixi100 – 11314Combined sources
Beta strandi115 – 1173Combined sources
Helixi121 – 13212Combined sources
Helixi134 – 1407Combined sources
Helixi141 – 1455Combined sources
Helixi152 – 1576Combined sources
Helixi159 – 1624Combined sources
Beta strandi164 – 1663Combined sources
Helixi171 – 1755Combined sources
Beta strandi183 – 1919Combined sources
Beta strandi194 – 2018Combined sources
Helixi208 – 2158Combined sources
Beta strandi220 – 2267Combined sources
Helixi227 – 2293Combined sources
Beta strandi238 – 2414Combined sources
Helixi242 – 25413Combined sources
Helixi257 – 2593Combined sources
Beta strandi260 – 26910Combined sources
Helixi271 – 2777Combined sources
Turni278 – 2803Combined sources
Helixi283 – 2853Combined sources
Helixi296 – 30813Combined sources
Turni314 – 3163Combined sources
Beta strandi319 – 3235Combined sources
Helixi329 – 34618Combined sources
Helixi348 – 3503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KJYX-ray2.70A/C30-354[»]
1Y3AX-ray2.50A/B/C/D26-354[»]
2G83X-ray2.80A/B33-345[»]
2GTPX-ray2.55A/B32-354[»]
2IK8X-ray2.71A/C31-354[»]
2OM2X-ray2.20A/C31-354[»]
2PZ3X-ray2.42A1-354[»]
2XNSX-ray3.41A/B30-354[»]
3ONWX-ray2.38A/B31-354[»]
3QE0X-ray3.00A/B/C33-354[»]
3QI2X-ray2.80A/B31-354[»]
3UMRX-ray2.24A1-354[»]
3UMSX-ray2.60A1-354[»]
4G5QX-ray2.90A/B/C/D25-354[»]
ProteinModelPortaliP63096.
SMRiP63096. Positions 5-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63096.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00760000118851.
HOVERGENiHBG063184.
InParanoidiP63096.
KOiK04630.
OMAiECEEYRR.
PhylomeDBiP63096.
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.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P63096-1) [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
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR
110 120 130 140 150
ADDARQLFVL AGAAEEGFMT AELAGVIKRL WKDSGVQACF NRSREYQLND
160 170 180 190 200
SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD

CGLF
Length:354
Mass (Da):40,361
Last modified:January 23, 2007 - v2
Checksum:i9F88311B46E62DE3
GO
Isoform 2 (identifier: P63096-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:302
Mass (Da):34,775
Checksum:iDA5ED62E61B790A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381A → G in CAB43212. (PubMed:11230166)Curated
Sequence conflicti219 – 2191T → A in AAH26326. (PubMed:15489334)Curated
Sequence conflicti244 – 2441H → Y in AAV38580. 1 PublicationCurated
Sequence conflicti249 – 2491L → M in AAV38580. 1 PublicationCurated
Sequence conflicti288 – 2881P → Q in AAH26326. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform 2. 1 PublicationVSP_045215Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF493905 mRNA. Translation: AAM12619.1.
AF055013 mRNA. Translation: AAC09361.1.
AL049933 mRNA. Translation: CAB43212.2.
BT019775 mRNA. Translation: AAV38580.1.
AK292953 mRNA. Translation: BAF85642.1.
AK304442 mRNA. Translation: BAG65263.1.
AC004159 Genomic DNA. No translation available.
AC080066 Genomic DNA. No translation available.
CH471091 Genomic DNA. Translation: EAW77011.1.
BC026326 mRNA. Translation: AAH26326.1.
M20596, M20594, M20595 Genomic DNA. Translation: AAA35893.1.
M17219 mRNA. Translation: AAA52581.1.
CCDSiCCDS5595.1. [P63096-1]
CCDS59061.1. [P63096-2]
PIRiA28318. RGHUI1.
RefSeqiNP_001243343.1. NM_001256414.1. [P63096-2]
NP_002060.4. NM_002069.5. [P63096-1]
UniGeneiHs.134587.

Genome annotation databases

EnsembliENST00000351004; ENSP00000343027; ENSG00000127955. [P63096-1]
ENST00000457358; ENSP00000410572; ENSG00000127955. [P63096-2]
GeneIDi2770.
KEGGihsa:2770.
UCSCiuc003uhb.1. human. [P63096-1]

Polymorphism databases

DMDMi52000964.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF493905 mRNA. Translation: AAM12619.1 .
AF055013 mRNA. Translation: AAC09361.1 .
AL049933 mRNA. Translation: CAB43212.2 .
BT019775 mRNA. Translation: AAV38580.1 .
AK292953 mRNA. Translation: BAF85642.1 .
AK304442 mRNA. Translation: BAG65263.1 .
AC004159 Genomic DNA. No translation available.
AC080066 Genomic DNA. No translation available.
CH471091 Genomic DNA. Translation: EAW77011.1 .
BC026326 mRNA. Translation: AAH26326.1 .
M20596 , M20594 , M20595 Genomic DNA. Translation: AAA35893.1 .
M17219 mRNA. Translation: AAA52581.1 .
CCDSi CCDS5595.1. [P63096-1 ]
CCDS59061.1. [P63096-2 ]
PIRi A28318. RGHUI1.
RefSeqi NP_001243343.1. NM_001256414.1. [P63096-2 ]
NP_002060.4. NM_002069.5. [P63096-1 ]
UniGenei Hs.134587.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KJY X-ray 2.70 A/C 30-354 [» ]
1Y3A X-ray 2.50 A/B/C/D 26-354 [» ]
2G83 X-ray 2.80 A/B 33-345 [» ]
2GTP X-ray 2.55 A/B 32-354 [» ]
2IK8 X-ray 2.71 A/C 31-354 [» ]
2OM2 X-ray 2.20 A/C 31-354 [» ]
2PZ3 X-ray 2.42 A 1-354 [» ]
2XNS X-ray 3.41 A/B 30-354 [» ]
3ONW X-ray 2.38 A/B 31-354 [» ]
3QE0 X-ray 3.00 A/B/C 33-354 [» ]
3QI2 X-ray 2.80 A/B 31-354 [» ]
3UMR X-ray 2.24 A 1-354 [» ]
3UMS X-ray 2.60 A 1-354 [» ]
4G5Q X-ray 2.90 A/B/C/D 25-354 [» ]
ProteinModelPortali P63096.
SMRi P63096. Positions 5-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109032. 62 interactions.
IntActi P63096. 19 interactions.
MINTi MINT-2913925.
STRINGi 9606.ENSP00000343027.

Chemistry

BindingDBi P63096.
ChEMBLi CHEMBL4741.

PTM databases

PhosphoSitei P63096.

Polymorphism databases

DMDMi 52000964.

Proteomic databases

MaxQBi P63096.
PaxDbi P63096.
PRIDEi P63096.

Protocols and materials databases

DNASUi 2770.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351004 ; ENSP00000343027 ; ENSG00000127955 . [P63096-1 ]
ENST00000457358 ; ENSP00000410572 ; ENSG00000127955 . [P63096-2 ]
GeneIDi 2770.
KEGGi hsa:2770.
UCSCi uc003uhb.1. human. [P63096-1 ]

Organism-specific databases

CTDi 2770.
GeneCardsi GC07P079763.
HGNCi HGNC:4384. GNAI1.
HPAi CAB022449.
MIMi 139310. gene.
neXtProti NX_P63096.
PharmGKBi PA172.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322962.
GeneTreei ENSGT00760000118851.
HOVERGENi HBG063184.
InParanoidi P63096.
KOi K04630.
OMAi ECEEYRR.
PhylomeDBi P63096.
TreeFami TF300673.

Enzyme and pathway databases

Reactomei REACT_15333. Adenylate cyclase inhibitory pathway.
REACT_15426. PLC beta mediated events.
REACT_15457. G-protein activation.
REACT_18325. Regulation of insulin secretion.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_19231. G alpha (i) signalling events.
REACT_19327. G alpha (s) signalling events.
REACT_19333. G alpha (z) signalling events.
REACT_20653. ADP signalling through P2Y purinoceptor 12.
SignaLinki P63096.

Miscellaneous databases

ChiTaRSi GNAI1. human.
EvolutionaryTracei P63096.
GeneWikii GNAI1.
GenomeRNAii 2770.
NextBioi 10896.
PROi P63096.
SOURCEi Search...

Gene expression databases

Bgeei P63096.
CleanExi HS_GNAI1.
ExpressionAtlasi P63096. baseline and differential.
Genevestigatori P63096.

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

« Hide 'large scale' publications
  1. "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 1).
  2. Yu W., Gibbs R.A.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Trachea.
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Brain.
  9. "Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs."
    Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.
    J. Biol. Chem. 263:6656-6664(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101.
  10. "Human cDNA clones for an alpha subunit of Gi signal-transduction protein."
    Bray P., Carter A., Guo V., Puckett C., Kamholz J., Spiegel A., Nirenberg M.
    Proc. Natl. Acad. Sci. U.S.A. 84:5115-5119(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-354.
  11. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 91-100 AND 162-176.
    Tissue: Adipocyte.
  12. "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, SUBCELLULAR LOCATION.
  13. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
    Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
    Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits."
    Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P.
    Nature 416:878-881(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-349 IN COMPLEX WITH RGS14 AND GDP.
  16. "Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange."
    Johnston C.A., Willard F.S., Jezyk M.R., Fredericks Z., Bodor E.T., Jones M.B., Blaesius R., Watts V.J., Harden T.K., Sondek J., Ramer J.K., Siderovski D.P.
    Structure 13:1069-1080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-354 IN COMPLEX WITH GDP.
  17. "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 31-354, MUTAGENESIS OF GLU-116 AND GLN-147.
  18. "Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity."
    Johnston C.A., Siderovski D.P.
    Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH DRD2 AND GDP, FUNCTION, INTERACTION WITH DRD2.
  19. Cited for: RETRACTION.
  20. "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 31-354 IN COMPLEX WITH RGS14 AND GDP, MUTAGENESIS OF GLU-116; GLN-147 AND GLU-245.

Entry informationi

Entry nameiGNAI1_HUMAN
AccessioniPrimary (citable) accession number: P63096
Secondary accession number(s): A8KA88
, B4E2V1, C9J3A4, P04898, P11015, P31871, Q5U074, Q8TAN5, Q9UGA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 124 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3