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P29387 (GBB4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein subunit beta-4
Alternative name(s):
Transducin beta chain 4
Gene names
Name:Gnb4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

Subunit structure

G proteins are composed of 3 units, alpha, beta and gamma.

Sequence similarities

Belongs to the WD repeat G protein beta family.

Contains 7 WD repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 340339Guanine nucleotide-binding protein subunit beta-4
PRO_0000127703

Regions

Repeat53 – 9240WD 1
Repeat95 – 13440WD 2
Repeat141 – 17939WD 3
Repeat182 – 22140WD 4
Repeat224 – 26340WD 5
Repeat268 – 30740WD 6
Repeat310 – 33930WD 7

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

Sequence conflict1321N → D in AAB21609. Ref.1
Sequence conflict1321N → D in AAA37756. Ref.1
Sequence conflict1321N → D in AAA37664. Ref.1
Sequence conflict1401P → A in AAB21609. Ref.1
Sequence conflict1401P → A in AAA37756. Ref.1
Sequence conflict1401P → A in AAA37664. Ref.1
Sequence conflict2381G → V in AAM15922. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P29387 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F06827EBC2F0E966

FASTA34037,379
        10         20         30         40         50         60 
MSELEQLRQE AEQLRNQIQD ARKACNDATL VQITSNMDSV GRIQMRTRRT LRGHLAKIYA 

        70         80         90        100        110        120 
MHWGYDSRLL VSASQDGKLI IWDSYTTNKM HAIPLRSSWV MTCAYAPSGN YVACGGLDNI 

       130        140        150        160        170        180 
CSIYNLKTRE GNVRVSRELP GHTGYLSCCR FLDDGQIITS SGDTTCALWD IETGQQTTTF 

       190        200        210        220        230        240 
TGHSGDVMSL SLSPDLKTFV SGACDASSKL WDIRDGMCRQ SFTGHISDIN AVSFFPSGYA 

       250        260        270        280        290        300 
FATGSDDATC RLFDLRADQE LLLYSHDNII CGITSVAFSK SGRLLLAGYD DFNCSVWDAL 

       310        320        330        340 
KGGRSGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLRIWN 

« Hide

References

« Hide 'large scale' references
[1]"Diversity among the beta subunits of heterotrimeric GTP-binding proteins: characterization of a novel beta-subunit cDNA."
von Weizsaecker E., Strathmann M.P., Simon M.I.
Biochem. Biophys. Res. Commun. 183:350-356(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Differential modulation of N-type 1B and P/Q-type 1A calcium channels by different G protein subunit isoforms."
Arnot M.I., Stotz S.C., Jarvis S.E., Zamponi G.W.
J. Physiol. (Lond.) 527:203-212(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Cloning, tissue distribution, and functional expression of the human G protein beta 4-subunit."
Ruiz-Velasco V., Ikeda S.R., Puhl H.L. III
Physiol. Genomics 8:41-50(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Placenta and Vagina.
[5]"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: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S86124 mRNA. Translation: AAB21609.1.
M87286 mRNA. Translation: AAA37756.1.
M63658 mRNA. Translation: AAA37664.1.
AF277893 mRNA. Translation: AAF82124.1.
AF501886 mRNA. Translation: AAM15922.1.
AK036816 mRNA. Translation: BAC29589.1.
AK152227 mRNA. Translation: BAE31054.1.
AK167416 mRNA. Translation: BAE39504.1.
BC028753 mRNA. Translation: AAH28753.1.
PIRRGMSB4. JS0669.
RefSeqNP_038559.2. NM_013531.4.
XP_006535466.1. XM_006535403.1.
UniGeneMm.139192.
Mm.393826.

3D structure databases

ProteinModelPortalP29387.
SMRP29387. Positions 1-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-604N.
IntActP29387. 3 interactions.
MINTMINT-4095682.

PTM databases

PhosphoSiteP29387.

2D gel databases

REPRODUCTION-2DPAGEP29387.

Proteomic databases

PaxDbP29387.
PRIDEP29387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000108234; ENSMUSP00000103869; ENSMUSG00000027669.
ENSMUST00000155737; ENSMUSP00000121127; ENSMUSG00000027669.
GeneID14696.
KEGGmmu:14696.
UCSCuc008owl.1. mouse.

Organism-specific databases

CTD59345.
MGIMGI:104581. Gnb4.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00740000115196.
HOGENOMHOG000176356.
HOVERGENHBG000188.
InParanoidP29387.
KOK04538.
OMAATSFTGH.
OrthoDBEOG7GN2N5.
PhylomeDBP29387.
TreeFamTF106149.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

BgeeP29387.
GenevestigatorP29387.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 7 hits.
[Graphical view]
PIRSFPIRSF002394. GN-bd_beta. 1 hit.
PRINTSPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286647.
PROP29387.
SOURCESearch...

Entry information

Entry nameGBB4_MOUSE
AccessionPrimary (citable) accession number: P29387
Secondary accession number(s): Q3TJJ1, Q8R475, Q9JHX8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot