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Protein

Phosphoinositide 3-kinase regulatory subunit 5

Gene

Pik3r5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG (By similarity).By similarity

Enzyme regulationi

Greatly activated by G gamma proteins.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
REACT_291272. G beta:gamma signalling through PI3Kgamma.
REACT_337915. GPVI-mediated activation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoinositide 3-kinase regulatory subunit 5
Short name:
PI3-kinase regulatory subunit 5
Alternative name(s):
PI3-kinase p101 subunit
Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit
Short name:
PtdIns-3-kinase regulatory subunit
PtdIns-3-kinase p101
p101-PI3K
Gene namesi
Name:Pik3r5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2443588. Pik3r5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 871871Phosphoinositide 3-kinase regulatory subunit 5PRO_0000058422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei451 – 4511PhosphoserineBy similarity
Modified residuei500 – 5001PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5SW28.

PTM databases

PhosphoSiteiQ5SW28.

Expressioni

Gene expression databases

BgeeiQ5SW28.
ExpressionAtlasiQ5SW28. baseline and differential.
GenevisibleiQ5SW28. MM.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit (PIK3CG/p120) and a regulatory (PIK3R5a/p101) subunit. Interacts with beta-gamma G protein dimers (By similarity).By similarity

Protein-protein interaction databases

IntActiQ5SW28. 2 interactions.
STRINGi10090.ENSMUSP00000021283.

Structurei

3D structure databases

ProteinModelPortaliQ5SW28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 10177HeterodimerizationBy similarityAdd
BLAST
Regioni646 – 746101Interaction with beta-gamma G protein dimersBy similarityAdd
BLAST

Domaini

The heterodimerization region allows the binding to the catalytic subunit.By similarity

Phylogenomic databases

eggNOGiNOG27692.
GeneTreeiENSGT00530000063753.
HOGENOMiHOG000115865.
HOVERGENiHBG079651.
InParanoidiQ5SW28.
KOiK02649.
OMAiIYSKGAI.
OrthoDBiEOG7RV9FH.
PhylomeDBiQ5SW28.
TreeFamiTF102035.

Family and domain databases

InterProiIPR019522. PIK3R5/6.
[Graphical view]
PfamiPF10486. PI3K_1B_p101. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SW28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPAATTCTE DRIQHALERC LHGLSLGRRS APWSAGLCLN CWSLQELVSR
60 70 80 90 100
DPGHFLILLE QILQKTQEVQ EKGTYDLLAP LALLFYSTVL CTPHFPPDSD
110 120 130 140 150
LLLKAASTYH CFLTWPVPYC SICREMLTFI DAELKAPGIS YQRLVRAEQG
160 170 180 190 200
LPVRSHRSST VTVLLLNPVE VQAEFLAVAD KLSTPGQSPH GTYTTLLLHA
210 220 230 240 250
FQATFGAHCD LPKLHRKLQS KTIEELEDIF TETTEAQELA SGIGDVAEAR
260 270 280 290 300
EWLRTKLQAV GEKAGFPGIL DTASPGKLHT IPIPVARCYT YSWNQDSFDI
310 320 330 340 350
LQEVLLKEQE LLQPGILGDD EEEEEEDLEM DRHCAERDSL LSTSSLVSHD
360 370 380 390 400
STLLLTSSQA SEPVLSRQML TTFVSGLSDG MDSGYVEDSE ENSEWPQKPG
410 420 430 440 450
SQKRQGHRRP GQKFNRFYKL LKSTSQLVLR RDSRSLESSV DPTLPLRRAG
460 470 480 490 500
SLCSPLDCPA QLPSRAQRSR SLPQAKLTTQ LPRWLLAPPS HHQRRRPFLS
510 520 530 540 550
GDEDPKASTL RVVVFGSDRI SGKVARAYSK LRRLETSHPI LTRFFKLQFF
560 570 580 590 600
YVPVKRSHGT SPSACPSSLS QASPLPADSL KYPSPTDLGM APWEDSTNDI
610 620 630 640 650
SHYLGMLDPW YERNVLGLMH LPPEVLCQQS LKADSRPLEG SATQLPILAD
660 670 680 690 700
MLLYYCRFAA RPVLLQVYQT ELTFVTGEKT TEIFIQSLEL GHSATTRAIK
710 720 730 740 750
ASGRGRKRLG IDDDREAVPL TLQIIYSKGA ISGRSRWSNL EKVCTSVNLS
760 770 780 790 800
KACQKPEELD SSMEALTLTL TEVVKRQNPK SKKGFNQIST SYIKVDKVQI
810 820 830 840 850
IGSSSCPFAV CLDQDERKIL QSVVRCEVSP CYKPEKSSLP PERSFSQPAE
860 870
TGSDLCSLLC LPIMTFSGAL P
Length:871
Mass (Da):96,954
Last modified:December 21, 2004 - v1
Checksum:i1D0F36A3D4042D62
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651K → E in BAE29119 (PubMed:16141072).Curated
Sequence conflicti269 – 2691I → T in BAC40901 (PubMed:16141072).Curated
Sequence conflicti369 – 3691M → V in AAN84787 (Ref. 1) Curated
Sequence conflicti642 – 6421A → V in AAN84787 (Ref. 1) Curated
Sequence conflicti647 – 6471I → T in AAN84787 (Ref. 1) Curated
Sequence conflicti651 – 6511M → V in AAN84787 (Ref. 1) Curated
Sequence conflicti796 – 7961D → G in BAE29119 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY156924 mRNA. Translation: AAN84787.1.
AK089483 mRNA. Translation: BAC40901.2.
AK149847 mRNA. Translation: BAE29119.1.
AK161050 mRNA. Translation: BAE36171.1.
AL606831 Genomic DNA. Translation: CAI25692.1.
CCDSiCCDS24865.1.
RefSeqiNP_796294.2. NM_177320.2.
XP_006533611.1. XM_006533548.1.
UniGeneiMm.244960.

Genome annotation databases

EnsembliENSMUST00000021283; ENSMUSP00000021283; ENSMUSG00000020901.
GeneIDi320207.
KEGGimmu:320207.
UCSCiuc007jno.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY156924 mRNA. Translation: AAN84787.1.
AK089483 mRNA. Translation: BAC40901.2.
AK149847 mRNA. Translation: BAE29119.1.
AK161050 mRNA. Translation: BAE36171.1.
AL606831 Genomic DNA. Translation: CAI25692.1.
CCDSiCCDS24865.1.
RefSeqiNP_796294.2. NM_177320.2.
XP_006533611.1. XM_006533548.1.
UniGeneiMm.244960.

3D structure databases

ProteinModelPortaliQ5SW28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5SW28. 2 interactions.
STRINGi10090.ENSMUSP00000021283.

PTM databases

PhosphoSiteiQ5SW28.

Proteomic databases

PRIDEiQ5SW28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021283; ENSMUSP00000021283; ENSMUSG00000020901.
GeneIDi320207.
KEGGimmu:320207.
UCSCiuc007jno.1. mouse.

Organism-specific databases

CTDi23533.
MGIiMGI:2443588. Pik3r5.

Phylogenomic databases

eggNOGiNOG27692.
GeneTreeiENSGT00530000063753.
HOGENOMiHOG000115865.
HOVERGENiHBG079651.
InParanoidiQ5SW28.
KOiK02649.
OMAiIYSKGAI.
OrthoDBiEOG7RV9FH.
PhylomeDBiQ5SW28.
TreeFamiTF102035.

Enzyme and pathway databases

ReactomeiREACT_272541. Synthesis of PIPs at the plasma membrane.
REACT_291272. G beta:gamma signalling through PI3Kgamma.
REACT_337915. GPVI-mediated activation cascade.

Miscellaneous databases

ChiTaRSiPik3r5. mouse.
NextBioi396255.
PROiQ5SW28.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SW28.
ExpressionAtlasiQ5SW28. baseline and differential.
GenevisibleiQ5SW28. MM.

Family and domain databases

InterProiIPR019522. PIK3R5/6.
[Graphical view]
PfamiPF10486. PI3K_1B_p101. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a murine ortholog of a PI3-kinase gamma regulatory protein."
    Procko E., McColl S.R.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "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.
    , 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 and Skin.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiPI3R5_MOUSE
AccessioniPrimary (citable) accession number: Q5SW28
Secondary accession number(s): Q3TU01
, Q3UDZ2, Q8C215, Q8CGQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 21, 2004
Last modified: July 22, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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.