Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Phosphatidylinositol 3-kinase regulatory subunit beta

Gene

Pik3r2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseImported, Transferase

Enzyme and pathway databases

ReactomeiR-RNO-109704. PI3K Cascade.
R-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-1660499. Synthesis of PIPs at the plasma membrane.
R-RNO-186763. Downstream signal transduction.
R-RNO-194840. Rho GTPase cycle.
R-RNO-198203. PI3K/AKT activation.
R-RNO-202424. Downstream TCR signaling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-210993. Tie2 Signaling.
R-RNO-2424491. DAP12 signaling.
R-RNO-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.

Names & Taxonomyi

Protein namesi
Submitted name:
Phosphatidylinositol 3-kinase regulatory subunit betaImported
Submitted name:
Phosphatidylinositol 3-kinase, regulatory subunit, polypeptide 2, isoform CRA_aImported
Submitted name:
Phosphoinositide-3-kinase, regulatory subunit 2 (Beta)Imported
Gene namesi
Name:Pik3r2Imported
ORF Names:rCG_38682Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi68341. Pik3r2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026210.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8077SH3InterPro annotationAdd
BLAST
Domaini112 – 289178Rho-GAPInterPro annotationAdd
BLAST
Domaini324 – 41996SH2InterPro annotationAdd
BLAST
Domaini616 – 71095SH2InterPro annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili440 – 46728Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coilSequence analysis, SH3 domainSAAS annotation

Phylogenomic databases

eggNOGiKOG4637. Eukaryota.
ENOG410XP6R. LUCA.
GeneTreeiENSGT00390000010431.
HOVERGENiHBG082100.
KOiK02649.
OMAiHYKHTSL.
OrthoDBiEOG7BP831.
TreeFamiTF102033.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR032498. PI3K_P85_iSH2.
IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF16454. PI3K_P85_iSH2. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5FVS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAEGFQYR AVYPFRRERP EDLELLPGDL LVVSRVALQA LGVADGGERC
60 70 80 90 100
PHNVGWMPGF NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP
110 120 130 140 150
LDGPSESGHT LASLAEQFSP PEPAPPILVK LIEAIEQAEL DSECYSRPEL
160 170 180 190 200
PAPRTDWSLS DLEQWDRTTL YDAVKGFLLA LPAAVVTPEA ASEAYRAMRE
210 220 230 240 250
VTGPVGLVLE PPTLPLHQAL TLQFLLQHLG RVARRAPSPA TAVHALASAF
260 270 280 290 300
GPLLLRAPPP GGEGDGSEPA PDFPVLLLER LVQEHVDEQD TAPPALPPKP
310 320 330 340 350
SKVKPAPTAL ANGGSTPSLQ DAEWYWGDIS REEVNERLRD TPDGTFLVRD
360 370 380 390 400
ASSKIQGEYT LTLRKGGNNK LIKVFHRDGH YGFSEPLTFC SVVELISHYR
410 420 430 440 450
HESLAQYNAK LDTRLLYPVS KYQQDQVVKE DSVEAVGAQL KVYHQQYQDK
460 470 480 490 500
SREYDQLYEE YTRTSQELQM KRTAIEAFNE TIKIFEEQGQ TQEKCSKEYL
510 520 530 540 550
ERFRREGNEK EMQRILLNSE RLKSRIAEIH ESRTKLEQDL RAQASDNREI
560 570 580 590 600
DKRMNSLKPD LMQLRKIRDQ YLVWLTQKGA RQRKINEWLG IKNETEDQYS
610 620 630 640 650
LMEDEDALPH HEERTWYVGK INRTQAEEML SGKRDGTFLI RESSQRGCYA
660 670 680 690 700
CSVVVDGDTK HCVIYRTATG FGFAEPYNLY GSLKELVLHY QHASLVQHND
710 720
ALTVTLAHPV RAPGPGPPPA AR
Length:722
Mass (Da):81,268
Last modified:March 1, 2005 - v1
Checksum:i7D3872BC46F90B1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07024876 Genomic DNA. No translation available.
BC089805 mRNA. Translation: AAH89805.1.
CH474031 Genomic DNA. Translation: EDL90737.1.
RefSeqiNP_071521.2. NM_022185.2.
XP_008769318.1. XM_008771096.1.
UniGeneiRn.22497.

Genome annotation databases

EnsembliENSRNOT00000026210; ENSRNOP00000026210; ENSRNOG00000019228.
GeneIDi29741.
KEGGirno:29741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07024876 Genomic DNA. No translation available.
BC089805 mRNA. Translation: AAH89805.1.
CH474031 Genomic DNA. Translation: EDL90737.1.
RefSeqiNP_071521.2. NM_022185.2.
XP_008769318.1. XM_008771096.1.
UniGeneiRn.22497.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026210; ENSRNOP00000026210; ENSRNOG00000019228.
GeneIDi29741.
KEGGirno:29741.

Organism-specific databases

CTDi5296.
RGDi68341. Pik3r2.

Phylogenomic databases

eggNOGiKOG4637. Eukaryota.
ENOG410XP6R. LUCA.
GeneTreeiENSGT00390000010431.
HOVERGENiHBG082100.
KOiK02649.
OMAiHYKHTSL.
OrthoDBiEOG7BP831.
TreeFamiTF102033.

Enzyme and pathway databases

ReactomeiR-RNO-109704. PI3K Cascade.
R-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-1660499. Synthesis of PIPs at the plasma membrane.
R-RNO-186763. Downstream signal transduction.
R-RNO-194840. Rho GTPase cycle.
R-RNO-198203. PI3K/AKT activation.
R-RNO-202424. Downstream TCR signaling.
R-RNO-2029485. Role of phospholipids in phagocytosis.
R-RNO-210993. Tie2 Signaling.
R-RNO-2424491. DAP12 signaling.
R-RNO-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-RNO-4420097. VEGFA-VEGFR2 Pathway.

Miscellaneous databases

NextBioi610248.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR032498. PI3K_P85_iSH2.
IPR001720. PI3kinase_P85.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10155. PTHR10155. 1 hit.
PfamiPF16454. PI3K_P85_iSH2. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00324. RhoGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: ThymusImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ5FVS6_RAT
AccessioniPrimary (citable) accession number: Q5FVS6
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: May 11, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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 one 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.