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O00750

- P3C2B_HUMAN

UniProt

O00750 - P3C2B_HUMAN

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Protein

Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta

Gene

PIK3C2B

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

Functioni

Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades.1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.

Cofactori

Calcium, magnesium, or manganese.1 Publication

Enzyme regulationi

Activated by GRB2.1 Publication

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-kinase activity Source: RefGenome
  2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. lipid kinase activity Source: Ensembl
  5. phosphatidylinositol binding Source: InterPro

GO - Biological processi

  1. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  2. phosphatidylinositol biosynthetic process Source: Reactome
  3. phosphatidylinositol-mediated signaling Source: InterPro
  4. phospholipid metabolic process Source: Reactome
  5. protein kinase B signaling Source: Ensembl
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.137. 2681.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
SignaLinkiO00750.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta (EC:2.7.1.154)
Short name:
PI3K-C2-beta
Short name:
PtdIns-3-kinase C2 subunit beta
Alternative name(s):
C2-PI3K
Phosphoinositide 3-kinase-C2-beta
Gene namesi
Name:PIK3C2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8972. PIK3C2B.

Subcellular locationi

Microsome 1 Publication. Cell membrane 1 Publication. Cytoplasmcytosol 1 Publication. Nucleus 1 Publication. Endoplasmic reticulum 1 Publication
Note: Found mostly in the microsome, but also in the plasma membrane and cytosol. Nuclear in testis.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endocytic vesicle Source: Ensembl
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. nucleus Source: UniProtKB-KW
  5. phosphatidylinositol 3-kinase complex Source: RefGenome
  6. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33305.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16341634Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit betaPRO_0000088798Add
BLAST

Proteomic databases

MaxQBiO00750.
PaxDbiO00750.
PeptideAtlasiO00750.
PRIDEiO00750.

PTM databases

PhosphoSiteiO00750.

Expressioni

Tissue specificityi

Expressed in columnar and transitional epithelia, mononuclear cells, and ganglion cells (at protein level). Widely expressed, with highest levels in thymus and placenta and lowest in peripheral blood, skeletal muscle and kidney.2 Publications

Gene expression databases

BgeeiO00750.
CleanExiHS_PIK3C2B.
ExpressionAtlasiO00750. baseline and differential.
GenevestigatoriO00750.

Organism-specific databases

HPAiHPA030515.

Interactioni

Subunit structurei

Part of a complex with ERBB2 and EGFR. Part of a complex with phosphorylated EGFR and GRB2. Interacts with phosphorylated EGFR and PDGFR, maybe indirectly. Interacts with GRB2 and SHC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005339EBI-641107,EBI-297353
ERBB2P046262EBI-641107,EBI-641062
GRB2P629932EBI-641107,EBI-401755
NCK1P163333EBI-641107,EBI-389883
TRIM27P143735EBI-641107,EBI-719493

Protein-protein interaction databases

BioGridi111305. 11 interactions.
IntActiO00750. 9 interactions.
MINTiMINT-2794980.
STRINGi9606.ENSP00000356155.

Structurei

3D structure databases

ProteinModelPortaliO00750.
SMRiO00750. Positions 653-1336, 1365-1475, 1506-1626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini375 – 46389PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini635 – 786152C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini805 – 981177PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini1079 – 1343265PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini1365 – 1481117PXPROSITE-ProRule annotationAdd
BLAST
Domaini1517 – 160892C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 298297Interaction with GRB2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi156 – 1627Pro-rich
Compositional biasi169 – 1746Pro-rich

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00760000119110.
HOVERGENiHBG082099.
InParanoidiO00750.
KOiK00923.
OMAiIHLQERP.
OrthoDBiEOG71CFK4.
PhylomeDBiO00750.
TreeFamiTF102031.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiPF00168. C2. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00750-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSTQGNGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHDKEENRAK
60 70 80 90 100
QNADPSLISW DEPGVDFYSK PAGRRTDLKL LRGLSGSDPT LNYNSLSPQE
110 120 130 140 150
GPPNHSTSQG PQPGSDPWPK GSLSGDYLYI FDGSDGGVSS SPGPGDIEGS
160 170 180 190 200
CKKLSPPPLP PRASIWDTPP LPPRKGSPSS SKISQPSDIN TFSLVEQLPG
210 220 230 240 250
KLLEHRILEE EEVLGGGGQG RLLGSVDYDG INDAITRLNL KSTYDAEMLR
260 270 280 290 300
DATRGWKEGR GPLDFSKDTS GKPVARSKTM PPQVPPRTYA SRYGNRKNAT
310 320 330 340 350
PGKNRRISAA PVGSRPHTVA NGHELFEVSE ERDEEVAAFC HMLDILRSGS
360 370 380 390 400
DIQDYFLTGY VWSAVTPSPE HLGDEVNLKV TVLCDRLQEA LTFTCNCSST
410 420 430 440 450
VDLLIYQTLC YTHDDLRNVD VGDFVLKPCG LEEFLQNKHA LGSHEYIQYC
460 470 480 490 500
RKFDIDIRLQ LMEQKVVRSD LARTVNDDQS PSTLNYLVHL QERPVKQTIS
510 520 530 540 550
RQALSLLFDT YHNEVDAFLL ADGDFPLKAD RVVQSVKAIC NALAAVETPE
560 570 580 590 600
ITSALNQLPP CPSRMQPKIQ KDPSVLAVRE NREKVVEALT AAILDLVELY
610 620 630 640 650
CNTFNADFQT AVPGSRKHDL VQEACHFARS LAFTVYATHR IPIIWATSYE
660 670 680 690 700
DFYLSCSLSH GGKELCSPLQ TRRAHFSKYL FHLIVWDQQI CFPVQVNRLP
710 720 730 740 750
RETLLCATLY ALPIPPPGSS SEANKQRRVP EALGWVTTPL FNFRQVLTCG
760 770 780 790 800
RKLLGLWPAT QENPSARWSA PNFHQPDSVI LQIDFPTSAF DIKFTSPPGD
810 820 830 840 850
KFSPRYEFGS LREEDQRKLK DIMQKESLYW LTDADKKRLW EKRYYCHSEV
860 870 880 890 900
SSLPLVLASA PSWEWACLPD IYVLLKQWTH MNHQDALGLL HATFPDQEVR
910 920 930 940 950
RMAVQWIGSL SDAELLDYLP QLVQALKYEC YLDSPLVRFL LKRAVSDLRV
960 970 980 990 1000
THYFFWLLKD GLKDSQFSIR YQYLLAALLC CCGKGLREEF NRQCWLVNAL
1010 1020 1030 1040 1050
AKLAQQVREA APSARQGILR TGLEEVKQFF ALNGSCRLPL SPSLLVKGIV
1060 1070 1080 1090 1100
PRDCSYFNSN AVPLKLSFQN VDPLGENIRV IFKCGDDLRQ DMLTLQMIRI
1110 1120 1130 1140 1150
MSKIWVQEGL DMRMVIFRCF STGRGRGMVE MIPNAETLRK IQVEHGVTGS
1160 1170 1180 1190 1200
FKDRPLADWL QKHNPGEDEY EKAVENFIYS CAGCCVATYV LGICDRHNDN
1210 1220 1230 1240 1250
IMLKTTGHMF HIDFGRFLGH AQMFGNIKRD RAPFVFTSDM AYVINGGDKP
1260 1270 1280 1290 1300
SSRFHDFVDL CCQAYNLIRK HTHLFLNLLG LMLSCGIPEL SDLEDLKYVY
1310 1320 1330 1340 1350
DALRPQDTEA NATTYFTRLI ESSLGSVATK LNFFIHNLAQ MKFTGSDDRL
1360 1370 1380 1390 1400
TLSFASRTHT LKSSGRISDV FLCRHEKIFH PNKGYIYVVK VMRENTHEAT
1410 1420 1430 1440 1450
YIQRTFEEFQ ELHNKLRLLF PSSHLPSFPS RFVIGRSRGE AVAERRREEL
1460 1470 1480 1490 1500
NGYIWHLIHA PPEVAECDLV YTFFHPLPRD EKAMGTSPAP KSSDGTWARP
1510 1520 1530 1540 1550
VGKVGGEVKL SISYKNNKLF IMVMHIRGLQ LLQDGNDPDP YVKIYLLPDP
1560 1570 1580 1590 1600
QKTTKRKTKV ARKTCNPTYN EMLVYDGIPK GDLQQRELQL SVLSEQGFWE
1610 1620 1630
NVLLGEVNIR LRELDLAQEK TGWFALGSRS HGTL
Length:1,634
Mass (Da):184,768
Last modified:August 30, 2005 - v2
Checksum:iCA817BA77C12E833
GO

Sequence cautioni

The sequence CAA74194.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61G → D in CAA72168. (PubMed:9144573)Curated
Sequence conflicti63 – 631P → S in CAA74194. (PubMed:9830063)Curated
Sequence conflicti75 – 751R → W in CAA74194. (PubMed:9830063)Curated
Sequence conflicti99 – 991Q → L in CAA74194. (PubMed:9830063)Curated
Sequence conflicti246 – 2461A → V in CAA72168. (PubMed:9144573)Curated
Sequence conflicti278 – 2781K → E in CAA74194. (PubMed:9830063)Curated
Sequence conflicti567 – 5671P → S in CAA74194. (PubMed:9830063)Curated
Sequence conflicti664 – 6652EL → DM in CAA72168. (PubMed:9144573)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11312 mRNA. Translation: CAA72168.1.
Y13892 mRNA. Translation: CAA74194.1. Different initiation.
AL606489 Genomic DNA. Translation: CAI16572.1.
CCDSiCCDS1446.1.
PIRiJC5500.
PC4346.
RefSeqiNP_002637.3. NM_002646.3.
XP_005245314.1. XM_005245257.1.
XP_006711447.1. XM_006711384.1.
UniGeneiHs.497487.

Genome annotation databases

EnsembliENST00000367187; ENSP00000356155; ENSG00000133056.
GeneIDi5287.
KEGGihsa:5287.
UCSCiuc001haw.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11312 mRNA. Translation: CAA72168.1 .
Y13892 mRNA. Translation: CAA74194.1 . Different initiation.
AL606489 Genomic DNA. Translation: CAI16572.1 .
CCDSi CCDS1446.1.
PIRi JC5500.
PC4346.
RefSeqi NP_002637.3. NM_002646.3.
XP_005245314.1. XM_005245257.1.
XP_006711447.1. XM_006711384.1.
UniGenei Hs.497487.

3D structure databases

ProteinModelPortali O00750.
SMRi O00750. Positions 653-1336, 1365-1475, 1506-1626.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111305. 11 interactions.
IntActi O00750. 9 interactions.
MINTi MINT-2794980.
STRINGi 9606.ENSP00000356155.

Chemistry

BindingDBi O00750.
ChEMBLi CHEMBL5554.
GuidetoPHARMACOLOGYi 2151.

PTM databases

PhosphoSitei O00750.

Proteomic databases

MaxQBi O00750.
PaxDbi O00750.
PeptideAtlasi O00750.
PRIDEi O00750.

Protocols and materials databases

DNASUi 5287.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367187 ; ENSP00000356155 ; ENSG00000133056 .
GeneIDi 5287.
KEGGi hsa:5287.
UCSCi uc001haw.3. human.

Organism-specific databases

CTDi 5287.
GeneCardsi GC01M204391.
HGNCi HGNC:8972. PIK3C2B.
HPAi HPA030515.
MIMi 602838. gene.
neXtProti NX_O00750.
PharmGKBi PA33305.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00760000119110.
HOVERGENi HBG082099.
InParanoidi O00750.
KOi K00923.
OMAi IHLQERP.
OrthoDBi EOG71CFK4.
PhylomeDBi O00750.
TreeFami TF102031.

Enzyme and pathway databases

BRENDAi 2.7.1.137. 2681.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
SignaLinki O00750.

Miscellaneous databases

ChiTaRSi PIK3C2B. human.
GeneWikii PIK3C2B.
GenomeRNAii 5287.
NextBioi 20430.
PROi O00750.
SOURCEi Search...

Gene expression databases

Bgeei O00750.
CleanExi HS_PIK3C2B.
ExpressionAtlasi O00750. baseline and differential.
Genevestigatori O00750.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 2 hits.
3.30.1520.10. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR001683. Phox.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
Pfami PF00168. C2. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
PF00787. PX. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K."
    Brown R.A., Ho L.K.F., Weber-Hall S.J., Shipley J.M., Fry M.J.
    Biochem. Biophys. Res. Commun. 233:537-544(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Mammary gland.
  2. "Human phosphoinositide 3-kinase C2beta, the role of calcium and the C2 domain in enzyme activity."
    Arcaro A., Volinia S., Zvelebil M.J., Stein R.C., Watton S.J., Layton M.J., Gout I., Ahmadi K., Downward J., Waterfield M.D.
    J. Biol. Chem. 273:33082-33090(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Monocyte.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."
    Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.
    Mol. Cell. Biol. 20:3817-3830(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ERBB2 AND EGFR, INTERACTION WITH EGFR AND PDGFR, COFACTOR, FUNCTION.
  5. "Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: role of Grb2."
    Wheeler M., Domin J.
    Mol. Cell. Biol. 21:6660-6667(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH GRB2 AND EGFR, INTERACTION WITH SHC1 AND GRB2, ENZYME REGULATION.
  6. "Topographical expression of class IA and class II phosphoinositide 3-kinase enzymes in normal human tissues is consistent with a role in differentiation."
    El Sheikh S.S., Domin J., Tomtitchong P., Abel P., Stamp G., Lalani E.-N.
    BMC Clin. Pathol. 3:4-4(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiP3C2B_HUMAN
AccessioniPrimary (citable) accession number: O00750
Secondary accession number(s): O95666, Q5SW99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 30, 2005
Last modified: October 29, 2014
This is version 152 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

Caution

It is uncertain whether Met-1 or Met-26 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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