Skip Header

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

Q00722

- PLCB2_HUMAN

UniProt

Q00722 - PLCB2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2

Gene

PLCB2

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

Functioni

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Ca2+Note: Binds 1 Ca(2+) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei327 – 3271PROSITE-ProRule annotation
Metal bindingi328 – 3281Calcium
Metal bindingi357 – 3571Calcium
Metal bindingi359 – 3591Calcium
Active sitei374 – 3741PROSITE-ProRule annotation
Metal bindingi408 – 4081Calcium

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: ProtInc
  3. phospholipase C activity Source: ProtInc
  4. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of phospholipase C activity Source: ProtInc
  2. inositol phosphate metabolic process Source: Reactome
  3. intracellular signal transduction Source: InterPro
  4. lipid catabolic process Source: UniProtKB-KW
  5. phospholipid metabolic process Source: ProtInc
  6. sensory perception of bitter taste Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06408-MONOMER.
BRENDAi3.1.4.11. 2681.
ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_15426. PLC beta mediated events.
REACT_172761. Ca2+ pathway.
REACT_18283. G alpha (q) signalling events.
REACT_18405. Acetylcholine regulates insulin secretion.
REACT_19145. G beta:gamma signalling through PLC beta.
REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_21254. Presynaptic function of Kainate receptors.
SignaLinkiQ00722.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-beta-2
Phospholipase C-beta-2
Short name:
PLC-beta-2
Gene namesi
Name:PLCB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:9055. PLCB2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521Q → A: Strongly reduces interaction with RAC1. 1 Publication

Organism-specific databases

PharmGKBiPA33385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 118511851-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2PRO_0000088489Add
BLAST

Proteomic databases

MaxQBiQ00722.
PaxDbiQ00722.
PRIDEiQ00722.

PTM databases

PhosphoSiteiQ00722.

Expressioni

Gene expression databases

BgeeiQ00722.
CleanExiHS_PLCB2.
ExpressionAtlasiQ00722. baseline and differential.
GenevestigatoriQ00722.

Organism-specific databases

HPAiCAB009443.

Interactioni

Subunit structurei

Interacts with RAC1.

Protein-protein interaction databases

BioGridi111346. 14 interactions.
DIPiDIP-29259N.
MINTiMINT-1726830.
STRINGi9606.ENSP00000260402.

Structurei

Secondary structure

1
1185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 195Combined sources
Beta strandi21 – 3111Combined sources
Beta strandi33 – 408Combined sources
Beta strandi46 – 516Combined sources
Beta strandi56 – 605Combined sources
Helixi61 – 633Combined sources
Beta strandi64 – 696Combined sources
Helixi70 – 723Combined sources
Helixi79 – 846Combined sources
Turni85 – 884Combined sources
Helixi94 – 963Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi111 – 12111Combined sources
Helixi122 – 13413Combined sources
Helixi137 – 1404Combined sources
Helixi144 – 15714Combined sources
Helixi167 – 1737Combined sources
Helixi178 – 18710Combined sources
Beta strandi193 – 1953Combined sources
Helixi200 – 2023Combined sources
Helixi207 – 2159Combined sources
Helixi219 – 2268Combined sources
Helixi238 – 24710Combined sources
Helixi269 – 2746Combined sources
Helixi288 – 2969Combined sources
Helixi305 – 3084Combined sources
Helixi318 – 3203Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi325 – 3284Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi335 – 3384Combined sources
Helixi343 – 3508Combined sources
Beta strandi355 – 3617Combined sources
Turni365 – 3684Combined sources
Helixi384 – 39411Combined sources
Turni395 – 3973Combined sources
Beta strandi403 – 4097Combined sources
Helixi414 – 42815Combined sources
Helixi429 – 4313Combined sources
Turni451 – 4566Combined sources
Beta strandi458 – 4614Combined sources
Turni523 – 53311Combined sources
Helixi534 – 5374Combined sources
Helixi544 – 5474Combined sources
Helixi561 – 5677Combined sources
Beta strandi572 – 5776Combined sources
Helixi578 – 59821Combined sources
Beta strandi599 – 6046Combined sources
Helixi618 – 6225Combined sources
Helixi637 – 6459Combined sources
Turni646 – 6483Combined sources
Helixi649 – 6513Combined sources
Beta strandi653 – 6564Combined sources
Helixi659 – 6613Combined sources
Beta strandi683 – 69311Combined sources
Beta strandi701 – 7088Combined sources
Beta strandi724 – 7263Combined sources
Beta strandi738 – 7403Combined sources
Helixi746 – 7483Combined sources
Beta strandi750 – 7578Combined sources
Turni758 – 7603Combined sources
Beta strandi761 – 7699Combined sources
Helixi770 – 7723Combined sources
Beta strandi776 – 7838Combined sources
Beta strandi789 – 80214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FJUX-ray2.20B1-803[»]
2ZKMX-ray1.62X1-799[»]
ProteinModelPortaliQ00722.
SMRiQ00722. Positions 11-803, 883-1151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00722.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini312 – 463152PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini546 – 662117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini669 – 76799C2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili988 – 1147160Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi500 – 54546Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000232046.
HOVERGENiHBG053609.
InParanoidiQ00722.
KOiK05858.
OMAiFIKWDDE.
OrthoDBiEOG7WDN1N.
PhylomeDBiQ00722.
TreeFamiTF313216.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR016280. PLC-beta.
IPR028403. PLC-beta2.
IPR014815. PLC-beta_C.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF10. PTHR10336:SF10. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF08703. PLC-beta_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000956. PLC-beta. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q00722-1) [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
MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT
60 70 80 90 100
YQSKEMEFLD ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT
110 120 130 140 150
VVSGPDMVDL TFHNFVSYKE NVGKAWAEDV LALVKHPLTA NASRSTFLDK
160 170 180 190 200
ILVKLKMQLN SEGKIPVKNF FQMFPADRKR VEAALSACHL PKGKNDAINP
210 220 230 240 250
EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH LTKFINQKQR
260 270 280 290 300
DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN
310 320 330 340 350
SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL
360 370 380 390 400
SGCRCVELDC WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP
410 420 430 440 450
YPIILSFENH VDSPRQQAKM AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS
460 470 480 490 500
PEDLRGKILI KNKKNQFSGP TSSSKDTGGE AEGSSPPSAP AGEGTVWAGE
510 520 530 540 550
EGTELEEEEV EEEEEEESGN LDEEEIKKMQ SDEGTAGLEV TAYEEMSSLV
560 570 580 590 600
NYIQPTKFVS FEFSAQKNRS YVISSFTELK AYDLLSKASV QFVDYNKRQM
610 620 630 640 650
SRIYPKGTRM DSSNYMPQMF WNAGCQMVAL NFQTMDLPMQ QNMAVFEFNG
660 670 680 690 700
QSGYLLKHEF MRRPDKQFNP FSVDRIDVVV ATTLSITVIS GQFLSERSVR
710 720 730 740 750
TYVEVELFGL PGDPKRRYRT KLSPSTNSIN PVWKEEPFVF EKILMPELAS
760 770 780 790 800
LRVAVMEEGN KFLGHRIIPI NALNSGYHHL CLHSESNMPL TMPALFIFLE
810 820 830 840 850
MKDYIPGAWA DLTVALANPI KFFSAHDTKS VKLKEAMGGL PEKPFPLASP
860 870 880 890 900
VASQVNGALA PTSNGSPAAR AGAREEAMKE AAEPRTASLE ELRELKGVVK
910 920 930 940 950
LQRRHEKELR ELERRGARRW EELLQRGAAQ LAELGPPGVG GVGACKLGPG
960 970 980 990 1000
KGSRKKRSLP REESAGAAPG EGPEGVDGRV RELKDRLELE LLRQGEEQYE
1010 1020 1030 1040 1050
CVLKRKEQHV AEQISKMMEL AREKQAAELK ALKETSENDT KEMKKKLETK
1060 1070 1080 1090 1100
RLERIQGMTK VTTDKMAQER LKREINNSHI QEVVQVIKQM TENLERHQEK
1110 1120 1130 1140 1150
LEEKQAACLE QIREMEKQFQ KEALAEYEAR MKGLEAEVKE SVRACLRTCF
1160 1170 1180
PSEAKDKPER ACECPPELCE QDPLIAKADA QESRL
Length:1,185
Mass (Da):134,024
Last modified:November 25, 2008 - v2
Checksum:iA0397309D943672A
GO
Isoform 2 (identifier: Q00722-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     492-495: Missing.

Show »
Length:1,181
Mass (Da):133,680
Checksum:i7A6889F204D17FA4
GO
Isoform 3 (identifier: Q00722-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     868-882: Missing.

Note: No experimental confirmation available.

Show »
Length:1,170
Mass (Da):132,511
Checksum:iBC9DC96247E5762D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191K → R in BAF84346. (PubMed:14702039)Curated
Sequence conflicti1060 – 10601K → R in BAF84346. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241N → I.
Corresponds to variant rs45628633 [ dbSNP | Ensembl ].
VAR_047509
Natural varianti598 – 5981R → H.
Corresponds to variant rs8025153 [ dbSNP | Ensembl ].
VAR_047510
Natural varianti664 – 6641P → L.
Corresponds to variant rs9972332 [ dbSNP | Ensembl ].
VAR_047511
Natural varianti712 – 7121G → R.
Corresponds to variant rs28395835 [ dbSNP | Ensembl ].
VAR_047512
Natural varianti1095 – 10951E → G.1 Publication
Corresponds to variant rs936212 [ dbSNP | Ensembl ].
VAR_047513

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei492 – 4954Missing in isoform 2. 1 PublicationVSP_035770
Alternative sequencei868 – 88215Missing in isoform 3. 1 PublicationVSP_054490Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95678 mRNA. Translation: AAA36453.1.
AK291657 mRNA. Translation: BAF84346.1.
AC020658 Genomic DNA. No translation available.
BC136467 mRNA. Translation: AAI36468.1.
CCDSiCCDS42020.1. [Q00722-1]
CCDS61591.1. [Q00722-3]
CCDS61592.1. [Q00722-2]
PIRiA43346.
RefSeqiNP_001271226.1. NM_001284297.1. [Q00722-2]
NP_001271227.1. NM_001284298.1. [Q00722-3]
NP_004564.2. NM_004573.2. [Q00722-1]
UniGeneiHs.355888.

Genome annotation databases

EnsembliENST00000260402; ENSP00000260402; ENSG00000137841. [Q00722-1]
ENST00000456256; ENSP00000411991; ENSG00000137841. [Q00722-3]
ENST00000557821; ENSP00000453975; ENSG00000137841. [Q00722-2]
GeneIDi5330.
KEGGihsa:5330.
UCSCiuc001zld.3. human. [Q00722-1]
uc010bbo.3. human. [Q00722-2]
uc010ucm.2. human.

Polymorphism databases

DMDMi215273902.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95678 mRNA. Translation: AAA36453.1 .
AK291657 mRNA. Translation: BAF84346.1 .
AC020658 Genomic DNA. No translation available.
BC136467 mRNA. Translation: AAI36468.1 .
CCDSi CCDS42020.1. [Q00722-1 ]
CCDS61591.1. [Q00722-3 ]
CCDS61592.1. [Q00722-2 ]
PIRi A43346.
RefSeqi NP_001271226.1. NM_001284297.1. [Q00722-2 ]
NP_001271227.1. NM_001284298.1. [Q00722-3 ]
NP_004564.2. NM_004573.2. [Q00722-1 ]
UniGenei Hs.355888.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FJU X-ray 2.20 B 1-803 [» ]
2ZKM X-ray 1.62 X 1-799 [» ]
ProteinModelPortali Q00722.
SMRi Q00722. Positions 11-803, 883-1151.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111346. 14 interactions.
DIPi DIP-29259N.
MINTi MINT-1726830.
STRINGi 9606.ENSP00000260402.

PTM databases

PhosphoSitei Q00722.

Polymorphism databases

DMDMi 215273902.

Proteomic databases

MaxQBi Q00722.
PaxDbi Q00722.
PRIDEi Q00722.

Protocols and materials databases

DNASUi 5330.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260402 ; ENSP00000260402 ; ENSG00000137841 . [Q00722-1 ]
ENST00000456256 ; ENSP00000411991 ; ENSG00000137841 . [Q00722-3 ]
ENST00000557821 ; ENSP00000453975 ; ENSG00000137841 . [Q00722-2 ]
GeneIDi 5330.
KEGGi hsa:5330.
UCSCi uc001zld.3. human. [Q00722-1 ]
uc010bbo.3. human. [Q00722-2 ]
uc010ucm.2. human.

Organism-specific databases

CTDi 5330.
GeneCardsi GC15M040580.
H-InvDB HIX0012125.
HGNCi HGNC:9055. PLCB2.
HPAi CAB009443.
MIMi 604114. gene.
neXtProti NX_Q00722.
PharmGKBi PA33385.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00760000118936.
HOGENOMi HOG000232046.
HOVERGENi HBG053609.
InParanoidi Q00722.
KOi K05858.
OMAi FIKWDDE.
OrthoDBi EOG7WDN1N.
PhylomeDBi Q00722.
TreeFami TF313216.

Enzyme and pathway databases

BioCyci MetaCyc:HS06408-MONOMER.
BRENDAi 3.1.4.11. 2681.
Reactomei REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_15426. PLC beta mediated events.
REACT_172761. Ca2+ pathway.
REACT_18283. G alpha (q) signalling events.
REACT_18405. Acetylcholine regulates insulin secretion.
REACT_19145. G beta:gamma signalling through PLC beta.
REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_21254. Presynaptic function of Kainate receptors.
SignaLinki Q00722.

Miscellaneous databases

ChiTaRSi PLCB2. human.
EvolutionaryTracei Q00722.
GeneWikii PLCB2.
GenomeRNAii 5330.
NextBioi 20640.
PROi Q00722.
SOURCEi Search...

Gene expression databases

Bgeei Q00722.
CleanExi HS_PLCB2.
ExpressionAtlasi Q00722. baseline and differential.
Genevestigatori Q00722.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProi IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR016280. PLC-beta.
IPR028403. PLC-beta2.
IPR014815. PLC-beta_C.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF10. PTHR10336:SF10. 1 hit.
Pfami PF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF08703. PLC-beta_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000956. PLC-beta. 1 hit.
PRINTSi PR00390. PHPHLIPASEC.
SMARTi SM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2."
    Park D., Jhon D.-Y., Kriz R., Knopf J., Rhee S.G.
    J. Biol. Chem. 267:16048-16055(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "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] (ISOFORM 1), VARIANT GLY-1095.
    Tissue: Placenta.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 3).
    Tissue: Testis.
  5. "Crystal structure of Rac1 bound to its effector phospholipase C-beta2."
    Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K., Sondek J.
    Nat. Struct. Mol. Biol. 13:1135-1140(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-803 (ISOFORM 2) IN COMPLEX WITH RAC1, MUTAGENESIS OF GLN-52.

Entry informationi

Entry nameiPLCB2_HUMAN
AccessioniPrimary (citable) accession number: Q00722
Secondary accession number(s): A8K6J2, B9EGH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 148 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

Miscellaneous

The receptor-mediated activation of PLC-beta-2 is most effectively mediated by one G-protein alpha subunit, alpha-16.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3