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Q9NQ66

- PLCB1_HUMAN

UniProt

Q9NQ66 - PLCB1_HUMAN

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Protein

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

Gene

PLCB1

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei331 – 3311PROSITE-ProRule annotation
Active sitei378 – 3781PROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. calmodulin binding Source: BHF-UCL
  3. enzyme binding Source: UniProtKB
  4. GTPase activator activity Source: BHF-UCL
  5. phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
  6. phosphatidylinositol phospholipase C activity Source: UniProtKB
  7. protein homodimerization activity Source: BHF-UCL
  8. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of meiosis involved in egg activation Source: BHF-UCL
  2. cerebral cortex development Source: BHF-UCL
  3. fat cell differentiation Source: Ensembl
  4. G2/M transition of mitotic cell cycle Source: BHF-UCL
  5. glutamate receptor signaling pathway Source: BHF-UCL
  6. G-protein coupled acetylcholine receptor signaling pathway Source: BHF-UCL
  7. inositol phosphate metabolic process Source: Reactome
  8. insulin-like growth factor receptor signaling pathway Source: BHF-UCL
  9. interleukin-12-mediated signaling pathway Source: BHF-UCL
  10. interleukin-15-mediated signaling pathway Source: BHF-UCL
  11. interleukin-1-mediated signaling pathway Source: BHF-UCL
  12. intracellular signal transduction Source: InterPro
  13. lipid catabolic process Source: UniProtKB-KW
  14. memory Source: BHF-UCL
  15. negative regulation of monocyte extravasation Source: BHF-UCL
  16. negative regulation of transcription, DNA-templated Source: BHF-UCL
  17. phosphatidylinositol metabolic process Source: BHF-UCL
  18. positive regulation of acrosome reaction Source: BHF-UCL
  19. positive regulation of CD24 biosynthetic process Source: BHF-UCL
  20. positive regulation of developmental growth Source: BHF-UCL
  21. positive regulation of embryonic development Source: BHF-UCL
  22. positive regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
  23. positive regulation of GTPase activity Source: GOC
  24. positive regulation of interleukin-12 production Source: BHF-UCL
  25. positive regulation of JNK cascade Source: BHF-UCL
  26. positive regulation of myoblast differentiation Source: BHF-UCL
  27. positive regulation of transcription, DNA-templated Source: BHF-UCL
  28. regulation of fertilization Source: BHF-UCL
  29. regulation of G-protein coupled receptor protein signaling pathway Source: BHF-UCL
  30. signal transduction Source: UniProtKB
  31. small molecule metabolic process Source: Reactome
  32. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

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.
SignaLinkiQ9NQ66.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC:3.1.4.11)
Alternative name(s):
PLC-154
Phosphoinositide phospholipase C-beta-1
Phospholipase C-I
Short name:
PLC-I
Phospholipase C-beta-1
Short name:
PLC-beta-1
Gene namesi
Name:PLCB1
Synonyms:KIAA0581
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15917. PLCB1.

Subcellular locationi

Nucleus membrane By similarity. Cytoplasm By similarity
Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB-KW
  5. nuclear chromatin Source: BHF-UCL
  6. nuclear speck Source: BHF-UCL
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 12 (EIEE12) [MIM:613722]: A form of epilepsy characterized by frequent tonic seizures or spasms beginning in infancy with a specific EEG finding of suppression-burst patterns, characterized by high-voltage bursts alternating with almost flat suppression phases. Patients may progress to West syndrome, which is characterized by tonic spasms with clustering, arrest of psychomotor development, and hypsarrhythmia on EEG.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Epilepsy

Organism-specific databases

MIMi613722. phenotype.
Orphaneti293181. Malignant migrating partial seizures of infancy.
3451. West syndrome.
PharmGKBiPA33384.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 121612161-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1PRO_0000088486Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei887 – 8871Phosphoserine; by PKCBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NQ66.
PaxDbiQ9NQ66.
PRIDEiQ9NQ66.

PTM databases

PhosphoSiteiQ9NQ66.

Expressioni

Gene expression databases

BgeeiQ9NQ66.
ExpressionAtlasiQ9NQ66. baseline and differential.
GenevestigatoriQ9NQ66.

Organism-specific databases

HPAiCAB004275.
CAB005334.

Interactioni

Subunit structurei

Interacts with DGKQ.1 Publication

Protein-protein interaction databases

BioGridi116841. 11 interactions.
IntActiQ9NQ66. 1 interaction.
MINTiMINT-5005654.

Structurei

3D structure databases

ProteinModelPortaliQ9NQ66.
SMRiQ9NQ66. Positions 11-830, 890-1170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini316 – 467152PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini540 – 656117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini663 – 76199C2PROSITE-ProRule annotationAdd
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

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
HOVERGENiHBG053609.
InParanoidiQ9NQ66.
KOiK05858.
OMAiMMDFINL.
OrthoDBiEOG7WDN1N.
PhylomeDBiQ9NQ66.
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.
IPR028400. PLC-beta1.
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:SF12. PTHR10336:SF12. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q9NQ66-1) [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
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF
60 70 80 90 100
FFYWTDQNKE TELLDLSLVK DARCGRHAKA PKDPKLRELL DVGNIGRLEQ
110 120 130 140 150
RMITVVYGPD LVNISHLNLV AFQEEVAKEW TNEVFSLATN LLAQNMSRDA
160 170 180 190 200
FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA DRKRVETALE ACSLPSSRND
210 220 230 240 250
SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL TVDQMMDFIN
260 270 280 290 300
LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLARKGQI SVDGFMRYLS
310 320 330 340 350
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR
360 370 380 390 400
QVLLSGCRCV ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF
410 420 430 440 450
KTSPFPILLS FENHVDSPKQ QAKMAEYCRL IFGDALLMEP LEKYPLESGV
460 470 480 490 500
PLPSPMDLMY KILVKNKKKS HKSSEGSGKK KLSEQASNTY SDSSSMFEPS
510 520 530 540 550
SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM SNLVNYIQPV
560 570 580 590 600
KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
610 620 630 640 650
GTRVDSSNYM PQLFWNAGCQ MVALNFQTMD LAMQINMGMY EYNGKSGYRL
660 670 680 690 700
KPEFMRRPDK HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD
710 720 730 740 750
MFGLPVDTRR KAFKTKTSQG NAVNPVWEEE PIVFKKVVLP TLACLRIAVY
760 770 780 790 800
EEGGKFIGHR ILPVQAIRPG YHYICLRNER NQPLTLPAVF VYIEVKDYVP
810 820 830 840 850
DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK EADPGETPSE
860 870 880 890 900
APSEARTTPA ENGVNHTTTL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS
910 920 930 940 950
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT
960 970 980 990 1000
KYNEIQNDYL RRRAALEKSA KKDSKKKSEP SSPDHGSSTI EQDLAALDAE
1010 1020 1030 1040 1050
MTQKLIDLKD KQQQQLLNLR QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ
1060 1070 1080 1090 1100
NNQLKKLKEI CEKEKKELKK KMDKKRQEKI TEAKSKDKSQ MEEEKTEMIR
1110 1120 1130 1140 1150
SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP KLQVELEQEY
1160 1170 1180 1190 1200
QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPLSLSSDP GKVNHKTPSS
1210
EELGGDIPGK EFDTPL
Length:1,216
Mass (Da):138,567
Last modified:October 1, 2000 - v1
Checksum:i6F4263D1A50C6FD1
GO
Isoform B (identifier: Q9NQ66-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1142-1216: LQVELEQEYQ...IPGKEFDTPL → GEGSSSFLSETCHEDPSVSPNFTPPNPQALKW

Show »
Length:1,173
Mass (Da):133,703
Checksum:iB9DA88251A5769FB
GO

Sequence cautioni

The sequence BAA25507.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14641.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 3434MAGAQ…KWDDD → MGSLQGIATKILIRILSDAL IRKETDLKS in AAF86613. (PubMed:10760467)CuratedAdd
BLAST
Sequence conflicti189 – 1891L → M in AAF86613. (PubMed:10760467)Curated
Sequence conflicti203 – 2031P → L in AAF86613. (PubMed:10760467)Curated
Sequence conflicti216 – 2161L → F in AAF86613. (PubMed:10760467)Curated
Sequence conflicti221 – 2211P → L in AAF86613. (PubMed:10760467)Curated
Sequence conflicti266 – 2661L → P in AAF86613. (PubMed:10760467)Curated
Sequence conflicti309 – 3091P → T in AAF86613. (PubMed:10760467)Curated
Sequence conflicti320 – 3201Q → R in AAF86613. (PubMed:10760467)Curated
Sequence conflicti352 – 3521V → A in AAF86613. (PubMed:10760467)Curated
Sequence conflicti366 – 3661K → R in AAF86613. (PubMed:10760467)Curated
Sequence conflicti393 – 3931E → K in AAF86613. (PubMed:10760467)Curated
Sequence conflicti983 – 9831P → S in CAB98143. (PubMed:11118617)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti854 – 8541E → K.
Corresponds to variant rs2076413 [ dbSNP | Ensembl ].
VAR_050541
Natural varianti907 – 9071A → P in a breast cancer sample; somatic mutation. 1 Publication
VAR_036547

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1142 – 121675LQVEL…FDTPL → GEGSSSFLSETCHEDPSVSP NFTPPNPQALKW in isoform B. 4 PublicationsVSP_004718Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278313 mRNA. Translation: CAB98142.1.
AJ278314 mRNA. Translation: CAB98143.1.
AY004175 mRNA. Translation: AAF86613.1.
AB011153 mRNA. Translation: BAA25507.3. Different initiation.
AL031683
, AL034551, AL049593, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI43121.1.
AL031683
, AL034551, AL050315, AL049632, AL050323 Genomic DNA. Translation: CAI43122.1.
AL034551
, AL031683, AL049593, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI21973.1.
AL034551
, AL031683, AL050315, AL049632, AL050323 Genomic DNA. Translation: CAI21974.1.
AL049593
, AL031683, AL034551, AL049632, AL050315, AL050323 Genomic DNA. Translation: CAI22175.1.
AL049632
, AL031683, AL034551, AL049593, AL050315, AL050323 Genomic DNA. Translation: CAI43151.1.
AL049632
, AL031683, AL034551, AL050315, AL050323 Genomic DNA. Translation: CAI43152.1.
AL050315
, AL031683, AL034551, AL049593, AL049632, AL050323 Genomic DNA. Translation: CAI42238.1.
AL050315
, AL031683, AL034551, AL049632, AL050323 Genomic DNA. Translation: CAI42239.1.
AL050323
, AL031683, AL034551, AL049593, AL049632, AL050315 Genomic DNA. Translation: CAI22830.1.
AL050323
, AL031683, AL034551, AL050315, AL049632 Genomic DNA. Translation: CAI22831.1.
CH471133 Genomic DNA. Translation: EAX10372.1.
CH471133 Genomic DNA. Translation: EAX10373.1.
CH471133 Genomic DNA. Translation: EAX10374.1.
CH471133 Genomic DNA. Translation: EAX10376.1.
BC069420 mRNA. Translation: AAH69420.1.
BC117231 mRNA. Translation: AAI17232.1.
AL137267 mRNA. Translation: CAB70666.1.
AK023689 mRNA. Translation: BAB14641.1. Different initiation.
CCDSiCCDS13102.1. [Q9NQ66-1]
CCDS13103.1. [Q9NQ66-2]
RefSeqiNP_056007.1. NM_015192.3. [Q9NQ66-1]
NP_877398.1. NM_182734.2. [Q9NQ66-2]
XP_006723618.1. XM_006723555.1. [Q9NQ66-2]
UniGeneiHs.431173.

Genome annotation databases

EnsembliENST00000338037; ENSP00000338185; ENSG00000182621. [Q9NQ66-1]
ENST00000378637; ENSP00000367904; ENSG00000182621. [Q9NQ66-2]
ENST00000378641; ENSP00000367908; ENSG00000182621. [Q9NQ66-2]
GeneIDi23236.
KEGGihsa:23236.
UCSCiuc002wna.4. human. [Q9NQ66-2]
uc002wnb.4. human. [Q9NQ66-1]

Polymorphism databases

DMDMi12643814.

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
AJ278313 mRNA. Translation: CAB98142.1 .
AJ278314 mRNA. Translation: CAB98143.1 .
AY004175 mRNA. Translation: AAF86613.1 .
AB011153 mRNA. Translation: BAA25507.3 . Different initiation.
AL031683
, AL034551 , AL049593 , AL049632 , AL050315 , AL050323 Genomic DNA. Translation: CAI43121.1 .
AL031683
, AL034551 , AL050315 , AL049632 , AL050323 Genomic DNA. Translation: CAI43122.1 .
AL034551
, AL031683 , AL049593 , AL049632 , AL050315 , AL050323 Genomic DNA. Translation: CAI21973.1 .
AL034551
, AL031683 , AL050315 , AL049632 , AL050323 Genomic DNA. Translation: CAI21974.1 .
AL049593
, AL031683 , AL034551 , AL049632 , AL050315 , AL050323 Genomic DNA. Translation: CAI22175.1 .
AL049632
, AL031683 , AL034551 , AL049593 , AL050315 , AL050323 Genomic DNA. Translation: CAI43151.1 .
AL049632
, AL031683 , AL034551 , AL050315 , AL050323 Genomic DNA. Translation: CAI43152.1 .
AL050315
, AL031683 , AL034551 , AL049593 , AL049632 , AL050323 Genomic DNA. Translation: CAI42238.1 .
AL050315
, AL031683 , AL034551 , AL049632 , AL050323 Genomic DNA. Translation: CAI42239.1 .
AL050323
, AL031683 , AL034551 , AL049593 , AL049632 , AL050315 Genomic DNA. Translation: CAI22830.1 .
AL050323
, AL031683 , AL034551 , AL050315 , AL049632 Genomic DNA. Translation: CAI22831.1 .
CH471133 Genomic DNA. Translation: EAX10372.1 .
CH471133 Genomic DNA. Translation: EAX10373.1 .
CH471133 Genomic DNA. Translation: EAX10374.1 .
CH471133 Genomic DNA. Translation: EAX10376.1 .
BC069420 mRNA. Translation: AAH69420.1 .
BC117231 mRNA. Translation: AAI17232.1 .
AL137267 mRNA. Translation: CAB70666.1 .
AK023689 mRNA. Translation: BAB14641.1 . Different initiation.
CCDSi CCDS13102.1. [Q9NQ66-1 ]
CCDS13103.1. [Q9NQ66-2 ]
RefSeqi NP_056007.1. NM_015192.3. [Q9NQ66-1 ]
NP_877398.1. NM_182734.2. [Q9NQ66-2 ]
XP_006723618.1. XM_006723555.1. [Q9NQ66-2 ]
UniGenei Hs.431173.

3D structure databases

ProteinModelPortali Q9NQ66.
SMRi Q9NQ66. Positions 11-830, 890-1170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116841. 11 interactions.
IntActi Q9NQ66. 1 interaction.
MINTi MINT-5005654.

Chemistry

BindingDBi Q9NQ66.
ChEMBLi CHEMBL4034.

PTM databases

PhosphoSitei Q9NQ66.

Polymorphism databases

DMDMi 12643814.

Proteomic databases

MaxQBi Q9NQ66.
PaxDbi Q9NQ66.
PRIDEi Q9NQ66.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338037 ; ENSP00000338185 ; ENSG00000182621 . [Q9NQ66-1 ]
ENST00000378637 ; ENSP00000367904 ; ENSG00000182621 . [Q9NQ66-2 ]
ENST00000378641 ; ENSP00000367908 ; ENSG00000182621 . [Q9NQ66-2 ]
GeneIDi 23236.
KEGGi hsa:23236.
UCSCi uc002wna.4. human. [Q9NQ66-2 ]
uc002wnb.4. human. [Q9NQ66-1 ]

Organism-specific databases

CTDi 23236.
GeneCardsi GC20P008061.
HGNCi HGNC:15917. PLCB1.
HPAi CAB004275.
CAB005334.
MIMi 607120. gene.
613722. phenotype.
neXtProti NX_Q9NQ66.
Orphaneti 293181. Malignant migrating partial seizures of infancy.
3451. West syndrome.
PharmGKBi PA33384.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00760000118936.
HOVERGENi HBG053609.
InParanoidi Q9NQ66.
KOi K05858.
OMAi MMDFINL.
OrthoDBi EOG7WDN1N.
PhylomeDBi Q9NQ66.
TreeFami TF313216.

Enzyme and pathway databases

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 Q9NQ66.

Miscellaneous databases

ChiTaRSi PLCB1. human.
GeneWikii PLCB1.
GenomeRNAii 23236.
NextBioi 44882.
PROi Q9NQ66.
SOURCEi Search...

Gene expression databases

Bgeei Q9NQ66.
ExpressionAtlasi Q9NQ66. baseline and differential.
Genevestigatori Q9NQ66.

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.
IPR028400. PLC-beta1.
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:SF12. PTHR10336:SF12. 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 and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLCbeta1)."
    Caricasole A., Sala C., Roncarati R., Formenti E., Terstappen G.C.
    Biochim. Biophys. Acta 1517:63-72(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
    Tissue: Brain.
  2. "Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta 1."
    Peruzzi D., Calabrese G., Faenza I., Manzoli L., Matteucci A., Gianfrancesco F., Billi A.M., Stuppia L., Palka G., Cocco L.
    Biochim. Biophys. Acta 1484:175-182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Tissue: Brain.
  3. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS A AND B).
    Tissue: Brain.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1216 (ISOFORM B).
    Tissue: Testis.
  9. "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] OF 417-1062 (ISOFORMS A AND B).
    Tissue: Placenta.
  10. Cited for: INTERACTION WITH DGKQ.
  11. Cited for: INVOLVEMENT IN EIEE12.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-907.

Entry informationi

Entry nameiPLCB1_HUMAN
AccessioniPrimary (citable) accession number: Q9NQ66
Secondary accession number(s): D3DW12
, D3DW13, O60325, Q17RQ6, Q5TFF7, Q5TGC9, Q8IV93, Q9BQW2, Q9H4H2, Q9H8H5, Q9NQ65, Q9NQH9, Q9NTH4, Q9UJP6, Q9UM26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 153 of the entry and version 1 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-1 is mediated by two G-protein alpha subunits, alpha-Q and alpha-11.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3