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Protein

Inactive phospholipase C-like protein 1

Gene

PLCL1

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

Functioni

Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor (By similarity). Regulates the turnover of receptors and thus contributes to the maintenance of GABA-mediated synaptic inhibition. Its aberrant expression could contribute to the genesis and progression of lung carcinoma. Acts as a inhibitor of PPP1C.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

BRENDAi2.7.11.10. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive phospholipase C-like protein 1
Short name:
PLC-L1
Alternative name(s):
Phospholipase C-deleted in lung carcinoma
Phospholipase C-related but catalytically inactive protein
Short name:
PRIP
Gene namesi
Name:PLCL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9063. PLCL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33394.

Chemistry

DrugBankiDB01103. Quinacrine.

Polymorphism and mutation databases

BioMutaiPLCL1.
DMDMi226694170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10951095Inactive phospholipase C-like protein 1PRO_0000319414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineCombined sources
Modified residuei93 – 931Phosphothreonine; by PKABy similarity
Modified residuei95 – 951PhosphoserineCombined sources
Modified residuei556 – 5561PhosphothreonineBy similarity
Modified residuei569 – 5691PhosphoserineBy similarity
Modified residuei1079 – 10791PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by the catalytic subunit of PKA. Phosphorylation of Thr-93 resulted in dissociation of PPP1C from PRIP1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15111.
PaxDbiQ15111.
PeptideAtlasiQ15111.
PRIDEiQ15111.

PTM databases

iPTMnetiQ15111.
PhosphoSiteiQ15111.

Expressioni

Tissue specificityi

Expressed in a variety of fetal and adult organs including brain, lung and kidney. Its expression was greatly reduced in small and non-small cell lung carcinoma. Isoform 1 is predominantly expressed in brain.2 Publications

Gene expression databases

BgeeiQ15111.
CleanExiHS_PLCL1.
ExpressionAtlasiQ15111. baseline and differential.
GenevisibleiQ15111. HS.

Organism-specific databases

HPAiHPA031849.

Interactioni

Subunit structurei

Interacts with PPP2CA (By similarity). Interacts with Ins(1,4,5)P3, Ins(1,4,5,6)P4, GABARAP, GABA receptor beta subunits, GABA receptor gamma-2 subunits and PPP1C. May form a ternary complex with GABA receptor beta subunit and GABARAP. The formation of a ternary complex with GABA receptor beta subunit and GABARAP could be the key step for facilitating the association of GABARAP with the GABA receptor gamma-2 subunit and to allow it to be transported at the right destination.By similarity5 Publications

Protein-protein interaction databases

STRINGi9606.ENSP00000402861.

Structurei

3D structure databases

ProteinModelPortaliQ15111.
SMRiQ15111. Positions 118-849.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 223111PHPROSITE-ProRule annotationAdd
BLAST
Domaini398 – 542145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini585 – 701117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini708 – 813106C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 222140Interaction with PPP1CAdd
BLAST
Regioni543 – 56725Interaction with GABA A beta subunitBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili894 – 91421Sequence analysisAdd
BLAST
Coiled coili1034 – 105926Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PH 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

eggNOGiKOG0169. Eukaryota.
ENOG410XPSW. LUCA.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
InParanoidiQ15111.
KOiK15375.
OMAiCSLPQQK.
OrthoDBiEOG7V49XT.
PhylomeDBiQ15111.
TreeFamiTF313216.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLC_EF-hand-like.
IPR028382. PLCL1.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF102. PTHR10336:SF102. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF16457. PH_12. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 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. AlignAdd to basket

Isoform 1 (identifier: Q15111-1) [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
MAEGAAGRED PAPPDAAGGE DDPRVGPDAA GDCVTAASGG RMRDRRSGVA
60 70 80 90 100
LPGAAGTPAD SEAGLLEAAR ATPRRSSIIK DPSNQKCGGR KKTVSFSSMP
110 120 130 140 150
SEKKISSAND CISFMQAGCE LKKVRPNSRI YNRFFTLDTD LQALRWEPSK
160 170 180 190 200
KDLEKAKLDI SAIKEIRLGK NTETFRNNGL ADQICEDCAF SILHGENYES
210 220 230 240 250
LDLVANSADV ANIWVSGLRY LVSRSKQPLD FMEGNQNTPR FMWLKTVFEA
260 270 280 290 300
ADVDGNGIML EDTSVELIKQ LNPTLKEAKI RLKFKEIQKS KEKLTTRVTE
310 320 330 340 350
EEFCEAFCEL CTRPEVYFLL VQISKNKEYL DANDLMLFLE AEQGVTHITE
360 370 380 390 400
DICLDIIRRY ELSEEGRQKG FLAIDGFTQY LLSSECDIFD PEQKKVAQDM
410 420 430 440 450
TQPLSHYYIN ASHNTYLIED QFRGPADING YIRALKMGCR SVELDVSDGS
460 470 480 490 500
DNEPILCNRN NMTTHVSFRS VIEVINKFAF VASEYPLILC LGNHCSLPQQ
510 520 530 540 550
KVMAQQMKKV FGNKLYTEAP LPSESYLPSP EKLKRMIIVK GKKLPSDPDV
560 570 580 590 600
LEGEVTDEDE EAEMSRRMSV DYNGEQKQIR LCRELSDLVS ICKSVQYRDF
610 620 630 640 650
ELSMKSQNYW EMCSFSETEA SRIANEYPED FVNYNKKFLS RIYPSAMRID
660 670 680 690 700
SSNLNPQDFW NCGCQIVAMN FQTPGPMMDL HTGWFLQNGG CGYVLRPSIM
710 720 730 740 750
RDEVSYFSAN TKGILPGVSP LALHIKIISG QNFPKPKGAC AKGDVIDPYV
760 770 780 790 800
CIEIHGIPAD CSEQRTKTVQ QNSDNPIFDE TFEFQVNLPE LAMIRFVVLD
810 820 830 840 850
DDYIGDEFIG QYTIPFECLQ PGYRHVPLRS FVGDIMEHVT LFVHIAITNR
860 870 880 890 900
SGGGKAQKRS LSVRMGKKVR EYTMLRNIGL KTIDDIFKIA VHPLREAIDM
910 920 930 940 950
RENMQNAIVS IKELCGLPPI ASLKQCLLTL SSRLITSDNT PSVSLVMKDS
960 970 980 990 1000
FPYLEPLGAI PDVQKKMLTA YDLMIQESRF LIEMADTVQE KIVQCQKAGM
1010 1020 1030 1040 1050
EFHEELHNLG AKEGLKGRKL NKATESFAWN ITVLKGQGDL LKNAKNEAIE
1060 1070 1080 1090
NMKQIQLACL SCGLSKAPSS SAEAKSKRSL EAIEEKESSE ENGKL
Note: No experimental confirmation available.
Length:1,095
Mass (Da):122,728
Last modified:April 14, 2009 - v3
Checksum:iC7B34D38C654E2D3
GO
Isoform 2 (identifier: Q15111-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.

Show »
Length:997
Mass (Da):113,012
Checksum:i0FC96A982056D1E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761R → T in BAA07688 (PubMed:7633416).Curated
Sequence conflicti563 – 5631E → Q in BAA07688 (PubMed:7633416).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti445 – 4451D → N.
Corresponds to variant rs45506698 [ dbSNP | Ensembl ].
VAR_038993
Natural varianti454 – 4541P → S.
Corresponds to variant rs45506696 [ dbSNP | Ensembl ].
VAR_038994
Natural varianti546 – 5461S → F.
Corresponds to variant rs45596936 [ dbSNP | Ensembl ].
VAR_038995
Natural varianti667 – 6671V → I.1 Publication
Corresponds to variant rs1064213 [ dbSNP | Ensembl ].
VAR_038996
Natural varianti684 – 6841W → C.
Corresponds to variant rs6741084 [ dbSNP | Ensembl ].
VAR_038997
Natural varianti937 – 9371S → N.
Corresponds to variant rs45452996 [ dbSNP | Ensembl ].
VAR_038998

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9898Missing in isoform 2. 2 PublicationsVSP_031475Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42108 mRNA. Translation: BAA07688.1.
AC011997 Genomic DNA. No translation available.
AC013478 Genomic DNA. No translation available.
AC020719 Genomic DNA. Translation: AAY14733.1.
BC101531 mRNA. Translation: AAI01532.1.
BC111985 mRNA. Translation: AAI11986.1.
BX537442 mRNA. Translation: CAD97684.1.
CCDSiCCDS2326.2. [Q15111-1]
PIRiI54390.
RefSeqiNP_006217.3. NM_006226.3. [Q15111-1]
UniGeneiHs.153322.

Genome annotation databases

EnsembliENST00000428675; ENSP00000402861; ENSG00000115896. [Q15111-1]
GeneIDi5334.
KEGGihsa:5334.
UCSCiuc010fsp.4. human. [Q15111-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D42108 mRNA. Translation: BAA07688.1.
AC011997 Genomic DNA. No translation available.
AC013478 Genomic DNA. No translation available.
AC020719 Genomic DNA. Translation: AAY14733.1.
BC101531 mRNA. Translation: AAI01532.1.
BC111985 mRNA. Translation: AAI11986.1.
BX537442 mRNA. Translation: CAD97684.1.
CCDSiCCDS2326.2. [Q15111-1]
PIRiI54390.
RefSeqiNP_006217.3. NM_006226.3. [Q15111-1]
UniGeneiHs.153322.

3D structure databases

ProteinModelPortaliQ15111.
SMRiQ15111. Positions 118-849.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000402861.

Chemistry

DrugBankiDB01103. Quinacrine.

PTM databases

iPTMnetiQ15111.
PhosphoSiteiQ15111.

Polymorphism and mutation databases

BioMutaiPLCL1.
DMDMi226694170.

Proteomic databases

MaxQBiQ15111.
PaxDbiQ15111.
PeptideAtlasiQ15111.
PRIDEiQ15111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000428675; ENSP00000402861; ENSG00000115896. [Q15111-1]
GeneIDi5334.
KEGGihsa:5334.
UCSCiuc010fsp.4. human. [Q15111-1]

Organism-specific databases

CTDi5334.
GeneCardsiPLCL1.
H-InvDBHIX0023967.
HGNCiHGNC:9063. PLCL1.
HPAiHPA031849.
MIMi600597. gene.
neXtProtiNX_Q15111.
PharmGKBiPA33394.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0169. Eukaryota.
ENOG410XPSW. LUCA.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
InParanoidiQ15111.
KOiK15375.
OMAiCSLPQQK.
OrthoDBiEOG7V49XT.
PhylomeDBiQ15111.
TreeFamiTF313216.

Enzyme and pathway databases

BRENDAi2.7.11.10. 2681.

Miscellaneous databases

ChiTaRSiPLCL1. human.
GenomeRNAii5334.
PROiQ15111.
SOURCEiSearch...

Gene expression databases

BgeeiQ15111.
CleanExiHS_PLCL1.
ExpressionAtlasiQ15111. baseline and differential.
GenevisibleiQ15111. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLC_EF-hand-like.
IPR028382. PLCL1.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF102. PTHR10336:SF102. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF16457. PH_12. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel phospholipase C family gene at chromosome 2q33 that is homozygously deleted in human small cell lung carcinoma."
    Kohno T., Otsuka T., Takano H., Yamamoto T., Hamaguchi M., Terada M., Yokota J.
    Hum. Mol. Genet. 4:667-674(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 2), VARIANT ILE-667.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 741-1095.
    Tissue: Rectum tumor.
  5. "Interaction of p130 with, and consequent inhibition of, the catalytic subunit of protein phosphatase 1alpha."
    Yoshimura K., Takeuchi H., Sato O., Hidaka K., Doira N., Terunuma M., Harada K., Ogawa Y., Ito Y., Kanematsu T., Hirata M.
    J. Biol. Chem. 276:17908-17913(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1C.
  6. Cited for: INTERACTION WITH GABARAP AND PPP1C.
  7. "PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in Ca2+ signaling and extension to neuroscience and beyond."
    Kanematsu T., Takeuchi H., Terunuma M., Hirata M.
    Mol. Cells 20:305-314(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1C; GABA A RECEPTOR SUBUNIT BETA; GABA A RECEPTOR AND SUBUNIT GAMMA-2.
  8. "Protein phosphatase regulation by PRIP, a PLC-related catalytically inactive protein -- implications in the phospho-modulation of the GABAA receptor."
    Yanagihori S., Terunuma M., Koyano K., Kanematsu T., Ho Ryu S., Hirata M.
    Adv. Enzyme Regul. 46:203-222(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1C.
  9. "Characterization of the human PRIP-1 gene structure and transcriptional regulation."
    Murakami A., Matsuda M., Nakasima A., Hirata M.
    Gene 382:129-139(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Modulation of GABA(A) receptor phosphorylation and membrane trafficking by phospholipase C-related inactive protein/protein phosphatase 1 and 2A signaling complex underlying brain-derived neurotrophic factor-dependent regulation of GABAergic inhibition."
    Jovanovic J.N., Takenaka K., Nakayama K.I., Fukami K., Takenawa T., Moss S.J., Nabekura J., Hirata M.
    J. Biol. Chem. 281:22180-22189(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GABA A RECEPTOR.
  11. "Phospholipase C-related inactive protein is implicated in the constitutive internalization of GABAA receptors mediated by clathrin and AP2 adaptor complex."
    Kanematsu T., Fujii M., Mizokami A., Kittler J.T., Nabekura J., Moss S.J., Hirata M.
    J. Neurochem. 101:898-905(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiPLCL1_HUMAN
AccessioniPrimary (citable) accession number: Q15111
Secondary accession number(s): Q3MJ90, Q53SD3, Q7Z3S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: April 14, 2009
Last modified: July 6, 2016
This is version 135 of the entry and version 3 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

In the PI-PLC X-box Asn-458 is present instead of the conserved His which is one of the active site residues. It is therefore expected that this protein lacks catalytic activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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.