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P19174

- PLCG1_HUMAN

UniProt

P19174 - PLCG1_HUMAN

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Protein

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

Gene

PLCG1

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

Functioni

Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration.1 Publication

Catalytic activityi

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

Cofactori

Calcium.

Enzyme regulationi

Activated by phosphorylation on tyrosine residues.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei335 – 3351PROSITE-ProRule annotation
Active sitei380 – 3801PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi165 – 17612PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. neurotrophin TRKA receptor binding Source: UniProtKB
  3. phosphatidylinositol phospholipase C activity Source: UniProtKB
  4. phospholipase C activity Source: Reactome
  5. protein kinase binding Source: BHF-UCL
  6. receptor signaling protein activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPKK activity Source: Reactome
  2. activation of phospholipase C activity Source: Reactome
  3. axon guidance Source: Reactome
  4. blood coagulation Source: Reactome
  5. calcium-mediated signaling Source: BHF-UCL
  6. cell migration Source: BHF-UCL
  7. cellular response to epidermal growth factor stimulus Source: UniProtKB
  8. cytokine-mediated signaling pathway Source: Reactome
  9. epidermal growth factor receptor signaling pathway Source: BHF-UCL
  10. Fc-epsilon receptor signaling pathway Source: Reactome
  11. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  12. fibroblast growth factor receptor signaling pathway Source: Reactome
  13. innate immune response Source: Reactome
  14. inositol phosphate metabolic process Source: Reactome
  15. in utero embryonic development Source: Ensembl
  16. leukocyte migration Source: Reactome
  17. neurotrophin TRK receptor signaling pathway Source: Reactome
  18. phospholipid catabolic process Source: InterPro
  19. positive regulation of angiogenesis Source: DFLAT
  20. positive regulation of blood vessel endothelial cell migration Source: DFLAT
  21. positive regulation of epithelial cell migration Source: UniProtKB
  22. positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  23. signal transduction Source: UniProtKB
  24. small molecule metabolic process Source: Reactome
  25. T cell receptor signaling pathway Source: Reactome
  26. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Host-virus interaction, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_111064. DAG and IP3 signaling.
REACT_115720. PLCG1 events in ERBB2 signaling.
REACT_115831. ISG15 antiviral mechanism.
REACT_115852. Signaling by constitutively active EGFR.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12076. Frs2-mediated activation.
REACT_12079. PLC-gamma1 signalling.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_121398. Signaling by FGFR mutants.
REACT_12478. EGFR interacts with phospholipase C-gamma.
REACT_12519. PECAM1 interactions.
REACT_12623. Generation of second messenger molecules.
REACT_147814. DAP12 signaling.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163701. FCERI mediated MAPK activation.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_17025. Downstream signal transduction.
REACT_21310. Phospholipase C-mediated cascade.
REACT_22228. Role of second messengers in netrin-1 signaling.
SignaLinkiP19174.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
Alternative name(s):
PLC-148
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-II
Short name:
PLC-II
Phospholipase C-gamma-1
Short name:
PLC-gamma-1
Gene namesi
Name:PLCG1
Synonyms:PLC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9065. PLCG1.

Subcellular locationi

Cell projectionlamellipodium. Cell projectionruffle
Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell projection Source: BHF-UCL
  3. COP9 signalosome Source: UniProtKB
  4. cytoplasm Source: MGI
  5. cytosol Source: UniProtKB
  6. lamellipodium Source: UniProtKB
  7. plasma membrane Source: UniProtKB
  8. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33392.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 129012891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei506 – 5061PhosphotyrosineBy similarity
Modified residuei771 – 7711Phosphotyrosine; by SYK4 Publications
Modified residuei775 – 7751Phosphotyrosine1 Publication
Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXK4 Publications
Modified residuei977 – 9771PhosphotyrosineBy similarity
Modified residuei1221 – 12211Phosphoserine3 Publications
Modified residuei1248 – 12481Phosphoserine1 Publication
Modified residuei1253 – 12531Phosphotyrosine2 Publications

Post-translational modificationi

Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases, in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells.By similarity15 Publications
Ubiquitinated by CBLB in activated T-cells.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP19174.
PaxDbiP19174.
PRIDEiP19174.

PTM databases

PhosphoSiteiP19174.

Expressioni

Gene expression databases

BgeeiP19174.
CleanExiHS_PLCG1.
ExpressionAtlasiP19174. baseline and differential.
GenevestigatoriP19174.

Organism-specific databases

HPAiCAB004277.
HPA036681.
HPA036682.

Interactioni

Subunit structurei

Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET. Interacts with FLT1 (tyrosine-phosphorylated) By similarity. Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK By similarity. Interacts with AXL, FLT4 and KIT. Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity. Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome.By similarity20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL2P426844EBI-79387,EBI-1102694
AKT1P317499EBI-79387,EBI-296087
ARP1027522EBI-79387,EBI-608057
ASAP1Q9ULH13EBI-79387,EBI-346622
ASAP2O431503EBI-79387,EBI-310968
CD22P202732EBI-79387,EBI-78277
DUSP15Q9H1R22EBI-79387,EBI-1752795
EEF1A2Q71V393EBI-79387,EBI-7645815From a different organism.
EGFRP005336EBI-79387,EBI-297353
ERBB2P046265EBI-79387,EBI-641062
ERBB3P218604EBI-79387,EBI-720706
FCGR2BP319942EBI-79387,EBI-724784
FGFR1P113625EBI-79387,EBI-1028277
FLT1P179482EBI-79387,EBI-1026718
GAB1Q1348036EBI-79387,EBI-517684
GRB2P629932EBI-79387,EBI-401755
HCKP086312EBI-79387,EBI-346340
INSRP062139EBI-79387,EBI-475899
KHDRBS1Q076662EBI-79387,EBI-1364
KITP1072131EBI-79387,EBI-1379503
LATO435616EBI-79387,EBI-1222766
LCP2Q130943EBI-79387,EBI-346946
MAP4K1Q929186EBI-79387,EBI-881
METP0858110EBI-79387,EBI-1039152
PDGFRBP096195EBI-79387,EBI-641237
RAC1P630007EBI-79387,EBI-413628
RETP079492EBI-79387,EBI-2480756
RIN3Q8TB243EBI-79387,EBI-1570523
SCARB2Q141082EBI-79387,EBI-1564650
SHANK2Q9UPX84EBI-79387,EBI-1570571
SHANK3Q9BYB02EBI-79387,EBI-1752330
SNX17Q150362EBI-79387,EBI-1752620
SOS1Q078893EBI-79387,EBI-297487
SOS2Q078904EBI-79387,EBI-298181
SYKP434054EBI-79387,EBI-78302
VIL1P093275EBI-79387,EBI-746958

Protein-protein interaction databases

BioGridi111351. 99 interactions.
DIPiDIP-100N.
IntActiP19174. 109 interactions.
MINTiMINT-102915.
STRINGi9606.ENSP00000244007.

Structurei

Secondary structure

1
1290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi551 – 5544
Beta strandi556 – 5583
Helixi561 – 57616
Beta strandi583 – 5875
Beta strandi589 – 5913
Beta strandi595 – 6017
Beta strandi604 – 61310
Helixi615 – 6173
Beta strandi620 – 6245
Beta strandi627 – 6315
Helixi632 – 64110
Beta strandi644 – 6463
Beta strandi649 – 6513
Helixi662 – 6654
Beta strandi669 – 6724
Helixi675 – 6839
Beta strandi690 – 6956
Beta strandi701 – 7088
Beta strandi711 – 72010
Beta strandi723 – 7264
Beta strandi729 – 7324
Helixi734 – 74310
Helixi758 – 7636
Beta strandi792 – 7943
Beta strandi805 – 8095
Beta strandi817 – 8204
Turni825 – 8273
Beta strandi834 – 8363
Turni843 – 8453

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HSQNMR-A790-851[»]
2HSPNMR-A790-851[»]
4EY0X-ray2.80A/B/C/D545-790[»]
4FBNX-ray2.40A545-790[»]
ProteinModelPortaliP19174.
SMRiP19174. Positions 73-483, 489-933, 952-1207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 142116PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 18736EF-handPROSITE-ProRule annotationAdd
BLAST
Domaini320 – 464145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini489 – 52335PH 2; first partPROSITE-ProRule annotationAdd
BLAST
Domaini550 – 657108SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini668 – 75689SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini791 – 85161SH3PROSITE-ProRule annotationAdd
BLAST
Domaini895 – 93137PH 2; second partPROSITE-ProRule annotationAdd
BLAST
Domaini953 – 1070118PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1075 – 1177103C2PROSITE-ProRule annotationAdd
BLAST

Domaini

The SH3 domain mediates interaction with CLNK By similarity. The SH3 domain also mediates interaction with RALGPS1.By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG268751.
GeneTreeiENSGT00730000110782.
HOVERGENiHBG053611.
InParanoidiP19174.
KOiK01116.
OMAiYRSLMYS.
OrthoDBiEOG7W419X.
PhylomeDBiP19174.
TreeFamiTF313216.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
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.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 3 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P19174-1) [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
MAGAASPCAN GCGPGAPSDA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAPTP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLEASTLRA GERPELCRVS
260 270 280 290 300
LPEFQQFLLD YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVEISADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSMM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEVSS STELHSNEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFIKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV
860 870 880 890 900
NPVALEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KIMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFMTGRHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCAI SIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGTSLRE RGSDASGQLF HGRAREGSFE
1260 1270 1280 1290
SRYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL
Length:1,290
Mass (Da):148,532
Last modified:November 1, 1990 - v1
Checksum:iAE05ABE2A18EDDAC
GO
Isoform 2 (identifier: P19174-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1215-1215: K → KQ

Note: Contains a phosphoserine at position 1222.

Show »
Length:1,291
Mass (Da):148,660
Checksum:iEDDBB8D4E49B2F3E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091T → N.1 Publication
Corresponds to variant rs2229348 [ dbSNP | Ensembl ].
VAR_025213
Natural varianti279 – 2791S → G.1 Publication
Corresponds to variant rs2228246 [ dbSNP | Ensembl ].
VAR_022130
Natural varianti739 – 7391S → T.1 Publication
Corresponds to variant rs34203315 [ dbSNP | Ensembl ].
VAR_025214
Natural varianti813 – 8131I → T.2 Publications
Corresponds to variant rs753381 [ dbSNP | Ensembl ].
VAR_011908

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1215 – 12151K → KQ in isoform 2. 1 PublicationVSP_038692

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34667 mRNA. Translation: AAA36452.1.
DQ297143 Genomic DNA. Translation: ABB84466.1.
AL022394 Genomic DNA. Translation: CAA18537.1.
CH471077 Genomic DNA. Translation: EAW75991.1.
CH471077 Genomic DNA. Translation: EAW75992.1.
BC136466 mRNA. Translation: AAI36467.1.
BC144136 mRNA. Translation: AAI44137.1.
CCDSiCCDS13313.1. [P19174-2]
CCDS13314.1. [P19174-1]
PIRiA36466.
RefSeqiNP_002651.2. NM_002660.2. [P19174-2]
NP_877963.1. NM_182811.1. [P19174-1]
UniGeneiHs.268177.

Genome annotation databases

EnsembliENST00000244007; ENSP00000244007; ENSG00000124181. [P19174-2]
ENST00000373271; ENSP00000362368; ENSG00000124181. [P19174-1]
GeneIDi5335.
KEGGihsa:5335.
UCSCiuc002xjp.1. human. [P19174-1]

Polymorphism databases

DMDMi130225.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34667 mRNA. Translation: AAA36452.1 .
DQ297143 Genomic DNA. Translation: ABB84466.1 .
AL022394 Genomic DNA. Translation: CAA18537.1 .
CH471077 Genomic DNA. Translation: EAW75991.1 .
CH471077 Genomic DNA. Translation: EAW75992.1 .
BC136466 mRNA. Translation: AAI36467.1 .
BC144136 mRNA. Translation: AAI44137.1 .
CCDSi CCDS13313.1. [P19174-2 ]
CCDS13314.1. [P19174-1 ]
PIRi A36466.
RefSeqi NP_002651.2. NM_002660.2. [P19174-2 ]
NP_877963.1. NM_182811.1. [P19174-1 ]
UniGenei Hs.268177.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HSQ NMR - A 790-851 [» ]
2HSP NMR - A 790-851 [» ]
4EY0 X-ray 2.80 A/B/C/D 545-790 [» ]
4FBN X-ray 2.40 A 545-790 [» ]
ProteinModelPortali P19174.
SMRi P19174. Positions 73-483, 489-933, 952-1207.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111351. 99 interactions.
DIPi DIP-100N.
IntActi P19174. 109 interactions.
MINTi MINT-102915.
STRINGi 9606.ENSP00000244007.

Chemistry

BindingDBi P19174.
ChEMBLi CHEMBL3964.

PTM databases

PhosphoSitei P19174.

Polymorphism databases

DMDMi 130225.

Proteomic databases

MaxQBi P19174.
PaxDbi P19174.
PRIDEi P19174.

Protocols and materials databases

DNASUi 5335.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244007 ; ENSP00000244007 ; ENSG00000124181 . [P19174-2 ]
ENST00000373271 ; ENSP00000362368 ; ENSG00000124181 . [P19174-1 ]
GeneIDi 5335.
KEGGi hsa:5335.
UCSCi uc002xjp.1. human. [P19174-1 ]

Organism-specific databases

CTDi 5335.
GeneCardsi GC20P039765.
HGNCi HGNC:9065. PLCG1.
HPAi CAB004277.
HPA036681.
HPA036682.
MIMi 172420. gene.
neXtProti NX_P19174.
PharmGKBi PA33392.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG268751.
GeneTreei ENSGT00730000110782.
HOVERGENi HBG053611.
InParanoidi P19174.
KOi K01116.
OMAi YRSLMYS.
OrthoDBi EOG7W419X.
PhylomeDBi P19174.
TreeFami TF313216.

Enzyme and pathway databases

Reactomei REACT_111064. DAG and IP3 signaling.
REACT_115720. PLCG1 events in ERBB2 signaling.
REACT_115831. ISG15 antiviral mechanism.
REACT_115852. Signaling by constitutively active EGFR.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12076. Frs2-mediated activation.
REACT_12079. PLC-gamma1 signalling.
REACT_121141. Signaling by FGFR1 fusion mutants.
REACT_121398. Signaling by FGFR mutants.
REACT_12478. EGFR interacts with phospholipase C-gamma.
REACT_12519. PECAM1 interactions.
REACT_12623. Generation of second messenger molecules.
REACT_147814. DAP12 signaling.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163701. FCERI mediated MAPK activation.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_17025. Downstream signal transduction.
REACT_21310. Phospholipase C-mediated cascade.
REACT_22228. Role of second messengers in netrin-1 signaling.
SignaLinki P19174.

Miscellaneous databases

ChiTaRSi PLCG1. human.
EvolutionaryTracei P19174.
GeneWikii PLCG1.
GenomeRNAii 5335.
NextBioi 20662.
PROi P19174.
SOURCEi Search...

Gene expression databases

Bgeei P19174.
CleanExi HS_PLCG1.
ExpressionAtlasi P19174. baseline and differential.
Genevestigatori P19174.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProi IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
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.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 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.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000952. PLC-gamma. 1 hit.
PRINTSi PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 3 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50004. C2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase."
    Burgess W.H., Dionne C.A., Kaplow J.M., Mudd R., Friesel R., Zilberstein A., Schlessinger J., Jaye M.
    Mol. Cell. Biol. 10:4770-4777(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
    Tissue: Brain and Vein.
  2. NIEHS SNPs program
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-209; GLY-279; THR-739 AND THR-813.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1 AND 2), VARIANT THR-813.
    Tissue: Brain and Testis.
  6. "A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1."
    Mohammadi M., Honegger A.M., Rotin D., Fischer R., Bellot F., Li W., Dionne C.A., Jaye M., Rubinstein M., Schlessinger J.
    Mol. Cell. Biol. 11:5068-5078(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR1.
  7. "Inhibition of CD3-linked phospholipase C by phorbol ester and by cAMP is associated with decreased phosphotyrosine and increased phosphoserine contents of PLC-gamma 1."
    Park D.J., Min H.K., Rhee S.G.
    J. Biol. Chem. 267:1496-1501(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1248.
  8. "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."
    Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K.
    J. Biol. Chem. 269:18320-18326(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR4.
  9. "Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk."
    Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.
    Mol. Cell. Biol. 16:1305-1315(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-771 AND TYR-783 BY SYK, INTERACTION WITH SYK.
  10. "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
    Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
    J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIT.
  11. "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
    Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
    Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXL.
  12. "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation."
    Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
    Cell 92:83-92(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAT.
  13. "Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells."
    Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.
    J. Biol. Chem. 274:28050-28057(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHB.
  14. "Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization."
    Dougher M., Terman B.I.
    Oncogene 18:1619-1627(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY KDR.
  15. "Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1."
    Felschow D.M., Civin C.I., Hoehn G.T.
    Biochem. Biophys. Res. Commun. 273:294-301(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNK1.
  16. "The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK."
    Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.
    J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
  17. "Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
    Rebhun J.F., Chen H., Quilliam L.A.
    J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALGPS1.
  18. "Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
    Baker J.E., Majeti R., Tangye S.G., Weiss A.
    Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
  19. Cited for: PHOSPHORYLATION AT TYR-783, SUBCELLULAR LOCATION.
  20. "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
    Lin J., Weiss A.
    J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE DEPHOSPHORYLATION BY PTPRJ.
  21. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. Cited for: INTERACTION WITH NTRK1.
  23. "Signal transduction via the stem cell factor receptor/c-Kit."
    Ronnstrand L.
    Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
  24. "Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx induced by the pre-B-cell receptor in human pre-B cells."
    Taguchi T., Kiyokawa N., Takenouch H., Matsui J., Tang W.-R., Nakajima H., Suzuki K., Shiozawa Y., Saito M., Katagiri Y.U., Takahashi T., Karasuyama H., Matsuo Y., Okita H., Fujimoto J.
    Immunology 112:575-582(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLNK; VAV1; GRB2 AND NCK1.
  25. "Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
    Wang J.F., Zhang X., Groopman J.E.
    J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT4.
  26. "Vascular endothelial growth factor (VEGF)-D and VEGF-A differentially regulate KDR-mediated signaling and biological function in vascular endothelial cells."
    Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.
    J. Biol. Chem. 279:36148-36157(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-783 IN RESPONSE TO KDR ACTIVATION.
  27. "Early phosphorylation kinetics of proteins involved in proximal TCR-mediated signaling pathways."
    Houtman J.C., Houghtling R.A., Barda-Saad M., Toda Y., Samelson L.E.
    J. Immunol. 175:2449-2458(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY ITK.
  28. "Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F."
    Hatch N.E., Hudson M., Seto M.L., Cunningham M.L., Bothwell M.
    J. Biol. Chem. 281:27292-27305(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR2, PHOSPHORYLATION.
  29. "Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration."
    Wang Y., Tomar A., George S.P., Khurana S.
    Am. J. Physiol. 292:C1775-C1786(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VIL1, SUBCELLULAR LOCATION.
  30. "Sustained phosphorylation of mutated FGFR3 is a crucial feature of genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell line via PLCgamma-activated STAT1."
    Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y., Tanaka H.
    Bone 41:273-281(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY FGFR3.
  31. "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation."
    Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H.
    J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRB.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  34. "A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells."
    Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D., Wilcox W.R., Thompson L.M.
    Hum. Mol. Genet. 18:1951-1961(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR3.
  35. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771; TYR-775; TYR-783 AND SER-1221, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  36. "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
    Wardega P., Heldin C.H., Lennartsson J.
    Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRB, PHOSPHORYLATION AT TYR-771.
  37. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221 AND TYR-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function."
    Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D.
    EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR1, PHOSPHORYLATION BY FGFR1.
  40. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "Tespa1 is involved in late thymocyte development through the regulation of TCR-mediated signaling."
    Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C., Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.
    Nat. Immunol. 13:560-568(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TESPA1.
    Tissue: Thymocyte.
  42. "Cellular signaling by fibroblast growth factor receptors."
    Eswarakumar V.P., Lax I., Schlessinger J.
    Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN FGF-ACTIVATED SIGNALING PATHWAYS.
  43. "Solution structure of the SH3 domain of phospholipase C-gamma."
    Kohda D., Hatanaka H., Odaka M., Mandiyan V., Ullrich A., Schlessinger J., Inagaki F.
    Cell 72:953-960(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.

Entry informationi

Entry nameiPLCG1_HUMAN
AccessioniPrimary (citable) accession number: P19174
Secondary accession number(s): B7ZLY7
, B9EGH4, E1P5W4, Q2V575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 190 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

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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