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Q9P212

- PLCE1_HUMAN

UniProt

Q9P212 - PLCE1_HUMAN

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Protein

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

Gene

PLCE1

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. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation.7 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.2 Publications

Cofactori

Calcium.1 Publication

Enzyme regulationi

Activated by the heterotrimeric G-protein subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by G(i)-coupled GPCRs.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1407 – 14071PROSITE-ProRule annotation
Active sitei1452 – 14521PROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. enzyme binding Source: UniProtKB
  3. guanyl-nucleotide exchange factor activity Source: UniProtKB
  4. phosphatidylinositol phospholipase C activity Source: UniProtKB
  5. phospholipase C activity Source: UniProtKB
  6. Ras GTPase binding Source: UniProtKB
  7. receptor signaling protein activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: UniProtKB
  2. calcium-mediated signaling Source: UniProtKB
  3. cell proliferation Source: UniProtKB
  4. cytoskeleton organization Source: UniProtKB
  5. diacylglycerol biosynthetic process Source: UniProtKB
  6. epidermal growth factor receptor signaling pathway Source: UniProtKB
  7. glomerulus development Source: HGNC
  8. heart development Source: UniProtKB
  9. inositol phosphate-mediated signaling Source: UniProtKB
  10. inositol phosphate metabolic process Source: Reactome
  11. lipid catabolic process Source: UniProtKB-KW
  12. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  13. phospholipid metabolic process Source: UniProtKB
  14. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  15. positive regulation of GTPase activity Source: GOC
  16. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  17. Ras protein signal transduction Source: UniProtKB
  18. regulation of cell growth Source: UniProtKB
  19. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  20. regulation of protein kinase activity Source: UniProtKB
  21. regulation of Ras protein signal transduction Source: UniProtKB
  22. regulation of smooth muscle contraction Source: UniProtKB
  23. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor, Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS06473-MONOMER.
ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 (EC:3.1.4.11)
Alternative name(s):
Pancreas-enriched phospholipase C
Phosphoinositide phospholipase C-epsilon-1
Phospholipase C-epsilon-1
Short name:
PLC-epsilon-1
Gene namesi
Name:PLCE1
Synonyms:KIAA1516, PLCE, PPLC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17175. PLCE1.

Subcellular locationi

Cytoplasmcytosol. Cell membrane. Golgi apparatus membrane
Note: Recruited to plasma membrane by activated HRAS and RAP2. Recruited to perinuclear membrane by activated RAP1A. Isoform 1 and isoform 2 associates with Golgi membranes.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. Golgi apparatus Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Nephrotic syndrome 3 (NPHS3) [MIM:610725]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. Most patients with NPHS3 show diffuse mesangial sclerosis on renal biopsy, which is a pathologic entity characterized by mesangial matrix expansion with no mesangial hypercellularity, hypertrophy of the podocytes, vacuolized podocytes, thickened basement membranes, and diminished patency of the capillary lumen.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1484 – 14841S → L in NPHS3; gives rise to focal segmental glomerulosclerosis rather than diffuse mesangial sclerosis. 1 Publication
VAR_029883

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1452 – 14521H → L: Loss of the phospholipase C enzymatic activity. Still activates HRAS and the MAP kinase pathway. 1 Publication
Mutagenesisi2140 – 21401Q → E: Increases 2.8-fold the affinity for HRAS. 1 Publication
Mutagenesisi2148 – 21481Q → E: Decreases 17.5-fold the affinity for HRAS. 1 Publication
Mutagenesisi2148 – 21481Q → K: Increases 1.4-fold the affinity for HRAS. 1 Publication
Mutagenesisi2150 – 21501R → L: Abolishes interaction with HRAS. 1 Publication
Mutagenesisi2171 – 21711K → L: No effect on HRAS-binding. 1 Publication
Mutagenesisi2174 – 21741Y → L: Reduces HRAS-binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610725. phenotype.
Orphaneti93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA33391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230223021-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1PRO_0000256238Add
BLAST

Proteomic databases

MaxQBiQ9P212.
PaxDbiQ9P212.
PRIDEiQ9P212.

PTM databases

PhosphoSiteiQ9P212.

Expressioni

Tissue specificityi

Widely expressed. Isoform 1 is broadly expressed and only absent in peripheral blood leukocytes. Isoform 2 is specifically expressed in placenta, lung and spleen.3 Publications

Inductioni

Overexpressed during heart failure.1 Publication

Gene expression databases

BgeeiQ9P212.
ExpressionAtlasiQ9P212. baseline and differential.
GenevestigatoriQ9P212.

Organism-specific databases

HPAiHPA015597.
HPA015598.

Interactioni

Subunit structurei

Interacts with RHOA (By similarity). Interacts with IQGAP1, HRAS, RAP1A, RAP2A, RAP2B and RRAS.By similarity5 Publications

Protein-protein interaction databases

BioGridi119370. 5 interactions.
IntActiQ9P212. 3 interactions.
MINTiMINT-1420367.

Structurei

Secondary structure

1
2302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2015 – 20206Combined sources
Beta strandi2022 – 203110Combined sources
Helixi2038 – 20469Combined sources
Beta strandi2049 – 20524Combined sources
Beta strandi2058 – 20647Combined sources
Beta strandi2069 – 20724Combined sources
Beta strandi2081 – 20844Combined sources
Beta strandi2086 – 20883Combined sources
Helixi2090 – 20967Combined sources
Turni2099 – 21035Combined sources
Beta strandi2107 – 21126Combined sources
Beta strandi2136 – 21438Combined sources
Beta strandi2150 – 21567Combined sources
Helixi2161 – 217111Combined sources
Turni2172 – 21743Combined sources
Helixi2176 – 21805Combined sources
Helixi2184 – 21863Combined sources
Beta strandi2187 – 21948Combined sources
Beta strandi2198 – 22047Combined sources
Beta strandi2207 – 22115Combined sources
Helixi2218 – 22236Combined sources
Beta strandi2229 – 22357Combined sources
Turni2236 – 22383Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BYENMR-A2006-2114[»]
2BYFNMR-A2131-2246[»]
2C5LX-ray1.90C/D2131-2246[»]
ProteinModelPortaliQ9P212.
SMRiQ9P212. Positions 600-742, 1362-1542, 1663-1983, 2006-2114, 2131-2246.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P212.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini531 – 790260Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini1392 – 1540149PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1730 – 1846117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1856 – 1956101C2PROSITE-ProRule annotationAdd
BLAST
Domaini2012 – 2114103Ras-associating 1PROSITE-ProRule annotationAdd
BLAST
Domaini2135 – 2238104Ras-associating 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1686 – 176479Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gammaBy similarityAdd
BLAST

Domaini

The Ras-associating domain 1 is degenerated and may not bind HRAS. The Ras-associating domain 2 mediates interaction with GTP-bound HRAS, RAP1A, RAP2A and RAP2B and recruitment of HRAS to the cell membrane.
The Ras-GEF domain has a GEF activity towards HRAS and RAP1A. Mediates activation of the mitogen-activated protein kinase pathway.

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
Contains 2 Ras-associating domains.PROSITE-ProRule annotation
Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00730000110782.
HOVERGENiHBG059220.
InParanoidiQ9P212.
KOiK05860.
OMAiVAKCCWN.
OrthoDBiEOG7SN8CX.
PhylomeDBiQ9P212.
TreeFamiTF314432.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.840.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 3 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR028398. PLC-epsilon1.
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.
IPR000159. Ras-assoc.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF6. PTHR10336:SF6. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 3 hits.
SSF54236. SSF54236. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9P212-1) [UniParc]FASTAAdd to Basket

Also known as: PLCepsilon1a

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
MTSEEMTASV LIPVTQRKVV SAQSAADESS EKVSDINISK AHTVRRSGET
60 70 80 90 100
SHTISQLNKL KEEPSGSNLP KILSIAREKI VSDENSNEKC WEKIMPDSAK
110 120 130 140 150
NLNINCNNIL RNHQHGLPQR QFYEMYNSVA EEDLCLETGI PSPLERKVFP
160 170 180 190 200
GIQLELDRPS MGISPLGNQS VIIETGRAHP DSRRAVFHFH YEVDRRMSDT
210 220 230 240 250
FCTLSENLIL DDCGNCVPLP GGEEKQKKNY VAYTCKLMEL AKNCDNKNEQ
260 270 280 290 300
LQCDHCDTLN DKYFCFEGSC EKVDMVYSGD SFCRKDFTDS QAAKTFLSHF
310 320 330 340 350
EDFPDNCDDV EEDAFKSKKE RSTLLVRRFC KNDREVKKSV YTGTRAIVRT
360 370 380 390 400
LPSGHIGLTA WSYIDQKRNG PLLPCGRVME PPSTVEIRQD GSQRLSEAQW
410 420 430 440 450
YPIYNAVRRE ETENTVGSLL HFLTKLPASE TAHGRISVGP CLKQCVRDTV
460 470 480 490 500
CEYRATLQRT SISQYITGSL LEATTSLGAR SGLLSTFGGS TGRMMLKERQ
510 520 530 540 550
PGPSVANSNA LPSSSAGISK ELIDLQPLIQ FPEEVASILM EQEQTIYRRV
560 570 580 590 600
LPVDYLCFLT RDLGTPECQS SLPCLKASIS ASILTTQNGE HNALEDLVMR
610 620 630 640 650
FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG
660 670 680 690 700
LRSRKVLKMW QFMDQSDIET MRSLKDAMAQ HESSCEYRKV VTRALHIPGC
710 720 730 740 750
KVVPFCGVFL KELCEVLDGA SGLMKLCPRY NSQEETLEFV ADYSGQDNFL
760 770 780 790 800
QRVGQNGLKN SEKESTVNSI FQVIRSCNRS LETDEEDSPS EGNSSRKSSL
810 820 830 840 850
KDKSRWQFII GDLLDSDNDI FEQSKEYDSH GSEDSQKAFD HGTELIPWYV
860 870 880 890 900
LSIQADVHQF LLQGATVIHY DQDTHLSARC FLQLQPDNST LTWVKPTTAS
910 920 930 940 950
PASSKAKLGV LNNTAEPGKF PLLGNAGLSS LTEGVLDLFA VKAVYMGHPG
960 970 980 990 1000
IDIHTVCVQN KLGSMFLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMLFS
1010 1020 1030 1040 1050
GLLELTRAVR KMRKFPDQRQ QWLRKQYVSL YQEDGRYEGP TLAHAVELFG
1060 1070 1080 1090 1100
GRRWSARNPS PGTSAKNAEK PNMQRNNTLG ISTTKKKKKI LMRGESGEVT
1110 1120 1130 1140 1150
DDEMATRKAK MHKECRSRSG SDPQDINEQE ESEVNAIANP PNPLPSRRAH
1160 1170 1180 1190 1200
SLTTAGSPNL AAGTSSPIRP VSSPVLSSSN KSPSSAWSSS SWHGRIKGGM
1210 1220 1230 1240 1250
KGFQSFMVSD SNMSFVEFVE LFKSFSVRSR KDLKDLFDVY AVPCNRSGSE
1260 1270 1280 1290 1300
SAPLYTNLTI DENTSDLQPD LDLLTRNVSD LGLFIKSKQQ LSDNQRQISD
1310 1320 1330 1340 1350
AIAAASIVTN GTGIESTSLG IFGVGILQLN DFLVNCQGEH CTYDEILSII
1360 1370 1380 1390 1400
QKFEPSISMC HQGLMSFEGF ARFLMDKENF ASKNDESQEN IKELQLPLSY
1410 1420 1430 1440 1450
YYIESSHNTY LTGHQLKGES SVELYSQVLL QGCRSVELDC WDGDDGMPII
1460 1470 1480 1490 1500
YHGHTLTTKI PFKEVVEAID RSAFINSDLP IIISIENHCS LPQQRKMAEI
1510 1520 1530 1540 1550
FKTVFGEKLV TKFLFETDFS DDPMLPSPDQ LRKKVLLKNK KLKAHQTPVD
1560 1570 1580 1590 1600
ILKQKAHQLA SMQVQAYNGG NANPRPANNE EEEDEEDEYD YDYESLSDDN
1610 1620 1630 1640 1650
ILEDRPENKS CNDKLQFEYN EEIPKRIKKA DNSACNKGKV YDMELGEEFY
1660 1670 1680 1690 1700
LDQNKKESRQ IAPELSDLVI YCQAVKFPGL STLNASGSSR GKERKSRKSI
1710 1720 1730 1740 1750
FGNNPGRMSP GETASFNKTS GKSSCEGIRQ TWEESSSPLN PTTSLSAIIR
1760 1770 1780 1790 1800
TPKCYHISSL NENAAKRLCR RYSQKLTQHT ACQLLRTYPA ATRIDSSNPN
1810 1820 1830 1840 1850
PLMFWLHGIQ LVALNYQTDD LPLHLNAAMF EANGGCGYVL KPPVLWDKNC
1860 1870 1880 1890 1900
PMYQKFSPLE RDLDSMDPAV YSLTIVSGQN VCPSNSMGSP CIEVDVLGMP
1910 1920 1930 1940 1950
LDSCHFRTKP IHRNTLNPMW NEQFLFHVHF EDLVFLRFAV VENNSSAVTA
1960 1970 1980 1990 2000
QRIIPLKALK RGYRHLQLRN LHNEVLEISS LFINSRRMEE NSSGNTMSAS
2010 2020 2030 2040 2050
SMFNTEERKC LQTHRVTVHG VPGPEPFTVF TINGGTKAKQ LLQQILTNEQ
2060 2070 2080 2090 2100
DIKPVTTDYF LMEEKYFISK EKNECRKQPF QRAIGPEEEI MQILSSWFPE
2110 2120 2130 2140 2150
EGYMGRIVLK TQQENLEEKN IVQDDKEVIL SSEEESFFVQ VHDVSPEQPR
2160 2170 2180 2190 2200
TVIKAPRVST AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVVKDTTNK
2210 2220 2230 2240 2250
KTTTPKSSQR VLLDQECVFQ AQSKWKGAGK FILKLKEQVQ ASREDKKKGI
2260 2270 2280 2290 2300
SFASELKKLT KSTKQPRGLT SPSQLLTSES IQTKEEKPVG GLSSSDTMDY

RQ
Length:2,302
Mass (Da):258,715
Last modified:October 31, 2006 - v3
Checksum:i71DDE446277077A3
GO
Isoform 2 (identifier: Q9P212-2) [UniParc]FASTAAdd to Basket

Also known as: PLCepsilon1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-308: Missing.
     309-402: DVEEDAFKSK...QRLSEAQWYP → MVSEGSAAGR...CGCWRLKEDQ

Show »
Length:1,994
Mass (Da):223,872
Checksum:i069358CFA0D7A1CD
GO

Sequence cautioni

The sequence AAF22005.1 differs from that shown. Reason: Frameshift at position 1131.
The sequence AAG17145.2 differs from that shown. Reason: Frameshift at position 2296.
The sequence BAA96040.2 differs from that shown. Reason: Erroneous initiation.
The sequence BAB14090.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAH70739.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH73288.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH73757.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI16674.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti502 – 5021G → S in AAG28341. (PubMed:11022047)Curated
Sequence conflicti703 – 7031V → F in AAG28341. (PubMed:11022047)Curated
Sequence conflicti1133 – 11331E → K in AAG28341. (PubMed:11022047)Curated
Sequence conflicti1229 – 12302SR → QA in AAF22005. 1 PublicationCurated
Sequence conflicti1456 – 14561L → P in AAG17145. (PubMed:11022048)Curated
Sequence conflicti1571 – 15711N → D in BAB14090. (PubMed:14702039)Curated
Sequence conflicti1575 – 15751R → Q in AAG28341. (PubMed:11022047)Curated
Sequence conflicti1672 – 16721C → R in AAG17145. (PubMed:11022048)Curated
Sequence conflicti1705 – 17051P → L in BAB14090. (PubMed:14702039)Curated
Sequence conflicti2125 – 21251D → G in BAB14090. (PubMed:14702039)Curated
Isoform 2 (identifier: Q9P212-2)
Sequence conflicti69 – 691L → P in AAG28341. (PubMed:11022047)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti469 – 4691S → T.
Corresponds to variant rs17508082 [ dbSNP | Ensembl ].
VAR_031843
Natural varianti548 – 5481R → L.
Corresponds to variant rs17417407 [ dbSNP | Ensembl ].
VAR_031844
Natural varianti1484 – 14841S → L in NPHS3; gives rise to focal segmental glomerulosclerosis rather than diffuse mesangial sclerosis. 1 Publication
VAR_029883
Natural varianti1575 – 15751R → P.
Corresponds to variant rs2274224 [ dbSNP | Ensembl ].
VAR_031845
Natural varianti1777 – 17771T → I.2 Publications
Corresponds to variant rs3765524 [ dbSNP | Ensembl ].
VAR_031846
Natural varianti1927 – 19271H → R.4 Publications
Corresponds to variant rs2274223 [ dbSNP | Ensembl ].
VAR_031847

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 308308Missing in isoform 2. 2 PublicationsVSP_021335Add
BLAST
Alternative sequencei309 – 40294DVEED…AQWYP → MVSEGSAAGRDFAGMEEVRQ LHVRFCKGIKIWHQAWFLCS LLGREPQEREAGCQLWLCTL SAVLKVGWLFPLSEVPNFTL LKDGCGCWRLKEDQ in isoform 2. 2 PublicationsVSP_021336Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190642 mRNA. Translation: AAG17145.2. Frameshift.
AF170071 mRNA. Translation: AAG28341.1.
AB040949 mRNA. Translation: BAA96040.2. Different initiation.
AL139118
, AL139124, AL365510, AL389885 Genomic DNA. Translation: CAH70739.1. Sequence problems.
AL139118
, AL139124, AL365510, AL389885 Genomic DNA. Translation: CAH70740.1.
AL389885
, AL139118, AL139124, AL365510 Genomic DNA. Translation: CAH73288.1. Sequence problems.
AL389885
, AL139118, AL139124, AL365510 Genomic DNA. Translation: CAH73289.1.
AL365510
, AL139118, AL139124, AL389885 Genomic DNA. Translation: CAH73757.1. Sequence problems.
AL365510
, AL139118, AL139124, AL389885 Genomic DNA. Translation: CAH73758.1.
AL139124
, AL139118, AL365510, AL389885 Genomic DNA. Translation: CAI16674.1. Sequence problems.
AL139124
, AL139118, AL365510, AL389885 Genomic DNA. Translation: CAI16675.1.
CH471066 Genomic DNA. Translation: EAW50042.1.
CH471066 Genomic DNA. Translation: EAW50043.1.
BC140705 mRNA. Translation: AAI40706.1.
BC151854 mRNA. Translation: AAI51855.1.
AF117948 mRNA. Translation: AAF22005.1. Frameshift.
AK022543 mRNA. Translation: BAB14090.1. Different initiation.
AK289852 mRNA. Translation: BAF82541.1.
AY995135 mRNA. Translation: AAY45890.1.
CCDSiCCDS41552.1. [Q9P212-1]
CCDS53555.1. [Q9P212-2]
RefSeqiNP_001159451.1. NM_001165979.2. [Q9P212-2]
NP_001275918.1. NM_001288989.1.
NP_057425.3. NM_016341.3. [Q9P212-1]
UniGeneiHs.655033.

Genome annotation databases

EnsembliENST00000260766; ENSP00000260766; ENSG00000138193. [Q9P212-1]
ENST00000371375; ENSP00000360426; ENSG00000138193. [Q9P212-2]
ENST00000371380; ENSP00000360431; ENSG00000138193. [Q9P212-1]
ENST00000371385; ENSP00000360438; ENSG00000138193. [Q9P212-2]
GeneIDi51196.
KEGGihsa:51196.
UCSCiuc001kjk.3. human. [Q9P212-1]
uc001kjm.3. human. [Q9P212-2]

Polymorphism databases

DMDMi118595723.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190642 mRNA. Translation: AAG17145.2 . Frameshift.
AF170071 mRNA. Translation: AAG28341.1 .
AB040949 mRNA. Translation: BAA96040.2 . Different initiation.
AL139118
, AL139124 , AL365510 , AL389885 Genomic DNA. Translation: CAH70739.1 . Sequence problems.
AL139118
, AL139124 , AL365510 , AL389885 Genomic DNA. Translation: CAH70740.1 .
AL389885
, AL139118 , AL139124 , AL365510 Genomic DNA. Translation: CAH73288.1 . Sequence problems.
AL389885
, AL139118 , AL139124 , AL365510 Genomic DNA. Translation: CAH73289.1 .
AL365510
, AL139118 , AL139124 , AL389885 Genomic DNA. Translation: CAH73757.1 . Sequence problems.
AL365510
, AL139118 , AL139124 , AL389885 Genomic DNA. Translation: CAH73758.1 .
AL139124
, AL139118 , AL365510 , AL389885 Genomic DNA. Translation: CAI16674.1 . Sequence problems.
AL139124
, AL139118 , AL365510 , AL389885 Genomic DNA. Translation: CAI16675.1 .
CH471066 Genomic DNA. Translation: EAW50042.1 .
CH471066 Genomic DNA. Translation: EAW50043.1 .
BC140705 mRNA. Translation: AAI40706.1 .
BC151854 mRNA. Translation: AAI51855.1 .
AF117948 mRNA. Translation: AAF22005.1 . Frameshift.
AK022543 mRNA. Translation: BAB14090.1 . Different initiation.
AK289852 mRNA. Translation: BAF82541.1 .
AY995135 mRNA. Translation: AAY45890.1 .
CCDSi CCDS41552.1. [Q9P212-1 ]
CCDS53555.1. [Q9P212-2 ]
RefSeqi NP_001159451.1. NM_001165979.2. [Q9P212-2 ]
NP_001275918.1. NM_001288989.1.
NP_057425.3. NM_016341.3. [Q9P212-1 ]
UniGenei Hs.655033.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BYE NMR - A 2006-2114 [» ]
2BYF NMR - A 2131-2246 [» ]
2C5L X-ray 1.90 C/D 2131-2246 [» ]
ProteinModelPortali Q9P212.
SMRi Q9P212. Positions 600-742, 1362-1542, 1663-1983, 2006-2114, 2131-2246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119370. 5 interactions.
IntActi Q9P212. 3 interactions.
MINTi MINT-1420367.

PTM databases

PhosphoSitei Q9P212.

Polymorphism databases

DMDMi 118595723.

Proteomic databases

MaxQBi Q9P212.
PaxDbi Q9P212.
PRIDEi Q9P212.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260766 ; ENSP00000260766 ; ENSG00000138193 . [Q9P212-1 ]
ENST00000371375 ; ENSP00000360426 ; ENSG00000138193 . [Q9P212-2 ]
ENST00000371380 ; ENSP00000360431 ; ENSG00000138193 . [Q9P212-1 ]
ENST00000371385 ; ENSP00000360438 ; ENSG00000138193 . [Q9P212-2 ]
GeneIDi 51196.
KEGGi hsa:51196.
UCSCi uc001kjk.3. human. [Q9P212-1 ]
uc001kjm.3. human. [Q9P212-2 ]

Organism-specific databases

CTDi 51196.
GeneCardsi GC10P095753.
H-InvDB HIX0009051.
HIX0035415.
HGNCi HGNC:17175. PLCE1.
HPAi HPA015597.
HPA015598.
MIMi 608414. gene.
610725. phenotype.
neXtProti NX_Q9P212.
Orphaneti 93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBi PA33391.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00730000110782.
HOVERGENi HBG059220.
InParanoidi Q9P212.
KOi K05860.
OMAi VAKCCWN.
OrthoDBi EOG7SN8CX.
PhylomeDBi Q9P212.
TreeFami TF314432.

Enzyme and pathway databases

BioCyci MetaCyc:HS06473-MONOMER.
Reactomei REACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

ChiTaRSi PLCE1. human.
EvolutionaryTracei Q9P212.
GeneWikii PLCE1.
GenomeRNAii 51196.
NextBioi 54210.
PROi Q9P212.
SOURCEi Search...

Gene expression databases

Bgeei Q9P212.
ExpressionAtlasi Q9P212. baseline and differential.
Genevestigatori Q9P212.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.840.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 3 hits.
InterProi IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR028398. PLC-epsilon1.
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.
IPR000159. Ras-assoc.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF6. PTHR10336:SF6. 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.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
[Graphical view ]
PRINTSi PR00390. PHPHLIPASEC.
SMARTi SM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48366. SSF48366. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 3 hits.
SSF54236. SSF54236. 2 hits.
PROSITEi PS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras."
    Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y., Shibatohge M., Wu D., Satoh T., Kataoka T.
    J. Biol. Chem. 276:2752-2757(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH HRAS AND RAP1A, SUBCELLULAR LOCATION, ENZYME REGULATION, VARIANTS ILE-1777 AND ARG-1927.
    Tissue: Fetal brain.
  2. "A novel bifunctional phospholipase C that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway."
    Lopez I., Mak E.C., Ding J., Hamm H.E., Lomasney J.W.
    J. Biol. Chem. 276:2758-2765(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF HIS-1452.
    Tissue: Heart.
  3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-1927.
    Tissue: Brain.
  4. Ohara O., Nagase T., Kikuno R.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [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] (ISOFORM 1), VARIANT ARG-1927.
    Tissue: Brain.
  8. "A novel phospholipase C enriched in pancreas."
    Kawasaki H., Chen E.J., Springett G.M., Graybiel A.M., Housman D.E.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1098-2302 (ISOFORMS 1/2), VARIANTS ILE-1777 AND ARG-1927.
    Tissue: Pancreas.
  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 1-1383 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1475-2302 (ISOFORMS 1/2).
    Tissue: Brain and Teratocarcinoma.
  10. "Sequence of cDNA clone MPMGp800D13530."
    Buessow K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2302 (ISOFORMS 1/2).
    Tissue: Brain.
  11. "Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling."
    Jin T.-G., Satoh T., Liao Y., Song C., Gao X., Kariya K., Hu C.-D., Kataoka T.
    J. Biol. Chem. 276:30301-30307(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "A new phospholipase-C-calcium signalling pathway mediated by cyclic AMP and a Rap GTPase."
    Schmidt M., Evellin S., Weernink P.A.O., von Dorp F., Rehmann H., Lomasney J.W., Jakobs K.H.
    Nat. Cell Biol. 3:1020-1024(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  13. "Stimulation of phospholipase C-epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B."
    Evellin S., Nolte J., Tysack K., vom Dorp F., Thiel M., Weernink P.A.O., Jakobs K.H., Webb E.J., Lomasney J.W., Schmidt M.
    J. Biol. Chem. 277:16805-16813(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  14. "Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon."
    Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.
    Oncogene 21:8105-8113(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAP1A; RAP2A AND RAP2B.
  15. Cited for: FUNCTION.
  16. Cited for: ENZYME REGULATION.
  17. "Phospholipase C epsilon modulates beta-adrenergic receptor-dependent cardiac contraction and inhibits cardiac hypertrophy."
    Wang H., Oestreich E.A., Maekawa N., Bullard T.A., Vikstrom K.L., Dirksen R.T., Kelley G.G., Blaxall B.C., Smrcka A.V.
    Circ. Res. 97:1305-1313(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  18. "Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants."
    Sorli S.C., Bunney T.D., Sugden P.H., Paterson H.F., Katan M.
    Oncogene 24:90-100(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  19. "The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon."
    Ada-Nguema A.S., Xenias H., Sheetz M.P., Keely P.J.
    J. Cell Sci. 119:1307-1319(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RRAS, ENZYME REGULATION.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2131-2246 OF MUTANT LEU-2176 IN COMPLEX WITH HRAS, STRUCTURE BY NMR OF 2006-2114 AND 2131-2246, MUTAGENESIS OF GLN-2140; GLN-2148; ARG-2150; LYS-2171 AND TYR-2174.
  21. Cited for: VARIANT NPHS3 LEU-1484, FUNCTION, INTERACTION WITH IQGAP1.

Entry informationi

Entry nameiPLCE1_HUMAN
AccessioniPrimary (citable) accession number: Q9P212
Secondary accession number(s): A6NGW0
, A6NLA1, A7MBN7, A8K1D7, B9EIJ6, Q1X6H8, Q5VWL4, Q5VWL5, Q9H9X8, Q9HBX6, Q9HC53, Q9UHV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: October 29, 2014
This is version 128 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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