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Q9P212

- PLCE1_HUMAN

UniProt

Q9P212 - PLCE1_HUMAN

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
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (31 Oct 2006)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    7. Ras GTPase binding Source: UniProtKB
    8. 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

    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 membrane Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB

    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

    ArrayExpressiQ9P212.
    BgeeiQ9P212.
    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 – 20206
    Beta strandi2022 – 203110
    Helixi2038 – 20469
    Beta strandi2049 – 20524
    Beta strandi2058 – 20647
    Beta strandi2069 – 20724
    Beta strandi2081 – 20844
    Beta strandi2086 – 20883
    Helixi2090 – 20967
    Turni2099 – 21035
    Beta strandi2107 – 21126
    Beta strandi2136 – 21438
    Beta strandi2150 – 21567
    Helixi2161 – 217111
    Turni2172 – 21743
    Helixi2176 – 21805
    Helixi2184 – 21863
    Beta strandi2187 – 21948
    Beta strandi2198 – 22047
    Beta strandi2207 – 22115
    Helixi2218 – 22236
    Beta strandi2229 – 22357
    Turni2236 – 22383

    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.
    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. RasGRF_CDC25.
    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

    MTSEEMTASV LIPVTQRKVV SAQSAADESS EKVSDINISK AHTVRRSGET     50
    SHTISQLNKL KEEPSGSNLP KILSIAREKI VSDENSNEKC WEKIMPDSAK 100
    NLNINCNNIL RNHQHGLPQR QFYEMYNSVA EEDLCLETGI PSPLERKVFP 150
    GIQLELDRPS MGISPLGNQS VIIETGRAHP DSRRAVFHFH YEVDRRMSDT 200
    FCTLSENLIL DDCGNCVPLP GGEEKQKKNY VAYTCKLMEL AKNCDNKNEQ 250
    LQCDHCDTLN DKYFCFEGSC EKVDMVYSGD SFCRKDFTDS QAAKTFLSHF 300
    EDFPDNCDDV EEDAFKSKKE RSTLLVRRFC KNDREVKKSV YTGTRAIVRT 350
    LPSGHIGLTA WSYIDQKRNG PLLPCGRVME PPSTVEIRQD GSQRLSEAQW 400
    YPIYNAVRRE ETENTVGSLL HFLTKLPASE TAHGRISVGP CLKQCVRDTV 450
    CEYRATLQRT SISQYITGSL LEATTSLGAR SGLLSTFGGS TGRMMLKERQ 500
    PGPSVANSNA LPSSSAGISK ELIDLQPLIQ FPEEVASILM EQEQTIYRRV 550
    LPVDYLCFLT RDLGTPECQS SLPCLKASIS ASILTTQNGE HNALEDLVMR 600
    FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG 650
    LRSRKVLKMW QFMDQSDIET MRSLKDAMAQ HESSCEYRKV VTRALHIPGC 700
    KVVPFCGVFL KELCEVLDGA SGLMKLCPRY NSQEETLEFV ADYSGQDNFL 750
    QRVGQNGLKN SEKESTVNSI FQVIRSCNRS LETDEEDSPS EGNSSRKSSL 800
    KDKSRWQFII GDLLDSDNDI FEQSKEYDSH GSEDSQKAFD HGTELIPWYV 850
    LSIQADVHQF LLQGATVIHY DQDTHLSARC FLQLQPDNST LTWVKPTTAS 900
    PASSKAKLGV LNNTAEPGKF PLLGNAGLSS LTEGVLDLFA VKAVYMGHPG 950
    IDIHTVCVQN KLGSMFLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMLFS 1000
    GLLELTRAVR KMRKFPDQRQ QWLRKQYVSL YQEDGRYEGP TLAHAVELFG 1050
    GRRWSARNPS PGTSAKNAEK PNMQRNNTLG ISTTKKKKKI LMRGESGEVT 1100
    DDEMATRKAK MHKECRSRSG SDPQDINEQE ESEVNAIANP PNPLPSRRAH 1150
    SLTTAGSPNL AAGTSSPIRP VSSPVLSSSN KSPSSAWSSS SWHGRIKGGM 1200
    KGFQSFMVSD SNMSFVEFVE LFKSFSVRSR KDLKDLFDVY AVPCNRSGSE 1250
    SAPLYTNLTI DENTSDLQPD LDLLTRNVSD LGLFIKSKQQ LSDNQRQISD 1300
    AIAAASIVTN GTGIESTSLG IFGVGILQLN DFLVNCQGEH CTYDEILSII 1350
    QKFEPSISMC HQGLMSFEGF ARFLMDKENF ASKNDESQEN IKELQLPLSY 1400
    YYIESSHNTY LTGHQLKGES SVELYSQVLL QGCRSVELDC WDGDDGMPII 1450
    YHGHTLTTKI PFKEVVEAID RSAFINSDLP IIISIENHCS LPQQRKMAEI 1500
    FKTVFGEKLV TKFLFETDFS DDPMLPSPDQ LRKKVLLKNK KLKAHQTPVD 1550
    ILKQKAHQLA SMQVQAYNGG NANPRPANNE EEEDEEDEYD YDYESLSDDN 1600
    ILEDRPENKS CNDKLQFEYN EEIPKRIKKA DNSACNKGKV YDMELGEEFY 1650
    LDQNKKESRQ IAPELSDLVI YCQAVKFPGL STLNASGSSR GKERKSRKSI 1700
    FGNNPGRMSP GETASFNKTS GKSSCEGIRQ TWEESSSPLN PTTSLSAIIR 1750
    TPKCYHISSL NENAAKRLCR RYSQKLTQHT ACQLLRTYPA ATRIDSSNPN 1800
    PLMFWLHGIQ LVALNYQTDD LPLHLNAAMF EANGGCGYVL KPPVLWDKNC 1850
    PMYQKFSPLE RDLDSMDPAV YSLTIVSGQN VCPSNSMGSP CIEVDVLGMP 1900
    LDSCHFRTKP IHRNTLNPMW NEQFLFHVHF EDLVFLRFAV VENNSSAVTA 1950
    QRIIPLKALK RGYRHLQLRN LHNEVLEISS LFINSRRMEE NSSGNTMSAS 2000
    SMFNTEERKC LQTHRVTVHG VPGPEPFTVF TINGGTKAKQ LLQQILTNEQ 2050
    DIKPVTTDYF LMEEKYFISK EKNECRKQPF QRAIGPEEEI MQILSSWFPE 2100
    EGYMGRIVLK TQQENLEEKN IVQDDKEVIL SSEEESFFVQ VHDVSPEQPR 2150
    TVIKAPRVST AQDVIQQTLC KAKYSYSILS NPNPSDYVLL EEVVKDTTNK 2200
    KTTTPKSSQR VLLDQECVFQ AQSKWKGAGK FILKLKEQVQ ASREDKKKGI 2250
    SFASELKKLT KSTKQPRGLT SPSQLLTSES IQTKEEKPVG GLSSSDTMDY 2300
    RQ 2302
    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.
    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

    ArrayExpressi Q9P212.
    Bgeei Q9P212.
    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. RasGRF_CDC25.
    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

    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 1, 2014
    This is version 127 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