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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3

Gene

PLCD3

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

Functioni

Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca2+ from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.

Catalytic activityi

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

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca(2+) ions per subunit. Two of the Ca2+ ions are bound to the C2 domain.1 Publication

Enzyme regulationi

Strongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer).2 Publications

Kineticsi

  1. KM=105.3 µM for PIP21 Publication
  1. Vmax=28.5 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei352 – 3521PROSITE-ProRule annotation
Metal bindingi353 – 3531Calcium 1; catalyticBy similarity
Metal bindingi382 – 3821Calcium 1; catalyticBy similarity
Metal bindingi384 – 3841Calcium 1; catalyticBy similarity
Active sitei397 – 3971PROSITE-ProRule annotation
Metal bindingi431 – 4311Calcium 1; catalyticBy similarity
Binding sitei480 – 4801SubstrateBy similarity
Binding sitei482 – 4821SubstrateBy similarity
Binding sitei557 – 5571SubstrateBy similarity
Binding sitei584 – 5841SubstrateBy similarity
Metal bindingi683 – 6831Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi685 – 6851Calcium 2By similarity
Metal bindingi709 – 7091Calcium 2By similarity
Metal bindingi738 – 7381Calcium 3By similarity
Metal bindingi739 – 7391Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi740 – 7401Calcium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi195 – 206121Sequence AnalysisAdd
BLAST
Calcium bindingi231 – 242122Sequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-delta-3
Phospholipase C-delta-3
Short name:
PLC-delta-3
Gene namesi
Name:PLCD3
Synonyms:KIAA1964
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9061. PLCD3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33389.

Polymorphism and mutation databases

BioMutaiPLCD3.
DMDMi158706388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7897891-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3PRO_0000306821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Phosphoserine1 Publication
Modified residuei496 – 4961PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8N3E9.
PaxDbiQ8N3E9.
PeptideAtlasiQ8N3E9.
PRIDEiQ8N3E9.

Expressioni

Tissue specificityi

Present in corneal epithelial cells (at protein level).1 Publication

Inductioni

Down-regulated by Ca2+ and cAMP.1 Publication

Gene expression databases

BgeeiQ8N3E9.
CleanExiHS_PLCD3.
ExpressionAtlasiQ8N3E9. baseline and differential.
GenevisibleiQ8N3E9. HS.

Organism-specific databases

HPAiHPA025711.

Interactioni

Protein-protein interaction databases

BioGridi125222. 8 interactions.
IntActiQ8N3E9. 1 interaction.
MINTiMINT-1193970.
STRINGi9606.ENSP00000313731.

Structurei

3D structure databases

ProteinModelPortaliQ8N3E9.
SMRiQ8N3E9. Positions 55-787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 172110PHAdd
BLAST
Domaini182 – 21736EF-hand 1Add
BLAST
Domaini218 – 25336EF-hand 2Add
BLAST
Domaini250 – 28536EF-hand 3Add
BLAST
Domaini337 – 482146PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini528 – 644117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini647 – 752106C2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 10129Substrate bindingBy similarityAdd
BLAST

Domaini

The C2 domain is a Ca2+-dependent membrane-targeting module.
The PH domain mediates interaction with the surface membrane by binding to PIP2.

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 3 EF-hand domains.Curated
Contains 1 PH domain.Curated
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8N3E9.
KOiK05857.
OMAiVVYCHAT.
OrthoDBiEOG7V49XT.
PhylomeDBiQ8N3E9.
TreeFamiTF313216.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N3E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCGRWRRCR RPPEEPPVAA QVAAQVAAPV ALPSPPTPSD GGTKRPGLRA
60 70 80 90 100
LKKMGLTEDE DVRAMLRGSR LRKIRSRTWH KERLYRLQED GLSVWFQRRI
110 120 130 140 150
PRAPSQHIFF VQHIEAVREG HQSEGLRRFG GAFAPARCLT IAFKGRRKNL
160 170 180 190 200
DLAAPTAEEA QRWVRGLTKL RARLDAMSQR ERLDHWIHSY LHRADSNQDS
210 220 230 240 250
KMSFKEIKSL LRMVNVDMND MYAYLLFKEC DHSNNDRLEG AEIEEFLRRL
260 270 280 290 300
LKRPELEEIF HQYSGEDRVL SAPELLEFLE DQGEEGATLA RAQQLIQTYE
310 320 330 340 350
LNETAKQHEL MTLDGFMMYL LSPEGAALDN THTCVFQDMN QPLAHYFISS
360 370 380 390 400
SHNTYLTDSQ IGGPSSTEAY VRAFAQGCRC VELDCWEGPG GEPVIYHGHT
410 420 430 440 450
LTSKILFRDV VQAVRDHAFT LSPYPVILSL ENHCGLEQQA AMARHLCTIL
460 470 480 490 500
GDMLVTQALD SPNPEELPSP EQLKGRVLVK GKKLPAARSE DGRALSDREE
510 520 530 540 550
EEEDDEEEEE EVEAAAQRRL AKQISPELSA LAVYCHATRL RTLHPAPNAP
560 570 580 590 600
QPCQVSSLSE RKAKKLIREA GNSFVRHNAR QLTRVYPLGL RMNSANYSPQ
610 620 630 640 650
EMWNSGCQLV ALNFQTPGYE MDLNAGRFLV NGQCGYVLKP ACLRQPDSTF
660 670 680 690 700
DPEYPGPPRT TLSIQVLTAQ QLPKLNAEKP HSIVDPLVRI EIHGVPADCA
710 720 730 740 750
RQETDYVLNN GFNPRWGQTL QFQLRAPELA LVRFVVEDYD ATSPNDFVGQ
760 770 780
FTLPLSSLKQ GYRHIHLLSK DGASLSPATL FIQIRIQRS
Length:789
Mass (Da):89,258
Last modified:October 2, 2007 - v3
Checksum:iC6901404D2C9D070
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071I → T in CAD39054 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti652 – 6521P → L.
Corresponds to variant rs734921 [ dbSNP | Ensembl ].
VAR_035316

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074240 mRNA. Translation: BAB85029.1.
BC010668 mRNA. Translation: AAH10668.2.
BC072384 mRNA. Translation: AAH72384.1.
AL834392 mRNA. Translation: CAD39054.2.
AB075844 mRNA. Translation: BAB85550.1.
CCDSiCCDS74077.1.
RefSeqiNP_588614.1. NM_133373.4.
UniGeneiHs.380094.

Genome annotation databases

EnsembliENST00000619929; ENSP00000479636; ENSG00000161714.
GeneIDi113026.
KEGGihsa:113026.
UCSCiuc002iib.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK074240 mRNA. Translation: BAB85029.1.
BC010668 mRNA. Translation: AAH10668.2.
BC072384 mRNA. Translation: AAH72384.1.
AL834392 mRNA. Translation: CAD39054.2.
AB075844 mRNA. Translation: BAB85550.1.
CCDSiCCDS74077.1.
RefSeqiNP_588614.1. NM_133373.4.
UniGeneiHs.380094.

3D structure databases

ProteinModelPortaliQ8N3E9.
SMRiQ8N3E9. Positions 55-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125222. 8 interactions.
IntActiQ8N3E9. 1 interaction.
MINTiMINT-1193970.
STRINGi9606.ENSP00000313731.

Polymorphism and mutation databases

BioMutaiPLCD3.
DMDMi158706388.

Proteomic databases

MaxQBiQ8N3E9.
PaxDbiQ8N3E9.
PeptideAtlasiQ8N3E9.
PRIDEiQ8N3E9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619929; ENSP00000479636; ENSG00000161714.
GeneIDi113026.
KEGGihsa:113026.
UCSCiuc002iib.3. human.

Organism-specific databases

CTDi113026.
GeneCardsiGC17M043186.
HGNCiHGNC:9061. PLCD3.
HPAiHPA025711.
MIMi608795. gene.
neXtProtiNX_Q8N3E9.
PharmGKBiPA33389.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149692.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8N3E9.
KOiK05857.
OMAiVVYCHAT.
OrthoDBiEOG7V49XT.
PhylomeDBiQ8N3E9.
TreeFamiTF313216.

Enzyme and pathway databases

ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

ChiTaRSiPLCD3. human.
GeneWikiiPLCD3.
GenomeRNAii113026.
NextBioi78735.
PROiQ8N3E9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N3E9.
CleanExiHS_PLCD3.
ExpressionAtlasiQ8N3E9. baseline and differential.
GenevisibleiQ8N3E9. HS.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR028406. PLC-delta3.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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].
    Tissue: Colon and Pancreas.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-789.
    Tissue: Amygdala.
  4. "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-789.
    Tissue: Brain.
  5. "Expression, purification and kinetic properties of human recombinant phospholipase C delta 3."
    Pawelczyk T., Matecki A.
    Acta Biochim. Pol. 44:221-229(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PURIFICATION.
  6. "Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties."
    Ghosh S., Pawelczyk T., Lowenstein J.M.
    Protein Expr. Purif. 9:262-278(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PURIFICATION.
  7. "Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium."
    Pawelczyk T., Matecki A.
    Eur. J. Biochem. 257:169-177(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, COFACTOR, ENZYME REGULATION.
  8. "Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization."
    Kim H., Suh P.-G., Ryu S.H., Park S.H.
    Cytogenet. Cell Genet. 87:209-210(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  9. "Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes."
    Pawelczyk T., Matecki A.
    Eur. J. Biochem. 262:291-298(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DOMAIN PH.
  10. Cited for: INDUCTION.
  11. "Membrane targeting of C2 domains of phospholipase C-delta isoforms."
    Ananthanarayanan B., Das S., Rhee S.-G., Murray D., Cho W.
    J. Biol. Chem. 277:3568-3575(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN C2.
  12. "Expression of phospholipases A2 and C in human corneal epithelial cells."
    Landreville S., Coulombe S., Carrier P., Gelb M.H., Guerin S.L., Salesse C.
    Invest. Ophthalmol. Vis. Sci. 45:3997-4003(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis."
    Naito Y., Okada M., Yagisawa H.
    J. Biochem. 140:785-791(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiPLCD3_HUMAN
AccessioniPrimary (citable) accession number: Q8N3E9
Secondary accession number(s): Q8TEC1, Q8TF37, Q96FL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: July 22, 2015
This is version 129 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.