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Q8N3E9

- PLCD3_HUMAN

UniProt

Q8N3E9 - PLCD3_HUMAN

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Protein
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
Gene
PLCD3, KIAA1964
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 3 calcium ions per subunit. Two of the calcium ions are bound to the C2 domain Inferred.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

Vmax=28.5 µmol/min/mg enzyme

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi195 – 206121 Reviewed prediction
Add
BLAST
Calcium bindingi231 – 242122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. inositol phosphate metabolic process Source: Reactome
  3. intracellular signal transduction Source: InterPro
  4. labyrinthine layer blood vessel development Source: Ensembl
  5. lipid catabolic process Source: UniProtKB-KW
  6. regulation of cell proliferation Source: Ensembl
  7. small molecule metabolic process Source: Reactome
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: Chromosome 17

Organism-specific databases

HGNCiHGNC:9061. PLCD3.

Subcellular locationi

Membrane; Peripheral membrane protein. Cytoplasm. Cleavage furrow
Note: Localizes at the cleavage furrow during cytokinesis.2 Publications

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB-SubCell
  2. cytosol Source: Ensembl
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33389.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Phosphoserine1 Publication
Modified residuei496 – 4961Phosphoserine By 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.3 Publications

Gene expression databases

ArrayExpressiQ8N3E9.
BgeeiQ8N3E9.
CleanExiHS_PLCD3.
GenevestigatoriQ8N3E9.

Organism-specific databases

HPAiHPA025711.
HPA053665.

Interactioni

Protein-protein interaction databases

BioGridi125222. 2 interactions.
IntActiQ8N3E9. 1 interaction.
MINTiMINT-1193970.
STRINGi9606.ENSP00000313731.

Structurei

3D structure databases

ProteinModelPortaliQ8N3E9.
SMRiQ8N3E9. Positions 55-787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 172110PH
Add
BLAST
Domaini182 – 21736EF-hand 1
Add
BLAST
Domaini218 – 25336EF-hand 2
Add
BLAST
Domaini250 – 28536EF-hand 3
Add
BLAST
Domaini337 – 482146PI-PLC X-box
Add
BLAST
Domaini528 – 644117PI-PLC Y-box
Add
BLAST
Domaini647 – 752106C2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 10129Substrate binding By similarity
Add
BLAST

Domaini

The C2 domain is a Ca2+-dependent membrane-targeting module.2 Publications
The PH domain mediates interaction with the surface membrane by binding to PIP2.2 Publications

Sequence similaritiesi

Contains 1 C2 domain.
Contains 3 EF-hand domains.
Contains 1 PH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000006871.
HOVERGENiHBG053610.
InParanoidiQ8N3E9.
KOiK05857.
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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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

MLCGRWRRCR RPPEEPPVAA QVAAQVAAPV ALPSPPTPSD GGTKRPGLRA    50
LKKMGLTEDE DVRAMLRGSR LRKIRSRTWH KERLYRLQED GLSVWFQRRI 100
PRAPSQHIFF VQHIEAVREG HQSEGLRRFG GAFAPARCLT IAFKGRRKNL 150
DLAAPTAEEA QRWVRGLTKL RARLDAMSQR ERLDHWIHSY LHRADSNQDS 200
KMSFKEIKSL LRMVNVDMND MYAYLLFKEC DHSNNDRLEG AEIEEFLRRL 250
LKRPELEEIF HQYSGEDRVL SAPELLEFLE DQGEEGATLA RAQQLIQTYE 300
LNETAKQHEL MTLDGFMMYL LSPEGAALDN THTCVFQDMN QPLAHYFISS 350
SHNTYLTDSQ IGGPSSTEAY VRAFAQGCRC VELDCWEGPG GEPVIYHGHT 400
LTSKILFRDV VQAVRDHAFT LSPYPVILSL ENHCGLEQQA AMARHLCTIL 450
GDMLVTQALD SPNPEELPSP EQLKGRVLVK GKKLPAARSE DGRALSDREE 500
EEEDDEEEEE EVEAAAQRRL AKQISPELSA LAVYCHATRL RTLHPAPNAP 550
QPCQVSSLSE RKAKKLIREA GNSFVRHNAR QLTRVYPLGL RMNSANYSPQ 600
EMWNSGCQLV ALNFQTPGYE MDLNAGRFLV NGQCGYVLKP ACLRQPDSTF 650
DPEYPGPPRT TLSIQVLTAQ QLPKLNAEKP HSIVDPLVRI EIHGVPADCA 700
RQETDYVLNN GFNPRWGQTL QFQLRAPELA LVRFVVEDYD ATSPNDFVGQ 750
FTLPLSSLKQ GYRHIHLLSK DGASLSPATL FIQIRIQRS 789
Length:789
Mass (Da):89,258
Last modified:October 2, 2007 - v3
Checksum:iC6901404D2C9D070
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071I → T in CAD39054. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqiNP_588614.1. NM_133373.4.
UniGeneiHs.380094.

Genome annotation databases

EnsembliENST00000322765; ENSP00000313731; ENSG00000161714.
GeneIDi113026.
KEGGihsa:113026.
UCSCiuc002iib.3. human.

Polymorphism databases

DMDMi158706388.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_588614.1. NM_133373.4.
UniGenei Hs.380094.

3D structure databases

ProteinModelPortali Q8N3E9.
SMRi Q8N3E9. Positions 55-787.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125222. 2 interactions.
IntActi Q8N3E9. 1 interaction.
MINTi MINT-1193970.
STRINGi 9606.ENSP00000313731.

Chemistry

DrugBanki DB00144. Phosphatidylserine.

Polymorphism databases

DMDMi 158706388.

Proteomic databases

MaxQBi Q8N3E9.
PaxDbi Q8N3E9.
PeptideAtlasi Q8N3E9.
PRIDEi Q8N3E9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322765 ; ENSP00000313731 ; ENSG00000161714 .
GeneIDi 113026.
KEGGi hsa:113026.
UCSCi uc002iib.3. human.

Organism-specific databases

CTDi 113026.
GeneCardsi GC17M043197.
HGNCi HGNC:9061. PLCD3.
HPAi HPA025711.
HPA053665.
MIMi 608795. gene.
neXtProti NX_Q8N3E9.
PharmGKBi PA33389.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149692.
HOGENOMi HOG000006871.
HOVERGENi HBG053610.
InParanoidi Q8N3E9.
KOi K05857.
OrthoDBi EOG7V49XT.
PhylomeDBi Q8N3E9.
TreeFami TF313216.

Enzyme and pathway databases

Reactomei REACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

ChiTaRSi PLCD3. human.
GeneWikii PLCD3.
GenomeRNAii 113026.
NextBioi 78735.
PROi Q8N3E9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8N3E9.
Bgeei Q8N3E9.
CleanExi HS_PLCD3.
Genevestigatori Q8N3E9.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProi IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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 ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF33. PTHR10336:SF33. 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.
[Graphical view ]
PRINTSi PR00390. PHPHLIPASEC.
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 121 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