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Protein

Protein kinase C epsilon type

Gene

Prkce

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-566 (activation loop of the kinase domain), Thr-710 (turn motif) and Ser-729 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei437 – 4371ATPPROSITE-ProRule annotation
Active sitei532 – 5321Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 22052Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri242 – 29251Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi414 – 4229ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calcium-independent protein kinase C activity Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: RGD
  • protein kinase C activity Source: UniProtKB
  • receptor binding Source: RGD
  • SH3 domain binding Source: RGD

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cellular response to platelet-derived growth factor stimulus Source: UniProtKB
  • intracellular signal transduction Source: RGD
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of mitochondrial calcium ion concentration Source: UniProtKB
  • negative regulation of mitochondrial membrane potential Source: UniProtKB
  • negative regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
  • peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of fibroblast migration Source: UniProtKB
  • positive regulation of wound healing Source: UniProtKB
  • TRAM-dependent toll-like receptor 4 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell adhesion, Cell cycle, Cell division, Immunity

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.13. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C epsilon type (EC:2.7.11.13)
Alternative name(s):
nPKC-epsilon
Gene namesi
Name:Prkce
Synonyms:Pkce
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61925. Prkce.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cell membrane By similarity
  • Cytoplasmperinuclear region By similarity
  • Nucleus By similarity

  • Note: Translocated to plasma membrane in epithelial cells stimulated by HGF. Associated with the Golgi at the perinuclear site in pre-passage fibroblasts. In passaging cells, translocated to the cell periphery. Translocated to the nucleus in PMA-treated cells (By similarity).By similarity

GO - Cellular componenti

  • cell periphery Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: RGD
  • Golgi membrane Source: RGD
  • mitochondrion Source: GOC
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2094266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 737737Protein kinase C epsilon typePRO_0000055700Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621PhosphoserineBy similarity
Modified residuei228 – 2281PhosphothreonineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei309 – 3091PhosphothreonineBy similarity
Modified residuei316 – 3161PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineCombined sources
Modified residuei337 – 3371PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei349 – 3491PhosphothreonineBy similarity
Modified residuei350 – 3501Phosphoserine; by MAPK11 and MAPK14By similarity
Modified residuei368 – 3681PhosphoserineCombined sources
Modified residuei388 – 3881PhosphoserineCombined sources
Modified residuei566 – 5661Phosphothreonine; by PDPK1By similarity
Modified residuei703 – 7031Phosphothreonine; by autocatalysisSequence analysis
Modified residuei710 – 7101PhosphothreonineCombined sources
Modified residuei729 – 7291PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729. Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP09216.

PTM databases

iPTMnetiP09216.
PhosphoSiteiP09216.
SwissPalmiP09216.

Interactioni

Subunit structurei

Interacts with DGKQ, STAT3 and YWHAB (By similarity). Forms a ternary complex with TRIM63 and GN2BL1. Can form a complex with PDLIM5 and N-type calcium channel. Interacts with COPB1.By similarity3 Publications

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • SH3 domain binding Source: RGD

Protein-protein interaction databases

BioGridi247999. 3 interactions.
IntActiP09216. 3 interactions.

Chemistry

BindingDBiP09216.

Structurei

Secondary structure

1
737
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1714Combined sources
Helixi22 – 254Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 535Combined sources
Beta strandi64 – 7613Combined sources
Beta strandi78 – 858Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 1019Combined sources
Helixi102 – 1054Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi124 – 13512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMIX-ray1.70A1-136[»]
ProteinModelPortaliP09216.
SMRiP09216. Positions 1-136, 239-295, 405-736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9999C2PROSITE-ProRule annotationAdd
BLAST
Domaini408 – 668261Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini669 – 73769AGC-kinase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi223 – 2286Interaction with actinBy similarity

Domaini

The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 22052Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri242 – 29251Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP09216.
KOiK18050.
PhylomeDBiP09216.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000551. PKC_delta. 1 hit.
PIRSF501106. Protein_kin_C_epsilon. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR
60 70 80 90 100
IGQTATKQKT NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI
110 120 130 140 150
QFEELLQNGS RHFEDWIDLE PEGKVYVIID LSGSSGEAPK DNEERVFRER
160 170 180 190 200
MRPRKRQGAV RRRVHQVNGH KFMATYLRQP TYCSHCRDFI WGVIGKQGYQ
210 220 230 240 250
CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN MPHKFGIHNY
260 270 280 290 300
KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
310 320 330 340 350
KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS
360 370 380 390 400
PCDQELKELE NNIRKALSFD NRGEEHRASS STDGQLASPG ENGEVRQGQA
410 420 430 440 450
KRLGLDEFNF IKVLGKGSFG KVMLAELKGK DEVYAVKVLK KDVILQDDDV
460 470 480 490 500
DCTMTEKRIL ALARKHPYLT QLYCCFQTKD RLFFVMEYVN GGDLMFQIQR
510 520 530 540 550
SRKFDEPRSG FYAAEVTSAL MFLHQHGVIY RDLKLDNILL DAEGHSKLAD
560 570 580 590 600
FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
610 620 630 640 650
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL
660 670 680 690 700
GCVAAQNGED AIKQHPFFKE IDWVLLEQKK MKPPFKPRIK TKRDVNNFDQ
710 720 730
DFTREEPILT LVDEAIVKQI NQEEFKGFSY FGEDLMP
Length:737
Mass (Da):83,478
Last modified:July 1, 1989 - v1
Checksum:i6AD6999EFDD2659F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18331 mRNA. Translation: AAA41872.1.
PIRiB28163. KIRTCE.
RefSeqiNP_058867.1. NM_017171.1.
UniGeneiRn.215207.

Genome annotation databases

GeneIDi29340.
KEGGirno:29340.
UCSCiRGD:61925. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18331 mRNA. Translation: AAA41872.1.
PIRiB28163. KIRTCE.
RefSeqiNP_058867.1. NM_017171.1.
UniGeneiRn.215207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GMIX-ray1.70A1-136[»]
ProteinModelPortaliP09216.
SMRiP09216. Positions 1-136, 239-295, 405-736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247999. 3 interactions.
IntActiP09216. 3 interactions.

Chemistry

BindingDBiP09216.
ChEMBLiCHEMBL2094266.

PTM databases

iPTMnetiP09216.
PhosphoSiteiP09216.
SwissPalmiP09216.

Proteomic databases

PRIDEiP09216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29340.
KEGGirno:29340.
UCSCiRGD:61925. rat.

Organism-specific databases

CTDi5581.
RGDi61925. Prkce.

Phylogenomic databases

HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP09216.
KOiK18050.
PhylomeDBiP09216.

Enzyme and pathway databases

BRENDAi2.7.11.13. 5301.

Miscellaneous databases

EvolutionaryTraceiP09216.
PROiP09216.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000551. PKC_delta. 1 hit.
PIRSF501106. Protein_kin_C_epsilon. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structure, expression, and properties of additional members of the protein kinase C family."
    Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
    J. Biol. Chem. 263:6927-6932(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Identification of three additional members of rat protein kinase C family: delta-, epsilon- and zeta-subspecies."
    Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
    FEBS Lett. 226:125-128(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 135-297.
  3. "The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon."
    Csukai M., Chen C.-H., de Matteis M.A., Mochly-Rosen D.
    J. Biol. Chem. 272:29200-29206(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPB1, SUBCELLULAR LOCATION.
  4. "Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C."
    Matsumoto M., Ogawa W., Hino Y., Furukawa K., Ono Y., Takahashi M., Ohba M., Kuroki T., Kasuga M.
    J. Biol. Chem. 276:14400-14406(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1.
  5. "Muscle ring finger protein-1 inhibits PKC-epsilon activation and prevents cardiomyocyte hypertrophy."
    Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., Patterson C.
    J. Cell Biol. 167:1147-1159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RACK1 AND TRIM63.
  6. "A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels."
    Maeno-Hikichi Y., Chang S., Matsumura K., Lai M., Lin H., Nakagawa N., Kuroda S., Zhang J.F.
    Nat. Neurosci. 6:468-475(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH PDLIM5 AND N-TYPE CALCIUM CHANNEL.
  7. "Protein kinase Cepsilon-dependent MARCKS phosphorylation in neonatal and adult rat ventricular myocytes."
    Heidkamp M.C., Iyengar R., Szotek E.L., Cribbs L.L., Samarel A.M.
    J. Mol. Cell. Cardiol. 42:422-431(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MARCKS.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-337; SER-346; SER-368; SER-388; THR-710 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains."
    Ochoa W.F., Garcia-Garcia J., Fita I., Corbalan-Garcia S., Verdaguer N., Gomez-Fernandez J.C.
    J. Mol. Biol. 311:837-849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-136.

Entry informationi

Entry nameiKPCE_RAT
AccessioniPrimary (citable) accession number: P09216
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 6, 2016
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.