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Protein

Protein kinase C eta type

Gene

PRKCH

Organism
Homo sapiens (Human)
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 is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization.10 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-513 (activation loop of the kinase domain), Thr-656 (turn motif) and Ser-675 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei384ATPPROSITE-ProRule annotation1
Active sitei479Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri171 – 222Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri245 – 295Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi361 – 369ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium-independent protein kinase C activity Source: Ensembl
  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein kinase C activity Source: ProtInc

GO - Biological processi

  • intracellular signal transduction Source: GO_Central
  • negative regulation of glial cell apoptotic process Source: UniProtKB
  • peptidyl-serine phosphorylation Source: GO_Central
  • platelet activation Source: Reactome
  • positive regulation of B cell receptor signaling pathway Source: UniProtKB
  • positive regulation of glial cell proliferation Source: UniProtKB
  • positive regulation of keratinocyte differentiation Source: UniProtKB
  • positive regulation of macrophage derived foam cell differentiation Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • protein kinase C signaling Source: Ensembl
  • protein phosphorylation Source: UniProtKB
  • regulation of bicellular tight junction assembly Source: UniProtKB
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS00456-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-418597. G alpha (z) signalling events.
SABIO-RKP24723.
SignaLinkiP24723.
SIGNORiP24723.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C eta type (EC:2.7.11.13)
Alternative name(s):
PKC-L
nPKC-eta
Gene namesi
Name:PRKCH
Synonyms:PKCL, PRKCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9403. PRKCH.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Ischemic stroke (ISCHSTR)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
See also OMIM:601367

Organism-specific databases

DisGeNETi5583.
MalaCardsiPRKCH.
MIMi601367. phenotype.
OpenTargetsiENSG00000027075.
PharmGKBiPA33767.

Chemistry databases

ChEMBLiCHEMBL3616.
GuidetoPHARMACOLOGYi1487.

Polymorphism and mutation databases

BioMutaiPRKCH.
DMDMi281185512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557051 – 683Protein kinase C eta typeAdd BLAST683

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei32Phosphoserine; by autocatalysis1 Publication1
Modified residuei317PhosphoserineBy similarity1
Modified residuei513Phosphothreonine; by PDPK1Curated1
Modified residuei656PhosphothreonineCombined sources1
Modified residuei675PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP24723.
MaxQBiP24723.
PaxDbiP24723.
PeptideAtlasiP24723.
PRIDEiP24723.

PTM databases

iPTMnetiP24723.
PhosphoSitePlusiP24723.

Expressioni

Tissue specificityi

Most abundant in lung, less in heart and skin.1 Publication

Gene expression databases

BgeeiENSG00000027075.
CleanExiHS_PRKCH.
ExpressionAtlasiP24723. baseline and differential.
GenevisibleiP24723. HS.

Organism-specific databases

HPAiCAB001998.
HPA026294.
HPA053709.

Interactioni

Subunit structurei

Interacts with FYN and RALA (By similarity). Interacts with DGKQ.By similarity1 Publication

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111569. 12 interactors.
DIPiDIP-44588N.
IntActiP24723. 5 interactors.
MINTiMINT-3973608.
STRINGi9606.ENSP00000329127.

Chemistry databases

BindingDBiP24723.

Structurei

Secondary structure

1683
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 20Combined sources13
Helixi26 – 30Combined sources5
Turni31 – 33Combined sources3
Beta strandi34 – 37Combined sources4
Beta strandi43 – 49Combined sources7
Beta strandi52 – 56Combined sources5
Beta strandi67 – 79Combined sources13
Beta strandi81 – 88Combined sources8
Beta strandi91 – 94Combined sources4
Beta strandi96 – 104Combined sources9
Helixi105 – 112Combined sources8
Beta strandi116 – 123Combined sources8
Beta strandi125 – 127Combined sources3
Beta strandi129 – 137Combined sources9
Beta strandi355 – 364Combined sources10
Beta strandi367 – 374Combined sources8
Turni375 – 377Combined sources3
Beta strandi380 – 387Combined sources8
Helixi388 – 394Combined sources7
Helixi397 – 409Combined sources13
Turni410 – 412Combined sources3
Beta strandi419 – 424Combined sources6
Beta strandi426 – 434Combined sources9
Helixi441 – 448Combined sources8
Helixi453 – 472Combined sources20
Helixi482 – 484Combined sources3
Beta strandi485 – 487Combined sources3
Beta strandi493 – 495Combined sources3
Helixi518 – 520Combined sources3
Helixi523 – 530Combined sources8
Helixi534 – 549Combined sources16
Helixi559 – 568Combined sources10
Helixi579 – 588Combined sources10
Helixi593 – 595Combined sources3
Helixi600 – 602Combined sources3
Helixi606 – 609Combined sources4
Helixi612 – 614Combined sources3
Helixi619 – 623Combined sources5
Helixi646 – 649Combined sources4
Helixi663 – 665Combined sources3
Helixi668 – 671Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FK9X-ray1.75A1-138[»]
3TXOX-ray2.05A333-683[»]
ProteinModelPortaliP24723.
SMRiP24723.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24723.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 113C2PROSITE-ProRule annotationAdd BLAST102
Domaini355 – 614Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini615 – 683AGC-kinase C-terminalAdd BLAST69

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)DescriptionActionsGraphical viewLength
Zinc fingeri171 – 222Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri245 – 295Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP24723.
KOiK18051.
OMAiYLKVRIG.
OrthoDBiEOG091G0QRS.
PhylomeDBiP24723.
TreeFamiTF351133.

Family and domain databases

CDDicd00029. C1. 2 hits.
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.
IPR027431. PKC_eta.
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.
PIRSF501107. Protein_kin_C_eta. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P24723-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD
60 70 80 90 100
QVRVGQTSTK QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN
110 120 130 140 150
CTLQFQELLR TTGASDTFEG WVDLEPEGKV FVVITLTGSF TEATLQRDRI
160 170 180 190 200
FKHFTRKRQR AMRRRVHQIN GHKFMATYLR QPTYCSHCRE FIWGVFGKQG
210 220 230 240 250
YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDSKIAEQRF GINIPHKFSI
260 270 280 290 300
HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
310 320 330 340 350
ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGKESSKEGN GIGVNSSNRL
360 370 380 390 400
GIDNFEFIRV LGKGSFGKVM LARVKETGDL YAVKVLKKDV ILQDDDVECT
410 420 430 440 450
MTEKRILSLA RNHPFLTQLF CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR
460 470 480 490 500
FDEARARFYA AEIISALMFL HDKGIIYRDL KLDNVLLDHE GHCKLADFGM
510 520 530 540 550
CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM GVLLYEMLCG
560 570 580 590 600
HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL
610 620 630 640 650
TQGGEHAILR HPFFKEIDWA QLNHRQIEPP FRPRIKSRED VSNFDPDFIK
660 670 680
EEPVLTPIDE GHLPMINQDE FRNFSYVSPE LQP
Length:683
Mass (Da):77,828
Last modified:December 15, 2009 - v4
Checksum:i0A29806CE31912F2
GO
Isoform 2 (identifier: P24723-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.

Note: No experimental confirmation available.
Show »
Length:522
Mass (Da):59,521
Checksum:iD6852F6089A763E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96Missing in AAA60100 (PubMed:1986216).Curated1
Sequence conflicti109L → R in AAA60100 (PubMed:1986216).Curated1
Sequence conflicti110R → G in AAA60100 (PubMed:1986216).Curated1
Sequence conflicti393Q → L in AAA60100 (PubMed:1986216).Curated1
Sequence conflicti472D → E in AAB32724 (PubMed:7988719).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04231219A → V.1 PublicationCorresponds to variant rs55645551dbSNPEnsembl.1
Natural variantiVAR_04231365K → R.1 PublicationCorresponds to variant rs55737090dbSNPEnsembl.1
Natural variantiVAR_042314149R → Q.1 PublicationCorresponds to variant rs55848048dbSNPEnsembl.1
Natural variantiVAR_042315359R → Q.1 PublicationCorresponds to variant rs55818778dbSNPEnsembl.1
Natural variantiVAR_034604374V → I Associated with susceptibility to ischemic stroke; increases autophosphorylation and kinase activity. 2 PublicationsCorresponds to variant rs2230500dbSNPEnsembl.1
Natural variantiVAR_060736497D → Y.Corresponds to variant rs11846991dbSNPEnsembl.1
Natural variantiVAR_042316575T → A in a aLL TEL/AML1+ sample; somatic mutation. 1 Publication1
Natural variantiVAR_042317594T → I in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042318612P → S.1 PublicationCorresponds to variant rs34159231dbSNPEnsembl.1
Natural variantiVAR_042438645D → V.Corresponds to variant rs35561533dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0565721 – 161Missing in isoform 2. 1 PublicationAdd BLAST161

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55284 mRNA. Translation: AAA60100.1.
AK290183 mRNA. Translation: BAF82872.1.
AK296158 mRNA. Translation: BAG58897.1.
AL138996 Genomic DNA. No translation available.
AL355916 Genomic DNA. No translation available.
AL359220 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80800.1.
CH471061 Genomic DNA. Translation: EAW80801.1.
BC037268 mRNA. Translation: AAH37268.1.
S74620 mRNA. Translation: AAB32724.1.
CCDSiCCDS9752.1. [P24723-1]
PIRiA39666.
RefSeqiNP_006246.2. NM_006255.4. [P24723-1]
XP_016876947.1. XM_017021458.1. [P24723-2]
UniGeneiHs.333907.

Genome annotation databases

EnsembliENST00000332981; ENSP00000329127; ENSG00000027075. [P24723-1]
ENST00000555082; ENSP00000450981; ENSG00000027075. [P24723-2]
GeneIDi5583.
KEGGihsa:5583.
UCSCiuc001xfn.4. human. [P24723-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55284 mRNA. Translation: AAA60100.1.
AK290183 mRNA. Translation: BAF82872.1.
AK296158 mRNA. Translation: BAG58897.1.
AL138996 Genomic DNA. No translation available.
AL355916 Genomic DNA. No translation available.
AL359220 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80800.1.
CH471061 Genomic DNA. Translation: EAW80801.1.
BC037268 mRNA. Translation: AAH37268.1.
S74620 mRNA. Translation: AAB32724.1.
CCDSiCCDS9752.1. [P24723-1]
PIRiA39666.
RefSeqiNP_006246.2. NM_006255.4. [P24723-1]
XP_016876947.1. XM_017021458.1. [P24723-2]
UniGeneiHs.333907.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FK9X-ray1.75A1-138[»]
3TXOX-ray2.05A333-683[»]
ProteinModelPortaliP24723.
SMRiP24723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111569. 12 interactors.
DIPiDIP-44588N.
IntActiP24723. 5 interactors.
MINTiMINT-3973608.
STRINGi9606.ENSP00000329127.

Chemistry databases

BindingDBiP24723.
ChEMBLiCHEMBL3616.
GuidetoPHARMACOLOGYi1487.

PTM databases

iPTMnetiP24723.
PhosphoSitePlusiP24723.

Polymorphism and mutation databases

BioMutaiPRKCH.
DMDMi281185512.

Proteomic databases

EPDiP24723.
MaxQBiP24723.
PaxDbiP24723.
PeptideAtlasiP24723.
PRIDEiP24723.

Protocols and materials databases

DNASUi5583.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332981; ENSP00000329127; ENSG00000027075. [P24723-1]
ENST00000555082; ENSP00000450981; ENSG00000027075. [P24723-2]
GeneIDi5583.
KEGGihsa:5583.
UCSCiuc001xfn.4. human. [P24723-1]

Organism-specific databases

CTDi5583.
DisGeNETi5583.
GeneCardsiPRKCH.
HGNCiHGNC:9403. PRKCH.
HPAiCAB001998.
HPA026294.
HPA053709.
MalaCardsiPRKCH.
MIMi601367. phenotype.
605437. gene.
neXtProtiNX_P24723.
OpenTargetsiENSG00000027075.
PharmGKBiPA33767.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP24723.
KOiK18051.
OMAiYLKVRIG.
OrthoDBiEOG091G0QRS.
PhylomeDBiP24723.
TreeFamiTF351133.

Enzyme and pathway databases

BioCyciZFISH:HS00456-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-418597. G alpha (z) signalling events.
SABIO-RKP24723.
SignaLinkiP24723.
SIGNORiP24723.

Miscellaneous databases

ChiTaRSiPRKCH. human.
EvolutionaryTraceiP24723.
GeneWikiiPRKCH.
GenomeRNAii5583.
PROiP24723.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000027075.
CleanExiHS_PRKCH.
ExpressionAtlasiP24723. baseline and differential.
GenevisibleiP24723. HS.

Family and domain databases

CDDicd00029. C1. 2 hits.
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.
IPR027431. PKC_eta.
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.
PIRSF501107. Protein_kin_C_eta. 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...

Entry informationi

Entry nameiKPCL_HUMAN
AccessioniPrimary (citable) accession number: P24723
Secondary accession number(s): B4DJN5, Q16246, Q8NE03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 2009
Last modified: November 30, 2016
This is version 178 of the entry and version 4 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 14
    Human chromosome 14: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.