Reviewed, UniProtKB/Swiss-Prot P41743 (KPCI_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein kinase C iota type
    EC=2.7.11.13
Alternative name(s):
    nPKC-iota
    Atypical protein kinase C-lambda/iota
      Short name=aPKC-lambda/iota
      Short name=PRKC-lambda/iota

Gene names

Name:	PRKCI
Synonyms:	DXS1179E

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. May play a role in the secretory response to nutrients. Involved in cell polarization processes and the formation of epithelial tight junctions. Implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. Functions in both pro- and anti-apoptotic pathways. Functions in the RAC1/ERK signaling required for transformed growth. Plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). Ref.1 Ref.6 Ref.9 Ref.15
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Might be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion. Two specific sites, Thr-412 (activation loop of the kinase domain) and Thr-564 (turn motif), need to be phosphorylated for its full activation By similarity. Atypical PCKs are not regulated by diacylglycerol, phorbol esters nor calcium ions.
Subunit structure	Forms a complex with SQSTM1 and MP2K5 By similarity. Interacts directly with SQSTM1 Probable. Interacts with IKBKB. Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs).
Subcellular location	Cytoplasm. Membrane. Endosome. Nucleus. Note: Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by cSrc, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Vesicular tubular clusters. Transported to VTCs through interaction with RAB2A. Ref.5 Ref.11 Ref.16 Ref.17
Tissue specificity	Predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. Highly expressed in non-small cell lung cancers. Ref.1 Ref.15 Ref.2
Domain	The OPR domain mediates interaction with SQSTM1 By similarity. The C1 domain does not bind diacylglycerol (DAG).
Post-translational modification	On neuronal growth factor (NGF) stimulation, phosphorylated by Src on Tyr-265, Tyr-280 and Tyr-334. Phosphorylation on Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus. Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation. Ref.11 Ref.17 Ref.10 Ref.18 Ref.22
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 OPR domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Endosome Membrane Nucleus
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene Tumor suppressor
Domain	Phorbol-ester binding Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell-cell junction organization Ref.8 Inferred from mutant phenotype. Source: UniProtKB cellular response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB establishment or maintenance of epithelial cell apical/basal polarity Traceable author statement. Source: UniProtKB intracellular signaling cascade Inferred from electronic annotation. Source: InterPro positive regulation of glucose import Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB protein targeting to membrane Ref.8 Non-traceable author statement. Source: UniProtKB regulation of establishment of protein localization Inferred from sequence or structural similarity. Source: UniProtKB secretion Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Ref.8 Inferred from direct assay. Source: UniProtKB endosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.7 Inferred from direct assay. Source: UniProtKB polarisome Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Ref.1 Traceable author statement. Source: UniProtKB diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Ref.1 Inferred from direct assay. Source: UniProtKB protein binding Ref.7 Ref.12 Ref.21 Inferred from physical interaction. Source: UniProtKB protein kinase C activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P60953	2	EBI-286199,EBI-81752
PARD6A	Q9NPB6	4	EBI-286199,EBI-81876
PARD6B	Q9BYG5	3	EBI-286199,EBI-295391

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 596

596

Protein kinase C iota type

PRO_0000055710

Regions

Domain

25 – 108

84

OPR

Domain

254 – 522

269

Protein kinase

Domain

523 – 594

72

AGC-kinase C-terminal

Zinc finger

140 – 190

51

Phorbol-ester/DAG-type

Nucleotide binding

260 – 268

9

ATP By similarity

Region

1 – 253

253

Regulatory domain

Region

1 – 28

28

Required for interaction with RAB2

Region

72 – 91

20

Interaction with PARD6A

Sites

Active site

378

1

Proton acceptor By similarity

Binding site

283

1

ATP By similarity

Amino acid modifications

Modified residue

265

1

Phosphotyrosine; by Src

Modified residue

280

1

Phosphotyrosine; by Src

Modified residue

334

1

Phosphotyrosine; by Src

Modified residue

412

1

Phosphothreonine

Modified residue

564

1

Phosphothreonine

Natural variations

Natural variant

118

1

P → L in a metastatic melanoma sample; somatic mutation.

VAR_042322

Natural variant

130

1

R → C

VAR_042323

Experimental info

Mutagenesis

29

1

K → A: No effect on interaction with SQSTM1.

Mutagenesis

72

1

D → A: Loss of interaction with PARD6A and with SQSTM1.

Mutagenesis

85

1

E → A: Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-91.

Mutagenesis

91

1

R → A: Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-85.

Mutagenesis

265

1

Y → F: No effect on the Src-mediated phosphorylation state. No effect on Src-induced enzyme activity. Little effect on TRAF6-mediated activation of NF-kappa-B. Decreased binding to KPNB1/importin-beta.

Mutagenesis

280

1

Y → F: No effect on the Src-mediated phosphorylation state. No effect on Src-induced enzyme activity. No effect on TRAF6-mediated activation of NF-kappa-B.

Mutagenesis

334

1

Y → F: No effect on the Src-mediated phosphorylation state. Significant reduction of Src-induced enzyme activity. Greatly reduced TRAF6-mediated activation of NF-kappa-B. Reduces NGF-dependent cell survival.

Sequence conflict

485

1

L → M in AAH22016. Ref.3

Sequence conflict

508

1

H → L in AAH22016. Ref.3

Sequence conflict

560

1

P → R in AAH22016. Ref.3

Secondary structure

1

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596

Helix Strand Turn

Details...

Beta strand

26 – 32

7

Beta strand

35 – 41

7

Helix

47 – 57

11

Beta strand

67 – 71

5

Beta strand

77 – 79

3

Helix

83 – 95

13

Beta strand

101 – 106

6

Beta strand

254 – 262

9

Beta strand

264 – 273

10

Turn

274 – 276

3

Beta strand

279 – 286

8

Helix

287 – 289

3

Turn

293 – 295

3

Helix

296 – 306

11

Turn

307 – 310

4

Beta strand

318 – 321

4

Beta strand

325 – 333

9

Helix

340 – 345

6

Helix

352 – 371

20

Helix

381 – 383

3

Beta strand

384 – 386

3

Beta strand

392 – 394

3

Helix

417 – 419

3

Helix

422 – 425

4

Helix

433 – 448

16

Helix

466 – 476

11

Helix

487 – 496

10

Beta strand

499 – 501

3

Turn

505 – 507

3

Turn

509 – 511

3

Helix

512 – 518

7

Helix

520 – 522

3

Helix

527 – 530

4

Turn

531 – 533

3

Helix

568 – 571

4

Helix

577 – 579

3

Sequences

	Sequence		Length	Mass (Da)
	P41743-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 1E3F8C1D4BFC734F	FASTA	596	68,262
	10 20 30 40 50 60 MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF 70 80 90 100 110 120 DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE 130 140 150 160 170 180 DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK 190 200 210 220 230 240 KCHKLVTIEC GRHSLPQEPV MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR 250 260 270 280 290 300 ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ 310 320 330 340 350 360 TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA 370 380 390 400 410 420 EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI 430 440 450 460 470 480 APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR 490 500 510 520 530 540 IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK 550 560 570 580 590 PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells." Selbie L.A., Schmitz-Peiffer C., Sheng Y., Biden T.J. J. Biol. Chem. 268:24296-24302(1993) [PubMed: 8226978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"Human protein kinase C iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3." Mazzarella R., Ciccodicola A., Esposito T., Arcucci A., Migliaccio C., Jones C., Schlessinger D., D'Urso M., D'Esposito M. Genomics 26:629-631(1995) [PubMed: 7607695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Teratocarcinoma.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo." Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J. Mol. Cell. Biol. 16:105-114(1996) [PubMed: 8524286] [Abstract] Cited for: INTERACTION WITH SMG1, ENZYME REGULATION.
[5]	"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62." Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T. Mol. Cell. Biol. 18:3069-3080(1998) [PubMed: 9566925] [Abstract] Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
[6]	"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation." Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J. EMBO J. 18:3044-3053(1999) [PubMed: 10356400] [Abstract] Cited for: INTERACTION WITH SQSTM1 AND IKBKB, FUNCTION.
[7]	"Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C." Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H. Genes Cells 6:107-119(2001) [PubMed: 11260256] [Abstract] Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX CONTAINING PARD6B AND CDC42/RAC1.
[8]	"Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures." Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., Ohno S. J. Cell Biol. 152:1183-1196(2001) [PubMed: 11257119] [Abstract] Cited for: INTERACTION WITH PARD3 AND PARD6B IN THE TERNARY AKPC/PAR3/PAR6 COMPLEX.
[9]	"Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway." Tisdale E.J. J. Biol. Chem. 277:3334-3341(2002) [PubMed: 11724794] [Abstract] Cited for: FUNCTION, INTERACTION WITH GAPDH.
[10]	"Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway." Wooten M.W., Vandenplas M.L., Seibenhener M.L., Geetha T., Diaz-Meco M.T. Mol. Cell. Biol. 21:8414-8427(2001) [PubMed: 11713277] [Abstract] Cited for: PHOSPHORYLATION AT TYR-265; TYR-280 AND TYR-334, MUTAGENESIS OF TYR-265; TYR-280 AND TYR-334.
[11]	"Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C." White W.O., Seibenhener M.L., Wooten M.W. J. Cell. Biochem. 85:42-53(2002) [PubMed: 11891849] [Abstract] Cited for: INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-265, MUTAGENESIS OF TYR-265.
[12]	"Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C." Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A. Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed: 12893243] [Abstract] Cited for: INTERACTION WITH ADAP1.
[13]	"Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity." Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A., Hirose T., Iwamatsu A., Shinohara A., Ohno S. Curr. Biol. 13:734-743(2003) [PubMed: 12725730] [Abstract] Cited for: INTERACTION WITH PARD6B/PAR-6 AND LLGL1.
[14]	"Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation." Tisdale E.J. J. Biol. Chem. 278:52524-52530(2003) [PubMed: 14570876] [Abstract] Cited for: INTERACTION WITH RAB2A.
[15]	"Atypical protein kinase Ciota plays a critical role in human lung cancer cell growth and tumorigenicity." Regala R.P., Weems C., Jamieson L., Copland J.A., Thompson E.A., Fields A.P. J. Biol. Chem. 280:31109-31115(2005) [PubMed: 15994303] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[16]	"Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells." Bicaku E., Patel R., Acevedo-Duncan M. Tissue Cell 37:53-58(2005) [PubMed: 15695176] [Abstract] Cited for: INTERACTION WITH CDK7, SUBCELLULAR LOCATION.
[17]	"Src-dependent aprotein kinase C iota/lambda (aPKCiota/lambda) tyrosine phosphorylation is required for aPKCiota/lambda association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-golgi intermediates." Tisdale E.J., Artalejo C.R. J. Biol. Chem. 281:8436-8442(2006) [PubMed: 16452474] [Abstract] Cited for: INTERACTION WITH RAB2A AND GADPH, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[18]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5." Hirano Y., Yoshinaga S., Ogura K., Yokochi M., Noda Y., Sumimoto H., Inagaki F. J. Biol. Chem. 279:31883-31890(2004) [PubMed: 15143057] [Abstract] Cited for: STRUCTURE BY NMR OF 25-108, INTERACTION WITH SQSTM1 AND MAP2K5, MUTAGENESIS OF LYS-29 AND ASP-72.
[21]	"Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains." Hirano Y., Yoshinaga S., Takeya R., Suzuki N.N., Horiuchi M., Kohjima M., Sumimoto H., Inagaki F. J. Biol. Chem. 280:9653-9661(2005) [PubMed: 15590654] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-108 IN COMPLEX WITH PARD6A, MUTAGENESIS OF ASP-72; GLU-85 AND ARG-91.
[22]	"Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif." Messerschmidt A., Macieira S., Velarde M., Baedeker M., Benda C., Jestel A., Brandstetter H., Neuefeind T., Blaesse M. J. Mol. Biol. 352:918-931(2005) [PubMed: 16125198] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-596, MASS SPECTROMETRY, PHOSPHORYLATION AT THR-412 AND THR-564.
[23]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-118 AND CYS-130.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L18964 mRNA. Translation: AAA60171.1. Different initiation.
L33881 mRNA. Translation: AAB17011.1. Different initiation.
BC022016 mRNA. Translation: AAH22016.3. Different initiation.

IPI

IPI00016639.

PIR

A49509.

RefSeq

NP_002731.4.

UniGene

Hs.478199

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VD2	NMR	-	A	25-108	[»]
1WMH	X-ray	1.50	A	25-108	[»]
1ZRZ	X-ray	3.00	A	233-596	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P41743. 10 interactions.

PTM databases

PhosphoSite

P41743.

Proteomic databases

PRIDE

P41743.

Genome annotation databases

Ensembl

ENSG00000163558. Homo sapiens. [Contig view]

GeneID

5584.

KEGG

hsa:5584.

UCSC

uc003fgs.2. human.

Organism-specific databases

GeneCards

GC03P171422.

H-InvDB

HIX0017930.

HGNC

HGNC:9404. PRKCI.

HPA

CAB016290.

MIM

600539. gene.

PharmGKB

PA33768.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P41743.

HOVERGEN

P41743.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

il1pathway. IL1-mediated signaling events.
insulin_pathway. Insulin Pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_11061. Signalling by NGF.

Gene expression databases

ArrayExpress

P41743.

Bgee

P41743.

CleanEx

HS_PRKCI.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR002219. DAG_PE_bd.
IPR000270. OPR_PB1.
IPR015745. PKC.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

PANTHER

PTHR22985:SF86. PKC. 1 hit.

Pfam

PF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000554. PKC_zeta. 1 hit.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS51285. AGC_KINASE_CTER. 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. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

21656.

SOURCE

Search...

Entry information

Entry name

KPCI_HUMAN

Accession

Primary (citable) accession number: P41743
Secondary accession number(s): Q8WW06

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 16, 2009
Last modified:	July 7, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)