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Reviewed, UniProtKB/Swiss-Prot Q16512 (PKN1_HUMAN)

Last modified January 19, 2010. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase N1
    EC=2.7.11.13
Alternative name(s):
    Protein kinase C-like 1
    Protein-kinase C-related kinase 1
    Protein kinase C-like PKN
    Serine-threonine protein kinase N
    Protein kinase PKN-alpha
Gene names
Name: PKN1
Synonyms: PKN, PRK1, PRKCL1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Can phosphorylate ribosomal protein S6. Mediates GTPase Rho dependent intracellular signaling By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids. Two specific sites, Thr-774 (activation loop of the kinase domain) and Ser-916 (turn motif), need to be phosphorylated for its full activation By similarity.

Subunit structure

Interacts with ZA20D3 By similarity. Interacts with RhoA and Rac1.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.

Domain

The C1 domain does not bind the diacylglycerol (DAG).

Post-translational modification

Autophosphorylated; preferably on serine. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

Activated by limited proteolysis with trypsin By similarity.

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 C2 domain.

Contains 1 protein kinase domain.

Contains 3 REM (Hr1) repeats.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16512-1)

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.
Isoform 2 (identifier: Q16512-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MASDAVQ → MAEANNPSEQELE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 942941Serine/threonine-protein kinase N1
PRO_0000055719

Regions

Repeat34 – 11077REM 1
Repeat123 – 20987REM 2
Repeat210 – 29182REM 3
Domain325 – 461137C2
Domain615 – 874260Protein kinase
Domain875 – 94268AGC-kinase C-terminal
Nucleotide binding621 – 6299ATP By similarity

Sites

Active site7401Proton acceptor By similarity
Binding site6441ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue2051Phosphoserine Ref.11 Ref.15
Modified residue3531Phosphothreonine Ref.11
Modified residue3761Phosphoserine Ref.7
Modified residue4481N6-acetyllysine Ref.16
Modified residue5331Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15
Modified residue5371Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15
Modified residue5591Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15
Modified residue5611Phosphoserine Ref.14
Modified residue5621Phosphoserine Ref.8 Ref.9 Ref.12 Ref.14 Ref.15
Modified residue7741Phosphothreonine Probable
Modified residue7781Phosphothreonine Ref.10
Modified residue9141Phosphothreonine Ref.15
Modified residue9161Phosphoserine Ref.6 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 77MASDAVQ → MAEANNPSEQELE in isoform 2.
VSP_038143
Natural variant1851R → C in a metastatic melanoma sample; somatic mutation. Ref.19
VAR_042337
Natural variant1971A → E
VAR_042338
Natural variant4361R → W: dbSNP rs35132656. Ref.19
VAR_042339
Natural variant5201R → Q: dbSNP rs56273055. Ref.19
VAR_042340
Natural variant5551L → I: dbSNP rs34309238. Ref.19 Ref.3
VAR_042341
Natural variant6351R → Q: dbSNP rs35416389. Ref.19
VAR_042342
Natural variant7181I → V: dbSNP rs2230539. Ref.19 Ref.5
VAR_042343
Natural variant8731F → L in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.19
VAR_042344
Natural variant9011V → I: dbSNP rs10846. Ref.19 Ref.3 Ref.4
VAR_014937
Natural variant9211A → V in a colorectal adenocarcinoma sample; somatic mutation. Ref.19
VAR_042345

Experimental info

Mutagenesis6441K → R: Substantial reduction of autophosphorylation. Ref.1
Sequence conflict1911G → D in AAB33345. Ref.2
Sequence conflict1911G → D in AAC50209. Ref.2
Sequence conflict5621S → P in BAG36611. Ref.3
Sequence conflict7361I → T Ref.5
Sequence conflict7501T → A Ref.5
Sequence conflict8001G → A Ref.5
Sequence conflict8121E → G in BAG36611. Ref.3
Sequence conflict8871L → P in BAG53845. Ref.3

Secondary structure

............. 942
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 61360295EC70BB8E

FASTA942103,932
        10         20         30         40         50         60 
MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR 

        70         80         90        100        110        120 
RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL PDPAATHDGP QSPGAGGPTC 

       130        140        150        160        170        180 
SATNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSTKDR KLLLTAQQML QDSKTKIDII 

       190        200        210        220        230        240 
RMQLRRALQA GQLENQAAPD DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS 

       250        260        270        280        290        300 
AAKAPDRKAV SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF 

       310        320        330        340        350        360 
STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG PGTPDSRPPF 

       370        380        390        400        410        420 
LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT VVGQTSWKPC GPNAWDQSFT 

       430        440        450        460        470        480 
LELERARELE LAVFWRDQRG LCALKFLKLE DFLDNERHEV QLDMEPQGCL VAEVTFRNPV 

       490        500        510        520        530        540 
IERIPRLRRQ KKIFSKQQGK AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS 

       550        560        570        580        590        600 
EARTTGDISV EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA 

       610        620        630        640        650        660 
LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD IVARDEVESL 

       670        680        690        700        710        720 
MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG GDLMLHIHSD VFSEPRAIFY 

       730        740        750        760        770        780 
SACVVLGLQF LHEHKIVYRD LKLDNLLLDT EGYVKIADFG LCKEGMGYGD RTSTFCGTPE 

       790        800        810        820        830        840 
FLAPEVLTDT SYTRAVDWWG LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA 

       850        860        870        880        890        900 
EAIGIMRRLL RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD 

       910        920        930        940 
VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC 

« Hide

Isoform 2.

Checksum: 882D58AABCFDCEE1
Show »

FASTA948104,673

References

« Hide 'large scale' references
[1]"A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C."
Mukai H., Ono Y.
Biochem. Biophys. Res. Commun. 199:897-904(1994) [PubMed: 8135837] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-644.
Tissue: Hippocampus.
[2]"Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family."
Palmer R.H., Ridden J., Parker P.J.
Eur. J. Biochem. 227:344-351(1995) [PubMed: 7851406] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[3]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ILE-555 AND ILE-901.
Tissue: Kidney, Synovium and Thymus.
[4]"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] (ISOFORM 1), VARIANT ILE-901.
Tissue: Brain.
[5]"Identification of multiple, novel, protein kinase C-related gene products."
Palmer R.H., Ridden J., Parker P.J.
FEBS Lett. 356:5-8(1994) [PubMed: 7988719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 700-800 (ISOFORMS 1/2), VARIANT VAL-718.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562 AND SER-916, MASS SPECTROMETRY.
[10]"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-778, MASS SPECTROMETRY.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; THR-353; SER-533; SER-537; SER-559 AND SER-916, MASS SPECTROMETRY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559; SER-562 AND SER-916, MASS SPECTROMETRY.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559; SER-561; SER-562 AND SER-916, MASS SPECTROMETRY.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537; SER-559; SER-562; THR-914 AND SER-916, MASS SPECTROMETRY.
Tissue: T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, MASS SPECTROMETRY.
[17]"Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
J. Struct. Biol. 126:166-170(1999) [PubMed: 10388627] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
[18]"Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)."
Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y., Parker P.J., Blundell T.L., Mott H.R.
J. Biol. Chem. 278:50578-50587(2003) [PubMed: 14514689] [Abstract]
Cited for: STRUCTURE BY NMR OF 116-199.
[19]"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. expand/collapse author list , 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] CYS-185; GLU-197; TRP-436; GLN-520; ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26181 mRNA. Translation: BAA05169.1.
S75546 mRNA. Translation: AAB33345.1.
U33053 mRNA. Translation: AAC50209.1.
AK123007 mRNA. Translation: BAG53845.1.
AK292130 mRNA. Translation: BAF84819.1.
AK313886 mRNA. Translation: BAG36611.1.
BC040061 mRNA. Translation: AAH40061.1.
IPIIPI00002803.
IPI00412672.
PIRJC2129.
S51162.
RefSeqNP_002732.3.
NP_998725.1.
UniGeneHs.466044

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXZX-ray2.20B13-98[»]
1URFNMR-A122-199[»]
2RMKNMR-B122-199[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ16512. 9 interactions.
STRINGQ16512.

PTM databases

PhosphoSiteQ16512.

Proteomic databases

PRIDEQ16512.

Genome annotation databases

EnsemblENST00000242783; ENSP00000242783; ENSG00000123143; Homo sapiens. [Genome view]
ENST00000342216; ENSP00000343325; ENSG00000123143; Homo sapiens. [Genome view]
GeneID5585.
KEGGhsa:5585.

Organism-specific databases

CTD5585.
GeneCardsGC19P014406.
H-InvDBHIX0027472.
HGNCHGNC:9405. PKN1.
HPACAB010278.
HPA003982.
MIM601032. gene.
PharmGKBPA33769.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11664.
HOVERGENQ16512.
OMATRAGHPF.

Enzyme and pathway databases

BRENDA2.7.11.13. 247.
Pathway_Interaction_DBar_tf_pathway. Regulation of Androgen receptor activity.
p38gammadeltapathway. Signaling mediated by p38-gamma and p38-delta.

Gene expression databases

ArrayExpressQ16512.
BgeeQ16512.
CleanExHS_PKN1.
GenevestigatorQ16512.
GermOnlineENSG00000123143. Homo sapiens.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR000861. HR1-like_rho-bd.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
Gene3DG3DSA:1.10.287.160. HR1_rho-bd. 3 hits.
PfamPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21660.
PMAP-CutDBQ16512.
SOURCESearch...

Entry information

Entry namePKN1_HUMAN
AccessionPrimary (citable) accession number: Q16512
Secondary accession number(s): A8K7W5 expand/collapse secondary AC list , B2R9R4, B3KVN3, Q15143, Q8IUV5, Q9UD44
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 22, 2009
Last modified: January 19, 2010
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents