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Q16513

- PKN2_HUMAN

UniProt

Q16513 - PKN2_HUMAN

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Protein

Serine/threonine-protein kinase N2

Gene

PKN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication.10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Kinase activity is activated upon binding to GTP-bound Rhoa/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-816 (activation loop of the kinase domain) and Thr-958 (turn motif), need to be phosphorylated for its full activation.3 Publications

Kineticsi

  1. KM=15.83 µM for HDAC51 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei117 – 1182Cleavage; by caspase-3
Binding sitei686 – 6861ATPPROSITE-ProRule annotation
Sitei700 – 7012Cleavage; by caspase-3
Active sitei782 – 7821Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi663 – 6719ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone deacetylase binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein kinase C activity Source: UniProtKB-EC
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apical junction assembly Source: UniProtKB
  2. apoptotic process Source: UniProtKB-KW
  3. cell adhesion Source: UniProtKB-KW
  4. cell cycle Source: UniProtKB-KW
  5. cell division Source: UniProtKB-KW
  6. epithelial cell migration Source: UniProtKB
  7. positive regulation of cytokinesis Source: UniProtKB
  8. positive regulation of mitotic cell cycle Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. regulation of cell motility Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB-KW
  12. signal transduction Source: ProtInc
  13. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell adhesion, Cell cycle, Cell division, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
SignaLinkiQ16513.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase N2 (EC:2.7.11.13)
Alternative name(s):
PKN gamma
Protein kinase C-like 2
Protein-kinase C-related kinase 2
Gene namesi
Name:PKN2
Synonyms:PRK2, PRKCL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9406. PKN2.

Subcellular locationi

Cytoplasm. Nucleus. Membrane By similarity. Cell projectionlamellipodium. Cytoplasmcytoskeleton. Cleavage furrow. Midbody. Cell junction
Note: Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells. In the course of viral infection, colocalizes with HCV NS5B at perinuclear region in the cytoplasm.

GO - Cellular componenti

  1. apical junction complex Source: UniProtKB
  2. centrosome Source: HPA
  3. cleavage furrow Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. intermediate filament cytoskeleton Source: HPA
  6. lamellipodium Source: UniProtKB
  7. membrane Source: UniProtKB-KW
  8. midbody Source: UniProtKB
  9. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171D → A: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700. 2 Publications
Mutagenesisi686 – 6861K → R: Does not inhibit interaction with PTPN13. 1 Publication
Mutagenesisi700 – 7001D → E: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117. 2 Publications
Mutagenesisi816 – 8161T → A: Reduces catalytic activity. 1 Publication
Mutagenesisi958 – 9581T → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi974 – 9741F → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 1 Publication
Mutagenesisi977 – 9771F → A or L: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%. 2 Publications
Mutagenesisi977 – 9771F → W or Y: Reduces catalytic activity by 50%. 2 Publications
Mutagenesisi978 – 9781D → A or S: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications
Mutagenesisi978 – 9781D → A: Does not inhibit catalytic activity. 2 Publications
Mutagenesisi979 – 9791Y → A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. 2 Publications
Mutagenesisi979 – 9791Y → A: Reduces catalytic activity by 50%. 2 Publications
Mutagenesisi979 – 9791Y → F, L or W: Reduces catalytic activity by 25%. 2 Publications
Mutagenesisi984 – 9841C → S: Inhibits interaction with PTPN13. 1 Publication

Organism-specific databases

PharmGKBiPA33770.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 984984Serine/threonine-protein kinase N2PRO_0000055722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei110 – 1101Phosphoserine1 Publication
Modified residuei121 – 1211Phosphothreonine1 Publication
Modified residuei124 – 1241Phosphothreonine1 Publication
Modified residuei302 – 3021Phosphoserine3 Publications
Modified residuei306 – 3061Phosphoserine3 Publications
Modified residuei360 – 3601Phosphoserine3 Publications
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei535 – 5351Phosphoserine1 Publication
Modified residuei583 – 5831Phosphoserine1 Publication
Modified residuei628 – 6281Phosphothreonine1 Publication
Modified residuei631 – 6311Phosphoserine1 Publication
Modified residuei816 – 8161Phosphothreonine; by PDPK11 Publication
Modified residuei958 – 9581Phosphothreonine4 Publications

Post-translational modificationi

Autophosphorylated. Phosphorylated during mitosis.7 Publications
Activated by limited proteolysis with trypsin (By similarity). Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death.By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16513.
PaxDbiQ16513.
PRIDEiQ16513.

PTM databases

PhosphoSiteiQ16513.

Miscellaneous databases

PMAP-CutDBQ16513.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in numerous tumor cell lines, especially in bladder tumor cells.2 Publications

Inductioni

Up-regulated during keratinocyte differentiation.1 Publication

Gene expression databases

BgeeiQ16513.
CleanExiHS_PKN2.
ExpressionAtlasiQ16513. baseline and differential.
GenevestigatoriQ16513.

Organism-specific databases

HPAiHPA034861.

Interactioni

Subunit structurei

Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially). Interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially). Interacts with NCK1 (via SH3 domains). Interacts with CD44 (By similarity). Interacts with RHOA (GTP-bound form preferentially) and RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation. Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity. Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity. Interacts (via C-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with HCV NS5B (via N-terminal finger domain). Interacts with NCK1, NCK2 and RHOC.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDK1Q151186EBI-2511350,EBI-7016221

Protein-protein interaction databases

BioGridi111572. 32 interactions.
IntActiQ16513. 16 interactions.
MINTiMINT-198348.
STRINGi9606.ENSP00000359552.

Structurei

Secondary structure

1
984
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi647 – 6493Combined sources
Beta strandi652 – 6543Combined sources
Beta strandi657 – 6659Combined sources
Beta strandi670 – 6767Combined sources
Beta strandi682 – 6898Combined sources
Helixi690 – 6956Combined sources
Helixi699 – 71416Combined sources
Beta strandi723 – 7297Combined sources
Beta strandi732 – 7387Combined sources
Helixi745 – 7495Combined sources
Helixi756 – 77419Combined sources
Turni775 – 7773Combined sources
Helixi785 – 7873Combined sources
Beta strandi788 – 7903Combined sources
Beta strandi796 – 7983Combined sources
Beta strandi805 – 8073Combined sources
Helixi821 – 8233Combined sources
Helixi826 – 8305Combined sources
Helixi838 – 85215Combined sources
Helixi862 – 87110Combined sources
Helixi882 – 89110Combined sources
Helixi896 – 8983Combined sources
Beta strandi903 – 9053Combined sources
Helixi907 – 9115Combined sources
Helixi914 – 9163Combined sources
Helixi921 – 9255Combined sources
Beta strandi944 – 9463Combined sources
Helixi948 – 9514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CRSX-ray2.75A646-984[»]
ProteinModelPortaliQ16513.
SMRiQ16513. Positions 56-107, 136-199, 618-984.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 11976REM 1Add
BLAST
Repeati133 – 21381REM 2Add
BLAST
Repeati214 – 29582REM 3Add
BLAST
Domaini330 – 463134C2Add
BLAST
Domaini657 – 916260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini917 – 98468AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni382 – 46382Necessary to rescue apical junction formationBy similarityAdd
BLAST
Regioni917 – 97761Necessary for the catalytic activityAdd
BLAST
Regioni978 – 9847Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA

Domaini

The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2.
The C1 domain does not bind the diacylglycerol (DAG).
The apoptotic C-terminal cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations.

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 3 REM (Hr1) repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120523.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ16513.
KOiK06071.
OMAiRSQQMFQ.
PhylomeDBiQ16513.
TreeFamiTF102005.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16513-1) [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
MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD
60 70 80 90 100
RIKREIRKEL KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL
110 120 130 140 150
QELNAHIVVS DPEDITDCPR TPDTPNNDPR CSTSNNRLKA LQKQLDIELK
160 170 180 190 200
VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL QDSKTKIEVI RMQILQAVQT
210 220 230 240 250
NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM KLLGSGKVTD
260 270 280 290 300
RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA
310 320 330 340 350
ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK
360 370 380 390 400
ATSVALPGWS PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD
410 420 430 440 450
NTVVGQTSWK PISNQSWDQK FTLELDRSRE LEISVYWRDW RSLCAVKFLR
460 470 480 490 500
LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN PVIERRPKLQ RQKKIFSKQQ
510 520 530 540 550
GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV PTTVPVVDVR
560 570 580 590 600
IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG
610 620 630 640 650
QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF
660 670 680 690 700
QFNLQDFRCC AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD
710 720 730 740 750
SLMCEKRIFE TVNSVRHPFL VNLFACFQTK EHVCFVMEYA AGGDLMMHIH
760 770 780 790 800
TDVFSEPRAV FYAACVVLGL QYLHEHKIVY RDLKLDNLLL DTEGFVKIAD
810 820 830 840 850
FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW WGLGVLIYEM
860 870 880 890 900
LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL
910 920 930 940 950
GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF
960 970 980
TSEAPILTPP REPRILSEEE QEMFRDFDYI ADWC
Length:984
Mass (Da):112,035
Last modified:November 1, 1996 - v1
Checksum:i687EC417A0F51C1D
GO
Isoform 2 (identifier: Q16513-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-390: Missing.

Show »
Length:968
Mass (Da):110,345
Checksum:iBE8D7EDA728D78EE
GO
Isoform 3 (identifier: Q16513-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     428-475: Missing.

Show »
Length:936
Mass (Da):106,217
Checksum:i43128E92FEDC05B4
GO
Isoform 4 (identifier: Q16513-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.

Show »
Length:827
Mass (Da):94,136
Checksum:iB08B24A67D1697CE
GO
Isoform 5 (identifier: Q16513-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-329: LTG → MNS

Show »
Length:658
Mass (Da):75,171
Checksum:iD0B6E1DEA98B3C0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti483 – 4831I → V in BAG62673. (PubMed:14702039)Curated
Sequence conflicti565 – 5651K → R in BAG60783. (PubMed:14702039)Curated
Sequence conflicti625 – 6251K → R in BAG62673. (PubMed:14702039)Curated
Sequence conflicti795 – 7951F → L in AAI25200. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941E → D.
Corresponds to variant rs12039846 [ dbSNP | Ensembl ].
VAR_050562
Natural varianti197 – 1971A → E.
Corresponds to variant rs35207128 [ dbSNP | Ensembl ].
VAR_050563
Natural varianti655 – 6551Q → R.
Corresponds to variant rs12085658 [ dbSNP | Ensembl ].
VAR_050564

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 326326Missing in isoform 5. 1 PublicationVSP_042180Add
BLAST
Alternative sequencei1 – 157157Missing in isoform 4. 1 PublicationVSP_042181Add
BLAST
Alternative sequencei327 – 3293LTG → MNS in isoform 5. 1 PublicationVSP_042182
Alternative sequencei375 – 39016Missing in isoform 2. 1 PublicationVSP_042183Add
BLAST
Alternative sequencei428 – 47548Missing in isoform 3. 1 PublicationVSP_042184Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33052 mRNA. Translation: AAC50208.1.
S75548 mRNA. Translation: AAB33346.1.
AK298595 mRNA. Translation: BAG60783.1.
AK300304 mRNA. Translation: BAG62057.1.
AK301066 mRNA. Translation: BAG62673.1.
AL136381, AC119426 Genomic DNA. Translation: CAI23271.1.
CH471097 Genomic DNA. Translation: EAW73161.1.
CH471097 Genomic DNA. Translation: EAW73164.1.
BC125199 mRNA. Translation: AAI25200.1.
CCDSiCCDS714.1. [Q16513-1]
PIRiS67527.
RefSeqiNP_006247.1. NM_006256.2. [Q16513-1]
XP_005271088.1. XM_005271031.1. [Q16513-2]
UniGeneiHs.440833.

Genome annotation databases

EnsembliENST00000370513; ENSP00000359544; ENSG00000065243. [Q16513-3]
ENST00000370521; ENSP00000359552; ENSG00000065243. [Q16513-1]
GeneIDi5586.
KEGGihsa:5586.
UCSCiuc001dmn.3. human. [Q16513-1]
uc009wcv.3. human. [Q16513-3]
uc010osp.2. human. [Q16513-2]

Polymorphism databases

DMDMi6225859.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33052 mRNA. Translation: AAC50208.1 .
S75548 mRNA. Translation: AAB33346.1 .
AK298595 mRNA. Translation: BAG60783.1 .
AK300304 mRNA. Translation: BAG62057.1 .
AK301066 mRNA. Translation: BAG62673.1 .
AL136381 , AC119426 Genomic DNA. Translation: CAI23271.1 .
CH471097 Genomic DNA. Translation: EAW73161.1 .
CH471097 Genomic DNA. Translation: EAW73164.1 .
BC125199 mRNA. Translation: AAI25200.1 .
CCDSi CCDS714.1. [Q16513-1 ]
PIRi S67527.
RefSeqi NP_006247.1. NM_006256.2. [Q16513-1 ]
XP_005271088.1. XM_005271031.1. [Q16513-2 ]
UniGenei Hs.440833.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4CRS X-ray 2.75 A 646-984 [» ]
ProteinModelPortali Q16513.
SMRi Q16513. Positions 56-107, 136-199, 618-984.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111572. 32 interactions.
IntActi Q16513. 16 interactions.
MINTi MINT-198348.
STRINGi 9606.ENSP00000359552.

Chemistry

BindingDBi Q16513.
ChEMBLi CHEMBL3032.
GuidetoPHARMACOLOGYi 1521.

PTM databases

PhosphoSitei Q16513.

Polymorphism databases

DMDMi 6225859.

Proteomic databases

MaxQBi Q16513.
PaxDbi Q16513.
PRIDEi Q16513.

Protocols and materials databases

DNASUi 5586.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370513 ; ENSP00000359544 ; ENSG00000065243 . [Q16513-3 ]
ENST00000370521 ; ENSP00000359552 ; ENSG00000065243 . [Q16513-1 ]
GeneIDi 5586.
KEGGi hsa:5586.
UCSCi uc001dmn.3. human. [Q16513-1 ]
uc009wcv.3. human. [Q16513-3 ]
uc010osp.2. human. [Q16513-2 ]

Organism-specific databases

CTDi 5586.
GeneCardsi GC01P089149.
HGNCi HGNC:9406. PKN2.
HPAi HPA034861.
MIMi 602549. gene.
neXtProti NX_Q16513.
PharmGKBi PA33770.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120523.
HOGENOMi HOG000233032.
HOVERGENi HBG108317.
InParanoidi Q16513.
KOi K06071.
OMAi RSQQMFQ.
PhylomeDBi Q16513.
TreeFami TF102005.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
SignaLinki Q16513.

Miscellaneous databases

ChiTaRSi PKN2. human.
GeneWikii PKN2.
GenomeRNAii 5586.
NextBioi 21666.
PMAP-CutDB Q16513.
PROi Q16513.
SOURCEi Search...

Gene expression databases

Bgeei Q16513.
CleanExi HS_PKN2.
ExpressionAtlasi Q16513. baseline and differential.
Genevestigatori Q16513.

Family and domain databases

Gene3Di 1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
InterProi IPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
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Publicationsi

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  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: B-cell and Spleen.
  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.
    , 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] (ISOFORMS 2; 4 AND 5).
    Tissue: Placenta and Spleen.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 3).
  7. "Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy."
    Cryns V.L., Byun Y., Rana A., Mellor H., Lustig K.D., Ghanem L., Parker P.J., Kirschner M.W., Yuan J.
    J. Biol. Chem. 272:29449-29453(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-117 AND ASP-700.
  8. "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
    Vincent S., Settleman J.
    Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAC1 AND RHOA, AUTOPHOSPHORYLATION.
  9. "PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2."
    Balendran A., Casamayor A., Deak M., Paterson A., Gaffney P., Currie R., Downes C.P., Alessi D.R.
    Curr. Biol. 9:393-404(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PDPK1, MUTAGENESIS OF PHE-974; PHE-977; ASP-978 AND TYR-979.
  10. "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck."
    Braverman L.E., Quilliam L.A.
    J. Biol. Chem. 274:5542-5549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCK1 AND NCK2, TISSUE SPECIFICITY.
  11. "MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase."
    Sun W., Vincent S., Settleman J., Johnson G.L.
    J. Biol. Chem. 275:24421-24428(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K2.
  12. "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage."
    Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.
    J. Biol. Chem. 275:34451-34458(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, FUNCTION IN AKT1 ACTIVITY INHIBITION, ENZYME REGULATION, INTERACTION WITH AKT1, MUTAGENESIS OF ASP-117 AND ASP-700.
  13. "Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton."
    Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.
    Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-816 BY PDPK1, INTERACTION WITH PDPK1.
  14. "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif."
    Gross C., Heumann R., Erdmann K.S.
    FEBS Lett. 496:101-104(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN13, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-686 AND CYS-984.
  15. "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment."
    Hodgkinson C.P., Sale G.J.
    Biochemistry 41:561-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KINASE ACTIVITY INHIBITION, INTERACTION WITH PDPK1.
  16. "Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion."
    Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P.
    J. Cell Biol. 156:137-148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL ADHESION, INDUCTION.
  17. "Protein kinase C-related kinase 2 regulates hepatitis C virus RNA polymerase function by phosphorylation."
    Kim S.J., Kim J.H., Kim Y.G., Lim H.S., Oh J.W.
    J. Biol. Chem. 279:50031-50041(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HCV REPLICATION, FUNCTION IN PHOSPHORYLATION OF NS5B, INTERACTION WITH HCV NS5B.
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-958, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306 AND SER-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis."
    Schmidt A., Durgan J., Magalhaes A., Hall A.
    EMBO J. 26:1624-1636(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  21. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "The C-terminus of PRK2/PKNgamma is required for optimal activation by RhoA in a GTP-dependent manner."
    Lim W.G., Chen X., Liu J.P., Tan B.J., Zhou S., Smith A., Lees N., Hou L., Gu F., Yu X.Y., Du Y., Smith D., Verma C., Liu K., Duan W.
    Arch. Biochem. Biophys. 479:170-178(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH PDPK1, MUTAGENESIS OF THR-816; THR-958; PHE-977; ASP-978 AND TYR-979.
  23. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-958, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-121; THR-124; SER-302; SER-306; SER-360; SER-362; SER-535; THR-628; SER-631 AND THR-958, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  29. "Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases."
    Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A.
    FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5, BIOPHYSICOCHEMICAL PROPERTIES.
  30. "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-302; SER-306; SER-360; SER-583 AND THR-958, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
    Wallace S.W., Magalhaes A., Hall A.
    Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAC1; RHOA AND RHOC.
  33. "Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration."
    Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S., Collazos A., Parker P.J.
    PLoS ONE 6:E21732-E21732(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPKN2_HUMAN
AccessioniPrimary (citable) accession number: Q16513
Secondary accession number(s): B4DQ21
, B4DTP5, B4DVG1, D3DT24, Q08AF4, Q9H1W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 150 of the entry and version 1 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 1
    Human chromosome 1: 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

External Data

Dasty 3