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Protein

cGMP-dependent protein kinase 2

Gene

PRKG2

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

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Binding of cGMP results in enzyme activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei482 – 4821ATPPROSITE-ProRule annotation
Active sitei576 – 5761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 285118cGMP 1Add
BLAST
Nucleotide bindingi286 – 417132cGMP 2Add
BLAST
Nucleotide bindingi459 – 4679ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cGMP binding Source: UniProtKB-KW
  • cGMP-dependent protein kinase activity Source: UniProtKB-EC
  • protein kinase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.12. 2681.
ReactomeiR-HSA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-HSA-4086398. Ca2+ pathway.
R-HSA-418457. cGMP effects.
SignaLinkiQ13237.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent protein kinase 2 (EC:2.7.11.12)
Short name:
cGK 2
Short name:
cGK2
Alternative name(s):
cGMP-dependent protein kinase II
Short name:
cGKII
Gene namesi
Name:PRKG2
Synonyms:PRKGR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9416. PRKG2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33778.

Chemistry

ChEMBLiCHEMBL2896.
GuidetoPHARMACOLOGYi1493.

Polymorphism and mutation databases

DMDMi6226833.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 762761cGMP-dependent protein kinase 2PRO_0000086123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei609 – 6091PhosphothreonineBy similarity

Post-translational modificationi

Myristoylation mediates membrane localization.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiQ13237.
PaxDbiQ13237.
PRIDEiQ13237.

PTM databases

iPTMnetiQ13237.
PhosphoSiteiQ13237.

Expressioni

Tissue specificityi

Highly concentrated in brain, lung and intestinal mucosa.

Gene expression databases

BgeeiQ13237.
CleanExiHS_PRKG2.
ExpressionAtlasiQ13237. baseline and differential.
GenevisibleiQ13237. HS.

Organism-specific databases

HPAiCAB018739.
HPA007386.

Interactioni

Protein-protein interaction databases

BioGridi111579. 7 interactions.
IntActiQ13237. 3 interactions.
STRINGi9606.ENSP00000264399.

Chemistry

BindingDBiQ13237.

Structurei

Secondary structure

1
762
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi153 – 16412Combined sources
Helixi169 – 1713Combined sources
Helixi174 – 18310Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi204 – 2118Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi230 – 2323Combined sources
Helixi233 – 2386Combined sources
Beta strandi243 – 2508Combined sources
Beta strandi252 – 2587Combined sources
Helixi259 – 2668Combined sources
Helixi270 – 28314Combined sources
Helixi285 – 2873Combined sources
Helixi292 – 30110Combined sources
Beta strandi303 – 3075Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi323 – 33513Combined sources
Beta strandi344 – 3507Combined sources
Helixi357 – 3626Combined sources
Beta strandi368 – 3725Combined sources
Beta strandi377 – 3826Combined sources
Helixi384 – 3896Combined sources
Turni390 – 3934Combined sources
Helixi395 – 41521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BV6X-ray1.94A269-418[»]
5C6CX-ray2.05A/B137-277[»]
5C8WX-ray1.80A/B/C/D/E/F137-277[»]
ProteinModelPortaliQ13237.
SMRiQ13237. Positions 47-762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini453 – 711259Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini712 – 76251AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000233033.
HOVERGENiHBG006211.
InParanoidiQ13237.
KOiK19477.
OMAiELQSKCI.
OrthoDBiEOG75B84Q.
PhylomeDBiQ13237.
TreeFamiTF313261.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSiPR00104. CGMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q13237-1) [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
MGNGSVKPKH SKHPDGHSGN LTTDALRNKV TELERELRRK DAEIQEREYH
60 70 80 90 100
LKELREQLSK QTVAIAELTE ELQNKCIQLN KLQDVVHMQG GSPLQASPDK
110 120 130 140 150
VPLEVHRKTS GLVSLHSRRG AKAGVSAEPT TRTYDLNKPP EFSFEKARVR
160 170 180 190 200
KDSSEKKLIT DALNKNQFLK RLDPQQIKDM VECMYGRNYQ QGSYIIKQGE
210 220 230 240 250
PGNHIFVLAE GRLEVFQGEK LLSSIPMWTT FGELAILYNC TRTASVKAIT
260 270 280 290 300
NVKTWALDRE VFQNIMRRTA QARDEQYRNF LRSVSLLKNL PEDKLTKIID
310 320 330 340 350
CLEVEYYDKG DYIIREGEEG STFFILAKGK VKVTQSTEGH DQPQLIKTLQ
360 370 380 390 400
KGEYFGEKAL ISDDVRSANI IAEENDVACL VIDRETFNQT VGTFEELQKY
410 420 430 440 450
LEGYVANLNR DDEKRHAKRS MSNWKLSKAL SLEMIQLKEK VARFSSSSPF
460 470 480 490 500
QNLEIIATLG VGGFGRVELV KVKNENVAFA MKCIRKKHIV DTKQQEHVYS
510 520 530 540 550
EKRILEELCS PFIVKLYRTF KDNKYVYMLL EACLGGELWS ILRDRGSFDE
560 570 580 590 600
PTSKFCVACV TEAFDYLHRL GIIYRDLKPE NLILDAEGYL KLVDFGFAKK
610 620 630 640 650
IGSGQKTWTF CGTPEYVAPE VILNKGHDFS VDFWSLGILV YELLTGNPPF
660 670 680 690 700
SGVDQMMTYN LILKGIEKMD FPRKITRRPE DLIRRLCRQN PTERLGNLKN
710 720 730 740 750
GINDIKKHRW LNGFNWEGLK ARSLPSPLQR ELKGPIDHSY FDKYPPEKGM
760
PPDELSGWDK DF
Length:762
Mass (Da):87,432
Last modified:November 1, 1996 - v1
Checksum:iFA7BA149906B5996
GO
Isoform 2 (identifier: Q13237-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     441-469: Missing.

Note: No experimental confirmation available.
Show »
Length:733
Mass (Da):84,398
Checksum:i913712AC4EC4F8BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 582QL → HG in BAA18934 (PubMed:7498513).Curated
Sequence conflicti154 – 1541S → I in CAA76073 (PubMed:9535793).Curated
Sequence conflicti388 – 3881N → D in BAG60035 (PubMed:14702039).Curated
Sequence conflicti460 – 4601G → A in BAA18934 (PubMed:7498513).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221T → S.
Corresponds to variant rs34956759 [ dbSNP | Ensembl ].
VAR_051633
Natural varianti106 – 1061H → R.1 Publication
Corresponds to variant rs34616910 [ dbSNP | Ensembl ].
VAR_040608
Natural varianti716 – 7161W → R in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040609

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei441 – 46929Missing in isoform 2. 1 PublicationVSP_055121Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94612 mRNA. Translation: CAA64318.1.
D70899 mRNA. Translation: BAA18934.1.
AK297673 mRNA. Translation: BAG60035.1.
AC098819 Genomic DNA. No translation available.
AC139722 Genomic DNA. No translation available.
Y16106
, Y16107, Y16108, Y16109, Y16110, Y16111, Y16112, Y16113, Y16114, Y16115, Y16116, Y16117, Y16118, Y16119, Y16120, Y16121, Y16122, Y16123 Genomic DNA. Translation: CAA76073.1.
CCDSiCCDS3589.1. [Q13237-1]
CCDS64005.1. [Q13237-2]
PIRiS68217.
RefSeqiNP_001269409.1. NM_001282480.1.
NP_001269410.1. NM_001282481.1.
NP_001269411.1. NM_001282482.1.
NP_001269412.1. NM_001282483.1.
NP_001269414.1. NM_001282485.1. [Q13237-2]
NP_006250.1. NM_006259.2. [Q13237-1]
XP_005263183.1. XM_005263126.2. [Q13237-1]
XP_011530416.1. XM_011532114.1. [Q13237-1]
XP_011530417.1. XM_011532115.1. [Q13237-1]
UniGeneiHs.232044.
Hs.570833.
Hs.739943.

Genome annotation databases

EnsembliENST00000264399; ENSP00000264399; ENSG00000138669. [Q13237-1]
ENST00000395578; ENSP00000378945; ENSG00000138669. [Q13237-1]
ENST00000628926; ENSP00000486129; ENSG00000138669. [Q13237-2]
GeneIDi5593.
KEGGihsa:5593.
UCSCiuc003hmh.3. human. [Q13237-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94612 mRNA. Translation: CAA64318.1.
D70899 mRNA. Translation: BAA18934.1.
AK297673 mRNA. Translation: BAG60035.1.
AC098819 Genomic DNA. No translation available.
AC139722 Genomic DNA. No translation available.
Y16106
, Y16107, Y16108, Y16109, Y16110, Y16111, Y16112, Y16113, Y16114, Y16115, Y16116, Y16117, Y16118, Y16119, Y16120, Y16121, Y16122, Y16123 Genomic DNA. Translation: CAA76073.1.
CCDSiCCDS3589.1. [Q13237-1]
CCDS64005.1. [Q13237-2]
PIRiS68217.
RefSeqiNP_001269409.1. NM_001282480.1.
NP_001269410.1. NM_001282481.1.
NP_001269411.1. NM_001282482.1.
NP_001269412.1. NM_001282483.1.
NP_001269414.1. NM_001282485.1. [Q13237-2]
NP_006250.1. NM_006259.2. [Q13237-1]
XP_005263183.1. XM_005263126.2. [Q13237-1]
XP_011530416.1. XM_011532114.1. [Q13237-1]
XP_011530417.1. XM_011532115.1. [Q13237-1]
UniGeneiHs.232044.
Hs.570833.
Hs.739943.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BV6X-ray1.94A269-418[»]
5C6CX-ray2.05A/B137-277[»]
5C8WX-ray1.80A/B/C/D/E/F137-277[»]
ProteinModelPortaliQ13237.
SMRiQ13237. Positions 47-762.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111579. 7 interactions.
IntActiQ13237. 3 interactions.
STRINGi9606.ENSP00000264399.

Chemistry

BindingDBiQ13237.
ChEMBLiCHEMBL2896.
GuidetoPHARMACOLOGYi1493.

PTM databases

iPTMnetiQ13237.
PhosphoSiteiQ13237.

Polymorphism and mutation databases

DMDMi6226833.

Proteomic databases

MaxQBiQ13237.
PaxDbiQ13237.
PRIDEiQ13237.

Protocols and materials databases

DNASUi5593.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264399; ENSP00000264399; ENSG00000138669. [Q13237-1]
ENST00000395578; ENSP00000378945; ENSG00000138669. [Q13237-1]
ENST00000628926; ENSP00000486129; ENSG00000138669. [Q13237-2]
GeneIDi5593.
KEGGihsa:5593.
UCSCiuc003hmh.3. human. [Q13237-1]

Organism-specific databases

CTDi5593.
GeneCardsiPRKG2.
HGNCiHGNC:9416. PRKG2.
HPAiCAB018739.
HPA007386.
MIMi601591. gene.
neXtProtiNX_Q13237.
PharmGKBiPA33778.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000233033.
HOVERGENiHBG006211.
InParanoidiQ13237.
KOiK19477.
OMAiELQSKCI.
OrthoDBiEOG75B84Q.
PhylomeDBiQ13237.
TreeFamiTF313261.

Enzyme and pathway databases

BRENDAi2.7.11.12. 2681.
ReactomeiR-HSA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-HSA-4086398. Ca2+ pathway.
R-HSA-418457. cGMP effects.
SignaLinkiQ13237.

Miscellaneous databases

GenomeRNAii5593.
NextBioi21704.
PROiQ13237.
SOURCEiSearch...

Gene expression databases

BgeeiQ13237.
CleanExiHS_PRKG2.
ExpressionAtlasiQ13237. baseline and differential.
GenevisibleiQ13237. HS.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSiPR00104. CGMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, cDNA structure, and chromosomal localization of the human type II cGMP-dependent protein kinase."
    Orstavik S., Solberg R., Taskn K., Nordahl M., Altherr M.R., Hansson V., Jahnsen T., Sandberg M.
    Biochem. Biophys. Res. Commun. 220:759-765(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression of the human cGMP-dependent protein kinase II gene is lost upon introduction of SV40 T antigen or immortalization in human cells."
    Fujii M., Ogata T., Takahashi E., Yamada K., Nakabayashi K., Oishi M., Ayusawa D.
    FEBS Lett. 375:263-267(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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] (ISOFORM 2).
    Tissue: Heart.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Characterization of the gene encoding the human type II cGMP-dependent protein kinase."
    Witczak O., Orstavik S., Natarajan V., Frengen E., Jahnsen T., Sandberg M.
    Biochem. Biophys. Res. Commun. 245:113-119(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-734.
  6. "N-terminal myristoylation is required for membrane localization of cGMP-dependent protein kinase type II."
    Vaandrager A.B., Ehlert E.M., Jarchau T., Lohmann S.M., de Jonge H.R.
    J. Biol. Chem. 271:7025-7029(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-106 AND ARG-716.

Entry informationi

Entry nameiKGP2_HUMAN
AccessioniPrimary (citable) accession number: Q13237
Secondary accession number(s): B4DMX3
, E7EPE6, O00125, O60916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 13, 2016
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 4
    Human chromosome 4: 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.