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Q9VPC0 (KP58_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PITSLRE

EC=2.7.11.22
Alternative name(s):
Cell division cycle 2-like
Gene names
Name:Pitslre
ORF Names:CG4268
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length952 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a negative regulator of the normal cell cycle progression. May function in regulating proliferation by the phosphorylation and subsequent plasma membrane targeting of galactosyltransferase By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + a protein tyrosine = ADP + protein tyrosine phosphate.

Subcellular location

Nucleus Potential.

Tissue specificity

Present throughout the early embryo. In late embryos levels are highest in the CNS. Ref.1

Developmental stage

Expressed both maternally and zygotically. Highest levels in early embryogenesis (0-6 hours), low levels during later embryogenesis, moderate levels in pupae and adults. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAM75018.1 differs from that shown. Reason: Intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 952952Serine/threonine-protein kinase PITSLRE
PRO_0000086160

Regions

Domain558 – 851294Protein kinase
Nucleotide binding564 – 5729ATP By similarity
Motif51 – 566Nuclear localization signal Potential
Compositional bias92 – 14655His-rich
Compositional bias386 – 504119Ser-rich

Sites

Active site6851Proton acceptor By similarity
Binding site5871ATP By similarity

Amino acid modifications

Modified residue4391Phosphoserine Ref.7
Modified residue4421Phosphoserine Ref.7
Modified residue4471Phosphotyrosine Ref.7
Modified residue4491Phosphoserine Ref.7
Modified residue8811Phosphoserine Ref.7
Modified residue8861Phosphoserine Ref.7

Experimental info

Sequence conflict691D → E in CAA67863. Ref.1
Sequence conflict2231V → A in CAA67863. Ref.1
Sequence conflict2831I → S in CAA67863. Ref.1
Sequence conflict4921V → A in CAA67863. Ref.1
Sequence conflict5841V → E Ref.6
Sequence conflict6031L → R Ref.6
Sequence conflict6121G → GG Ref.6
Sequence conflict6701Missing Ref.6
Sequence conflict6801Missing Ref.6
Sequence conflict7171Missing Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9VPC0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9CBDE8D459D0713D

FASTA952108,838
        10         20         30         40         50         60 
MVNSSGSEDG QLRSPNDVHY HSRGEEDEHE GDADALYIQP PQASRESGSG PRREKKKHSR 

        70         80         90        100        110        120 
ERRRHKERDD VGGAALALER DHRYDYRSRE EHYHHHQRER SSNAAAAYAK HHLGHAYHYP 

       130        140        150        160        170        180 
QPPQQQQQPL PPAPSYAAHH YHHHQHLSGA RAAPREYHSY PSGYHSGSRH GDYPMEEPTR 

       190        200        210        220        230        240 
RSSKYAESKD AESLEQDLRS RLLKKRHNYV KDYETEENYE HRVERSDRRE GGRKERERTV 

       250        260        270        280        290        300 
RSTHKQNRHD RVIELLDSPE QEHHHQHQHK SHRSKWREEV EVIRRKVPED LELLARREKL 

       310        320        330        340        350        360 
LAAERESRQR KQTAREELEA RRELLRERNE HSDALSPTTV AASVTAGLNI HVKRKSKPDN 

       370        380        390        400        410        420 
YEKEIKLKKR REDDIEVIRD DDDEESEESD SNEEVPEQDS EGSATESGSE DSYASKKKSK 

       430        440        450        460        470        480 
IKSKSQLEDD DEDLPLPDSP LSVGELYKSP KQRQRSRSVS SKSSSQSSRS SRSRSRSRSQ 

       490        500        510        520        530        540 
SSLEDEVDRQ DVGADASPSS STRSEERGMT QEQPEEKPEE KLKEKQKSLE EQIPCDDKGI 

       550        560        570        580        590        600 
PLPNYYPGVQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKRT NEIVALKRLK MEKEKEGFPI 

       610        620        630        640        650        660 
TSLREINTLL KGQHPNIVTV REIVVGSNMD KIFIVMDYVE HDLKSLMETM KNRKQSFFPG 

       670        680        690        700        710        720 
EVKCLTQQLL RAVAHLHDNW ILHRDLKTSN LLLSHKGILK VGDFGLAREY GSPIKKYTSL 

       730        740        750        760        770        780 
VVTLWYRAPE LLLCSPVYST PIDVWSVGCI FAEFLQMLPL FPGKSEIDEL NRIFKELGTP 

       790        800        810        820        830        840 
NEKIWPGYTE LPAVKNMLSQ NSQFTEYPVS QLRKHFQEKT SEMGLSLLQG LLTYDPKQRL 

       850        860        870        880        890        900 
SADAALKHGF FKELPLPIDP SMFPTWPAKS ELGARKAQAS SPKPPSGGSQ FKQLGRDEPI 

       910        920        930        940        950 
IVGPGNKLSS GIITGNKKSH GAGGSSASTG FVLNAGITQR QLAMGPGFSL KF 

« Hide

References

« Hide 'large scale' references
[1]"Novel members of the cdc2-related kinase family in Drosophila: cdk4/6, cdk5, PFTAIRE, and PITSLRE kinase."
Sauer K., Weigmann K., Sigrist S., Lehner C.F.
Mol. Biol. Cell 7:1759-1769(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Embryo.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-952.
Strain: Berkeley.
Tissue: Head.
[6]"Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase."
Biggs W.H. III, Zipursky S.L.
Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 571-722.
Tissue: Imaginal disk.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-442; TYR-447; SER-449; SER-881 AND SER-886, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99513 mRNA. Translation: CAA67863.1.
AE014296 Genomic DNA. Translation: AAF51635.1.
AE014296 Genomic DNA. Translation: AAN12141.1.
BT016092 mRNA. Translation: AAV36977.1.
AY128425 mRNA. Translation: AAM75018.1. Sequence problems.
RefSeqNP_001246851.1. NM_001259922.2.
NP_001246852.1. NM_001259923.2.
NP_001262122.1. NM_001275193.1.
NP_649251.2. NM_140994.4.
NP_730563.1. NM_168869.3.
UniGeneDm.1019.

3D structure databases

ProteinModelPortalQ9VPC0.
SMRQ9VPC0. Positions 555-885.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9VPC0. 2 interactions.

Proteomic databases

PaxDbQ9VPC0.
PRIDEQ9VPC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078247; FBpp0077905; FBgn0016696.
FBtr0078250; FBpp0077908; FBgn0016696.
GeneID40292.
KEGGdme:Dmel_CG4268.
UCSCCG4268-RC. d. melanogaster.

Organism-specific databases

CTD40292.
FlyBaseFBgn0016696. Pitslre.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000114964.
InParanoidQ9VPC0.
KOK08818.
OMAFPGEVKC.
OrthoDBEOG74BJS4.
PhylomeDBQ9VPC0.

Enzyme and pathway databases

BRENDA2.7.11.22. 1994.
SignaLinkQ9VPC0.

Gene expression databases

BgeeQ9VPC0.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40292.
NextBio818015.
PROQ9VPC0.

Entry information

Entry nameKP58_DROME
AccessionPrimary (citable) accession number: Q9VPC0
Secondary accession number(s): Q5U100 expand/collapse secondary AC list , Q8MQR7, Q94889, Q9TXB3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase