Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9VPC0

- KP58_DROME

UniProt

Q9VPC0 - KP58_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine/threonine-protein kinase PITSLRE

Gene

Pitslre

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei587 – 5871ATPPROSITE-ProRule annotation
Active sitei685 – 6851Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi564 – 5729ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. protein serine/threonine kinase activity Source: FlyBase

GO - Biological processi

  1. cell adhesion Source: FlyBase
  2. mitotic cell cycle Source: FlyBase
  3. protein phosphorylation Source: FlyBase
  4. regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 1994.
SignaLinkiQ9VPC0.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PITSLRE (EC:2.7.11.22)
Alternative name(s):
Cell division cycle 2-like
Gene namesi
Name:Pitslre
ORF Names:CG4268
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0016696. Pitslre.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 952952Serine/threonine-protein kinase PITSLREPRO_0000086160Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei439 – 4391Phosphoserine1 Publication
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei447 – 4471Phosphotyrosine1 Publication
Modified residuei449 – 4491Phosphoserine1 Publication
Modified residuei881 – 8811Phosphoserine1 Publication
Modified residuei886 – 8861Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VPC0.
PRIDEiQ9VPC0.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiQ9VPC0.
ExpressionAtlasiQ9VPC0. differential.

Interactioni

Protein-protein interaction databases

IntActiQ9VPC0. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9VPC0.
SMRiQ9VPC0. Positions 529-901.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini558 – 851294Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 566Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 14655His-richAdd
BLAST
Compositional biasi386 – 504119Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120511.
InParanoidiQ9VPC0.
KOiK08818.
OMAiFPGEVKC.
OrthoDBiEOG74BJS4.
PhylomeDBiQ9VPC0.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VPC0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVNSSGSEDG QLRSPNDVHY HSRGEEDEHE GDADALYIQP PQASRESGSG
60 70 80 90 100
PRREKKKHSR ERRRHKERDD VGGAALALER DHRYDYRSRE EHYHHHQRER
110 120 130 140 150
SSNAAAAYAK HHLGHAYHYP QPPQQQQQPL PPAPSYAAHH YHHHQHLSGA
160 170 180 190 200
RAAPREYHSY PSGYHSGSRH GDYPMEEPTR RSSKYAESKD AESLEQDLRS
210 220 230 240 250
RLLKKRHNYV KDYETEENYE HRVERSDRRE GGRKERERTV RSTHKQNRHD
260 270 280 290 300
RVIELLDSPE QEHHHQHQHK SHRSKWREEV EVIRRKVPED LELLARREKL
310 320 330 340 350
LAAERESRQR KQTAREELEA RRELLRERNE HSDALSPTTV AASVTAGLNI
360 370 380 390 400
HVKRKSKPDN YEKEIKLKKR REDDIEVIRD DDDEESEESD SNEEVPEQDS
410 420 430 440 450
EGSATESGSE DSYASKKKSK IKSKSQLEDD DEDLPLPDSP LSVGELYKSP
460 470 480 490 500
KQRQRSRSVS SKSSSQSSRS SRSRSRSRSQ SSLEDEVDRQ DVGADASPSS
510 520 530 540 550
STRSEERGMT QEQPEEKPEE KLKEKQKSLE EQIPCDDKGI PLPNYYPGVQ
560 570 580 590 600
GCRSVEEFQC LNRIEEGTYG VVYRAKDKRT NEIVALKRLK MEKEKEGFPI
610 620 630 640 650
TSLREINTLL KGQHPNIVTV REIVVGSNMD KIFIVMDYVE HDLKSLMETM
660 670 680 690 700
KNRKQSFFPG EVKCLTQQLL RAVAHLHDNW ILHRDLKTSN LLLSHKGILK
710 720 730 740 750
VGDFGLAREY GSPIKKYTSL VVTLWYRAPE LLLCSPVYST PIDVWSVGCI
760 770 780 790 800
FAEFLQMLPL FPGKSEIDEL NRIFKELGTP NEKIWPGYTE LPAVKNMLSQ
810 820 830 840 850
NSQFTEYPVS QLRKHFQEKT SEMGLSLLQG LLTYDPKQRL SADAALKHGF
860 870 880 890 900
FKELPLPIDP SMFPTWPAKS ELGARKAQAS SPKPPSGGSQ FKQLGRDEPI
910 920 930 940 950
IVGPGNKLSS GIITGNKKSH GAGGSSASTG FVLNAGITQR QLAMGPGFSL

KF
Length:952
Mass (Da):108,838
Last modified:May 1, 2000 - v1
Checksum:i9CBDE8D459D0713D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691D → E in CAA67863. (PubMed:8930898)Curated
Sequence conflicti223 – 2231V → A in CAA67863. (PubMed:8930898)Curated
Sequence conflicti283 – 2831I → S in CAA67863. (PubMed:8930898)Curated
Sequence conflicti492 – 4921V → A in CAA67863. (PubMed:8930898)Curated
Sequence conflicti584 – 5841V → E(PubMed:1378625)Curated
Sequence conflicti603 – 6031L → R(PubMed:1378625)Curated
Sequence conflicti612 – 6121G → GG(PubMed:1378625)Curated
Sequence conflicti670 – 6701Missing(PubMed:1378625)Curated
Sequence conflicti680 – 6801Missing(PubMed:1378625)Curated
Sequence conflicti717 – 7171Missing(PubMed:1378625)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_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.
UniGeneiDm.1019.

Genome annotation databases

EnsemblMetazoaiFBtr0078247; FBpp0077905; FBgn0016696.
FBtr0078250; FBpp0077908; FBgn0016696.
GeneIDi40292.
KEGGidme:Dmel_CG4268.
UCSCiCG4268-RC. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqi NP_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.
UniGenei Dm.1019.

3D structure databases

ProteinModelPortali Q9VPC0.
SMRi Q9VPC0. Positions 529-901.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9VPC0. 2 interactions.

Proteomic databases

PaxDbi Q9VPC0.
PRIDEi Q9VPC0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0078247 ; FBpp0077905 ; FBgn0016696 .
FBtr0078250 ; FBpp0077908 ; FBgn0016696 .
GeneIDi 40292.
KEGGi dme:Dmel_CG4268.
UCSCi CG4268-RC. d. melanogaster.

Organism-specific databases

CTDi 40292.
FlyBasei FBgn0016696. Pitslre.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120511.
InParanoidi Q9VPC0.
KOi K08818.
OMAi FPGEVKC.
OrthoDBi EOG74BJS4.
PhylomeDBi Q9VPC0.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 1994.
SignaLinki Q9VPC0.

Miscellaneous databases

GenomeRNAii 40292.
NextBioi 818015.
PROi Q9VPC0.

Gene expression databases

Bgeei Q9VPC0.
ExpressionAtlasi Q9VPC0. differential.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiKP58_DROME
AccessioniPrimary (citable) accession number: Q9VPC0
Secondary accession number(s): Q5U100
, Q8MQR7, Q94889, Q9TXB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3