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Reviewed, UniProtKB/Swiss-Prot Q960Z0 (KI10A_DROME)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kinesin-like protein Klp10A
Alternative name(s):
    Kinesin-like protein at cytological position 10A
Gene names
Name: Klp10A
ORF Names: CG1453
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a "poleward flux". Ref.4

Subcellular location

Centrosome. Note: Localizes to mitotic centrosomes, spindle poles and centromeres through metaphase. However, the centromeric localization diminishes markedly at the onset of anaphase, leaving the majority of the protein on the spindle poles. Concentrated around the minus ends focused at the poles. Ref.4

Disruption phenotype

Marked perturbation of mitotic spindle architecture. Ref.4

Sequence similarities

Belongs to the kinesin-like protein family. MCAK/KIF2 subfamily.

Contains 1 kinesin-motor domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 805805Kinesin-like protein Klp10A
PRO_0000125424

Regions

Domain275 – 540266Kinesin-motor
Nucleotide binding368 – 3758ATP By similarity
Region1 – 274274Globular Potential
Coiled coil205 – 24440 Potential
Compositional bias676 – 68914Asn-rich

Amino acid modifications

Modified residue1571Phosphoserine Ref.6
Modified residue6301Phosphothreonine Ref.6
Modified residue7951Phosphoserine Ref.6
Modified residue7971Phosphoserine Ref.6 Ref.5
Modified residue8001Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q960Z0-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1667DE7C5478138D

FASTA80588,672
        10         20         30         40         50         60 
MDMITVGQSV KIKRTDGRVH MAVVAVINQS GKCITVEWYE RGETKGKEVE LDAILTLNPE 

        70         80         90        100        110        120 
LMQDTVEQHA APEPKKQATA PMNLSRNPTQ SAIGGNLTSR MTMAGNMLNK IQESQSIPNP 

       130        140        150        160        170        180 
IVSSNSVNTN SNSNTTAGGG GGTTTSTTTG LQRPRYSQAA TGQQQTRIAS AVPNNTLPNP 

       190        200        210        220        230        240 
SAAASAGPAA QGVATAATTQ GAGGASTRRS HALKEVERLK ENREKRRARQ AEMKEEKVAL 

       250        260        270        280        290        300 
MNQDPGNPNW ETAQMIREYQ STLEFVPLLD GQAVDDHQIT VCVRKRPISR KEVNRKEIDV 

       310        320        330        340        350        360 
ISVPRKDMLI VHEPRSKVDL TKFLENHKFR FDYAFNDTCD NAMVYKYTAK PLVKTIFEGG 

       370        380        390        400        410        420 
MATCFAYGQT GSGKTHTMGG EFNGKVQDCK NGIYAMAAKD VFVTLNMPRY RAMNLVVSAS 

       430        440        450        460        470        480 
FFEIYSGKVF DLLSDKQKLR VLEDGKQQVQ VVGLTEKVVD GVEEVLKLIQ HGNAARTSGQ 

       490        500        510        520        530        540 
TSANSNSSRS HAVFQIVLRP QGSTKIHGKF SFIDLAGNER GVDTSSADRQ TRMEGAEINK 

       550        560        570        580        590        600 
SLLALKECIR ALGKQSAHLP FRVSKLTQVL RDSFIGEKSK TCMIAMISPG LSSCEHTLNT 

       610        620        630        640        650        660 
LRYADRVKEL VVKDIVEVCP GGDTEPIEIT DDEEEEELNM VHPHSHQLHP NSHAPASQSN 

       670        680        690        700        710        720 
NQRAPASHHS GAVIHNNNNN NNKNGNAGNM DLAMLSSLSE HEMSDELIVQ HQAIDDLQQT 

       730        740        750        760        770        780 
EEMVVEYHRT VNATLETFLA ESKALYNLTN YVDYDQDSYC KRGESMFSQL LDIAIQCRDM 

       790        800 
MAEYRAKLAK EEMLSCSFNS PNGKR 

« Hide

References

« Hide 'large scale' references
[1]"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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]"Two mitotic kinesins cooperate to drive sister chromatid separation during anaphase."
Rogers G.C., Rogers S.L., Schwimmer T.A., Ems-McClung S.C., Walczak C.E., Vale R.D., Scholey J.M., Sharp D.J.
Nature 427:364-370(2004) [PubMed: 14681690] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[5]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, MASS SPECTROMETRY.
[6]"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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; THR-630; SER-795; SER-797 AND SER-800, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

AE014298 Genomic DNA. Translation: AAN09282.1.
AY051763 mRNA. Translation: AAK93187.1.
RefSeqNP_572687.1.
NP_727491.1.
NP_727492.1.
NP_727493.1.
NP_727494.1.
UniGeneDm.130

3D structure databases

HSSPHSSP built from PDB template 1F9T based on UniProtKB P17119.
SMRQ960Z0. Positions 248-610.
ModBaseSearch...

Protein-protein interaction databases

IntActQ960Z0. 1 interaction.

Proteomic databases

PRIDEQ960Z0.

Genome annotation databases

EnsemblFBgn0030268. Drosophila melanogaster. [Contig view]
GeneID32049.
KEGGdme:Dmel_CG1453.

Organism-specific databases

FlyBaseFBgn0030268. Klp10A.

Phylogenomic databases

HOGENOMQ960Z0.
OMAQ960Z0. QTSANSN.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-001434-MON.
DMEL-XXX-02:DMEL-XXX-02-001435-MON.
DMEL-XXX-02:DMEL-XXX-02-001436-MON.
DMEL-XXX-02:DMEL-XXX-02-001437-MON.
DMEL-XXX-02:DMEL-XXX-02-001438-MON.

Gene expression databases

ArrayExpressQ960Z0.
GermOnlineCG1453. Drosophila melanogaster.

Family and domain databases

InterProIPR001752. Kinesin_motor.
IPR019821. Kinesin_motor_CS.
[Graphical view]
Gene3DG3DSA:3.40.850.10. kinesin_motor. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00129. KISc. 1 hit.
[Graphical view]
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio776553.

Entry information

Entry nameKI10A_DROME
AccessionPrimary (citable) accession number: Q960Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

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