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Q9QZB7 (ARP10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 86. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-related protein 10
Alternative name(s):
Actin-related protein 11
Gene names
Name:Actr10
Synonyms:Act11, Actr11, Arp11
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Cytoplasm › cytoskeleton By similarity.

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmicrotubule-based movement

Inferred from direct assay Ref.1. Source: MGI

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

dynactin complex

Inferred from direct assay Ref.1. Source: MGI

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTR1BP420252EBI-367600,EBI-367493From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Actin-related protein 10
PRO_0000089132

Amino acid modifications

Modified residue4141Phosphoserine Ref.4

Experimental info

Sequence conflict91S → T in AAF05617. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QZB7 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: DFA8D7CFF0C64B0D

FASTA41746,208
        10         20         30         40         50         60 
MPLYEGLGSG GEKTAVVIDL GEAFTKCGFA GETGPRCIIP SVIKRAGMSK PIKVVQYNIN 

        70         80         90        100        110        120 
TEELYSYLKE FIHILYFRHL LVNPRDRRVV VIESVLCPSH FRETLTRVLF KYFEVPSVLL 

       130        140        150        160        170        180 
APSHLMALLT LGINSAMVLD CGYRESLVLP IYEGIPILNC WGALPLGGKA LHKELETQLL 

       190        200        210        220        230        240 
EQCTVDTGAA KGQSLPSVMG SVPEGVLEDI KVRTCFVSDL KRGLQIQAAK FNIDGNNERP 

       250        260        270        280        290        300 
TPPPNVDYPL DGEKILHVLG SIRDSVVEIL FEQDNEEKSV ATLILDSLLQ CPIDTRKQLA 

       310        320        330        340        350        360 
ENLVIIGGTS MLPGFLHRLL AEIRYLVEKP KYKKTLGTKN FRIHTPPAKA NCVAWLGGAV 

       370        380        390        400        410 
FGALQDILGS RSISKEYYNQ TGRIPDWCSL NNPPLEMMFD VGKAQPPLMK RAFSTEK

« Hide

References

« Hide 'large scale' references
[1]"Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end."
Eckley D.M., Gill S.R., Melkonian K.A., Bingham J.B., Goodson H.V., Heuser J.E., Schroer T.A.
J. Cell Biol. 147:307-320(1999) [PubMed: 10525537] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF190797 mRNA. Translation: AAF05617.1.
AK161642 mRNA. Translation: BAE36507.1.
BC002227 mRNA. Translation: AAH02227.1.
IPIIPI00137206.
RefSeqNP_062759.2. NM_019785.2.
UniGeneMm.29317.

3D structure databases

ProteinModelPortalQ9QZB7.
SMRQ9QZB7. Positions 10-392.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9QZB7. 2 interactions.
STRINGQ9QZB7.

PTM databases

PhosphoSiteQ9QZB7.

Proteomic databases

PRIDEQ9QZB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021479; ENSMUSP00000021479; ENSMUSG00000021076.
GeneID56444.
KEGGmmu:56444.

Organism-specific databases

CTD55860.
MGIMGI:1891654. Actr10.

Phylogenomic databases

GeneTreeENSGT00600000084502.
HOGENOMHBG713850.
HOVERGENHBG050578.
InParanoidQ9QZB7.
OrthoDBEOG4X0MSF.

Gene expression databases

ArrayExpressQ9QZB7.
BgeeQ9QZB7.
CleanExMM_ACTR10.
GenevestigatorQ9QZB7.
GermOnlineENSMUSG00000021076. Mus musculus.

Family and domain databases

InterProIPR004000. Actin-like.
[Graphical view]
PANTHERPTHR11937. Actin_like. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312646.
SOURCESearch...

Entry information

Entry nameARP10_MOUSE
AccessionPrimary (citable) accession number: Q9QZB7
Secondary accession number(s): Q3TT18, Q99LU1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: November 16, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents