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Reviewed, UniProtKB/Swiss-Prot Q8BZ60 (STON2_MOUSE)

Last modified November 3, 2009. Version 55. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Stonin-2
Alternative name(s):
    Stoned B
Gene names
Name: Ston2
Synonyms: Stn2, Stnb
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length895 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Adapter protein involved in endocytic machinery. May be involved in the vesicle recycling. May facilitate clathrin-coated vesicle uncoating By similarity.

Subunit structure

Interacts with the second C2 domain of synaptotagmins SYT1 and SYT2. Interacts with EPS15, EPS15R and ITSN1. Interacts indirectly with the AP-2 adapter complex By similarity.

Subcellular location

Cytoplasm By similarity. Membrane By similarity. Note: Some fraction is membrane-associated.

Domain

The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, mediate the interaction with the EH domain of SYT1, SYT2, EPS15, EPS15R and ITSN1 By similarity.

Sequence similarities

Belongs to the Stoned B family.

Contains 1 MHD (mu homology) domain.

Contains 1 SHD (stonin homology) domain.

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Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCytoplasm
Membrane
   DomainRepeat
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

regulation of endocytosis

Inferred from direct assay. Source: UniProtKB

   Cellular componentclathrin adaptor complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ap2a2P184841EBI-539385,EBI-539360From a different organism.
Ap2m1P840921EBI-539385,EBI-297693From a different organism.
Syt1P217071EBI-539385,EBI-458098From a different organism.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 895895Stonin-2
PRO_0000185733

Regions

Domain424 – 557134SHD
Domain562 – 871310MHD
Motif310 – 3123NPF 1
Motif326 – 3283NPF 2

Amino acid modifications

Modified residue2991Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8BZ60-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2CA089956349B96F

FASTA89599,611
        10         20         30         40         50         60 
MTTLDHVIAT HQSEWVSFSE EPLFPTPLEG GTEEHFPGLS SSSERSESSS GENHVVDEGS 

        70         80         90        100        110        120 
QDLSHSEQDD SSEKMGLISE AASPPGSPVQ PTPDLASAIS NWVQFEDDTP WSSTSPPHKE 

       130        140        150        160        170        180 
TALTLTMPCW TCPSFDSLRR CPLTSESSWT THSEDTSSPS VAPSYTDLQL INTEEQASGR 

       190        200        210        220        230        240 
ASGTDSTDNS SSLQEDEEVE MEAISWWAGS PAMNGHPAAP PVTTARFPSW VTFEDNEVGC 

       250        260        270        280        290        300 
PSPPVPSPKK PNTPSAATAA PDVPFNSTGS FKRDRPKSTL MNLPKVQKLD ISSLNRPPSV 

       310        320        330        340        350        360 
IEAPPWRATN PFLNETLQDV QPSPINPFSA FFEEQERRSQ NSSVSSTTGK SQRDSLIVVY 

       370        380        390        400        410        420 
QDAISFDDSG KSQPHPDAIE KLKQLQIDDP DPVGNTALPD DDPTASVELD APSPASALSQ 

       430        440        450        460        470        480 
PRDGWPMMLR IPEKKNIMSS RHWGPIYIKL TASGYLQLYY EQGLEKPFRE FKLEICHEVS 

       490        500        510        520        530        540 
EPRLQNYDEN GRIHSLRIDR VTYKEKKKYQ PKPAVAHAAE REQVIKLGTT NYDDFRSFIH 

       550        560        570        580        590        600 
AVQDRLMDLP VLSMDLSTVG LNYLEEEITV DVRDEFSGTV GKGDNQILQH HVLTRIHILS 

       610        620        630        640        650        660 
FLSGLAECRL GLNDILIKGN EIVSRQDIMP TTTTKWIKLH ECRFHGCVDE DVFNSSRVIL 

       670        680        690        700        710        720 
FNPLDACRFE LMRFRTVFAE KTLPFTLRTA ASINGAEVEV QSWLRMSPGF SSNRDPLTQV 

       730        740        750        760        770        780 
PCENVMVRYP VPSEWVKNFR RDSVLGEKSL KAKVNRGASF GSAGASGSEP VMRVTLGTAK 

       790        800        810        820        830        840 
YEHAFNSIVW RINRLPDKNS ASGHPHCFFC HLELGSDREV PSRFANYVNV EFSMPTTSAS 

       850        860        870        880        890 
KAAVRSVSVE DKPDVRKWVN YSAHYSYKVE IEQKKSLKPD FEGEDLENPK ECGVQ

« Hide

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References

[1]"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.
Tissue: Bone.
[2]"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].
Tissue: Brain.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK036612 mRNA. Translation: BAC29507.1.
BC132531 mRNA. Translation: AAI32532.1.
BC138054 mRNA. Translation: AAI38055.1.
IPIIPI00227349.
RefSeqNP_780576.1.
UniGeneMm.312234

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8BZ60. 3 interactions.
STRINGQ8BZ60.

PTM databases

PhosphoSiteQ8BZ60.

Proteomic databases

PRIDEQ8BZ60.

Genome annotation databases

EnsemblENSMUST00000052969; ENSMUSP00000053908; ENSMUSG00000020961; Mus musculus. [Genome view]
GeneID108800.
KEGGmmu:108800.
UCSCuc007okt.1. mouse.

Organism-specific databases

CTD108800.
MGIMGI:1918272. Ston2.

Phylogenomic databases

HOGENOMQ8BZ60.
HOVERGENQ8BZ60.
OMANIMSSRH.

Gene expression databases

ArrayExpressQ8BZ60.
BgeeQ8BZ60.
CleanExMM_STON2.
GenevestigatorQ8BZ60.

Family and domain databases

InterProIPR008968. Clathrin_mu_C.
IPR012320. SHD.
IPR017110. Stonin.
[Graphical view]
PfamPF00928. Adap_comp_sub. 1 hit.
[Graphical view]
PIRSFPIRSF037099. Stonin. 1 hit.
PROSITEPS51072. MHD. 1 hit.
PS51070. SHD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio361329.
SOURCESearch...

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Entry information

Entry nameSTON2_MOUSE
AccessionPrimary (citable) accession number: Q8BZ60
Secondary accession number(s): A2RTJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2003
Last modified: November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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