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Q8WXE9 (STON2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

Names and origin

Protein namesRecommended name:
Stonin-2
Alternative name(s):
Stoned B
Gene names
Name:STON2
Synonyms:STN2, STNB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length905 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein involved in endocytic machinery. May be involved in the vesicle recycling. May facilitate clathrin-coated vesicle uncoating. Ref.1 Ref.5

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. Ref.1 Ref.5

Subcellular location

Cytoplasm. Membrane. Note: Some fraction is membrane-associated. Ref.5

Tissue specificity

Ubiquitous. Ref.5

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.

Sequence similarities

Belongs to the Stoned B family.

Contains 1 MHD (mu homology) domain.

Contains 1 SHD (stonin homology) domain.

Sequence caution

The sequence AAK57558.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAK57558.1 differs from that shown. Reason: Intron retention.

The sequence AAK76362.1 differs from that shown. Reason: Frameshift at position 122.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
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 sequence or structural similarity. Source: UniProtKB

   Cellular componentclathrin adaptor complex

Inferred from electronic annotation. Source: InterPro

nucleolus

Inferred from direct assay. Source: HPA

   Molecular functionprotein binding

Inferred from physical interaction Ref.1. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Syt1P217072EBI-539742,EBI-458098From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 905905Stonin-2
PRO_0000185732

Regions

Domain427 – 560134SHD
Domain565 – 874310MHD
Motif313 – 3153NPF 1
Motif329 – 3313NPF 2

Amino acid modifications

Modified residue3001Phosphothreonine Ref.6
Modified residue3021Phosphoserine Ref.6

Natural variations

Natural variant3071S → P. Ref.1 Ref.4
Corresponds to variant rs3813535 [ dbSNP | Ensembl ].
VAR_020182
Natural variant6461R → H.
Corresponds to variant rs34323725 [ dbSNP | Ensembl ].
VAR_046643
Natural variant6941T → A.
Corresponds to variant rs35689202 [ dbSNP | Ensembl ].
VAR_046644
Natural variant8511S → A.
Corresponds to variant rs2241621 [ dbSNP | Ensembl ].
VAR_021912

Experimental info

Mutagenesis7381W → A: Reduces interaction with SYT1. Ref.1
Mutagenesis7401K → A: Reduces interaction with SYT1. Ref.1
Sequence conflict121 – 1222TA → NS in AAK76362. Ref.1

Secondary structure

...... 905
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WXE9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 59F5810DEC540CA3

FASTA905101,165
        10         20         30         40         50         60 
MTTLDHVIAT HQSEWVSFNE EPPFPAHSQG GTEEHLPGLS SSPDQSESSS GENHVVDGGS 

        70         80         90        100        110        120 
QDHSHSEQDD SSEKMGLISE AASPPGSPEQ PPPDLASAIS NWVQFEDDTP WASTSPPHQE 

       130        140        150        160        170        180 
TAETALPLTM PCWTCPSFDS LGRCPLTSES SWTTHSEDTS SPSFGCSYTD LQLINAEEQT 

       190        200        210        220        230        240 
SGQASGADST DNSSSLQEDE EVEMEAISWQ ASSPAMNGHP APPVTSARFP SWVTFDDNEV 

       250        260        270        280        290        300 
SCPLPPVTSP LKPNTPPSAS VIPDVPYNSM GSFKKRDRPK STLMNFSKVQ KLDISSLNRT 

       310        320        330        340        350        360 
PSVTEASPWR ATNPFLNETL QDVQPSPINP FSAFFEEQER RSQNSSISST TGKSQRDSLI 

       370        380        390        400        410        420 
VIYQDAISFD DSSKTQSHSD AVEKLKQLQI DDPDHFGSAT LPDDDPVAWI ELDAHPPGSA 

       430        440        450        460        470        480 
RSQPRDGWPM MLRIPEKKNI MSSRHWGPIF VKLTDTGYLQ LYYEQGLEKP FREFKLEICH 

       490        500        510        520        530        540 
EISEPRLQNY DENGRIHSLR IDRVTYKEKK KYQPKPAVAH TAEREQVIKL GTTNYDDFLS 

       550        560        570        580        590        600 
FIHAVQDRLM DLPVLSMDLS TVGLNYLEEE ITVDVRDEFS GIVSKGDNQI LQHHVLTRIH 

       610        620        630        640        650        660 
ILSFLSGLAE CRLGLNDILV KGNEIVLRQD IMPTTTTKWI KLHECRFHGC VDEDVFHNSR 

       670        680        690        700        710        720 
VILFNPLDAC RFELMRFRTV FAEKTLPFTL RTATSVNGAE VEVQSWLRMS TGFSANRDPL 

       730        740        750        760        770        780 
TQVPCENVMI RYPVPSEWVK NFRRESVLGE KSLKAKVNRG ASFGSTSVSG SEPVMRVTLG 

       790        800        810        820        830        840 
TAKYEHAFNS IVWRINRLPD KNSASGHPHC FFCHLELGSD REVPSRFANH VNVEFSMPTT 

       850        860        870        880        890        900 
SASKASVRSI SVEDKTDVRK WVNYSAHYSY QVALGSIWLM LPTPFVHPTT LPLLFLLAML 


TMFAW 

« Hide

References

« Hide 'large scale' references
[1]"Human stoned B interacts with AP-2 and synaptotagmin and facilitates clathrin-coated vesicle uncoating."
Walther K., Krauss M., Diril M.K., Lemke S., Ricotta D., Hoening S., Kaiser S., Haucke V.
EMBO Rep. 2:634-640(2001) [PubMed: 11454741] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SYT1 AND WITH THE AP-2 COMPLEX, MUTAGENESIS OF TRP-738 AND LYS-740, VARIANT PRO-307.
Tissue: Brain.
[2]Erratum
Walther K., Krauss M., Diril M.K., Lemke S., Ricotta D., Hoening S., Kaiser S., Haucke V.
EMBO Rep. 3:197-197(2002)
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed: 12508121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT PRO-307.
Tissue: Brain.
[5]"Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery."
Martina J.A., Bonangelino C.J., Aguilar R.C., Bonifacino J.S.
J. Cell Biol. 153:1111-1120(2001) [PubMed: 11381094] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 191-905, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EPS15; EPS15R; ITSN1; SYT1 AND SYT2.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-300 AND SER-302, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity."
Rumpf J., Simon B., Jung N., Maritzen T., Haucke V., Sattler M., Groemping Y.
EMBO J. 27:558-569(2008) [PubMed: 18200045] [Abstract]
Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH EPS15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF380833 mRNA. Translation: AAK76362.1. Frameshift.
AF449430 mRNA. Translation: AAL47008.1.
AL121769 Genomic DNA. No translation available.
AL136040 Genomic DNA. No translation available.
BC069389 mRNA. Translation: AAH69389.1.
BC117493 mRNA. Translation: AAI17494.1.
AF255309 mRNA. Translation: AAK57558.1. Sequence problems.
IPIIPI00103521.
RefSeqNP_149095.2. NM_033104.2.
UniGeneHs.14248.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXCNMR-B301-340[»]
ProteinModelPortalQ8WXE9.
SMRQ8WXE9. Positions 301-340, 557-872.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8WXE9. 4 interactions.
MINTMINT-6179820.
STRINGQ8WXE9.

PTM databases

PhosphoSiteQ8WXE9.

Polymorphism databases

DMDM34098614.

Proteomic databases

PRIDEQ8WXE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267540; ENSP00000267540; ENSG00000140022.
GeneID85439.
KEGGhsa:85439.
UCSCuc001xvl.1. human.
uc001xvm.1. human.

Organism-specific databases

CTD85439.
GeneCardsGC14M081736.
H-InvDBHIX0011863.
HGNCHGNC:30652. STON2.
HPAHPA003086.
MIM608467. gene.
neXtProtNX_Q8WXE9.
PharmGKBPA143485624.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00530000063152.
HOVERGENHBG097637.
InParanoidQ8WXE9.
OMAFFCHLEL.
OrthoDBEOG4XSKP6.
PhylomeDBQ8WXE9.

Gene expression databases

ArrayExpressQ8WXE9.
BgeeQ8WXE9.
CleanExHS_STON2.
GenevestigatorQ8WXE9.
GermOnlineENSG00000140022. Homo sapiens.

Family and domain databases

InterProIPR008968. Clathrin_mu_C.
IPR012320. SHD.
IPR017110. Stonin.
IPR022699. Stonin2_N.
[Graphical view]
PfamPF00928. Adap_comp_sub. 1 hit.
PF12016. Stonin2_N. 1 hit.
[Graphical view]
PIRSFPIRSF037099. Stonin. 1 hit.
SUPFAMSSF49447. AP50. 1 hit.
PROSITEPS51072. MHD. 1 hit.
PS51070. SHD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio76012.
SOURCESearch...

Entry information

Entry nameSTON2_HUMAN
AccessionPrimary (citable) accession number: Q8WXE9
Secondary accession number(s): Q17R24 expand/collapse secondary AC list , Q6NT47, Q96RI7, Q96RU6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families