Annotation for this protein is in progress - please check future releases for more complete information



DP00251: Epsin-1FASTA viewXML view

General information
DisProt:DP00251
Name:Epsin-1
Synonym(s):EPN1_RAT
EPS-15-interacting protein 1
First appeared in release:Release 3.0 (02/17/2006)
UniProt:O88339
UniGene:Rn.30007
SwissProt: EPN1_RAT
TrEMBL:  
NCBI (GI): 41016934
Source organism:Rattus norvegicus (Rat)
Sequence length:575
Percent disordered:75%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI - 60
WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG - 120
VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS - 180
SGEEELQLQL ALAMSKEEAD QPPSCGPEDD VQLQLALSLS REEHDKEERI RRGDDLRLQM - 240
AIEESKRETG GKEESSLMDL ADVFTTPAPP QASDPWGGPA SVPTAVPVAA AASDPWGAPA - 300
VPPAADPWGG AAPTPASGDP WRPAAPTGPS VDPWGGTPAP AAGEGPTSDP WGSADGGAPV - 360
SGPPSSDPWA PAPAFSDPWG GSPAKPSSNG TAVGGFDTEP DEFSDFDRLR TALPTSGSST - 420
GELELLAGEV PARSPGAFDM SGVGGSLAES VGSPPPAATP TPTPPTRKTP ESFLGPNAAL - 480
VDLDSLVSRP GPTPPGAKAS NPFLPSGAPA TGPSVTNPFQ PAPPATLTLN QLRLSPVPPV - 540
PGAPPTYISP LGGGPGLPPM MPPGPPAPNT NPFLL

Region 1: 144-575

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:144 - 575
Length:432
Region sequence:

RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPP
SCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADV
FTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRP
AAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSP
AKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGV
GGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPF
LPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPP
GPPAPNTNPFLL

Modification type: Fragment
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV

  2. Size exclusion/gel filtration chromatography (cytosol 500 uL)

  3. Analytical ultracentrifugation (293 K; )

References:
  1. Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. "Unusual structural organization of the endocytic proteins AP180 and epsin 1." J Biol Chem. 2002; 277(10): 8209-16. PubMed: 11756460

Comments:
 



References

  1. Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH, Di Fiore PP, De Camilli P. "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis." Nature. 1998; 394(6695): 793-7. PubMed: 9723620


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