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Protein

Epidermal growth factor receptor substrate 15

Gene

EPS15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2.4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi173 – 1841Add BLAST12
Calcium bindingi236 – 2472Add BLAST12

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • polyubiquitin binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: ProtInc
  • clathrin coat assembly Source: BHF-UCL
  • endocytic recycling Source: BHF-UCL
  • epidermal growth factor receptor signaling pathway Source: ProtInc
  • Golgi to endosome transport Source: UniProtKB
  • negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
  • positive regulation of receptor recycling Source: Ensembl
  • protein transport Source: UniProtKB-KW
  • receptor-mediated endocytosis of virus by host cell Source: CACAO
  • regulation of cell proliferation Source: Ensembl
  • vesicle organization Source: UniProtKB
  • viral entry into host cell Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085832-MONOMER.
ReactomeiR-HSA-182971. EGFR downregulation.
R-HSA-6807004. Negative regulation of MET activity.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP42566.
SIGNORiP42566.

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor substrate 15
Short name:
Protein Eps15
Alternative name(s):
Protein AF-1p
Gene namesi
Name:EPS15
Synonyms:AF1P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3419. EPS15.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • aggresome Source: UniProtKB
  • AP-2 adaptor complex Source: Ensembl
  • apical plasma membrane Source: Ensembl
  • basal plasma membrane Source: Ensembl
  • cell-cell adherens junction Source: BHF-UCL
  • ciliary membrane Source: Ensembl
  • clathrin-coated pit Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • early endosome membrane Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • plasma membrane Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving EPS15 is found in acute leukemias. Translocation t(1;11)(p32;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi154V → E: Loss of interaction with STON2 NPF motifs. 1 Publication1
Mutagenesisi169W → A: Loss of interaction with STON2 NPF motifs. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi2060.
OpenTargetsiENSG00000085832.
PharmGKBiPA27838.

Polymorphism and mutation databases

BioMutaiEPS15.
DMDMi67476728.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001461162 – 896Epidermal growth factor receptor substrate 15Add BLAST895

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei108PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei324PhosphoserineCombined sources1
Modified residuei467PhosphoserineCombined sources1
Modified residuei470PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei562PhosphoserineBy similarity1
Modified residuei563PhosphoserineBy similarity1
Modified residuei746PhosphoserineCombined sources1
Modified residuei777PhosphothreonineCombined sources1
Modified residuei779PhosphothreonineBy similarity1
Modified residuei790PhosphoserineCombined sources1
Modified residuei796PhosphoserineCombined sources1
Modified residuei814PhosphoserineCombined sources1
Modified residuei849Phosphotyrosine; by EGFRCombined sources1

Post-translational modificationi

Phosphorylation on Tyr-849 is involved in the internalization of EGFR. Not required for membrane translocation after EGF treatment or for targeting to coated pits, but essential for a subsequent step in EGFR endocytosis (By similarity). Phosphorylated on serine upon DNA damage, probably by ATM or ATR.By similarity
Ubiquitinated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP42566.
MaxQBiP42566.
PaxDbiP42566.
PeptideAtlasiP42566.
PRIDEiP42566.

2D gel databases

OGPiP42566.

PTM databases

iPTMnetiP42566.
PhosphoSitePlusiP42566.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000085832.
CleanExiHS_EPS15.
ExpressionAtlasiP42566. baseline and differential.
GenevisibleiP42566. HS.

Organism-specific databases

HPAiCAB010164.
HPA008451.

Interactioni

Subunit structurei

Interacts with SGIP1 (By similarity). Interacts with HGS; the interaction bridges the interaction of STAM or STAM2 with EPS15. Isoform 2 interacts with HGS and AP2A2. Part of a complex at least composed of EPS15, HGS, and either STAM or STAM2. Binds AP2A2. Interacts with AP2B1; clathrin competes with EPS15. Binds STON2 and EPN1. Interacts (via its SH3-binding sites) with CRK. Interacts with SH3BP4/TTP. Interacts with ERBB2. Interacts with FCHO1. Interacts with FCHO2. Interacts (via EH domains) with DAB2. Interacts (via UIM repeats) with CORO7 (when ubiquitinated at 'Lys-472'). Interacts (via UIM domains) with UBQLN1 (via ubiquitin-like domain) and can interact with both the ubiquitinated and the non-ubiquitinated forms of UBQLN1. Interacts with UBQLN2.By similarity18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FCHO2Q0JRZ93EBI-396684,EBI-2609756
Fcho2Q3UQN23EBI-396684,EBI-6094986From a different organism.
ITSN1Q158112EBI-396684,EBI-602041
NCK1P163332EBI-396684,EBI-389883
NumbQ9QZS3-13EBI-396684,EBI-9547433From a different organism.
NumbQ9QZS3-23EBI-396684,EBI-3896014From a different organism.
STON2Q8WXE917EBI-396684,EBI-539742
UBQLN1Q9UMX05EBI-396684,EBI-741480

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108374. 153 interactors.
DIPiDIP-33064N.
IntActiP42566. 73 interactors.
MINTiMINT-107223.
STRINGi9606.ENSP00000360798.

Structurei

Secondary structure

1896
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi126 – 136Combined sources11
Beta strandi142 – 144Combined sources3
Beta strandi145 – 147Combined sources3
Helixi148 – 156Combined sources9
Turni157 – 159Combined sources3
Helixi162 – 172Combined sources11
Beta strandi177 – 179Combined sources3
Helixi182 – 197Combined sources16
Turni207 – 209Combined sources3
Helixi212 – 214Combined sources3
Helixi223 – 235Combined sources13
Beta strandi240 – 243Combined sources4
Helixi245 – 253Combined sources9
Turni254 – 256Combined sources3
Helixi259 – 269Combined sources11
Beta strandi274 – 278Combined sources5
Turni279 – 281Combined sources3
Helixi282 – 293Combined sources12
Turni305 – 307Combined sources3
Turni624 – 627Combined sources4
Turni630 – 633Combined sources4
Helixi723 – 726Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C07NMR-A217-311[»]
1EH2NMR-A121-218[»]
1F8HNMR-A121-215[»]
1FF1NMR-A121-215[»]
2IV9X-ray1.90P723-730[»]
2JXCNMR-A121-215[»]
4RH5X-ray1.60B846-854[»]
4RH9X-ray1.60B846-854[»]
4RHGX-ray1.58B846-854[»]
4S0GX-ray1.72B846-854[»]
5AWTX-ray2.70B640-649[»]
5AWUX-ray2.70B645-654[»]
5JP2X-ray2.40E/F615-637[»]
ProteinModelPortaliP42566.
SMRiP42566.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42566.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 104EH 1PROSITE-ProRule annotationAdd BLAST90
Domaini128 – 216EH 2PROSITE-ProRule annotationAdd BLAST89
Domaini160 – 195EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini223 – 258EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini224 – 314EH 3PROSITE-ProRule annotationAdd BLAST91
Repeati599 – 60113
Repeati623 – 62523
Repeati629 – 63133
Repeati634 – 63643
Repeati640 – 64253
Repeati645 – 64763
Repeati651 – 65373
Repeati664 – 66683
Repeati672 – 67493
Repeati692 – 694103
Repeati709 – 711113
Repeati737 – 739123
Repeati798 – 800133
Repeati804 – 806143
Repeati825 – 827153
Domaini851 – 870UIM 1PROSITE-ProRule annotationAdd BLAST20
Domaini877 – 896UIM 2PROSITE-ProRule annotationAdd BLAST20

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 330Interaction with DAB2By similarityAdd BLAST329
Regioni599 – 82715 X 3 AA repeats of D-P-FAdd BLAST229

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi768 – 774SH3-binding7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi768 – 850Pro-richAdd BLAST83

Domaini

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.1 Publication
The UIM (ubiquitin-interacting motif) repeats specifically bind 'Lys-33'-linked ubiquitin.2 Publications

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 3 EH domains.PROSITE-ProRule annotation
Contains 2 UIM (ubiquitin-interacting motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiKOG0998. Eukaryota.
ENOG410XTDR. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000004804.
HOVERGENiHBG005591.
InParanoidiP42566.
KOiK12472.
OMAiHAEGQGN.
OrthoDBiEOG091G01RG.
PhylomeDBiP42566.
TreeFamiTF324293.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF12763. EF-hand_4. 3 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 3 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P42566-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAQLSLT QLSSGNPVYE KYYRQVDTGN TGRVLASDAA AFLKKSGLPD
60 70 80 90 100
LILGKIWDLA DTDGKGILNK QEFFVALRLV ACAQNGLEVS LSSLNLAVPP
110 120 130 140 150
PRFHDTSSPL LISGTSAAEL PWAVKPEDKA KYDAIFDSLS PVNGFLSGDK
160 170 180 190 200
VKPVLLNSKL PVDILGRVWE LSDIDHDGML DRDEFAVAMF LVYCALEKEP
210 220 230 240 250
VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD GFVSGLEVRE
260 270 280 290 300
IFLKTGLPST LLAHIWSLCD TKDCGKLSKD QFALAFHLIS QKLIKGIDPP
310 320 330 340 350
HVLTPEMIPP SDRASLQKNI IGSSPVADFS AIKELDTLNN EIVDLQREKN
360 370 380 390 400
NVEQDLKEKE DTIKQRTSEV QDLQDEVQRE NTNLQKLQAQ KQQVQELLDE
410 420 430 440 450
LDEQKAQLEE QLKEVRKKCA EEAQLISSLK AELTSQESQI STYEEELAKA
460 470 480 490 500
REELSRLQQE TAELEESVES GKAQLEPLQQ HLQDSQQEIS SMQMKLMEMK
510 520 530 540 550
DLENHNSQLN WCSSPHSILV NGATDYCSLS TSSSETANLN EHVEGQSNLE
560 570 580 590 600
SEPIHQESPA RSSPELLPSG VTDENEVTTA VTEKVCSELD NNRHSKEEDP
610 620 630 640 650
FNVDSSSLTG PVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS
660 670 680 690 700
DPFASDCFFR QSTDPFATSS TDPFSAANNS SITSVETLKH NDPFAPGGTV
710 720 730 740 750
VAASDSATDP FASVFGNESF GGGFADFSTL SKVNNEDPFR SATSSSVSNV
760 770 780 790 800
VITKNVFEET SVKSEDEPPA LPPKIGTPTR PCPLPPGKRS INKLDSPDPF
810 820 830 840 850
KLNDPFQPFP GNDSPKEKDP EIFCDPFTSA TTTTNKEADP SNFANFSAYP
860 870 880 890
SEEDMIEWAK RESEREEEQR LARLNQQEQE DLELAIALSK SEISEA
Length:896
Mass (Da):98,656
Last modified:June 7, 2005 - v2
Checksum:iA1B9FE15B47ABAFF
GO
Isoform 2 (identifier: P42566-2) [UniParc]FASTAAdd to basket
Also known as: Eps15b

The sequence of this isoform differs from the canonical sequence as follows:
     1-314: Missing.
     315-346: SLQKNIIGSSPVADFSAIKELDTLNNEIVDLQ → MYLKSDSGLGGWITIPAVADVLKYSCIVCWSS

Show »
Length:582
Mass (Da):64,376
Checksum:i2A7BACA24604E8CA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti446Missing in BX647676 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016142822I → M.1 PublicationCorresponds to variant rs17567dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0361681 – 314Missing in isoform 2. 1 PublicationAdd BLAST314
Alternative sequenceiVSP_036169315 – 346SLQKN…IVDLQ → MYLKSDSGLGGWITIPAVAD VLKYSCIVCWSS in isoform 2. 1 PublicationAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07707 mRNA. Translation: AAA52101.1.
Z29064 mRNA. Translation: CAA82305.1.
AK313396 mRNA. Translation: BAG36194.1.
DQ367924 mRNA. Translation: ABD34786.1.
BX647676 mRNA. No translation available.
AL671986, AC104170 Genomic DNA. Translation: CAI13030.1.
CH471059 Genomic DNA. Translation: EAX06823.1.
CCDSiCCDS557.1. [P42566-1]
PIRiS43074.
RefSeqiNP_001153441.1. NM_001159969.1. [P42566-2]
NP_001972.1. NM_001981.2. [P42566-1]
UniGeneiHs.83722.

Genome annotation databases

EnsembliENST00000371733; ENSP00000360798; ENSG00000085832. [P42566-1]
GeneIDi2060.
KEGGihsa:2060.
UCSCiuc001csq.2. human. [P42566-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07707 mRNA. Translation: AAA52101.1.
Z29064 mRNA. Translation: CAA82305.1.
AK313396 mRNA. Translation: BAG36194.1.
DQ367924 mRNA. Translation: ABD34786.1.
BX647676 mRNA. No translation available.
AL671986, AC104170 Genomic DNA. Translation: CAI13030.1.
CH471059 Genomic DNA. Translation: EAX06823.1.
CCDSiCCDS557.1. [P42566-1]
PIRiS43074.
RefSeqiNP_001153441.1. NM_001159969.1. [P42566-2]
NP_001972.1. NM_001981.2. [P42566-1]
UniGeneiHs.83722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C07NMR-A217-311[»]
1EH2NMR-A121-218[»]
1F8HNMR-A121-215[»]
1FF1NMR-A121-215[»]
2IV9X-ray1.90P723-730[»]
2JXCNMR-A121-215[»]
4RH5X-ray1.60B846-854[»]
4RH9X-ray1.60B846-854[»]
4RHGX-ray1.58B846-854[»]
4S0GX-ray1.72B846-854[»]
5AWTX-ray2.70B640-649[»]
5AWUX-ray2.70B645-654[»]
5JP2X-ray2.40E/F615-637[»]
ProteinModelPortaliP42566.
SMRiP42566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108374. 153 interactors.
DIPiDIP-33064N.
IntActiP42566. 73 interactors.
MINTiMINT-107223.
STRINGi9606.ENSP00000360798.

PTM databases

iPTMnetiP42566.
PhosphoSitePlusiP42566.

Polymorphism and mutation databases

BioMutaiEPS15.
DMDMi67476728.

2D gel databases

OGPiP42566.

Proteomic databases

EPDiP42566.
MaxQBiP42566.
PaxDbiP42566.
PeptideAtlasiP42566.
PRIDEiP42566.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371733; ENSP00000360798; ENSG00000085832. [P42566-1]
GeneIDi2060.
KEGGihsa:2060.
UCSCiuc001csq.2. human. [P42566-1]

Organism-specific databases

CTDi2060.
DisGeNETi2060.
GeneCardsiEPS15.
HGNCiHGNC:3419. EPS15.
HPAiCAB010164.
HPA008451.
MIMi600051. gene.
neXtProtiNX_P42566.
OpenTargetsiENSG00000085832.
PharmGKBiPA27838.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0998. Eukaryota.
ENOG410XTDR. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000004804.
HOVERGENiHBG005591.
InParanoidiP42566.
KOiK12472.
OMAiHAEGQGN.
OrthoDBiEOG091G01RG.
PhylomeDBiP42566.
TreeFamiTF324293.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085832-MONOMER.
ReactomeiR-HSA-182971. EGFR downregulation.
R-HSA-6807004. Negative regulation of MET activity.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP42566.
SIGNORiP42566.

Miscellaneous databases

ChiTaRSiEPS15. human.
EvolutionaryTraceiP42566.
GeneWikiiEPS15.
GenomeRNAii2060.
PROiP42566.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000085832.
CleanExiHS_EPS15.
ExpressionAtlasiP42566. baseline and differential.
GenevisibleiP42566. HS.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR003903. UIM_dom.
[Graphical view]
PfamiPF12763. EF-hand_4. 3 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 3 hits.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEPS15_HUMAN
AccessioniPrimary (citable) accession number: P42566
Secondary accession number(s): B2R8J7, D3DPJ2, Q5SRH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Studies in clathrin-mediated endocytosis of ITGB1 and TFR used a siRNA mixture of EPS15 and EPS15L1, and a Dab2 mutant with impaired binding to EH domain-containing proteins EPS15 and ITSN1 suggesting a partially overlapping role of the EH domain-containing proteins.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.