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P42566

- EPS15_HUMAN

UniProt

P42566 - EPS15_HUMAN

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Protein

Epidermal growth factor receptor substrate 15

Gene

EPS15

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi173 – 184121Add
BLAST
Calcium bindingi236 – 247122Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. polyubiquitin binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. clathrin coat assembly Source: BHF-UCL
  3. endocytic recycling Source: BHF-UCL
  4. endocytosis Source: UniProtKB-KW
  5. epidermal growth factor receptor signaling pathway Source: Reactome
  6. Golgi to endosome transport Source: UniProtKB
  7. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
  8. protein transport Source: UniProtKB-KW
  9. vesicle organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_12484. EGFR downregulation.
SignaLinkiP42566.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3419. EPS15.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membraneclathrin-coated pit
Note: Recruited to the plasma membrane upon EGFR activation and localizes to coated pits.
Isoform 2 : Early endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
Note: Colocalizes with HGS on bilayered clathrin coats on endosomes.

GO - Cellular componenti

  1. AP-2 adaptor complex Source: Ensembl
  2. ciliary membrane Source: Ensembl
  3. coated pit Source: UniProtKB
  4. cytoplasm Source: HPA
  5. cytosol Source: Reactome
  6. endosome Source: UniProtKB-KW
  7. intracellular membrane-bounded organelle Source: HPA
  8. membrane Source: UniProtKB
  9. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541V → E: Loss of interaction with STON2 NPF motifs. 1 Publication
Mutagenesisi169 – 1691W → A: Loss of interaction with STON2 NPF motifs. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA27838.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 896895Epidermal growth factor receptor substrate 15PRO_0000146116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei108 – 1081Phosphoserine1 Publication
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei323 – 3231Phosphoserine3 Publications
Modified residuei324 – 3241Phosphoserine3 Publications
Modified residuei467 – 4671Phosphoserine1 Publication
Modified residuei470 – 4701Phosphoserine1 Publication
Modified residuei485 – 4851Phosphoserine3 Publications
Modified residuei777 – 7771PhosphothreonineBy similarity
Modified residuei790 – 7901Phosphoserine2 Publications
Modified residuei796 – 7961Phosphoserine3 Publications
Modified residuei814 – 8141Phosphoserine5 Publications
Modified residuei849 – 8491Phosphotyrosine; by EGFR1 Publication

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 similarity7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP42566.
PaxDbiP42566.
PeptideAtlasiP42566.
PRIDEiP42566.

2D gel databases

OGPiP42566.

PTM databases

PhosphoSiteiP42566.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiP42566.
CleanExiHS_EPS15.
ExpressionAtlasiP42566. baseline and differential.
GenevestigatoriP42566.

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 STAM1 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').By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FCHO2Q0JRZ93EBI-396684,EBI-2609756
Fcho2Q3UQN23EBI-396684,EBI-6094986From a different organism.
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

Protein-protein interaction databases

BioGridi108374. 116 interactions.
DIPiDIP-33064N.
IntActiP42566. 42 interactions.
MINTiMINT-107223.
STRINGi9606.ENSP00000360798.

Structurei

Secondary structure

1
896
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi126 – 13611Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi145 – 1473Combined sources
Helixi148 – 1569Combined sources
Turni157 – 1593Combined sources
Helixi162 – 17211Combined sources
Beta strandi177 – 1793Combined sources
Helixi182 – 19716Combined sources
Turni207 – 2093Combined sources
Helixi212 – 2143Combined sources
Helixi223 – 23513Combined sources
Beta strandi240 – 2434Combined sources
Helixi245 – 2539Combined sources
Turni254 – 2563Combined sources
Helixi259 – 26911Combined sources
Beta strandi274 – 2785Combined sources
Turni279 – 2813Combined sources
Helixi282 – 29312Combined sources
Turni305 – 3073Combined sources
Helixi723 – 7264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C07NMR-A217-311[»]
1EH2NMR-A121-218[»]
1F8HNMR-A121-215[»]
1FF1NMR-A121-215[»]
2IV9X-ray1.90P723-730[»]
2JXCNMR-A121-215[»]
ProteinModelPortaliP42566.
SMRiP42566. Positions 7-105, 121-215, 217-311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42566.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 10490EH 1PROSITE-ProRule annotationAdd
BLAST
Domaini128 – 21689EH 2PROSITE-ProRule annotationAdd
BLAST
Domaini160 – 19536EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini223 – 25836EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini224 – 31491EH 3PROSITE-ProRule annotationAdd
BLAST
Repeati599 – 60131
Repeati623 – 62532
Repeati629 – 63133
Repeati634 – 63634
Repeati640 – 64235
Repeati645 – 64736
Repeati651 – 65337
Repeati664 – 66638
Repeati672 – 67439
Repeati692 – 694310
Repeati709 – 711311
Repeati737 – 739312
Repeati798 – 800313
Repeati804 – 806314
Repeati825 – 827315
Repeati851 – 87020UIM 1Add
BLAST
Repeati877 – 89620UIM 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 330329Interaction with DAB2By similarityAdd
BLAST
Regioni599 – 82722915 X 3 AA repeats of D-P-FAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi768 – 7747SH3-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi768 – 85083Pro-richAdd
BLAST

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) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiNOG301764.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000004804.
HOVERGENiHBG005591.
InParanoidiP42566.
KOiK12472.
OMAiPPPRFHD.
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. EPS15_homology.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 3 hits.
[Graphical view]
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti446 – 4461Missing in BX647676. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti822 – 8221I → M.1 Publication
Corresponds to variant rs17567 [ dbSNP | Ensembl ].
VAR_016142

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 314314Missing in isoform 2. 1 PublicationVSP_036168Add
BLAST
Alternative sequencei315 – 34632SLQKN…IVDLQ → MYLKSDSGLGGWITIPAVAD VLKYSCIVCWSS in isoform 2. 1 PublicationVSP_036169Add
BLAST

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.
UCSCiuc001csp.3. human. [P42566-2]
uc001csq.1. human. [P42566-1]

Polymorphism databases

DMDMi67476728.

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 .
CCDSi CCDS557.1. [P42566-1 ]
PIRi S43074.
RefSeqi NP_001153441.1. NM_001159969.1. [P42566-2 ]
NP_001972.1. NM_001981.2. [P42566-1 ]
UniGenei Hs.83722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C07 NMR - A 217-311 [» ]
1EH2 NMR - A 121-218 [» ]
1F8H NMR - A 121-215 [» ]
1FF1 NMR - A 121-215 [» ]
2IV9 X-ray 1.90 P 723-730 [» ]
2JXC NMR - A 121-215 [» ]
ProteinModelPortali P42566.
SMRi P42566. Positions 7-105, 121-215, 217-311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108374. 116 interactions.
DIPi DIP-33064N.
IntActi P42566. 42 interactions.
MINTi MINT-107223.
STRINGi 9606.ENSP00000360798.

PTM databases

PhosphoSitei P42566.

Polymorphism databases

DMDMi 67476728.

2D gel databases

OGPi P42566.

Proteomic databases

MaxQBi P42566.
PaxDbi P42566.
PeptideAtlasi P42566.
PRIDEi P42566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371733 ; ENSP00000360798 ; ENSG00000085832 . [P42566-1 ]
GeneIDi 2060.
KEGGi hsa:2060.
UCSCi uc001csp.3. human. [P42566-2 ]
uc001csq.1. human. [P42566-1 ]

Organism-specific databases

CTDi 2060.
GeneCardsi GC01M051819.
HGNCi HGNC:3419. EPS15.
HPAi CAB010164.
HPA008451.
MIMi 600051. gene.
neXtProti NX_P42566.
PharmGKBi PA27838.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301764.
GeneTreei ENSGT00760000118985.
HOGENOMi HOG000004804.
HOVERGENi HBG005591.
InParanoidi P42566.
KOi K12472.
OMAi PPPRFHD.
PhylomeDBi P42566.
TreeFami TF324293.

Enzyme and pathway databases

Reactomei REACT_12484. EGFR downregulation.
SignaLinki P42566.

Miscellaneous databases

ChiTaRSi EPS15. human.
EvolutionaryTracei P42566.
GeneWikii EPS15.
GenomeRNAii 2060.
NextBioi 8377.
PROi P42566.
SOURCEi Search...

Gene expression databases

Bgeei P42566.
CleanExi HS_EPS15.
ExpressionAtlasi P42566. baseline and differential.
Genevestigatori P42566.

Family and domain databases

Gene3Di 1.10.238.10. 3 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR003903. Ubiquitin-int_motif.
[Graphical view ]
SMARTi SM00054. EFh. 3 hits.
SM00027. EH. 3 hits.
SM00726. UIM. 3 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS50031. EH. 3 hits.
PS50330. UIM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32."
    Wong W.T., Kraus M.H., Carlomagno F., Zelano A., Druck T., Croce C.M., Huebner K., di Fiore P.P.
    Oncogene 9:1591-1597(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-822.
    Tissue: Melanoma.
  2. "A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9 nor ENL."
    Bernard O.A., Mauchauffe M., Mecucci C., van den Berghe H., Berger R.
    Oncogene 9:1039-1045(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Trachea.
  4. "Eps15 in human umbilical vein endothelial cells."
    Kronstein R., Grossklaus S., Schnittler H.-J.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins."
    Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T., Nagashima K., Kurata T.
    J. Biol. Chem. 271:14468-14472(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRK.
  9. "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis."
    Chen H., Fre S., Slepnev V.I., Capua M.R., Takei K., Butler M.H., Di Fiore P.P., De Camilli P.
    Nature 394:793-797(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPN1.
  10. "STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes."
    Bache K.G., Raiborg C., Mehlum A., Stenmark H.
    J. Biol. Chem. 278:12513-12521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HGS AND STAM2.
  11. "TTP specifically regulates the internalization of the transferrin receptor."
    Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P.
    Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3BP4.
  12. "Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor."
    Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.
    Mol. Cell. Biol. 25:11005-11018(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB2.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. "An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor."
    Roxrud I., Raiborg C., Pedersen N.M., Stang E., Stenmark H.
    J. Cell Biol. 180:1205-1218(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH HSG AND AP2A2.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  17. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-323; SER-485 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits."
    Mettlen M., Stoeber M., Loerke D., Antonescu C.N., Danuser G., Schmid S.L.
    Mol. Biol. Cell 20:3251-3260(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-323; SER-324; SER-814 AND TYR-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-467; SER-470; SER-790; SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
    Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
    Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO2.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Characterization of the EFC/F-BAR domain protein, FCHO2."
    Uezu A., Umeda K., Tsujita K., Suetsugu S., Takenawa T., Nakanishi H.
    Genes Cells 16:868-878(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO2.
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-485; SER-790; SER-796 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate integrin beta1 endocytosis."
    Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.
    Mol. Biol. Cell 23:2905-2916(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAB2.
  28. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
    Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
    Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO1.
  30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
    Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
    Mol. Cell 54:586-600(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CORO7.
  32. "Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain."
    de Beer T., Carter R.E., Lobel-Rice K.E., Sorkin A., Overduin M.
    Science 281:1357-1360(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH CALCIUM IONS.
  33. "Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites."
    Enmon J.L., de Beer T., Overduin M.
    Biochemistry 39:4309-4319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 217-311 IN COMPLEX WITH CALCIUM IONS.
  34. Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH PEPTIDE LIGAND AND CALCIUM IONS, DOMAIN.
  35. "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
    Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
    PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 719-730 IN COMPLEX WITH AP2B1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
  36. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 121-215 IN COMPLEX WITH STON2 AND CALCIUM IONS, MUTAGENESIS OF VAL-154 AND TRP-169, SUBCELLULAR LOCATION.

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 26, 2014
This is version 164 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

External Data

Dasty 3