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Q9Y6I3

- EPN1_HUMAN

UniProt

Q9Y6I3 - EPN1_HUMAN

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Protein
Epsin-1
Gene
EPN1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations By similarity. Regulates receptor-mediated endocytosis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Phosphatidylinositol lipid headgroup By similarity
Binding sitei11 – 111Phosphatidylinositol lipid headgroup By similarity
Binding sitei25 – 251Phosphatidylinositol lipid headgroup By similarity
Binding sitei30 – 301Phosphatidylinositol lipid headgroup By similarity
Binding sitei63 – 631Phosphatidylinositol lipid headgroup By similarity
Binding sitei73 – 731Phosphatidylinositol lipid headgroup By similarity

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. Notch signaling pathway Source: Ensembl
  2. embryonic organ development Source: Ensembl
  3. endocytosis Source: ProtInc
  4. epidermal growth factor receptor signaling pathway Source: Reactome
  5. female pregnancy Source: Ensembl
  6. in utero embryonic development Source: Ensembl
  7. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_12484. EGFR downregulation.
SignaLinkiQ9Y6I3.

Names & Taxonomyi

Protein namesi
Recommended name:
Epsin-1
Alternative name(s):
EH domain-binding mitotic phosphoprotein
EPS-15-interacting protein 1
Gene namesi
Name:EPN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:21604. EPN1.

Subcellular locationi

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Membraneclathrin-coated pit By similarity
Note: Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 By similarity.

GO - Cellular componenti

  1. coated pit Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi382 – 3821S → A: Abolishes phosphorylation by CDK1. 1 Publication
Mutagenesisi382 – 3821S → D: Abolishes phosphorylation by CDK1 and reduces REPS2 binding. 1 Publication
Mutagenesisi404 – 4041F → A: Reduces interaction with AP2B1. 1 Publication

Organism-specific databases

PharmGKBiPA134860916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576Epsin-1
PRO_0000074513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei382 – 3821Phosphoserine; by CDK11 Publication
Modified residuei419 – 4191Phosphoserine1 Publication
Modified residuei420 – 4201Phosphoserine1 Publication
Modified residuei435 – 4351Phosphoserine3 Publications
Modified residuei454 – 4541Phosphoserine4 Publications
Modified residuei460 – 4601Phosphothreonine4 Publications
Modified residuei470 – 4701Phosphothreonine1 Publication
Modified residuei494 – 4941Phosphothreonine3 Publications

Post-translational modificationi

Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation.1 Publication
Ubiquitinated By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y6I3.
PaxDbiQ9Y6I3.
PRIDEiQ9Y6I3.

PTM databases

PhosphoSiteiQ9Y6I3.

Expressioni

Gene expression databases

ArrayExpressiQ9Y6I3.
BgeeiQ9Y6I3.
CleanExiHS_EPN1.
GenevestigatoriQ9Y6I3.

Organism-specific databases

HPAiCAB009729.

Interactioni

Subunit structurei

Monomer. Binds clathrin, ZBTB16/ZNF145 and ITSN1. Binds ubiquitinated proteins By similarity. Binds REPS2, EPS15, AP2A1 and AP2A2. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1.4 Publications

Protein-protein interaction databases

BioGridi118965. 41 interactions.
IntActiQ9Y6I3. 9 interactions.
MINTiMINT-110599.
STRINGi9606.ENSP00000406209.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 278
Helixi39 – 479
Helixi51 – 6212
Helixi63 – 653
Helixi72 – 8615
Helixi90 – 989
Helixi100 – 1089
Helixi121 – 13414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1INZNMR-A1-144[»]
ProteinModelPortaliQ9Y6I3.
SMRiQ9Y6I3. Positions 1-158.

Miscellaneous databases

EvolutionaryTraceiQ9Y6I3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 144133ENTH
Add
BLAST
Repeati183 – 20220UIM 1
Add
BLAST
Repeati208 – 22720UIM 2
Add
BLAST
Repeati233 – 25220UIM 3
Add
BLAST
Repeati274 – 27631
Repeati294 – 29632
Repeati306 – 30833
Repeati319 – 32134
Repeati332 – 33435
Repeati349 – 35136
Repeati367 – 36937
Repeati377 – 37938
Repeati502 – 50431
Repeati518 – 52032
Repeati572 – 57433

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 3791068 X 3 AA repeats of [ED]-P-W
Add
BLAST
Regioni502 – 574733 X 3 AA repeats of N-P-F
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi402 – 41110[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 573307Ala/Gly/Pro-rich
Add
BLAST

Domaini

The NPF repeat domain is involved in EPS15 binding.
The DPW repeat domain is involved in AP2A2 and clathrin binding.
The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction with the AP-2 complex subunit AP2B1 By similarity.

Sequence similaritiesi

Belongs to the epsin family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG263730.
HOGENOMiHOG000008298.
HOVERGENiHBG006690.
KOiK12471.
OMAiDPWGGTQ.
OrthoDBiEOG7F511Z.
TreeFamiTF313361.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PfamiPF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]
SMARTiSM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view]
SUPFAMiSSF48464. SSF48464. 1 hit.
PROSITEiPS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6I3-2) [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

MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV    50
VAFSEIMSMI WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM 100
YAVQTLKDFQ YVDRDGKDQG VNVREKAKQL VALLRDEDRL REERAHALKT 150
KEKLAQTATA SSAAVGSGPP PEAEQAWPQS SGEEELQLQL ALAMSKEEAD 200
QPPSCGPEDD AQLQLALSLS REEHDKEERI RRGDDLRLQM AIEESKRETG 250
GKEESSLMDL ADVFTAPAPA PTTDPWGGPA PMAAAVPTAA PTSDPWGGPP 300
VPPAADPWGG PAPTPASGDP WRPAAPAGPS VDPWGGTPAP AAGEGPTPDP 350
WGSSDGGVPV SGPSASDPWT PAPAFSDPWG GSPAKPSTNG TTAAGGFDTE 400
PDEFSDFDRL RTALPTSGSS AGELELLAGE VPARSPGAFD MSGVRGSLAE 450
AVGSPPPAAT PTPTPPTRKT PESFLGPNAA LVDLDSLVSR PGPTPPGAKA 500
SNPFLPGGGP ATGPSVTNPF QPAPPATLTL NQLRLSPVPP VPGAPPTYIS 550
PLGGGPGLPP MMPPGPPAPN TNPFLL 576
Length:576
Mass (Da):60,293
Last modified:May 3, 2011 - v2
Checksum:i68DD433F3168E975
GO
Isoform 2 (identifier: Q9Y6I3-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGDQSWLWNQ...CPLLLQPGTM
     202-226: Missing.

Show »
Length:662
Mass (Da):69,040
Checksum:iBE8DD37499E2DB6A
GO
Isoform 3 (identifier: Q9Y6I3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     202-226: Missing.
     393-393: Missing.

Note: May be due to a competing donor splice site. No experimental confirmation available.

Show »
Length:550
Mass (Da):57,504
Checksum:iDC8BA5EBEB1D5111
GO

Sequence cautioni

Isoform 2 : The sequence AAD38326.1 differs from that shown. Reason: Frameshift at position 98.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGDQSWLWNQAAPGVRSPVF ACSVEKGNVPLVLSEHLAHS RDPGSGAVRFLISPEPWASA ILGTSGLLASPVLPAALDAV TCQHLPQPSSGSRPISPRIG ALCPLLLQPGTM in isoform 2.
VSP_041010
Alternative sequencei202 – 22625Missing in isoform 2 and isoform 3.
VSP_041011Add
BLAST
Alternative sequencei393 – 3931Missing in isoform 3.
VSP_041012

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF073727 mRNA. Translation: AAD38326.1. Frameshift.
AK022454 mRNA. Translation: BAB14041.1.
AC008735 Genomic DNA. No translation available.
AC010525 Genomic DNA. No translation available.
BC044651 mRNA. Translation: AAH44651.1.
CCDSiCCDS46198.1. [Q9Y6I3-1]
CCDS46199.1. [Q9Y6I3-2]
CCDS46200.1. [Q9Y6I3-3]
RefSeqiNP_001123543.1. NM_001130071.1. [Q9Y6I3-1]
NP_001123544.1. NM_001130072.1. [Q9Y6I3-2]
NP_037465.2. NM_013333.3. [Q9Y6I3-3]
XP_005258886.1. XM_005258829.1. [Q9Y6I3-2]
UniGeneiHs.279953.

Genome annotation databases

EnsembliENST00000085079; ENSP00000085079; ENSG00000063245. [Q9Y6I3-3]
ENST00000270460; ENSP00000270460; ENSG00000063245. [Q9Y6I3-2]
ENST00000411543; ENSP00000406209; ENSG00000063245. [Q9Y6I3-1]
GeneIDi29924.
KEGGihsa:29924.
UCSCiuc002qlv.3. human. [Q9Y6I3-3]
uc002qlw.3. human. [Q9Y6I3-2]
uc002qlx.3. human. [Q9Y6I3-1]

Polymorphism databases

DMDMi332278179.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

The bubble's bend - Issue 42 of January 2004

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF073727 mRNA. Translation: AAD38326.1 . Frameshift.
AK022454 mRNA. Translation: BAB14041.1 .
AC008735 Genomic DNA. No translation available.
AC010525 Genomic DNA. No translation available.
BC044651 mRNA. Translation: AAH44651.1 .
CCDSi CCDS46198.1. [Q9Y6I3-1 ]
CCDS46199.1. [Q9Y6I3-2 ]
CCDS46200.1. [Q9Y6I3-3 ]
RefSeqi NP_001123543.1. NM_001130071.1. [Q9Y6I3-1 ]
NP_001123544.1. NM_001130072.1. [Q9Y6I3-2 ]
NP_037465.2. NM_013333.3. [Q9Y6I3-3 ]
XP_005258886.1. XM_005258829.1. [Q9Y6I3-2 ]
UniGenei Hs.279953.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1INZ NMR - A 1-144 [» ]
ProteinModelPortali Q9Y6I3.
SMRi Q9Y6I3. Positions 1-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118965. 41 interactions.
IntActi Q9Y6I3. 9 interactions.
MINTi MINT-110599.
STRINGi 9606.ENSP00000406209.

PTM databases

PhosphoSitei Q9Y6I3.

Polymorphism databases

DMDMi 332278179.

Proteomic databases

MaxQBi Q9Y6I3.
PaxDbi Q9Y6I3.
PRIDEi Q9Y6I3.

Protocols and materials databases

DNASUi 29924.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000085079 ; ENSP00000085079 ; ENSG00000063245 . [Q9Y6I3-3 ]
ENST00000270460 ; ENSP00000270460 ; ENSG00000063245 . [Q9Y6I3-2 ]
ENST00000411543 ; ENSP00000406209 ; ENSG00000063245 . [Q9Y6I3-1 ]
GeneIDi 29924.
KEGGi hsa:29924.
UCSCi uc002qlv.3. human. [Q9Y6I3-3 ]
uc002qlw.3. human. [Q9Y6I3-2 ]
uc002qlx.3. human. [Q9Y6I3-1 ]

Organism-specific databases

CTDi 29924.
GeneCardsi GC19P056186.
H-InvDB HIX0202721.
HGNCi HGNC:21604. EPN1.
HPAi CAB009729.
MIMi 607262. gene.
neXtProti NX_Q9Y6I3.
PharmGKBi PA134860916.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263730.
HOGENOMi HOG000008298.
HOVERGENi HBG006690.
KOi K12471.
OMAi DPWGGTQ.
OrthoDBi EOG7F511Z.
TreeFami TF313361.

Enzyme and pathway databases

Reactomei REACT_12484. EGFR downregulation.
SignaLinki Q9Y6I3.

Miscellaneous databases

EvolutionaryTracei Q9Y6I3.
GeneWikii EPN1.
GenomeRNAii 29924.
NextBioi 52535.
PROi Q9Y6I3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y6I3.
Bgeei Q9Y6I3.
CleanExi HS_EPN1.
Genevestigatori Q9Y6I3.

Family and domain databases

Gene3Di 1.25.40.90. 1 hit.
InterProi IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view ]
Pfami PF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view ]
SMARTi SM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view ]
SUPFAMi SSF48464. SSF48464. 1 hit.
PROSITEi PS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis."
    Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A., Kikuchi A.
    Oncogene 18:5915-5922(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH REPS2.
    Tissue: Brain.
  2. "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: Mammary gland.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  5. "Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation."
    Kariya K., Koyama S., Nakashima S., Oshiro T., Morinaka K., Kikuchi A.
    J. Biol. Chem. 275:18399-18406(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-382, MUTAGENESIS OF SER-382, INTERACTION WITH REPS2; EPS15 AND AP-2 ALPHA SUBUNIT.
  6. "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
    Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
    J. Biol. Chem. 278:30597-30604(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALBP1.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
    Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
    Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1, MUTAGENESIS OF PHE-404.
  9. "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-454 AND THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-454; THR-460 AND THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-419; SER-420; SER-435; SER-454; THR-460 AND THR-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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-435; SER-454; THR-460 AND THR-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin."
    Koshiba S., Kigawa T., Kikuchi A., Yokoyama S.
    J. Struct. Funct. Genomics 2:1-8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-144.

Entry informationi

Entry nameiEPN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6I3
Secondary accession number(s): Q86ST3, Q9HA18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: May 3, 2011
Last modified: September 3, 2014
This is version 135 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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