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O95208 (EPN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epsin-2
Alternative name(s):
EPS-15-interacting protein 2
Gene names
Name:EPN2
Synonyms:KIAA1065
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the formation of clathrin-coated invaginations and endocytosis. Ref.1

Subunit structure

Binds EPS15 By similarity. Binds AP-2 and clathrin.

Subcellular location

Cytoplasm. Cytoplasmic vesicleclathrin-coated vesicle. Note: In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex. Ref.1

Tissue specificity

Highest expression is found in brain. Detected at lower levels in lung and liver. Ref.1

Domain

The NPF repeat domain is involved in EPS15 binding.

The DPW repeat domain is involved in AP-2 and clathrin binding.

Post-translational modification

Ubiquitinated By similarity.

Sequence similarities

Belongs to the epsin family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Contains 2 UIM (ubiquitin-interacting motif) repeats.

Sequence caution

The sequence BAA83017.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG52540.1 differs from that shown. Reason: Erroneous termination at position 324. Translated as Glu.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95208-1)

Also known as: 2b;

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.
Isoform 2 (identifier: O95208-2)

Also known as: 2a;

The sequence of this isoform differs from the canonical sequence as follows:
     200-256: Missing.
Note: Contains a phosphoserine at position 192. Contains a phosphoserine at position 195.
Isoform 3 (identifier: O95208-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     200-256: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 153. Contains a phosphoserine at position 156.
Isoform 4 (identifier: O95208-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-285: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 641641Epsin-2
PRO_0000074516

Regions

Domain12 – 144133ENTH
Repeat275 – 29420UIM 1
Repeat300 – 31920UIM 2
Repeat352 – 35431
Repeat364 – 36632
Repeat377 – 37933
Repeat391 – 39334
Repeat409 – 41135
Repeat427 – 42936
Repeat537 – 53931
Repeat552 – 55432
Repeat637 – 63933
Region352 – 6392886 X 3 AA repeats of [DE]-P-W
Region537 – 6391033 X 3 AA repeats of N-P-F

Sites

Binding site81Phosphatidylinositol lipid headgroup By similarity
Binding site111Phosphatidylinositol lipid headgroup By similarity
Binding site251Phosphatidylinositol lipid headgroup By similarity
Binding site301Phosphatidylinositol lipid headgroup By similarity
Binding site631Phosphatidylinositol lipid headgroup By similarity
Binding site731Phosphatidylinositol lipid headgroup By similarity

Natural variations

Alternative sequence1 – 285285Missing in isoform 4.
VSP_047003
Alternative sequence1 – 3939Missing in isoform 3.
VSP_009154
Alternative sequence200 – 25657Missing in isoform 2 and isoform 3.
VSP_009155
Natural variant4011V → A. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs6587220 [ dbSNP | Ensembl ].
VAR_053080
Natural variant5311P → T.
Corresponds to variant rs1062727 [ dbSNP | Ensembl ].
VAR_047923
Natural variant5321P → T.
Corresponds to variant rs1062727 [ dbSNP | Ensembl ].
VAR_053081

Experimental info

Sequence conflict2561A → AS in AAC78609. Ref.1
Sequence conflict5471T → N in AAC78608. Ref.1
Sequence conflict5471T → N in AAC78609. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (2b) [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: 0BE24CBD824F357A

FASTA64168,482
        10         20         30         40         50         60 
MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV VAFSEIMSMV 

        70         80         90        100        110        120 
WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI FAIQTLKDFQ YIDRDGKDQG 

       130        140        150        160        170        180 
INVREKSKQL VALLKDEERL KAERAQALKT KERMAQVATG MGSNQITFGR GSSQPNLSTS 

       190        200        210        220        230        240 
HSEQEYGKAG GSPASYHGSP EASLCPQHRT GAPLGQSEEL QPLSQRHPFL PHLGLASRPN 

       250        260        270        280        290        300 
GDWSQPCLTC DRAARATSPR VSSELEQARP QTSGEEELQL QLALAMSREV AEQEERLRRG 

       310        320        330        340        350        360 
DDLRLQMALE ESRRDTVKIP KKKEHGSLPQ QTTLLDLMDA LPSSGPAAQK AEPWGPSAST 

       370        380        390        400        410        420 
NQTNPWGGPA APASTSDPWP SFGTKPAASI DPWGVPTGAT VQSVPKNSDP WAASQQPASS 

       430        440        450        460        470        480 
AGKRASDAWG AVSTTKPVSV SGSFELFSNL NGTIKDDFSE FDNLRTSKKT AESVTSLPSQ 

       490        500        510        520        530        540 
NNGTTSPDPF ESQPLTVASS KPSSARKTPE SFLGPNAALV NLDSLVTRPA PPAQSLNPFL 

       550        560        570        580        590        600 
APGAPATSAP VNPFQVNQPQ PLTLNQLRGS PVLGTSTSFG PGPGVESMAV ASMTSAAPQP 

       610        620        630        640 
ALGATGSSLT PLGPAMMNMV GSVGIPPSAA QATGTTNPFL L 

« Hide

Isoform 2 (2a) [UniParc].

Checksum: D668242ECACD26EF
Show »

FASTA58462,300
Isoform 3 [UniParc].

Checksum: C8D6661429926997
Show »

FASTA54557,919
Isoform 4 [UniParc].

Checksum: EF6741C03E5744A3
Show »

FASTA35636,729

References

« Hide 'large scale' references
[1]"The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module."
Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E., Di Fiore P.P., De Camilli P.
J. Biol. Chem. 274:33959-33965(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH AP-2 AND CLATHRIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ALA-401.
Tissue: Brain.
[2]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-401.
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORM 3), VARIANT ALA-401.
Tissue: Embryo, Fetal brain and Placenta.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-401.
[6]"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], VARIANT ALA-401.
Tissue: Brain.
[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 SER-192 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-192 AND SER-195 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-156 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF062084 mRNA. Translation: AAC78608.1.
AF062085 mRNA. Translation: AAC78609.1.
AB028988 mRNA. Translation: BAA83017.2. Different initiation.
AK001996 mRNA. Translation: BAG51000.1.
AK024115 mRNA. Translation: BAB14831.1.
AK092366 mRNA. Translation: BAG52540.1. Sequence problems.
AC106017 Genomic DNA. No translation available.
AC124066 Genomic DNA. No translation available.
CH471212 Genomic DNA. Translation: EAW50876.1.
BC093972 mRNA. Translation: AAH93972.1.
BC093974 mRNA. Translation: AAH93974.1.
CCDSCCDS11203.1. [O95208-1]
CCDS11204.1. [O95208-2]
CCDS42277.1. [O95208-5]
RefSeqNP_001096134.1. NM_001102664.1. [O95208-5]
NP_055779.2. NM_014964.4. [O95208-1]
NP_683723.2. NM_148921.3. [O95208-2]
UniGeneHs.743983.

3D structure databases

ProteinModelPortalO95208.
SMRO95208. Positions 1-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116569. 8 interactions.
STRING9606.ENSP00000320543.

PTM databases

PhosphoSiteO95208.

Proteomic databases

MaxQBO95208.
PaxDbO95208.
PRIDEO95208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314728; ENSP00000320543; ENSG00000072134. [O95208-1]
ENST00000347697; ENSP00000261495; ENSG00000072134. [O95208-2]
ENST00000395618; ENSP00000378980; ENSG00000072134. [O95208-5]
ENST00000395620; ENSP00000378982; ENSG00000072134. [O95208-2]
GeneID22905.
KEGGhsa:22905.
UCSCuc002gvd.4. human. [O95208-1]

Organism-specific databases

CTD22905.
GeneCardsGC17P019118.
H-InvDBHIX0013614.
HGNCHGNC:18639. EPN2.
HPAHPA049809.
HPA053360.
MIM607263. gene.
neXtProtNX_O95208.
PharmGKBPA38615.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263730.
HOGENOMHOG000008298.
HOVERGENHBG006690.
InParanoidO95208.
KOK12471.
OMAQEYGKSG.
OrthoDBEOG7F511Z.
PhylomeDBO95208.
TreeFamTF313361.

Gene expression databases

ArrayExpressO95208.
BgeeO95208.
CleanExHS_EPN2.
GenevestigatorO95208.

Family and domain databases

Gene3D1.25.40.90. 1 hit.
InterProIPR008942. ENTH_VHS.
IPR027319. Epsin-2_metazoa.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view]
PANTHERPTHR12276:SF50. PTHR12276:SF50. 1 hit.
PfamPF01417. ENTH. 1 hit.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
SM00726. UIM. 2 hits.
[Graphical view]
SUPFAMSSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPN2. human.
GeneWikiEPN2.
GenomeRNAi22905.
NextBio43557.
PMAP-CutDBO95208.
PROO95208.
SOURCESearch...

Entry information

Entry nameEPN2_HUMAN
AccessionPrimary (citable) accession number: O95208
Secondary accession number(s): A8MTV8 expand/collapse secondary AC list , B3KRX8, E9PBC2, O95207, Q52LD0, Q9H7Z2, Q9UPT7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 123 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM