Q9Y6I3 (EPN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epsin-1

Alternative name(s):
EH domain-binding mitotic phosphoprotein
EPS-15-interacting protein 1

Gene names

Name:

EPN1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Subunit structure	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. Ref.1 Ref.5 Ref.6 Ref.8
Subcellular location	Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity. Membrane › clathrin-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.
Domain	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.
Post-translational modification	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. Ref.5 Ubiquitinated By similarity.
Sequence similarities	Belongs to the epsin family. Contains 1 ENTH (epsin N-terminal homology) domain. Contains 3 UIM (ubiquitin-interacting motif) repeats.
Sequence caution	Isoform 2: The sequence AAD38326.1 differs from that shown. Reason: Frameshift at position 98.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Coated pit Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Lipid-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Inferred from electronic annotation. Source: Compara embryonic organ development Inferred from electronic annotation. Source: Compara endocytosis Traceable author statement PubMed 9723620. Source: ProtInc epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome female pregnancy Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: Reactome
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y6I3-2)

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: Q9Y6I3-1)

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

Isoform 3 (identifier: Q9Y6I3-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 576

576

Epsin-1

PRO_0000074513

Regions

Domain

12 – 144

133

ENTH

Repeat

183 – 202

20

UIM 1

Repeat

208 – 227

20

UIM 2

Repeat

233 – 252

20

UIM 3

Repeat

274 – 276

3

1

Repeat

294 – 296

3

2

Repeat

306 – 308

3

3

Repeat

319 – 321

3

4

Repeat

332 – 334

3

5

Repeat

349 – 351

3

6

Repeat

367 – 369

3

7

Repeat

377 – 379

3

8

Repeat

502 – 504

3

1

Repeat

518 – 520

3

2

Repeat

572 – 574

3

3

Region

274 – 379

106

8 X 3 AA repeats of [ED]-P-W

Region

502 – 574

73

3 X 3 AA repeats of N-P-F

Motif

402 – 411

10

[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

Compositional bias

267 – 573

307

Ala/Gly/Pro-rich

Sites

Binding site

8

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

11

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

25

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

30

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

63

1

Phosphatidylinositol lipid headgroup By similarity

Binding site

73

1

Phosphatidylinositol lipid headgroup By similarity

Amino acid modifications

Modified residue

382

1

Phosphoserine; by CDK1 Ref.5

Modified residue

419

1

Phosphoserine Ref.12

Modified residue

420

1

Phosphoserine Ref.12

Modified residue

435

1

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

454

1

Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13

Modified residue

460

1

Phosphothreonine Ref.9 Ref.11 Ref.12 Ref.13

Modified residue

470

1

Phosphothreonine Ref.12

Modified residue

494

1

Phosphothreonine Ref.7 Ref.11 Ref.13

Natural variations

Alternative sequence

1

1

M → MGDQSWLWNQAAPGVRSPVF ACSVEKGNVPLVLSEHLAHS RDPGSGAVRFLISPEPWASA ILGTSGLLASPVLPAALDAV TCQHLPQPSSGSRPISPRIG ALCPLLLQPGTM in isoform 2.

VSP_041010

Alternative sequence

202 – 226

25

Missing in isoform 2 and isoform 3.

VSP_041011

Alternative sequence

393

1

Missing in isoform 3.

VSP_041012

Experimental info

Mutagenesis

382

1

S → A: Abolishes phosphorylation by CDK1. Ref.5

Mutagenesis

382

1

S → D: Abolishes phosphorylation by CDK1 and reduces REPS2 binding. Ref.5

Mutagenesis

404

1

F → A: Reduces interaction with AP2B1. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

576

Helix Strand Turn

Details...

Helix

20 – 27

8

Helix

39 – 47

9

Helix

51 – 62

12

Helix

63 – 65

3

Helix

72 – 86

15

Helix

90 – 98

9

Helix

100 – 108

9

Helix

121 – 134

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 3, 2011. Version 2. Checksum: 68DD433F3168E975	FASTA	576	60,293
	10 20 30 40 50 60 MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI 70 80 90 100 110 120 WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG 130 140 150 160 170 180 VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS 190 200 210 220 230 240 SGEEELQLQL ALAMSKEEAD QPPSCGPEDD AQLQLALSLS REEHDKEERI RRGDDLRLQM 250 260 270 280 290 300 AIEESKRETG GKEESSLMDL ADVFTAPAPA PTTDPWGGPA PMAAAVPTAA PTSDPWGGPP 310 320 330 340 350 360 VPPAADPWGG PAPTPASGDP WRPAAPAGPS VDPWGGTPAP AAGEGPTPDP WGSSDGGVPV 370 380 390 400 410 420 SGPSASDPWT PAPAFSDPWG GSPAKPSTNG TTAAGGFDTE PDEFSDFDRL RTALPTSGSS 430 440 450 460 470 480 AGELELLAGE VPARSPGAFD MSGVRGSLAE AVGSPPPAAT PTPTPPTRKT PESFLGPNAA 490 500 510 520 530 540 LVDLDSLVSR PGPTPPGAKA SNPFLPGGGP ATGPSVTNPF QPAPPATLTL NQLRLSPVPP 550 560 570 VPGAPPTYIS PLGGGPGLPP MMPPGPPAPN TNPFLL
	Isoform 2 [UniParc]. Checksum: BE8DD37499E2DB6A	FASTA	662	69,040
	10 20 30 40 50 60 MGDQSWLWNQ AAPGVRSPVF ACSVEKGNVP LVLSEHLAHS RDPGSGAVRF LISPEPWASA 70 80 90 100 110 120 ILGTSGLLAS PVLPAALDAV TCQHLPQPSS GSRPISPRIG ALCPLLLQPG TMSTSSLRRQ 130 140 150 160 170 180 MKNIVHNYSE AEIKVREATS NDPWGPSSSL MSEIADLTYN VVAFSEIMSM IWKRLNDHGK 190 200 210 220 230 240 NWRHVYKAMT LMEYLIKTGS ERVSQQCKEN MYAVQTLKDF QYVDRDGKDQ GVNVREKAKQ 250 260 270 280 290 300 LVALLRDEDR LREERAHALK TKEKLAQTAT ASSAAVGSGP PPEAEQAWPQ SSGEEELQLQ 310 320 330 340 350 360 LALAMSKEEA DQEERIRRGD DLRLQMAIEE SKRETGGKEE SSLMDLADVF TAPAPAPTTD 370 380 390 400 410 420 PWGGPAPMAA AVPTAAPTSD PWGGPPVPPA ADPWGGPAPT PASGDPWRPA APAGPSVDPW 430 440 450 460 470 480 GGTPAPAAGE GPTPDPWGSS DGGVPVSGPS ASDPWTPAPA FSDPWGGSPA KPSTNGTTAA 490 500 510 520 530 540 GGFDTEPDEF SDFDRLRTAL PTSGSSAGEL ELLAGEVPAR SPGAFDMSGV RGSLAEAVGS 550 560 570 580 590 600 PPPAATPTPT PPTRKTPESF LGPNAALVDL DSLVSRPGPT PPGAKASNPF LPGGGPATGP 610 620 630 640 650 660 SVTNPFQPAP PATLTLNQLR LSPVPPVPGA PPTYISPLGG GPGLPPMMPP GPPAPNTNPF LL
	Isoform 3 [UniParc]. Checksum: DC8BA5EBEB1D5111	FASTA	550	57,504
	10 20 30 40 50 60 MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI 70 80 90 100 110 120 WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG 130 140 150 160 170 180 VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS 190 200 210 220 230 240 SGEEELQLQL ALAMSKEEAD QEERIRRGDD LRLQMAIEES KRETGGKEES SLMDLADVFT 250 260 270 280 290 300 APAPAPTTDP WGGPAPMAAA VPTAAPTSDP WGGPPVPPAA DPWGGPAPTP ASGDPWRPAA 310 320 330 340 350 360 PAGPSVDPWG GTPAPAAGEG PTPDPWGSSD GGVPVSGPSA SDPWTPAPAF SDPWGGSPAK 370 380 390 400 410 420 PSTNGTTAGG FDTEPDEFSD FDRLRTALPT SGSSAGELEL LAGEVPARSP GAFDMSGVRG 430 440 450 460 470 480 SLAEAVGSPP PAATPTPTPP TRKTPESFLG PNAALVDLDS LVSRPGPTPP GAKASNPFLP 490 500 510 520 530 540 GGGPATGPSV TNPFQPAPPA TLTLNQLRLS PVPPVPGAPP TYISPLGGGP GLPPMMPPGP 550 PAPNTNPFLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-454; THR-460 AND THR-494, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The bubble's bend - Issue 42 of January 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00027082.
IPI00397365.
IPI00647389.

RefSeq

NP_001123543.1. NM_001130071.1.
NP_001123544.1. NM_001130072.1.
NP_037465.2. NM_013333.3.

UniGene

Hs.279953.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1INZ	NMR	-	A	1-144	[»]

ProteinModelPortal

Q9Y6I3.

SMR

Q9Y6I3. Positions 1-158.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y6I3. 6 interactions.

MINT

MINT-110599.

STRING

9606.ENSP00000406209.

PTM databases

PhosphoSite

Q9Y6I3.

Polymorphism databases

DMDM

41017059.

Proteomic databases

PaxDb

Q9Y6I3.

PRIDE

Q9Y6I3.

Protocols and materials databases

DNASU

29924.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000085079; ENSP00000085079; ENSG00000063245.
ENST00000270460; ENSP00000270460; ENSG00000063245.
ENST00000411543; ENSP00000406209; ENSG00000063245.

GeneID

29924.

KEGG

hsa:29924.

UCSC

uc002qlv.3. human.
uc002qlw.3. human.
uc002qlx.3. human.

Organism-specific databases

CTD

29924.

GeneCards

GC19P056186.

H-InvDB

HIX0202721.

HGNC

HGNC:21604. EPN1.

HPA

CAB009729.

MIM

607262. gene.

neXtProt

NX_Q9Y6I3.

PharmGKB

PA134860916.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG263730.

HOGENOM

HOG000008298.

HOVERGEN

HBG006690.

KO

K12471.

OMA

PWGSSDG.

OrthoDB

EOG4SF97B.

PhylomeDB

Q9Y6I3.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q9Y6I3.

Bgee

Q9Y6I3.

CleanEx

HS_EPN1.

Genevestigator

Q9Y6I3.

GermOnline

ENSG00000063245. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.90. 1 hit.

InterPro

IPR008942. ENTH_VHS.
IPR027320. Epsin-1_mammalian.
IPR013809. Epsin-like_N.
IPR001026. Epsin_dom_N.
IPR003903. Ubiquitin-int_motif.
[Graphical view]

PANTHER

PTHR12276:SF17. PTHR12276:SF17. 1 hit.

Pfam

PF01417. ENTH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]

SMART

SM00273. ENTH. 1 hit.
SM00726. UIM. 3 hits.
[Graphical view]

SUPFAM

SSF48464. ENTH_VHS. 1 hit.

PROSITE

PS50942. ENTH. 1 hit.
PS50330. UIM. 3 hits.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9Y6I3.

GenomeRNAi

29924.

NextBio

52535.

SOURCE

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Entry information

Entry name

EPN1_HUMAN

Accession

Primary (citable) accession number: Q9Y6I3
Secondary accession number(s): Q86ST3, Q9HA18

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 3, 2011
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.