Reviewed, UniProtKB/Swiss-Prot P34216 (EDE1_YEAST)

Names and origin

Protein names

Recommended name:
    EH domain-containing and endocytosis protein 1
Alternative name(s):
    Bud site selection protein 15

Gene names

Name:	EDE1
Synonyms:	BUD15
Ordered Locus Names:	YBL047C
ORF Names:	YBL0520, YBL0501

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions at the internalization step of the clathrin-mediated endocytosis (CME) as an early-acting scaffold protein. Requires clathrin adapter proteins, ENT1/2 and YAP1801/2, for normal spatiotemporal dynamics and viability. Binds to biological membranes in a ubiquitin-dependent manner. Ref.4 Ref.7 Ref.10 Ref.15
Subunit structure	Interacts (via UBA domain) with monoubiquitin and ENT1 (via asparagine-proline-phenylalanine tripeptide motif called NPF). Ref.7 Ref.17
Subcellular location	Cytoplasm. Note: Localized to actin cortical patches concentrated in the developing bud tip in cells with small buds and at the mother-daughter neck in cells undergoing cytokinesis. Localization can be maintained in the absence of polymerized actin filaments. Ref.4 Ref.15 Ref.5 Ref.8
Disruption phenotype	Random budding pattern and morphological defects. Defects in fluid-phase endocytosis and defective internalization of the pheromone alpha-factor and uracil permease. Deletion has only a small impact on actin cytoskeleton organization. Deletion shows synthetic growth defects with thermosensitive mutants of PAN1, END3 and RSP5. Ref.4 Ref.5
Miscellaneous	Present with 1380 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the VDP/USO1/EDE1 family. Contains 3 EH domains. Contains 1 UBA domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	endocytosis Ref.4 Inferred from mutant phenotype. Source: SGD endoplasmic reticulum unfolded protein response Inferred from mutant phenotype. Source: SGD
Cellular component	actin cortical patch Ref.4 Inferred from direct assay. Source: SGD cellular bud neck Ref.5 Inferred from direct assay. Source: SGD cellular bud tip Ref.5 Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro ubiquitin binding Ref.17 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1381

1381

EH domain-containing and endocytosis protein 1

PRO_0000202457

Regions

Domain

14 – 113

100

EH 1

Domain

135 – 227

93

EH 2

Domain

277 – 366

90

EH 3

Domain

1338 – 1380

43

UBA

Region

1217 – 1381

165

Able to bind biological membranes

Coiled coil

593 – 882

290

Potential

Compositional bias

550 – 575

26

Ala-rich

Amino acid modifications

Modified residue

238

1

Phosphothreonine Ref.12 Ref.16

Modified residue

241

1

Phosphoserine Ref.12 Ref.16 Ref.6 Ref.11 Ref.14

Modified residue

244

1

Phosphoserine Ref.12 Ref.16 Ref.14

Modified residue

245

1

Phosphothreonine Ref.12 Ref.16 Ref.6 Ref.11

Modified residue

248

1

Phosphoserine Ref.12 Ref.16

Modified residue

249

1

Phosphoserine Ref.12 Ref.16

Modified residue

251

1

Phosphothreonine Ref.16

Modified residue

261

1

Phosphothreonine Ref.16

Modified residue

265

1

Phosphoserine Ref.16

Modified residue

419

1

Phosphoserine Ref.16

Modified residue

423

1

Phosphoserine Ref.16

Modified residue

433

1

Phosphoserine Ref.16

Modified residue

438

1

Phosphoserine Ref.16

Modified residue

487

1

Phosphothreonine Ref.12 Ref.16

Modified residue

489

1

Phosphothreonine Ref.16

Modified residue

495

1

Phosphoserine Ref.16

Modified residue

511

1

Phosphoserine Ref.16

Modified residue

513

1

Phosphothreonine Ref.16

Modified residue

527

1

Phosphoserine Ref.14

Modified residue

534

1

Phosphoserine Ref.16

Modified residue

603

1

Phosphothreonine Ref.16

Modified residue

848

1

Phosphoserine Ref.16

Modified residue

911

1

Phosphoserine Ref.13

Modified residue

931

1

Phosphoserine Ref.16

Modified residue

950

1

Phosphoserine Ref.16

Modified residue

964

1

Phosphoserine Ref.16

Modified residue

1006

1

Phosphoserine Ref.16 Ref.14

Modified residue

1008

1

Phosphoserine Ref.16 Ref.14

Modified residue

1011

1

Phosphoserine Ref.16

Modified residue

1012

1

Phosphoserine Ref.16

Modified residue

1020

1

Phosphoserine Ref.16

Modified residue

1062

1

Phosphothreonine Ref.16

Modified residue

1064

1

Phosphoserine Ref.16

Modified residue

1065

1

Phosphothreonine Ref.16

Modified residue

1069

1

Phosphoserine Ref.16

Modified residue

1072

1

Phosphothreonine Ref.16

Modified residue

1087

1

Phosphoserine Ref.16 Ref.14

Modified residue

1093

1

Phosphoserine Ref.12 Ref.16 Ref.14 Ref.13

Modified residue

1095

1

Phosphoserine Ref.16 Ref.14 Ref.13

Modified residue

1096

1

Phosphoserine Ref.12 Ref.16 Ref.14

Modified residue

1100

1

Phosphoserine Ref.12 Ref.16 Ref.14 Ref.13

Modified residue

1111

1

Phosphothreonine Ref.16

Modified residue

1160

1

Phosphothreonine Ref.16

Modified residue

1161

1

Phosphoserine Ref.16

Modified residue

1178

1

Phosphothreonine Ref.16

Modified residue

1179

1

Phosphoserine Ref.14 Ref.13

Modified residue

1181

1

Phosphoserine Ref.16 Ref.13

Modified residue

1307

1

Phosphothreonine Ref.12 Ref.16 Ref.11

Modified residue

1309

1

Phosphoserine Ref.16

Modified residue

1339

1

Phosphothreonine Ref.16

Modified residue

1340

1

Phosphothreonine Ref.16 Ref.6 Ref.14 Ref.13

Modified residue

1343

1

Phosphoserine Ref.16 Ref.14

Experimental info

Mutagenesis

56

1

W → A: Abnormal spatiotemporal behavior. Ref.15

Mutagenesis

176

1

W → A: Abnormal spatiotemporal behavior. Ref.15

Mutagenesis

319

1

W → A: Abnormal spatiotemporal behavior. Ref.15

Mutagenesis

1352

1

M → A: Reduced ubiquitin-binding. Ref.17

Mutagenesis

1370

1

L → A: Reduced ubiquitin-binding. Ref.17

Mutagenesis

1374

1

T → A: Enhanced ubiquitin-binding. Ref.17

Mutagenesis

1378

1

L → A: Reduced ubiquitin-binding. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

1381

Helix Strand Turn

Details...

Helix

1341 – 1350

10

Turn

1351 – 1353

3

Helix

1356 – 1365

10

Helix

1370 – 1378

9

Sequences

	Sequence		Length	Mass (Da)
	P34216-1 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 626FD261DCBA7D99	FASTA	1,381	150,783
	10 20 30 40 50 60 MASITFRTPL SSQEQAFYNQ KFHQLDTEDL GVVTGEAVRP LFASSGLPGQ LLSQVWATVD 70 80 90 100 110 120 IDNKGFLNLN EFSAALRMIA QLQNAPNQPI SAALYESTPT QLASFSINQN PAPMQSGSAT 130 140 150 160 170 180 GNTNNTDIPA LSSNDIAKFS QLFDRTAKGA QTVAGDKAKD IFLKARLPNQ TLGEIWALCD 190 200 210 220 230 240 RDASGVLDKS EFIMAMYLIQ LCMSHHPSMN TPPAVLPTQL WDSIRLEPVV VNQPNRTTPL 250 260 270 280 290 300 SANSTGVSSL TRHSTISRLS TGAFSNAASD WSLSFEKKQQ FDAIFDSLDK QHAGSLSSAV 310 320 330 340 350 360 LVPFFLSSRL NQETLATIWD LADIHNNAEF TKLEFAIAMF LIQKKNAGVE LPDVIPNELL 370 380 390 400 410 420 QSPALGLYPP NPLPQQQSAP QIAIPSRASK PSLQDMPHQV SAPAVNTQPT VPQVLPQNSN 430 440 450 460 470 480 NGSLNDLLAL NPSFSSPSPT KAQTVVQNNT NNSFSYDNNN GQATLQQQQP QQPPPLTHSS 490 500 510 520 530 540 SGLKKFTPTS NFGQSIIKEE PEEQEQLRES SDTFSAQPPP VPKHASSPVK RTASTTLPQV 550 560 570 580 590 600 PNFSVFSMPA GAATSAATGA AVGAAVGAAA LGASAFSRSS NNAFKNQDLF ADGEASAQLS 610 620 630 640 650 660 NATTEMANLS NQVNSLSKQA SITNDKKSRA TQELKRVTEM KNSIQIKLNN LRSTHDQNVK 670 680 690 700 710 720 QTEQLEAQVL QVNKENETLA QQLAVSEANY HAAESKLNEL TTDLQESQTK NAELKEQITN 730 740 750 760 770 780 LNSMTASLQS QLNEKQQQVK QERSMVDVNS KQLELNQVTV ANLQKEIDGL GEKISVYLTK 790 800 810 820 830 840 QKELNDYQKT VEEQHAQLQA KYQDLSNKDT DLTDREKQLE ERNRQIEEQE NLYHQHVSKL 850 860 870 880 890 900 QEMFDDLSQR KASFEKADQE LKERNIEYAN NVRELSERQM NLAMGQLPED AKDIIAKSAS 910 920 930 940 950 960 NTDTTTKEAT SRGNVHEDTV SKFVETTVEN SNLNVNRVKD DEEKTERTES DVFDRDVPTL 970 980 990 1000 1010 1020 GSQSDSENAN TNNGTQSGNE TANPNLTETL SDRFDGDLNE YGIPRSQSLT SSVANNAPQS 1030 1040 1050 1060 1070 1080 VRDDVELPET LEERDTINNT ANRDNTGNLS HIPGEWEATP ATASTDVLSN ETTEVIEDGS 1090 1100 1110 1120 1130 1140 TTKRANSNED GESVSSIQES PKISAQPKAK TINEEFPPIQ ELHIDESDSS SSDDDEFEDT 1150 1160 1170 1180 1190 1200 REIPSATVKT LQTPYNAQPT SSLEIHTEQV IKYPAPGTSP SHNEGNSKKA STNSILPVKD 1210 1220 1230 1240 1250 1260 EFDDEFAGLE QAAVEEDNGA DSESEFENVA NAGSMEQFET IDHKDLDDEL QMNAFTGTLT 1270 1280 1290 1300 1310 1320 SSSNPTIPKP QVQQQSTSDP AQVSNDEWDE IFAGFGNSKA EPTKVATPSI PQQPIPLKND 1330 1340 1350 1360 1370 1380 PIVDASLSKG PIVNRGVATT PKSLAVEELS GMGFTEEEAH NALEKCNWDL EAATNFLLDS A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein." de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J., Goffeau A. Yeast 10:1489-1496(1994) [PubMed: 7871888] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-961. Strain: ATCC 204508 / S288c.
[3]	"Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes." Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F. Yeast 9:1355-1371(1993) [PubMed: 8154187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 579-1381. Strain: ATCC 204508 / S288c.
[4]	"A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis." Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H., Haguenauer-Tsapis R. J. Cell Sci. 113:3309-3319(2000) [PubMed: 10954428] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[5]	"A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae." Ni L., Snyder M. Mol. Biol. Cell 12:2147-2170(2001) [PubMed: 11452010] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
[6]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-245 AND THR-1340, MASS SPECTROMETRY.
[7]	"The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions." Aguilar R.C., Watson H.A., Wendland B. J. Biol. Chem. 278:10737-10743(2003) [PubMed: 12529323] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBIQUITIN AND ENT1, REGION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"A modular design for the clathrin- and actin-mediated endocytosis machinery." Kaksonen M., Toret C.P., Drubin D.G. Cell 123:305-320(2005) [PubMed: 16239147] [Abstract] Cited for: FUNCTION, DISRUPTION MUTANT.
[11]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-245 AND THR-1307, MASS SPECTROMETRY.
[12]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238; SER-241; SER-244; THR-245; SER-248; SER-249; THR-487; SER-1093; SER-1096; SER-1100 AND THR-1307, MASS SPECTROMETRY.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; SER-1093; SER-1095; SER-1100; SER-1179; SER-1181 AND THR-1340, MASS SPECTROMETRY.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-244; SER-527; SER-1006; SER-1008; SER-1087; SER-1093; SER-1095; SER-1096; SER-1100; SER-1179; THR-1340 AND SER-1343, MASS SPECTROMETRY.
[15]	"Interaction between Epsin/Yap180 adaptors and the scaffolds Ede1/Pan1 is required for endocytosis." Maldonado-Baez L., Dores M.R., Perkins E.M., Drivas T.G., Hicke L., Wendland B. Mol. Biol. Cell 19:2936-2948(2008) [PubMed: 18448668] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-56; TRP-176 AND TRP-319.
[16]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238; SER-241; SER-244; THR-245; SER-248; SER-249; THR-251; THR-261; SER-265; SER-419; SER-423; SER-433; SER-438; THR-487; THR-489; SER-495; SER-511; THR-513; SER-534; THR-603; SER-848; SER-931; SER-950; SER-964; SER-1006; SER-1008; SER-1011; SER-1012; SER-1020; THR-1062; SER-1064; THR-1065; SER-1069; THR-1072; SER-1087; SER-1093; SER-1095; SER-1096; SER-1100; THR-1111; THR-1160; SER-1161; THR-1178; SER-1181; THR-1307; SER-1309; THR-1339; THR-1340 AND SER-1343, MASS SPECTROMETRY.
[17]	"Structural basis for monoubiquitin recognition by the Ede1 UBA domain." Swanson K.A., Hicke L., Radhakrishnan I. J. Mol. Biol. 358:713-724(2006) [PubMed: 16563434] [Abstract] Cited for: STRUCTURE BY NMR OF 1339-1381 IN COMPLEX WITH MONOUBIQUITIN, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MONOUBIQUITIN, UBA DOMAIN, MUTAGENESIS OF MET-1352; LEU-1370; THR-1374 AND LEU-1378.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z35808 Genomic DNA. Translation: CAA84867.1.
X78214 Genomic DNA. Translation: CAA55048.1.
Z23261 Genomic DNA. Translation: CAA80797.1.

PIR

S45781.

RefSeq

NP_009506.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G3Q	NMR	-	A	1339-1381	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5817N.

IntAct

P34216. 28 interactions.

STRING

P34216.

Proteomic databases

PeptideAtlas

P34216.

PRIDE

P34216.

Genome annotation databases

Ensembl

YBL047C; YBL047C; YBL047C; Saccharomyces cerevisiae. [Genome view]

GeneID

852233.

KEGG

sce:YBL047C.

NMPDR

fig|4932.3.peg.196.

Organism-specific databases

CYGD

YBL047c.

SGD

S000000143. EDE1.

Phylogenomic databases

HOGENOM

HBG204251.

OMA

NDEWEQL.

OrthoDB

EOG9641VM.

Gene expression databases

ArrayExpress

P34216.

Genevestigator

P34216.

GermOnline

YBL047C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011992. EF-Hand_type.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR018248. EF_Hand_dom.
IPR000261. EPS15_homology.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 3 hits.

Pfam

PF00036. efhand. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]

SMART

SM00054. EFh. 2 hits.
SM00027. EH. 3 hits.
SM00165. UBA. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
PS50031. EH. 3 hits.
PS50030. UBA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

970769.

Entry information

Entry name

EDE1_YEAST

Accession

Primary (citable) accession number: P34216

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 1, 1994
Last modified:	December 15, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)