Q86VN1 (VPS36_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein-sorting-associated protein 36

Alternative name(s):
ELL-associated protein of 45 kDa
ESCRT-II complex subunit VPS36

Gene names

Name:	VPS36
Synonyms:	C13orf9, EAP45
ORF Names:	CGI-145

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	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3. Ref.10
Subunit structure	Component of a complex at least composed of ELL, SNF8/EAP30, VPS25/EAP20 and VPS36/EAP45 By similarity. Component of the endosomal sorting complex required for transport II (ESCRT-II), composed of SNF8, VPS36 and two copies of VPS25. Interacts with VPS25, SNF8, TSG101 and VPS36. Interacts (via GLUE domain) with ubiquitin. Interacts with RILPL1 (via the C-terminal domain); which recruits ESCRT-II to the endosome membranes. Interacts with ECM29. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14
Subcellular location	Cytoplasm. Endosome. Late endosome. Membrane. Nucleus Probable. Note: Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Domain	The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates the binding to ubiquitin and phosphoinosides. Ref.10
Sequence similarities	Belongs to the VPS36 family. Contains 1 GLUE C-terminal domain. Contains 1 GLUE N-terminal domain.
Sequence caution	The sequence BAB14451.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	Lipid-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular membrane organization Traceable author statement. Source: Reactome endosomal transport Traceable author statement. Source: Reactome protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome endosome Inferred from direct assay Ref.14. Source: UniProtKB late endosome Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: Compara membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatidylinositol-3-phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86VN1-1)

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: Q86VN1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Vacuolar protein-sorting-associated protein 36

PRO_0000215222

Regions

Domain

1 – 88

88

GLUE N-terminal

Domain

105 – 138

34

GLUE C-terminal

Coiled coil

160 – 185

26

Potential

Natural variations

Alternative sequence

1 – 58

58

Missing in isoform 2.

VSP_015342

Experimental info

Mutagenesis

10

1

L → D: No effect on interaction with ubiquitin. Ref.16

Mutagenesis

67

1

V → A: Reduces affinity for ubiquitin up to 10-fold. Ref.16

Mutagenesis

68

1

F → A: Reduces affinity for ubiquitin up to 10-fold. Ref.16

Mutagenesis

70

1

E → A: Reduces affinity for ubiquitin up to 10-fold. Ref.16

Sequence conflict

185

1

M → V in CAI45953. Ref.3

Sequence conflict

223

1

S → R in AAD34140. Ref.1

Secondary structure

1

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386

Helix Strand Turn

Details...

Beta strand

17 – 28

12

Beta strand

38 – 51

14

Beta strand

59 – 62

4

Helix

63 – 65

3

Beta strand

66 – 72

7

Beta strand

81 – 86

6

Beta strand

93 – 95

3

Beta strand

105 – 110

6

Helix

115 – 128

14

Helix

175 – 193

19

Helix

197 – 199

3

Helix

215 – 224

10

Helix

229 – 232

4

Helix

233 – 235

3

Helix

240 – 259

20

Beta strand

262 – 265

4

Helix

266 – 275

10

Beta strand

278 – 280

3

Helix

284 – 292

9

Turn

293 – 298

6

Beta strand

300 – 305

6

Beta strand

309 – 315

7

Helix

320 – 323

4

Helix

324 – 333

10

Helix

339 – 346

8

Helix

350 – 362

13

Beta strand

365 – 373

9

Beta strand

375 – 379

5

Helix

381 – 383

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 21E1E66F71BA7764	FASTA	386	43,817
	10 20 30 40 50 60 MDRFVWTSGL LEINETLVIQ QRGVRIYDGE EKIKFDAGTL LLSTHRLIWR DQKNHECCMA 70 80 90 100 110 120 ILLSQIVFIE EQAAGIGKSA KIVVHLHPAP PNKEPGPFQS SKNSYIKLSF KEHGQIEFYR 130 140 150 160 170 180 RLSEEMTQRR WENMPVSQSL QTNRGPQPGR IRAVGIVGIE RKLEEKRKET DKNISEAFED 190 200 210 220 230 240 LSKLMIKAKE MVELSKSIAN KIKDKQGDIT EDETIRFKSY LLSMGIANPV TRETYGSGTQ 250 260 270 280 290 300 YHMQLAKQLA GILQVPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP 310 320 330 340 350 360 LRLRVFDSGV MVIELQSHKE EEMVASALET VSEKGSLTSE EFAKLVGMSV LLAKERLLLA 370 380 EKMGHLCRDD SVEGLRFYPN LFMTQS
	Isoform 2 [UniParc]. Checksum: F6078BBD25CC0032	FASTA	328	36,958
	10 20 30 40 50 60 MAILLSQIVF IEEQAAGIGK SAKIVVHLHP APPNKEPGPF QSSKNSYIKL SFKEHGQIEF 70 80 90 100 110 120 YRRLSEEMTQ RRWENMPVSQ SLQTNRGPQP GRIRAVGIVG IERKLEEKRK ETDKNISEAF 130 140 150 160 170 180 EDLSKLMIKA KEMVELSKSI ANKIKDKQGD ITEDETIRFK SYLLSMGIAN PVTRETYGSG 190 200 210 220 230 240 TQYHMQLAKQ LAGILQVPLE ERGGIMSLTE VYCLVNRARG MELLSPEDLV NACKMLEALK 250 260 270 280 290 300 LPLRLRVFDS GVMVIELQSH KEEEMVASAL ETVSEKGSLT SEEFAKLVGM SVLLAKERLL 310 320 LAEKMGHLCR DDSVEGLRFY PNLFMTQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-386. Tissue: Brain and Teratocarcinoma.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Retina.
[4]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [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. , 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].
[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] (ISOFORM 1). Tissue: Brain.
[7]	"The protein network of HIV budding." von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I. Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VPS25; SNF8 AND TSG101.
[8]	"Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins." Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D. Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ESCRT-II COMPLEX, INTERACTION WITH VPS36; SNF8 AND CHMP6.
[9]	Erratum Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D. Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
[10]	"Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain." Slagsvold T., Aasland R., Hirano S., Bache K.G., Raiborg C., Trambaiolo D., Wakatsuki S., Stenmark H. J. Biol. Chem. 280:19600-19606(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, INTERACTION WITH UBIQUITIN.
[11]	"RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment." Wang T., Hong W. Biochem. Biophys. Res. Commun. 350:413-423(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VPS25 AND RILPL1, SUBCELLULAR LOCATION.
[12]	"Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release." Langelier C., von Schwedler U.K., Fisher R.D., De Domenico I., White P.L., Hill C.P., Kaplan J., Ward D., Sundquist W.I. J. Virol. 80:9465-9480(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VPS25; SNF8 AND TSG101, UBIQUITIN-BINDING, SUBCELLULAR LOCATION.
[13]	"Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation." Maleroed L., Stuffers S., Brech A., Stenmark H. Traffic 8:1617-1629(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components." Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M. J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
[15]	"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].
[16]	"Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain." Alam S.L., Langelier C., Whitby F.G., Koirala S., Robinson H., Hill C.P., Sundquist W.I. Nat. Struct. Mol. Biol. 13:1029-1030(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-138 IN COMPLEX WITH UBIQUITIN, MUTAGENESIS OF LEU-10; VAL-67; PHE-68 AND GLU-70.
[17]	"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex." Im Y.J., Hurley J.H. Dev. Cell 14:902-913(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 169-386 IN COMPLEX WITH VPS25 AND SNF8.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF151903 mRNA. Translation: AAD34140.1.
AK023182 mRNA. Translation: BAB14451.1. Different initiation.
AK289740 mRNA. Translation: BAF82429.1.
CR933653 mRNA. Translation: CAI45953.1.
AL359513 Genomic DNA. Translation: CAH71658.1.
CH471274 Genomic DNA. Translation: EAW55895.1.
BC037279 mRNA. Translation: AAH37279.1.
BC050439 mRNA. Translation: AAH50439.1.

IPI

IPI00328932.
IPI00646971.

RefSeq

NP_057159.2. NM_016075.2.

UniGene

Hs.109520.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HTH	X-ray	2.70	B	1-138	[»]
2ZME	X-ray	2.90	B	149-386	[»]
3CUQ	X-ray	2.61	B	169-386	[»]

ProteinModelPortal

Q86VN1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29249N.

STRING

9606.ENSP00000367299.

PTM databases

PhosphoSite

Q86VN1.

Polymorphism databases

DMDM

73920464.

Proteomic databases

PaxDb

Q86VN1.

PRIDE

Q86VN1.

Protocols and materials databases

DNASU

51028.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000378060; ENSP00000367299; ENSG00000136100.

GeneID

51028.

KEGG

hsa:51028.

UCSC

uc001vgq.3. human.

Organism-specific databases

CTD

51028.

GeneCards

GC13M052986.

HGNC

HGNC:20312. VPS36.

HPA

HPA039734.
HPA043947.

MIM

610903. gene.

neXtProt

NX_Q86VN1.

PharmGKB

PA134990943.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG262969.

HOVERGEN

HBG083632.

InParanoid

Q86VN1.

KO

K12190.

OMA

CCIAIPL.

OrthoDB

EOG4XPQG2.

PhylomeDB

Q86VN1.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

Bgee

Q86VN1.

CleanEx

HS_VPS36.

Genevestigator

Q86VN1.

GermOnline

ENSG00000136100. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 2 hits.

InterPro

IPR007286. EAP30.
IPR021648. VPS36_GLUE.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF04157. EAP30. 1 hit.
PF11605. Vps36_ESCRT-II. 1 hit.
[Graphical view]

PROSITE

PS51495. GLUE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VPS36. human.

EvolutionaryTrace

Q86VN1.

GenomeRNAi

51028.

NextBio

53573.

SOURCE

Search...

Entry information

Entry name

VPS36_HUMAN

Accession

Primary (citable) accession number: Q86VN1
Secondary accession number(s): A8K125 , Q3ZCV7, Q5H9S1, Q5VXB6, Q9H8Z5, Q9Y3E3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 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.