Q13144 (EI2BE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Translation initiation factor eIF-2B subunit epsilon

Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit epsilon

Gene names

Name:	EIF2B5
Synonyms:	EIF2BE

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

General annotation (Comments)

Function	Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subunit structure	Complex of five different subunits; alpha, beta, gamma, delta and epsilon. Interacts with RGS2. Ref.10
Post-translational modification	Phosphorylated at Ser-544 by DYRK2; this is required for subsequent phosphorylation by GSK3B By similarity. Phosphorylated on serine and threonine residues by GSK3B; phosphorylation inhibits its function. Ref.6
Involvement in disease	Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Sequence similarities	Belongs to the eIF-2B gamma/epsilon subunits family. Contains 1 W2 domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Coding sequence diversity	Polymorphism
Disease	Disease mutation Leukodystrophy
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA metabolic process Inferred from electronic annotation. Source: InterPro astrocyte development Inferred from mutant phenotype PubMed 15723074. Source: UniProtKB myelination Inferred from mutant phenotype PubMed 14566705PubMed 15723074. Source: UniProtKB negative regulation of translational initiation in response to stress Inferred from sequence or structural similarity. Source: UniProtKB oligodendrocyte development Inferred from mutant phenotype PubMed 15217090. Source: UniProtKB ovarian follicle development Inferred from mutant phenotype PubMed 15507143. Source: UniProtKB positive regulation of translational initiation Inferred from sequence or structural similarity. Source: UniProtKB response to glucose stimulus Inferred from sequence or structural similarity. Source: UniProtKB response to heat Inferred from mutant phenotype PubMed 15723074. Source: UniProtKB response to peptide hormone stimulus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 2B complex Inferred from direct assay PubMed 11323413PubMed 15060152. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	guanyl-nucleotide exchange factor activity Inferred from mutant phenotype PubMed 15054402. Source: UniProtKB transferase activity Inferred from electronic annotation. Source: InterPro translation initiation factor activity Non-traceable author statement Ref.5. Source: UniProtKB translation initiation factor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 721

721

Translation initiation factor eIF-2B subunit epsilon

PRO_0000156073

Regions

Domain

543 – 720

178

W2

Compositional bias

505 – 509

5

Poly-Glu

Amino acid modifications

Modified residue

544

1

Phosphoserine; by DYRK2 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14

Modified residue

717

1

Phosphoserine Ref.11

Modified residue

718

1

Phosphoserine Ref.11

Natural variations

Natural variant

62

1

D → V in VWM. Ref.19

VAR_068457

Natural variant

68

1

L → S in VWM. Ref.18

VAR_068458

Natural variant

73

1

V → G in VWM. Ref.15

VAR_012323

Natural variant

74

1

A → T in VWM. Ref.18

VAR_068459

Natural variant

91

1

T → A in VWM. Ref.15
Corresponds to variant rs28939717 [ dbSNP | Ensembl ].

VAR_012291

Natural variant

106

1

L → F in VWM. Ref.15

VAR_012324

Natural variant

113

1

R → C in VWM. Ref.19

VAR_068460

Natural variant

113

1

R → H in VWM; with ovarian failure. Ref.15 Ref.17 Ref.18

VAR_012292

Natural variant

195

1

R → C in VWM; with ovarian failure. Ref.17

VAR_016845

Natural variant

195

1

R → H in VWM; Cree leukoencephalopathy type. Ref.16

VAR_016846

Natural variant

200

1

N → T.
Corresponds to variant rs2971409 [ dbSNP | Ensembl ].

VAR_048919

Natural variant

269

1

R → G in VWM. Ref.18

VAR_068461

Natural variant

269

1

R → Q in VWM. Ref.19

VAR_068462

Natural variant

270

1

D → H in VWM. Ref.20

VAR_068463

Natural variant

299

1

R → H in VWM. Ref.15

VAR_012325

Natural variant

310

1

C → F in VWM. Ref.18

VAR_068464

Natural variant

315

1

R → C in VWM. Ref.19

VAR_068465

Natural variant

315

1

R → G in VWM. Ref.15

VAR_012326

Natural variant

315

1

R → H in VWM. Ref.15

VAR_012327

Natural variant

335

1

C → R in VWM. Ref.18

VAR_068466

Natural variant

335

1

C → S in VWM. Ref.19

VAR_068467

Natural variant

339

1

R → P in VWM. Ref.15 Ref.19

VAR_012328

Natural variant

339

1

R → Q in VWM. Ref.15

VAR_012329

Natural variant

339

1

R → W in VWM. Ref.15

VAR_012330

Natural variant

376

1

N → D in VWM. Ref.19

VAR_068468

Natural variant

386

1

G → V in VWM. Ref.15 Ref.19

VAR_012293

Natural variant

430

1

V → A in VWM. Ref.15

VAR_012331

Natural variant

447

1

S → L in VWM. Ref.19

VAR_068469

Natural variant

587

1

I → V. Ref.1 Ref.3 Ref.4 Ref.5 Ref.15
Corresponds to variant rs843358 [ dbSNP | Ensembl ].

VAR_012332

Natural variant

628

1

W → R in VWM. Ref.15
Corresponds to variant rs28937596 [ dbSNP | Ensembl ].

VAR_012294

Natural variant

650

1

E → K in VWM. Ref.15

VAR_012333

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

721

Helix Strand Turn

Details...

Helix

547 – 567

21

Helix

571 – 584

14

Helix

589 – 602

14

Helix

603 – 607

5

Helix

614 – 635

22

Helix

639 – 655

17

Helix

657 – 662

6

Helix

663 – 672

10

Helix

678 – 685

8

Helix

693 – 697

5

Helix

701 – 714

14

Sequences

	Sequence		Length	Mass (Da)
	Q13144 [UniParc]. Last modified October 23, 2007. Version 3. Checksum: 08B39D3A5EE7D905	FASTA	721	80,380
	10 20 30 40 50 60 MAAPVVAPPG VVVSRANKRS GAGPGGSGGG GARGAEEEPP PPLQAVLVAD SFDRRFFPIS 70 80 90 100 110 120 KDQPRVLLPL ANVALIDYTL EFLTATGVQE TFVFCCWKAA QIKEHLLKSK WCRPTSLNVV 130 140 150 160 170 180 RIITSELYRS LGDVLRDVDA KALVRSDFLL VYGDVISNIN ITRALEEHRL RRKLEKNVSV 190 200 210 220 230 240 MTMIFKESSP SHPTRCHEDN VVVAVDSTTN RVLHFQKTQG LRRFAFPLSL FQGSSDGVEV 250 260 270 280 290 300 RYDLLDCHIS ICSPQVAQLF TDNFDYQTRD DFVRGLLVNE EILGNQIHMH VTAKEYGARV 310 320 330 340 350 360 SNLHMYSAVC ADVIRRWVYP LTPEANFTDS TTQSCTHSRH NIYRGPEVSL GHGSILEENV 370 380 390 400 410 420 LLGSGTVIGS NCFITNSVIG PGCHIGDNVV LDQTYLWQGV RVAAGAQIHQ SLLCDNAEVK 430 440 450 460 470 480 ERVTLKPRSV LTSQVVVGPN ITLPEGSVIS LHPPDAEEDE DDGEFSDDSG ADQEKDKVKM 490 500 510 520 530 540 KGYNPAEVGA AGKGYLWKAA GMNMEEEEEL QQNLWGLKIN MEEESESESE QSMDSEEPDS 550 560 570 580 590 600 RGGSPQMDDI KVFQNEVLGT LQRGKEENIS CDNLVLEINS LKYAYNISLK EVMQVLSHVV 610 620 630 640 650 660 LEFPLQQMDS PLDSSRYCAL LLPLLKAWSP VFRNYIKRAA DHLEALAAIE DFFLEHEALG 670 680 690 700 710 720 ISMAKVLMAF YQLEILAEET ILSWFSQRDT TDKGQQLRKN QQLQRFIQWL KEAEEESSED D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], VARIANT VAL-587. Tissue: Brain.
[2]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-587.
[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], VARIANT VAL-587. Tissue: Lung.
[5]	"Cloning and characterization of cDNAs encoding the epsilon-subunit of eukaryotic initiation factor-2B from rabbit and human." Asuru A.I., Mellor H., Thomas N.S.B., Yu L., Chen J.-J., Crosby J.S., Hartson S.D., Kimball S.R., Jefferson L.S., Matts R.L. Biochim. Biophys. Acta 1307:309-317(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-721, VARIANT VAL-587.
[6]	"Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B." Welsh G.I., Proud C.G. Biochem. J. 294:625-629(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY GSK3B.
[7]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-544, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Translational control by RGS2." Nguyen C.H., Ming H., Zhao P., Hugendubler L., Gros R., Kimball S.R., Chidiac P. J. Cell Biol. 186:755-765(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RGS2.
[11]	"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-717 AND SER-718, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-544, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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-544, MASS SPECTROMETRY.
[15]	"Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter." Leegwater P.A.J., Vermeulen G., Koenst A.A.M., Naidu S., Mulders J., Visser A., Kersbergen P., Mobach D., Fonds D., van Berkel C.G.M., Lemmers R.J.L.F., Frants R.R., Oudejans C.B.M., Schutgens R.B.H., Pronk J.C., van der Knaap M.S. Nat. Genet. 29:383-388(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VWM GLY-73; ALA-91; PHE-106; HIS-113; HIS-299; GLY-315; HIS-315; PRO-339; GLN-339; TRP-339; VAL-386; ALA-430; ARG-628 AND LYS-650, VARIANT VAL-587.
[16]	"Cree leukoencephalopathy and CACH/VWM disease are allelic at the EIF2B5 locus." Fogli A., Wong K., Eymard-Pierre E., Wenger J., Bouffard J.-P., Goldin E., Black D.N., Boespflug-Tanguy O., Schiffmann R. Ann. Neurol. 52:506-510(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VWM HIS-195.
[17]	"Ovarian failure related to eukaryotic initiation factor 2B mutations." Fogli A., Rodriguez D., Eymard-Pierre E., Bouhour F., Labauge P., Meaney B.F., Zeesman S., Kaneski C.R., Schiffmann R., Boespflug-Tanguy O. Am. J. Hum. Genet. 72:1544-1550(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VWM HIS-113 AND CYS-195.
[18]	"Identification of ten novel mutations in patients with eIF2B-related disorders." Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F., Kohlschutter A., Gartner J. Hum. Mutat. 25:411-411(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VWM SER-68; THR-74; HIS-113; GLY-269; PHE-310 AND ARG-335.
[19]	"Identification of novel EIF2B mutations in Chinese patients with vanishing white matter disease." Wu Y., Pan Y., Du L., Wang J., Gu Q., Gao Z., Li J., Leng X., Qin J., Wu X., Jiang Y. J. Hum. Genet. 54:74-77(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VWM VAL-62; CYS-113; GLN-269; CYS-315; SER-335; PRO-339; ASP-376; VAL-386 AND LEU-447.
[20]	"Adult-onset leukoencephalopathies with vanishing white matter with novel missense mutations in EIF2B2, EIF2B3, and EIF2B5." Matsukawa T., Wang X., Liu R., Wortham N.C., Onuki Y., Kubota A., Hida A., Kowa H., Fukuda Y., Ishiura H., Mitsui J., Takahashi Y., Aoki S., Takizawa S., Shimizu J., Goto J., Proud C.G., Tsuji S. Neurogenetics 12:259-261(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VWM HIS-270.
+	Additional computationally mapped references.

Web resources

GeneReviews

Mendelian genes eukaryotic translation initiation factor 2B, subunit 5 epsilon, 82kDa (EIF2B5)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK091646 mRNA. Translation: BAC03712.1.
AC131235 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78299.1.
BC013590 mRNA. Translation: AAH13590.1.
U23028 mRNA. Translation: AAC50646.1.

IPI

IPI00011898.

RefSeq

NP_003898.2. NM_003907.2.

UniGene

Hs.283551.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JUI	X-ray	2.00	A	547-721	[»]

ProteinModelPortal

Q13144.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13144. 1 interaction.

STRING

9606.ENSP00000273783.

PTM databases

PhosphoSite

Q13144.

Polymorphism databases

DMDM

160359049.

Proteomic databases

PaxDb

Q13144.

PRIDE

Q13144.

Protocols and materials databases

DNASU

8893.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000273783; ENSP00000273783; ENSG00000145191.

GeneID

8893.

KEGG

hsa:8893.

UCSC

uc003fmp.3. human.

Organism-specific databases

CTD

8893.

GeneCards

GC03P183852.

H-InvDB

HIX0003921.

HGNC

HGNC:3261. EIF2B5.

HPA

CAB015412.

MIM

603896. phenotype.
603945. gene.

neXtProt

NX_Q13144.

Orphanet

99854. Cree leukoencephalopathy.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.

PharmGKB

PA27692.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1208.

HOGENOM

HOG000216610.

HOVERGEN

HBG051460.

InParanoid

Q13144.

KO

K03240.

OMA

ESEQSMD.

OrthoDB

EOG4THVSP.

PhylomeDB

Q13144.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q13144.

Bgee

Q13144.

CleanEx

HS_EIF2B5.

Genevestigator

Q13144.

GermOnline

ENSG00000145191. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.180. 1 hit.

InterPro

IPR016024. ARM-type_fold.
IPR001451. Hexapep_transf.
IPR016021. MIF4-like_typ_1/2/3.
IPR011004. Trimer_LpxA-like.
IPR003307. W2_domain.
[Graphical view]

Pfam

PF00132. Hexapep. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]

SMART

SM00515. eIF5C. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF51161. Trimer_LpxA_like. 1 hit.

PROSITE

PS51363. W2. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q13144.

GenomeRNAi

8893.

NextBio

33399.

SOURCE

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Entry information

Entry name

EI2BE_HUMAN

Accession

Primary (citable) accession number: Q13144
Secondary accession number(s): Q541Z1, Q96D04

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
This is version 128 of the entry and version 3 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.