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Q9NR50

- EI2BG_HUMAN

UniProt

Q9NR50 - EI2BG_HUMAN

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Protein

Translation initiation factor eIF-2B subunit gamma

Gene
EIF2B3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: Ensembl
  2. nucleotidyltransferase activity Source: InterPro
  3. protein binding Source: UniProtKB
  4. translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to stimulus Source: UniProtKB
  3. gene expression Source: Reactome
  4. negative regulation of translational initiation in response to stress Source: UniProtKB
  5. oligodendrocyte development Source: UniProtKB
  6. regulation of GTPase activity Source: GOC
  7. response to glucose Source: UniProtKB
  8. response to heat Source: UniProtKB
  9. response to peptide hormone Source: UniProtKB
  10. translation Source: Reactome
  11. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1815. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor eIF-2B subunit gamma
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit gamma
Gene namesi
Name:EIF2B3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3259. EIF2B3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic translation initiation factor 2B complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271L → Q in VWM. 1 Publication
VAR_068470
Natural varianti47 – 471G → E in VWM. 1 Publication
VAR_068471
Natural varianti87 – 871A → V in VWM. 1 Publication
VAR_015409
Natural varianti225 – 2251R → Q in VWM. 2 Publications
VAR_015410
Natural varianti346 – 3461I → T in VWM. 1 Publication
VAR_068472

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

MIMi603896. phenotype.
Orphaneti99854. Cree leukoencephalopathy.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBiPA27690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Translation initiation factor eIF-2B subunit gammaPRO_0000156079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NR50.
PaxDbiQ9NR50.
PRIDEiQ9NR50.

2D gel databases

REPRODUCTION-2DPAGEIPI00006504.

PTM databases

PhosphoSiteiQ9NR50.

Expressioni

Gene expression databases

ArrayExpressiQ9NR50.
BgeeiQ9NR50.
CleanExiHS_EIF2B3.
GenevestigatoriQ9NR50.

Organism-specific databases

HPAiCAB032233.
HPA024213.
HPA024218.
HPA024219.

Interactioni

Subunit structurei

Complex of five different subunits; alpha, beta, gamma, delta and epsilon.

Protein-protein interaction databases

BioGridi114408. 30 interactions.
IntActiQ9NR50. 5 interactions.
MINTiMINT-3072682.
STRINGi9606.ENSP00000353575.

Structurei

3D structure databases

ProteinModelPortaliQ9NR50.
SMRiQ9NR50. Positions 1-56, 345-378, 391-449.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1208.
HOVERGENiHBG051461.
InParanoidiQ9NR50.
KOiK03241.
OMAiEGVKPRT.
PhylomeDBiQ9NR50.
TreeFamiTF101507.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
InterProiIPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 4 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9NR50-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE    50
VIVVTTRDVQ KALCAEFKMK MKPDIVCIPD DADMGTADSL RYIYPKLKTD 100
VLVLSCDLIT DVALHEVVDL FRAYDASLAM LMRKGQDSIE PVPGQKGKKK 150
AVEQRDFIGV DSTGKRLLFM ANEADLDEEL VIKGSILQKH PRIRFHTGLV 200
DAHLYCLKKY IVDFLMENGS ITSIRSELIP YLVRKQFSSA SSQQGQEEKE 250
EDLKKKELKS LDIYSFIKEA NTLNLAPYDA CWNACRGDRW EDLSRSQVRC 300
YVHIMKEGLC SRVSTLGLYM EANRQVPKLL SALCPEEPPV HSSAQIVSKH 350
LVGVDSLIGP ETQIGEKSSI KRSVIGSSCL IKDRVTITNC LLMNSVTVEE 400
GSNIQGSVIC NNAVIEKGAD IKDCLIGSGQ RIEAKAKRVN EVIVGNDQLM 450
EI 452
Length:452
Mass (Da):50,240
Last modified:October 1, 2000 - v1
Checksum:i6F73137F59E52773
GO
Isoform 2 (identifier: Q9NR50-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     402-452: SNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI → YVSPCTHLRQR

Show »
Length:412
Mass (Da):46,145
Checksum:i2D3F23DE8D1C6C5A
GO
Isoform 3 (identifier: Q9NR50-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     402-452: Missing.

Show »
Length:401
Mass (Da):44,803
Checksum:i3D643091793D31BF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271L → Q in VWM. 1 Publication
VAR_068470
Natural varianti47 – 471G → E in VWM. 1 Publication
VAR_068471
Natural varianti87 – 871A → V in VWM. 1 Publication
VAR_015409
Natural varianti225 – 2251R → Q in VWM. 2 Publications
VAR_015410
Natural varianti288 – 2881D → E.
Corresponds to variant rs3738247 [ dbSNP | Ensembl ].
VAR_048920
Natural varianti346 – 3461I → T in VWM. 1 Publication
VAR_068472

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei402 – 45251SNIQG…QLMEI → YVSPCTHLRQR in isoform 2. VSP_001436Add
BLAST
Alternative sequencei402 – 45251Missing in isoform 3. VSP_001435Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561S → G in BAB14770. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF257077 mRNA. Translation: AAF91351.1.
AK024006 mRNA. Translation: BAB14770.1.
AK314668 mRNA. Translation: BAG37225.1.
AL834288 mRNA. Translation: CAD38962.1.
AL136380 Genomic DNA. Translation: CAI23131.1.
AL136380 Genomic DNA. Translation: CAI23132.1.
CH471059 Genomic DNA. Translation: EAX07013.1.
CH471059 Genomic DNA. Translation: EAX07015.1.
BC018728 mRNA. Translation: AAH18728.1.
CCDSiCCDS517.1. [Q9NR50-1]
CCDS53313.1. [Q9NR50-2]
RefSeqiNP_001160060.1. NM_001166588.2. [Q9NR50-2]
NP_001248347.1. NM_001261418.1. [Q9NR50-3]
NP_065098.1. NM_020365.4. [Q9NR50-1]
UniGeneiHs.533549.

Genome annotation databases

EnsembliENST00000360403; ENSP00000353575; ENSG00000070785. [Q9NR50-1]
ENST00000372183; ENSP00000361257; ENSG00000070785. [Q9NR50-2]
GeneIDi8891.
KEGGihsa:8891.
UCSCiuc001cmt.3. human. [Q9NR50-1]
uc001cmw.4. human. [Q9NR50-2]

Polymorphism databases

DMDMi18203317.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mendelian genes eukaryotic translation initiation factor 2B, subunit 3 gamma, 58kDa (EIF2B3)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF257077 mRNA. Translation: AAF91351.1 .
AK024006 mRNA. Translation: BAB14770.1 .
AK314668 mRNA. Translation: BAG37225.1 .
AL834288 mRNA. Translation: CAD38962.1 .
AL136380 Genomic DNA. Translation: CAI23131.1 .
AL136380 Genomic DNA. Translation: CAI23132.1 .
CH471059 Genomic DNA. Translation: EAX07013.1 .
CH471059 Genomic DNA. Translation: EAX07015.1 .
BC018728 mRNA. Translation: AAH18728.1 .
CCDSi CCDS517.1. [Q9NR50-1 ]
CCDS53313.1. [Q9NR50-2 ]
RefSeqi NP_001160060.1. NM_001166588.2. [Q9NR50-2 ]
NP_001248347.1. NM_001261418.1. [Q9NR50-3 ]
NP_065098.1. NM_020365.4. [Q9NR50-1 ]
UniGenei Hs.533549.

3D structure databases

ProteinModelPortali Q9NR50.
SMRi Q9NR50. Positions 1-56, 345-378, 391-449.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114408. 30 interactions.
IntActi Q9NR50. 5 interactions.
MINTi MINT-3072682.
STRINGi 9606.ENSP00000353575.

PTM databases

PhosphoSitei Q9NR50.

Polymorphism databases

DMDMi 18203317.

2D gel databases

REPRODUCTION-2DPAGE IPI00006504.

Proteomic databases

MaxQBi Q9NR50.
PaxDbi Q9NR50.
PRIDEi Q9NR50.

Protocols and materials databases

DNASUi 8891.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360403 ; ENSP00000353575 ; ENSG00000070785 . [Q9NR50-1 ]
ENST00000372183 ; ENSP00000361257 ; ENSG00000070785 . [Q9NR50-2 ]
GeneIDi 8891.
KEGGi hsa:8891.
UCSCi uc001cmt.3. human. [Q9NR50-1 ]
uc001cmw.4. human. [Q9NR50-2 ]

Organism-specific databases

CTDi 8891.
GeneCardsi GC01M045316.
GeneReviewsi EIF2B3.
HGNCi HGNC:3259. EIF2B3.
HPAi CAB032233.
HPA024213.
HPA024218.
HPA024219.
MIMi 603896. phenotype.
606273. gene.
neXtProti NX_Q9NR50.
Orphaneti 99854. Cree leukoencephalopathy.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBi PA27690.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1208.
HOVERGENi HBG051461.
InParanoidi Q9NR50.
KOi K03241.
OMAi EGVKPRT.
PhylomeDBi Q9NR50.
TreeFami TF101507.

Enzyme and pathway databases

Reactomei REACT_1815. Recycling of eIF2:GDP.

Miscellaneous databases

GeneWikii EIF2B3.
GenomeRNAii 8891.
NextBioi 33391.
PROi Q9NR50.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NR50.
Bgeei Q9NR50.
CleanExi HS_EIF2B3.
Genevestigatori Q9NR50.

Family and domain databases

Gene3Di 3.90.550.10. 2 hits.
InterProi IPR005835. NTP_transferase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF00483. NTP_transferase. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of eIF2B gamma and eIF2 gamma as cofactors of hepatitis C virus internal ribosome entry site-mediated translation using a functional genomics approach."
    Krueger M., Beger C., Li Q.-X., Welch P.J., Tritz R., Leavitt M., Barber J.R., Wong-Staal F.
    Proc. Natl. Acad. Sci. U.S.A. 97:8566-8571(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [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).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lymph node.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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 3).
    Tissue: Blood.
  7. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-15; 226-234 AND 260-268, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter."
    van der Knaap M.S., Leegwater P.A.J., Koenst A.A.M., Visser A., Naidu S., Oudejans C.B.M., Schutgens R.B.H., Pronk J.C.
    Ann. Neurol. 51:264-270(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VWM VAL-87 AND GLN-225.
  12. "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 GLU-47; GLN-225 AND THR-346.
  13. "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 GLN-27.

Entry informationi

Entry nameiEI2BG_HUMAN
AccessioniPrimary (citable) accession number: Q9NR50
Secondary accession number(s): B2RBH8
, D3DPZ2, Q5QP89, Q5QP90, Q8NDB5, Q8WV57, Q9H850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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