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Protein

Translation initiation factor eIF-2B subunit delta

Gene

EIF2B4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • cellular response to stimulus Source: UniProtKB
  • gene expression Source: Reactome
  • myelination Source: UniProtKB
  • negative regulation of translational initiation Source: GO_Central
  • negative regulation of translational initiation in response to stress Source: UniProtKB
  • oligodendrocyte development Source: UniProtKB
  • ovarian follicle development Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • regulation of translation Source: UniProtKB
  • regulation of translational initiation Source: GO_Central
  • response to glucose Source: UniProtKB
  • response to heat Source: UniProtKB
  • response to peptide hormone Source: UniProtKB
  • translation Source: Reactome
  • 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 delta
Alternative name(s):
eIF-2B GDP-GTP exchange factor subunit delta
Gene namesi
Name:EIF2B4
Synonyms:EIF2BD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3260. EIF2B4.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy with vanishing white matter (VWM)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:603896
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091R → Q in VWM. 1 Publication
VAR_068455
Natural varianti228 – 2281A → V in VWM. 1 Publication
VAR_015405
Natural varianti269 – 2691L → R in VWM. 1 Publication
VAR_068456
Natural varianti357 – 3571R → Q in VWM. 1 Publication
VAR_015407
Natural varianti374 – 3741R → C in VWM. 2 Publications
VAR_015408
Natural varianti465 – 4651C → R in VWM; with ovarian failure. 1 Publication
VAR_016843
Natural varianti489 – 4891Y → H in VWM; with ovarian failure. 1 Publication
VAR_016844

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

MIMi603896. phenotype.
Orphaneti157713. Congenital or early infantile CACH syndrome.
99854. Cree leukoencephalopathy.
157719. Juvenile or adult CACH syndrome.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBiPA27691.

Polymorphism and mutation databases

BioMutaiEIF2B4.
DMDMi28381357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 523522Translation initiation factor eIF-2B subunit deltaPRO_0000156067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei86 – 861Phosphothreonine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UI10.
PaxDbiQ9UI10.
PRIDEiQ9UI10.

PTM databases

PhosphoSiteiQ9UI10.

Expressioni

Gene expression databases

BgeeiQ9UI10.
CleanExiHS_EIF2B4.
ExpressionAtlasiQ9UI10. baseline and differential.
GenevestigatoriQ9UI10.

Organism-specific databases

HPAiCAB032234.
HPA039993.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF2B2Q53XC24EBI-2340132,EBI-10288660

Protein-protein interaction databases

BioGridi114407. 24 interactions.
IntActiQ9UI10. 8 interactions.
MINTiMINT-4990902.
STRINGi9606.ENSP00000394869.

Structurei

3D structure databases

ProteinModelPortaliQ9UI10.
SMRiQ9UI10. Positions 219-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1184.
GeneTreeiENSGT00550000075009.
HOGENOMiHOG000176924.
HOVERGENiHBG051459.
InParanoidiQ9UI10.
KOiK03680.
OrthoDBiEOG7XSTF0.
PhylomeDBiQ9UI10.
TreeFamiTF101508.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UI10-1) [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

        10         20         30         40         50
MAAVAVAVRE DSGSGMKAEL PPGPGAVGRE MTKEEKLQLR KEKKQQKKKR
60 70 80 90 100
KEEKGAEPET GSAVSAAQCQ VGPTRELPES GIQLGTPREK VPAGRSKAEL
110 120 130 140 150
RAERRAKQEA ERALKQARKG EQGGPPPKAS PSTAGETPSG VKRLPEYPQV
160 170 180 190 200
DDLLLRRLVK KPERQQVPTR KDYGSKVSLF SHLPQYSRQN SLTQFMSIPS
210 220 230 240 250
SVIHPAMVRL GLQYSQGLVS GSNARCIALL RALQQVIQDY TTPPNEELSR
260 270 280 290 300
DLVNKLKPYM SFLTQCRPLS ASMHNAIKFL NKEITSVGSS KREEEAKSEL
310 320 330 340 350
RAAIDRYVQE KIVLAAQAIS RFAYQKISNG DVILVYGCSS LVSRILQEAW
360 370 380 390 400
TEGRRFRVVV VDSRPWLEGR HTLRSLVHAG VPASYLLIPA ASYVLPEVSK
410 420 430 440 450
VLLGAHALLA NGSVMSRVGT AQLALVARAH NVPVLVCCET YKFCERVQTD
460 470 480 490 500
AFVSNELDDP DDLQCKRGEH VALANWQNHA SLRLLNLVYD VTPPELVDLV
510 520
ITELGMIPCS SVPVVLRVKS SDQ
Length:523
Mass (Da):57,557
Last modified:February 12, 2003 - v2
Checksum:i5F38CF10CAD5A45E
GO
Isoform 2 (identifier: Q9UI10-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MAAVAVAVRE → MPTQQPAAPSTRAPKPSRSLSGSLCALFSDA
     71-71: Missing.

Show »
Length:543
Mass (Da):59,615
Checksum:iC65253AD9431E074
GO
Isoform 3 (identifier: Q9UI10-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-71: Missing.

Show »
Length:522
Mass (Da):57,458
Checksum:iD9A7E6FD35CD75F1
GO

Sequence cautioni

The sequence CAB57305.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971S → T in CAB57260 (Ref. 2) Curated
Sequence conflicti197 – 1971S → T in CAB57261 (Ref. 2) Curated
Sequence conflicti197 – 1971S → T in CAB57304 (Ref. 2) Curated
Sequence conflicti197 – 1971S → T in CAB57305 (Ref. 2) Curated
Sequence conflicti323 – 3231A → S in AAF17195 (PubMed:10931946).Curated
Sequence conflicti481 – 4811S → L in AAF17195 (PubMed:10931946).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931A → V.
Corresponds to variant rs34155621 [ dbSNP | Ensembl ].
VAR_048918
Natural varianti209 – 2091R → Q in VWM. 1 Publication
VAR_068455
Natural varianti228 – 2281A → V in VWM. 1 Publication
VAR_015405
Natural varianti269 – 2691L → R in VWM. 1 Publication
VAR_068456
Natural varianti306 – 3061R → G.1 Publication
Corresponds to variant rs78599355 [ dbSNP | Ensembl ].
VAR_015406
Natural varianti357 – 3571R → Q in VWM. 1 Publication
VAR_015407
Natural varianti374 – 3741R → C in VWM. 2 Publications
VAR_015408
Natural varianti465 – 4651C → R in VWM; with ovarian failure. 1 Publication
VAR_016843
Natural varianti489 – 4891Y → H in VWM; with ovarian failure. 1 Publication
VAR_016844

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1010MAAVAVAVRE → MPTQQPAAPSTRAPKPSRSL SGSLCALFSDA in isoform 2. 1 PublicationVSP_001433
Alternative sequencei71 – 711Missing in isoform 2 and isoform 3. 1 PublicationVSP_040130

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112207 mRNA. Translation: AAF17195.1.
AJ011305 mRNA. Translation: CAB57260.1.
AJ011306 mRNA. Translation: CAB57261.1.
AJ011307, AJ011308 Genomic DNA. Translation: CAB57304.1.
AJ011307, AJ011308 Genomic DNA. Translation: CAB57305.1. Sequence problems.
AC074117 Genomic DNA. Translation: AAY14843.1.
CH471053 Genomic DNA. Translation: EAX00591.1.
BC001870 mRNA. Translation: AAH01870.1.
BC091502 mRNA. Translation: AAH91502.1.
CCDSiCCDS33164.1. [Q9UI10-1]
CCDS46244.1. [Q9UI10-3]
CCDS46245.1. [Q9UI10-2]
RefSeqiNP_001029288.1. NM_001034116.1. [Q9UI10-1]
NP_056451.3. NM_015636.3. [Q9UI10-3]
NP_751945.2. NM_172195.3. [Q9UI10-2]
UniGeneiHs.169474.

Genome annotation databases

EnsembliENST00000347454; ENSP00000233552; ENSG00000115211. [Q9UI10-1]
ENST00000445933; ENSP00000394397; ENSG00000115211. [Q9UI10-3]
ENST00000451130; ENSP00000394869; ENSG00000115211. [Q9UI10-2]
GeneIDi8890.
KEGGihsa:8890.
UCSCiuc002rjz.3. human. [Q9UI10-2]
uc002rka.3. human. [Q9UI10-1]
uc002rkc.3. human. [Q9UI10-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mendelian genes eukaryotic translation initiation factor 2B, subunit 4 delta, 67kDa (EIF2B4)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112207 mRNA. Translation: AAF17195.1.
AJ011305 mRNA. Translation: CAB57260.1.
AJ011306 mRNA. Translation: CAB57261.1.
AJ011307, AJ011308 Genomic DNA. Translation: CAB57304.1.
AJ011307, AJ011308 Genomic DNA. Translation: CAB57305.1. Sequence problems.
AC074117 Genomic DNA. Translation: AAY14843.1.
CH471053 Genomic DNA. Translation: EAX00591.1.
BC001870 mRNA. Translation: AAH01870.1.
BC091502 mRNA. Translation: AAH91502.1.
CCDSiCCDS33164.1. [Q9UI10-1]
CCDS46244.1. [Q9UI10-3]
CCDS46245.1. [Q9UI10-2]
RefSeqiNP_001029288.1. NM_001034116.1. [Q9UI10-1]
NP_056451.3. NM_015636.3. [Q9UI10-3]
NP_751945.2. NM_172195.3. [Q9UI10-2]
UniGeneiHs.169474.

3D structure databases

ProteinModelPortaliQ9UI10.
SMRiQ9UI10. Positions 219-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114407. 24 interactions.
IntActiQ9UI10. 8 interactions.
MINTiMINT-4990902.
STRINGi9606.ENSP00000394869.

PTM databases

PhosphoSiteiQ9UI10.

Polymorphism and mutation databases

BioMutaiEIF2B4.
DMDMi28381357.

Proteomic databases

MaxQBiQ9UI10.
PaxDbiQ9UI10.
PRIDEiQ9UI10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000347454; ENSP00000233552; ENSG00000115211. [Q9UI10-1]
ENST00000445933; ENSP00000394397; ENSG00000115211. [Q9UI10-3]
ENST00000451130; ENSP00000394869; ENSG00000115211. [Q9UI10-2]
GeneIDi8890.
KEGGihsa:8890.
UCSCiuc002rjz.3. human. [Q9UI10-2]
uc002rka.3. human. [Q9UI10-1]
uc002rkc.3. human. [Q9UI10-3]

Organism-specific databases

CTDi8890.
GeneCardsiGC02M027587.
GeneReviewsiEIF2B4.
HGNCiHGNC:3260. EIF2B4.
HPAiCAB032234.
HPA039993.
MIMi603896. phenotype.
606687. gene.
neXtProtiNX_Q9UI10.
Orphaneti157713. Congenital or early infantile CACH syndrome.
99854. Cree leukoencephalopathy.
157719. Juvenile or adult CACH syndrome.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBiPA27691.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1184.
GeneTreeiENSGT00550000075009.
HOGENOMiHOG000176924.
HOVERGENiHBG051459.
InParanoidiQ9UI10.
KOiK03680.
OrthoDBiEOG7XSTF0.
PhylomeDBiQ9UI10.
TreeFamiTF101508.

Enzyme and pathway databases

ReactomeiREACT_1815. Recycling of eIF2:GDP.

Miscellaneous databases

GeneWikiiEIF2B4.
GenomeRNAii8890.
NextBioi33383.
PROiQ9UI10.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UI10.
CleanExiHS_EIF2B4.
ExpressionAtlasiQ9UI10. baseline and differential.
GenevestigatoriQ9UI10.

Family and domain databases

InterProiIPR000649. IF-2B-related.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  2. "cDNA cloning, genomic organization and chromosomal localization of the human eIF2B delta subunit."
    Wightman P.J., Bonthron D.T.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Lung and Testis.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 THR-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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 THR-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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-228; GLN-357 AND CYS-374, VARIANT GLY-306.
  15. Cited for: VARIANTS VWM ARG-465 AND HIS-489.
  16. "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 GLN-209; ARG-269 AND CYS-374.

Entry informationi

Entry nameiEI2BD_HUMAN
AccessioniPrimary (citable) accession number: Q9UI10
Secondary accession number(s): Q53RY7
, Q5BJF4, Q9BUV9, Q9UBG4, Q9UIQ9, Q9UJ95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 12, 2003
Last modified: May 27, 2015
This is version 133 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.