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Q9UI10

- EI2BD_HUMAN

UniProt

Q9UI10 - EI2BD_HUMAN

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Protein

Translation initiation factor eIF-2B subunit delta

Gene
EIF2B4, EIF2BD
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. protein binding Source: UniProtKB
  2. translation initiation factor activity Source: UniProtKB-KW
  3. translation initiation factor binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to stimulus Source: UniProtKB
  3. gene expression Source: Reactome
  4. myelination Source: UniProtKB
  5. negative regulation of translational initiation Source: RefGenome
  6. negative regulation of translational initiation in response to stress Source: UniProtKB
  7. oligodendrocyte development Source: UniProtKB
  8. ovarian follicle development Source: UniProtKB
  9. regulation of GTPase activity Source: GOC
  10. regulation of translation Source: UniProtKB
  11. regulation of translational initiation Source: RefGenome
  12. response to glucose Source: UniProtKB
  13. response to heat Source: UniProtKB
  14. response to peptide hormone Source: UniProtKB
  15. translation Source: Reactome
  16. 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: Chromosome 2

Organism-specific databases

HGNCiHGNC:3260. EIF2B4.

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 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.
Orphaneti99854. Cree leukoencephalopathy.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBiPA27691.

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

ArrayExpressiQ9UI10.
BgeeiQ9UI10.
CleanExiHS_EIF2B4.
GenevestigatoriQ9UI10.

Organism-specific databases

HPAiCAB032234.
HPA039993.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi114407. 7 interactions.
IntActiQ9UI10. 7 interactions.
MINTiMINT-4990902.
STRINGi9606.ENSP00000394869.

Structurei

3D structure databases

ProteinModelPortaliQ9UI10.
SMRiQ9UI10. Positions 219-517.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1184.
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. Align

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

MAAVAVAVRE DSGSGMKAEL PPGPGAVGRE MTKEEKLQLR KEKKQQKKKR    50
KEEKGAEPET GSAVSAAQCQ VGPTRELPES GIQLGTPREK VPAGRSKAEL 100
RAERRAKQEA ERALKQARKG EQGGPPPKAS PSTAGETPSG VKRLPEYPQV 150
DDLLLRRLVK KPERQQVPTR KDYGSKVSLF SHLPQYSRQN SLTQFMSIPS 200
SVIHPAMVRL GLQYSQGLVS GSNARCIALL RALQQVIQDY TTPPNEELSR 250
DLVNKLKPYM SFLTQCRPLS ASMHNAIKFL NKEITSVGSS KREEEAKSEL 300
RAAIDRYVQE KIVLAAQAIS RFAYQKISNG DVILVYGCSS LVSRILQEAW 350
TEGRRFRVVV VDSRPWLEGR HTLRSLVHAG VPASYLLIPA ASYVLPEVSK 400
VLLGAHALLA NGSVMSRVGT AQLALVARAH NVPVLVCCET YKFCERVQTD 450
AFVSNELDDP DDLQCKRGEH VALANWQNHA SLRLLNLVYD VTPPELVDLV 500
ITELGMIPCS SVPVVLRVKS SDQ 523
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.

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. VSP_001433
Alternative sequencei71 – 711Missing in isoform 2 and isoform 3. VSP_040130

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971S → T in CAB57260. 1 Publication
Sequence conflicti197 – 1971S → T in CAB57261. 1 Publication
Sequence conflicti197 – 1971S → T in CAB57304. 1 Publication
Sequence conflicti197 – 1971S → T in CAB57305. 1 Publication
Sequence conflicti323 – 3231A → S in AAF17195. 1 Publication
Sequence conflicti481 – 4811S → L in AAF17195. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi28381357.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS33164.1. [Q9UI10-1 ]
CCDS46244.1. [Q9UI10-3 ]
CCDS46245.1. [Q9UI10-2 ]
RefSeqi NP_001029288.1. NM_001034116.1. [Q9UI10-1 ]
NP_056451.3. NM_015636.3. [Q9UI10-3 ]
NP_751945.2. NM_172195.3. [Q9UI10-2 ]
UniGenei Hs.169474.

3D structure databases

ProteinModelPortali Q9UI10.
SMRi Q9UI10. Positions 219-517.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114407. 7 interactions.
IntActi Q9UI10. 7 interactions.
MINTi MINT-4990902.
STRINGi 9606.ENSP00000394869.

PTM databases

PhosphoSitei Q9UI10.

Polymorphism databases

DMDMi 28381357.

Proteomic databases

MaxQBi Q9UI10.
PaxDbi Q9UI10.
PRIDEi Q9UI10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000347454 ; ENSP00000233552 ; ENSG00000115211 . [Q9UI10-1 ]
ENST00000445933 ; ENSP00000394397 ; ENSG00000115211 . [Q9UI10-3 ]
ENST00000451130 ; ENSP00000394869 ; ENSG00000115211 . [Q9UI10-2 ]
GeneIDi 8890.
KEGGi hsa:8890.
UCSCi uc002rjz.3. human. [Q9UI10-2 ]
uc002rka.3. human. [Q9UI10-1 ]
uc002rkc.3. human. [Q9UI10-3 ]

Organism-specific databases

CTDi 8890.
GeneCardsi GC02M027587.
GeneReviewsi EIF2B4.
HGNCi HGNC:3260. EIF2B4.
HPAi CAB032234.
HPA039993.
MIMi 603896. phenotype.
606687. gene.
neXtProti NX_Q9UI10.
Orphaneti 99854. Cree leukoencephalopathy.
157716. Late infantile CACH syndrome.
99853. Ovarioleukodystrophy.
PharmGKBi PA27691.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1184.
HOGENOMi HOG000176924.
HOVERGENi HBG051459.
InParanoidi Q9UI10.
KOi K03680.
OrthoDBi EOG7XSTF0.
PhylomeDBi Q9UI10.
TreeFami TF101508.

Enzyme and pathway databases

Reactomei REACT_1815. Recycling of eIF2:GDP.

Miscellaneous databases

GeneWikii EIF2B4.
GenomeRNAii 8890.
NextBioi 33383.
PROi Q9UI10.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UI10.
Bgeei Q9UI10.
CleanExi HS_EIF2B4.
Genevestigatori Q9UI10.

Family and domain databases

InterProi IPR000649. IF-2B-related.
[Graphical view ]
Pfami PF01008. IF-2B. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  14. Cited for: VARIANTS VWM ARG-465 AND HIS-489.
  15. "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: September 3, 2014
This is version 126 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