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Protein

Eukaryotic initiation factor 4A-II

Gene

EIF4A2

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

Functioni

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 848ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATPase activity Source: AgBase
  2. ATP binding Source: UniProtKB-KW
  3. helicase activity Source: ProtInc
  4. poly(A) RNA binding Source: UniProtKB
  5. translation initiation factor activity Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. gene expression Source: Reactome
  4. negative regulation of RNA-directed RNA polymerase activity Source: AgBase
  5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  6. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  7. regulation of translational initiation Source: ProtInc
  8. translation Source: Reactome
  9. translational initiation Source: Reactome
  10. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic initiation factor 4A-II (EC:3.6.4.13)
Short name:
eIF-4A-II
Short name:
eIF4A-II
Alternative name(s):
ATP-dependent RNA helicase eIF4A-2
Cleaved into the following chain:
Gene namesi
Name:EIF4A2
Synonyms:DDX2B, EIF4F
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3284. EIF4A2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 4F complex Source: ProtInc
  3. perinuclear region of cytoplasm Source: AgBase
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Eukaryotic initiation factor 4A-IIPRO_0000054938Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 407406Eukaryotic initiation factor 4A-II, N-terminally processedPRO_0000432207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei119 – 1191N6-acetyllysineBy similarity
Modified residuei159 – 1591PhosphothreonineBy similarity
Modified residuei175 – 1751N6-acetyllysineBy similarity
Modified residuei194 – 1941N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysineBy similarity
Modified residuei292 – 2921N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14240.
PaxDbiQ14240.
PRIDEiQ14240.

PTM databases

PhosphoSiteiQ14240.

Miscellaneous databases

PMAP-CutDBQ14240.

Expressioni

Gene expression databases

BgeeiQ14240.
CleanExiHS_EIF4A2.
ExpressionAtlasiQ14240. baseline and differential.
GenevestigatoriQ14240.

Organism-specific databases

HPAiCAB011690.

Interactioni

Subunit structurei

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3 (By similarity). Interacts with EIF4E. May interact with NOM1. Interacts with HHV-1 Vhs.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279584EBI-73473,EBI-6904388From a different organism.
HSPB1P047922EBI-73473,EBI-352682

Protein-protein interaction databases

BioGridi108290. 52 interactions.
IntActiQ14240. 19 interactions.
MINTiMINT-202114.
STRINGi9606.ENSP00000326381.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 373Combined sources
Helixi42 – 5110Combined sources
Helixi58 – 6811Combined sources
Beta strandi73 – 753Combined sources
Helixi81 – 9414Combined sources
Beta strandi104 – 1074Combined sources
Helixi111 – 12414Combined sources
Turni125 – 1295Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi154 – 1585Combined sources
Helixi160 – 1689Combined sources
Beta strandi179 – 1846Combined sources
Helixi185 – 1906Combined sources
Helixi194 – 20310Combined sources
Beta strandi209 – 2135Combined sources
Helixi219 – 22810Combined sources
Beta strandi233 – 2353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BORX-ray1.85A22-240[»]
ProteinModelPortaliQ14240.
SMRiQ14240. Positions 23-401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14240.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 235172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini246 – 407162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi33 – 6129Q motifAdd
BLAST
Motifi183 – 1864DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00530000062880.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiQ14240.
KOiK03257.
OMAiMPANIAD.
PhylomeDBiQ14240.
TreeFamiTF101524.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14240-1) [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
MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA
60 70 80 90 100
YGFEKPSAIQ QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK
110 120 130 140 150
ETQALVLAPT RELAQQIQKV ILALGDYMGA TCHACIGGTN VRNEMQKLQA
160 170 180 190 200
EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF VLDEADEMLS RGFKDQIYEI
210 220 230 240 250
FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE ELTLEGIKQF
260 270 280 290 300
YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV
310 320 330 340 350
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL
360 370 380 390 400
PTNRENYIHR IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP

MNVADLI
Length:407
Mass (Da):46,402
Last modified:March 15, 2004 - v2
Checksum:iFAA7D3BA9D8C6DA0
GO
Isoform 2 (identifier: Q14240-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-9: N → NS

Show »
Length:408
Mass (Da):46,489
Checksum:i0F47C0C4EEF00DD3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271N → S in AAH15842 (PubMed:15489334).Curated
Sequence conflicti212 – 2132LL → FA in BAA06336 (PubMed:8521730).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931Q → H.
Corresponds to variant rs11538616 [ dbSNP | Ensembl ].
VAR_052158
Natural varianti181 – 1811V → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_035838

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 91N → NS in isoform 2. 1 PublicationVSP_009629

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30655 mRNA. Translation: BAA06336.1.
BT009860 mRNA. Translation: AAP88862.1.
AC112907 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78172.1.
CH471052 Genomic DNA. Translation: EAW78177.1.
BC012547 mRNA. Translation: AAH12547.1.
BC013708 mRNA. Translation: AAH13708.1.
BC015842 mRNA. Translation: AAH15842.1.
BC048105 mRNA. Translation: AAH48105.1.
CCDSiCCDS3282.1. [Q14240-1]
RefSeqiNP_001958.2. NM_001967.3. [Q14240-1]
UniGeneiHs.518475.
Hs.599481.

Genome annotation databases

EnsembliENST00000323963; ENSP00000326381; ENSG00000156976. [Q14240-1]
ENST00000440191; ENSP00000398370; ENSG00000156976. [Q14240-2]
GeneIDi1974.
KEGGihsa:1974.
UCSCiuc003fqs.3. human. [Q14240-1]
uc003fqu.3. human. [Q14240-2]

Polymorphism databases

DMDMi45645183.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30655 mRNA. Translation: BAA06336.1.
BT009860 mRNA. Translation: AAP88862.1.
AC112907 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78172.1.
CH471052 Genomic DNA. Translation: EAW78177.1.
BC012547 mRNA. Translation: AAH12547.1.
BC013708 mRNA. Translation: AAH13708.1.
BC015842 mRNA. Translation: AAH15842.1.
BC048105 mRNA. Translation: AAH48105.1.
CCDSiCCDS3282.1. [Q14240-1]
RefSeqiNP_001958.2. NM_001967.3. [Q14240-1]
UniGeneiHs.518475.
Hs.599481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BORX-ray1.85A22-240[»]
ProteinModelPortaliQ14240.
SMRiQ14240. Positions 23-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108290. 52 interactions.
IntActiQ14240. 19 interactions.
MINTiMINT-202114.
STRINGi9606.ENSP00000326381.

PTM databases

PhosphoSiteiQ14240.

Polymorphism databases

DMDMi45645183.

Proteomic databases

MaxQBiQ14240.
PaxDbiQ14240.
PRIDEiQ14240.

Protocols and materials databases

DNASUi1974.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323963; ENSP00000326381; ENSG00000156976. [Q14240-1]
ENST00000440191; ENSP00000398370; ENSG00000156976. [Q14240-2]
GeneIDi1974.
KEGGihsa:1974.
UCSCiuc003fqs.3. human. [Q14240-1]
uc003fqu.3. human. [Q14240-2]

Organism-specific databases

CTDi1974.
GeneCardsiGC03P186574.
H-InvDBHIX0003899.
HGNCiHGNC:3284. EIF4A2.
HPAiCAB011690.
MIMi601102. gene.
neXtProtiNX_Q14240.
PharmGKBiPA27712.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00530000062880.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiQ14240.
KOiK03257.
OMAiMPANIAD.
PhylomeDBiQ14240.
TreeFamiTF101524.

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSiEIF4A2. human.
EvolutionaryTraceiQ14240.
GeneWikiiEIF4A2.
GenomeRNAii1974.
NextBioi7991.
PMAP-CutDBQ14240.
PROiQ14240.
SOURCEiSearch...

Gene expression databases

BgeeiQ14240.
CleanExiHS_EIF4A2.
ExpressionAtlasiQ14240. baseline and differential.
GenevestigatoriQ14240.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and mapping of the human EIF4A2 gene homologous to the murine protein synthesis initiation factor 4A-II gene Eif4a2."
    Sudo K., Takahashi E., Nakamura Y.
    Cytogenet. Cell Genet. 71:385-388(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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].
  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] (ISOFORMS 1 AND 2).
    Tissue: Bone marrow, Brain, Lymph and Skeletal muscle.
  6. "Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo."
    Li W., Belsham G.J., Proud C.G.
    J. Biol. Chem. 276:29111-29115(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF4E.
  7. "Identification of NOM1, a nucleolar, eIF4A binding protein encoded within the chromosome 7q36 breakpoint region targeted in cases of pediatric acute myeloid leukemia."
    Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.
    Gene 347:137-145(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INTERACTION WITH NOM1.
  8. "mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A."
    Feng P., Everly D.N. Jr., Read G.S.
    J. Virol. 79:9651-9664(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-1 VHS.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-240.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-181.

Entry informationi

Entry nameiIF4A2_HUMAN
AccessioniPrimary (citable) accession number: Q14240
Secondary accession number(s): D3DNU9
, Q53XJ6, Q96B90, Q96EA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 15, 2004
Last modified: March 4, 2015
This is version 157 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.