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Protein

Probable ATP-dependent RNA helicase DDX58

Gene

Ddx58

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: newcastle disease virus (NDV) and Sendai virus (SeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and orthoreovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.6 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi811ZincPROSITE-ProRule annotation1
Metal bindingi814ZincPROSITE-ProRule annotation1
Metal bindingi865ZincPROSITE-ProRule annotation1
Metal bindingi870ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi265 – 272ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • double-stranded DNA binding Source: MGI
  • double-stranded RNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • single-stranded RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5689880. Ub-specific processing proteases.
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX58 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 58
RIG-I-like receptor 1
Short name:
RLR-1
Retinoic acid-inducible gene 1 protein
Short name:
RIG-1
Retinoic acid-inducible gene I protein
Short name:
RIG-I
Gene namesi
Name:Ddx58
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2442858. Ddx58.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

Pathology & Biotechi

Disruption phenotypei

Death between E12.5 and E14 due to liver apoptosis. Those who are born alive show growth retardation and die within 3 weeks.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001440941 – 926Probable ATP-dependent RNA helicase DDX58Add BLAST926

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei771Phosphothreonine; by CK2By similarity1
Modified residuei859N6-acetyllysineBy similarity1

Post-translational modificationi

ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response (By similarity).By similarity
Sumoylated, probably by MUL1; inhibiting its polyubiquitination.By similarity
Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. Lys-154 and Lys-164 are critical sites for RNF135-mediated and TRIM4-mediated ubiquitination. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'- and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6Q899.
PaxDbiQ6Q899.
PeptideAtlasiQ6Q899.
PRIDEiQ6Q899.

PTM databases

iPTMnetiQ6Q899.
PhosphoSitePlusiQ6Q899.

Expressioni

Inductioni

By interferon (IFN).

Gene expression databases

BgeeiENSMUSG00000040296.
CleanExiMM_DDX58.
ExpressionAtlasiQ6Q899. baseline and differential.
GenevisibleiQ6Q899. MM.

Interactioni

Subunit structurei

Monomer; maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts (via tandem CARD domain) with MAVS/IPS1 promoting its filamentation. Interacts with DHX58/LGP2, IKBKE, TBK1 and TMEM173/STING. Interacts (via CARD domain) with TRIM25 (via SPRY domain). Interacts with RNF135. Interacts with CYLD. Interacts with NLRC5; blocks the interaction of MAVS/IPS1 to DDX58. Interacts with SRC. Interacts with DDX60. Interacts with ZC3HAV1 (via zinc-fingers) in an RNA-dependent manner. Interacts (via tandem CARD domain) with SEC14L1; the interaction is direct and impairs the interaction of DDX58 with MAVS/IPS1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CblP226823EBI-6841237,EBI-640919
SiglecgQ80ZE37EBI-6841237,EBI-6841023

Protein-protein interaction databases

BioGridi230926. 5 interactors.
DIPiDIP-61741N.
IntActiQ6Q899. 3 interactors.
STRINGi10090.ENSMUSP00000042433.

Structurei

Secondary structure

1926
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi246 – 256Combined sources11
Beta strandi261 – 264Combined sources4
Helixi271 – 284Combined sources14
Beta strandi294 – 297Combined sources4
Helixi301 – 316Combined sources16
Turni317 – 319Combined sources3
Beta strandi322 – 325Combined sources4
Turni327 – 329Combined sources3
Helixi330 – 332Combined sources3
Helixi335 – 341Combined sources7
Beta strandi343 – 347Combined sources5
Helixi349 – 357Combined sources9
Beta strandi359 – 361Combined sources3
Helixi364 – 366Combined sources3
Beta strandi368 – 372Combined sources5
Helixi375 – 377Combined sources3
Helixi383 – 395Combined sources13
Beta strandi405 – 411Combined sources7
Helixi421 – 434Combined sources14
Beta strandi438 – 441Combined sources4
Helixi447 – 451Combined sources5
Beta strandi459 – 463Combined sources5
Helixi471 – 488Combined sources18
Helixi492 – 495Combined sources4
Helixi496 – 499Combined sources4
Beta strandi505 – 507Combined sources3
Helixi508 – 522Combined sources15
Helixi529 – 558Combined sources30
Helixi561 – 575Combined sources15
Helixi583 – 592Combined sources10
Helixi595 – 603Combined sources9
Helixi605 – 607Combined sources3
Helixi610 – 625Combined sources16
Beta strandi631 – 634Combined sources4
Helixi638 – 650Combined sources13
Helixi652 – 654Combined sources3
Beta strandi659 – 661Combined sources3
Beta strandi693 – 697Combined sources5
Beta strandi711 – 717Combined sources7
Turni733 – 735Combined sources3
Beta strandi738 – 744Combined sources7
Helixi746 – 771Combined sources26
Helixi774 – 793Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TBKX-ray2.14A240-794[»]
ProteinModelPortaliQ6Q899.
SMRiQ6Q899.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6Q899.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 87CARD 1Add BLAST87
Domaini92 – 172CARD 2Add BLAST81
Domaini252 – 431Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST180
Domaini611 – 777Helicase C-terminalPROSITE-ProRule annotationAdd BLAST167
Domaini791 – 926RLR CTRPROSITE-ProRule annotationAdd BLAST136

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni219 – 926Interaction with ZC3HAV1By similarityAdd BLAST708

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi373 – 376DECH box4

Domaini

The helicase domain is responsible for dsRNA recognition. Interacts with IFIT3 (via N-terminus).By similarity
The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton.By similarity
The RLR CTR domain controls homomultimerization and interaction with MAVS/IPS1. In the absence of viral infection, the protein is maintained as a monomer in an autoinhibited state with the CARD domains masked through intramolecular interactions mediated by the RLR CTR domain. Upon binding to viral RNA in the presence of ATP, the RLR CTR domain induces a conformational change exposing the CARD domain and promotes dimerization and CARD interactions with the adapter protein MAVS/IPS1 leading to the induction of downstream signaling.
The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.By similarity

Sequence similaritiesi

Belongs to the helicase family. RLR subfamily.Curated
Contains 2 CARD domains.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 RLR CTR (RLR C-terminal regulatory) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0354. Eukaryota.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000230911.
HOVERGENiHBG052325.
InParanoidiQ6Q899.
KOiK12646.
OMAiRTTDRFK.
OrthoDBiEOG091G01PQ.
TreeFamiTF330258.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR031964. CARD_dom.
IPR011029. DEATH-like_dom.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view]
PfamiPF16739. CARD_2. 2 hits.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51789. RLR_CTR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6Q899-1) [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
MTAEQRQNLQ AFRDYIKKIL DPTYILSYMS SWLEDEEVQY IQAEKNNKGP
60 70 80 90 100
MEAASLFLQY LLKLQSEGWF QAFLDALYHA GYCGLCEAIE SWDFQKIEKL
110 120 130 140 150
EEHRLLLRRL EPEFKATVDP NDILSELSEC LINQECEEIR QIRDTKGRMA
160 170 180 190 200
GAEKMAECLI RSDKENWPKV LQLALEKDNS KFSELWIVDK GFKRAESKAD
210 220 230 240 250
EDDGAEASSI QIFIQEEPEC QNLSQNPGPP SEASSNNLHS PLKPRNYQLE
260 270 280 290 300
LALPAKKGKN TIICAPTGCG KTFVSLLICE HHLKKFPCGQ KGKVVFFANQ
310 320 330 340 350
IPVYEQQATV FSRYFERLGY NIASISGATS DSVSVQHIIE DNDIIILTPQ
360 370 380 390 400
ILVNNLNNGA IPSLSVFTLM IFDECHNTSK NHPYNQIMFR YLDHKLGESR
410 420 430 440 450
DPLPQVVGLT ASVGVGDAKT AEEAMQHICK LCAALDASVI ATVRDNVAEL
460 470 480 490 500
EQVVYKPQKI SRKVASRTSN TFKCIISQLM KETEKLAKDV SEELGKLFQI
510 520 530 540 550
QNREFGTQKY EQWIVGVHKA CSVFQMADKE EESRVCKALF LYTSHLRKYN
560 570 580 590 600
DALIISEDAQ MTDALNYLKA FFHDVREAAF DETERELTRR FEEKLEELEK
610 620 630 640 650
VSRDPSNENP KLRDLYLVLQ EEYHLKPETK TILFVKTRAL VDALKKWIEE
660 670 680 690 700
NPALSFLKPG ILTGRGRTNR ATGMTLPAQK CVLEAFRASG DNNILIATSV
710 720 730 740 750
ADEGIDIAEC NLVILYEYVG NVIKMIQTRG RGRARDSKCF LLTSSADVIE
760 770 780 790 800
KEKANMIKEK IMNESILRLQ TWDEMKFGKT VHRIQVNEKL LRDSQHKPQP
810 820 830 840 850
VPDKENKKLL CGKCKNFACY TADIRVVETS HYTVLGDAFK ERFVCKPHPK
860 870 880 890 900
PKIYDNFEKK AKIFCAKQNC SHDWGIFVRY KTFEIPVIKI ESFVVEDIVS
910 920
GVQNRHSKWK DFHFERIQFD PAEMSV
Length:926
Mass (Da):105,975
Last modified:July 27, 2011 - v2
Checksum:i119FC0F88BC56957
GO
Isoform 2 (identifier: Q6Q899-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-454: Missing.
     455-460: YKPQKI → MPLTPV

Note: No experimental confirmation available.
Show »
Length:472
Mass (Da):54,658
Checksum:iD4614CA1A8BAC4EF
GO
Isoform 3 (identifier: Q6Q899-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-410: VGLT → FPIF
     411-926: Missing.

Note: No experimental confirmation available.
Show »
Length:410
Mass (Da):46,841
Checksum:iECC9E3D2D2BC5FE0
GO
Isoform 4 (identifier: Q6Q899-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     192-227: FKRAESKADEDDGAEASSIQIFIQEEPECQNLSQNP → GVLQERTLDPAALLPVLPTLLSIRGAVHFRYQRLYP
     228-926: Missing.

Note: No experimental confirmation available.
Show »
Length:227
Mass (Da):26,479
Checksum:i4FCBEE047EFB9AD0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4E → A in AAS59532 (Ref. 1) Curated1
Sequence conflicti282H → R in AAS59532 (Ref. 1) Curated1
Sequence conflicti604D → G in AAS59532 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0160551 – 454Missing in isoform 2. 1 PublicationAdd BLAST454
Alternative sequenceiVSP_016056192 – 227FKRAE…LSQNP → GVLQERTLDPAALLPVLPTL LSIRGAVHFRYQRLYP in isoform 4. 1 PublicationAdd BLAST36
Alternative sequenceiVSP_016057228 – 926Missing in isoform 4. 1 PublicationAdd BLAST699
Alternative sequenceiVSP_016058407 – 410VGLT → FPIF in isoform 3. 1 Publication4
Alternative sequenceiVSP_016059411 – 926Missing in isoform 3. 1 PublicationAdd BLAST516
Alternative sequenceiVSP_016060455 – 460YKPQKI → MPLTPV in isoform 2. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553221 mRNA. Translation: AAS59532.1.
AL831793 Genomic DNA. Translation: CAM27574.1.
CH466538 Genomic DNA. Translation: EDL05445.1.
AK049305 mRNA. Translation: BAC33670.1.
AK078287 mRNA. Translation: BAC37205.1.
AK087261 mRNA. Translation: BAC39830.1.
CCDSiCCDS18043.1. [Q6Q899-1]
RefSeqiNP_766277.3. NM_172689.3. [Q6Q899-1]
UniGeneiMm.86382.

Genome annotation databases

EnsembliENSMUST00000037907; ENSMUSP00000042433; ENSMUSG00000040296. [Q6Q899-1]
GeneIDi230073.
KEGGimmu:230073.
UCSCiuc008she.1. mouse. [Q6Q899-2]
uc008shf.1. mouse. [Q6Q899-1]
uc008shg.1. mouse. [Q6Q899-3]
uc008shh.1. mouse. [Q6Q899-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553221 mRNA. Translation: AAS59532.1.
AL831793 Genomic DNA. Translation: CAM27574.1.
CH466538 Genomic DNA. Translation: EDL05445.1.
AK049305 mRNA. Translation: BAC33670.1.
AK078287 mRNA. Translation: BAC37205.1.
AK087261 mRNA. Translation: BAC39830.1.
CCDSiCCDS18043.1. [Q6Q899-1]
RefSeqiNP_766277.3. NM_172689.3. [Q6Q899-1]
UniGeneiMm.86382.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TBKX-ray2.14A240-794[»]
ProteinModelPortaliQ6Q899.
SMRiQ6Q899.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230926. 5 interactors.
DIPiDIP-61741N.
IntActiQ6Q899. 3 interactors.
STRINGi10090.ENSMUSP00000042433.

PTM databases

iPTMnetiQ6Q899.
PhosphoSitePlusiQ6Q899.

Proteomic databases

EPDiQ6Q899.
PaxDbiQ6Q899.
PeptideAtlasiQ6Q899.
PRIDEiQ6Q899.

Protocols and materials databases

DNASUi230073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037907; ENSMUSP00000042433; ENSMUSG00000040296. [Q6Q899-1]
GeneIDi230073.
KEGGimmu:230073.
UCSCiuc008she.1. mouse. [Q6Q899-2]
uc008shf.1. mouse. [Q6Q899-1]
uc008shg.1. mouse. [Q6Q899-3]
uc008shh.1. mouse. [Q6Q899-4]

Organism-specific databases

CTDi23586.
MGIiMGI:2442858. Ddx58.

Phylogenomic databases

eggNOGiKOG0354. Eukaryota.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000230911.
HOVERGENiHBG052325.
InParanoidiQ6Q899.
KOiK12646.
OMAiRTTDRFK.
OrthoDBiEOG091G01PQ.
TreeFamiTF330258.

Enzyme and pathway databases

ReactomeiR-MMU-5689880. Ub-specific processing proteases.
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiDdx58. mouse.
EvolutionaryTraceiQ6Q899.
PROiQ6Q899.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000040296.
CleanExiMM_DDX58.
ExpressionAtlasiQ6Q899. baseline and differential.
GenevisibleiQ6Q899. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR031964. CARD_dom.
IPR011029. DEATH-like_dom.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view]
PfamiPF16739. CARD_2. 2 hits.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51789. RLR_CTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDDX58_MOUSE
AccessioniPrimary (citable) accession number: Q6Q899
Secondary accession number(s): A2AP28
, Q8C320, Q8C5I3, Q8C7T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.