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Protein

Probable ATP-dependent RNA helicase DDX41

Gene

DDX41

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

Functioni

Probable ATP-dependent RNA helicase. Is required during post-transcriptional gene expression. May be involved in pre-mRNA splicing.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi225 – 2328ATPPROSITE-ProRule annotation
Zinc fingeri580 – 59718CCHC-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: ProtInc
  • cellular response to interferon-beta Source: Ensembl
  • defense response to virus Source: Ensembl
  • mRNA splicing, via spliceosome Source: UniProtKB
  • multicellular organism development Source: ProtInc
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of type I interferon production Source: Reactome
  • regulation of type I interferon production Source: Reactome
  • RNA processing Source: ProtInc
  • RNA secondary structure unwinding Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
SignaLinkiQ9UJV9.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX41 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 41
DEAD box protein abstrakt homolog
Gene namesi
Name:DDX41
Synonyms:ABS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:18674. DDX41.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: Ensembl
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134908862.

Polymorphism and mutation databases

BioMutaiDDX41.
DMDMi20532370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Probable ATP-dependent RNA helicase DDX41PRO_0000054970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei33 – 331PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UJV9.
MaxQBiQ9UJV9.
PaxDbiQ9UJV9.
PeptideAtlasiQ9UJV9.
PRIDEiQ9UJV9.

PTM databases

iPTMnetiQ9UJV9.
PhosphoSiteiQ9UJV9.

Expressioni

Gene expression databases

BgeeiQ9UJV9.
CleanExiHS_DDX41.
ExpressionAtlasiQ9UJV9. baseline and differential.
GenevisibleiQ9UJV9. HS.

Organism-specific databases

HPAiHPA017911.
HPA048803.

Interactioni

Subunit structurei

Identified in the spliceosome C complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP70Q8NHQ13EBI-1046350,EBI-739624
NKAPQ8N5F72EBI-1046350,EBI-721539
SIAH1Q8IUQ43EBI-1046350,EBI-747107

Protein-protein interaction databases

BioGridi119534. 31 interactions.
IntActiQ9UJV9. 157 interactions.
MINTiMINT-3081244.
STRINGi9606.ENSP00000422753.

Structurei

Secondary structure

1
622
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi408 – 4147Combined sources
Helixi417 – 4193Combined sources
Helixi420 – 4289Combined sources
Beta strandi435 – 4384Combined sources
Helixi442 – 45514Combined sources
Beta strandi459 – 4624Combined sources
Helixi468 – 48013Combined sources
Beta strandi484 – 4885Combined sources
Helixi490 – 4934Combined sources
Beta strandi502 – 5087Combined sources
Helixi513 – 5208Combined sources
Beta strandi531 – 5366Combined sources
Helixi542 – 55413Combined sources
Helixi561 – 5644Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P6NX-ray2.60A/B402-569[»]
ProteinModelPortaliQ9UJV9.
SMRiQ9UJV9. Positions 161-566.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UJV9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini212 – 396185Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini407 – 567161Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi181 – 20929Q motifAdd
BLAST
Motifi344 – 3474DEAD box

Sequence similaritiesi

Contains 1 CCHC-type zinc finger.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri580 – 59718CCHC-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0341. Eukaryota.
ENOG410XQQC. LUCA.
GeneTreeiENSGT00820000127023.
HOGENOMiHOG000268792.
HOVERGENiHBG015893.
InParanoidiQ9UJV9.
KOiK13116.
PhylomeDBiQ9UJV9.
TreeFamiTF300340.

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.
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. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UJV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESEPERKR ARTDEVPAGG SRSEAEDEDD EDYVPYVPLR QRRQLLLQKL
60 70 80 90 100
LQRRRKGAAE EEQQDSGSEP RGDEDDIPLG PQSNVSLLDQ HQHLKEKAEA
110 120 130 140 150
RKESAKEKQL KEEEKILESV AEGRALMSVK EMAKGITYDD PIKTSWTPPR
160 170 180 190 200
YVLSMSEERH ERVRKKYHIL VEGDGIPPPI KSFKEMKFPA AILRGLKKKG
210 220 230 240 250
IHHPTPIQIQ GIPTILSGRD MIGIAFTGSG KTLVFTLPVI MFCLEQEKRL
260 270 280 290 300
PFSKREGPYG LIICPSRELA RQTHGILEYY CRLLQEDSSP LLRCALCIGG
310 320 330 340 350
MSVKEQMETI RHGVHMMVAT PGRLMDLLQK KMVSLDICRY LALDEADRMI
360 370 380 390 400
DMGFEGDIRT IFSYFKGQRQ TLLFSATMPK KIQNFAKSAL VKPVTINVGR
410 420 430 440 450
AGAASLDVIQ EVEYVKEEAK MVYLLECLQK TPPPVLIFAE KKADVDAIHE
460 470 480 490 500
YLLLKGVEAV AIHGGKDQEE RTKAIEAFRE GKKDVLVATD VASKGLDFPA
510 520 530 540 550
IQHVINYDMP EEIENYVHRI GRTGRSGNTG IATTFINKAC DESVLMDLKA
560 570 580 590 600
LLLEAKQKVP PVLQVLHCGD ESMLDIGGER GCAFCGGLGH RITDCPKLEA
610 620
MQTKQVSNIG RKDYLAHSSM DF
Length:622
Mass (Da):69,838
Last modified:May 10, 2002 - v2
Checksum:iE0A328724E0DF99A
GO

Sequence cautioni

The sequence CAE46035.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 4327PAGGS…LRQRR → LPEEAAPRRKMRTTRTTCPM CRYAAP in AAF04150 (PubMed:10607561).CuratedAdd
BLAST
Sequence conflicti56 – 561K → E in BAA91585 (PubMed:14702039).Curated
Sequence conflicti64 – 641Q → E in BAB55355 (PubMed:14702039).Curated
Sequence conflicti165 – 1651K → E in BAB55355 (PubMed:14702039).Curated
Sequence conflicti191 – 1911A → T in BAA91585 (PubMed:14702039).Curated
Sequence conflicti352 – 3521M → T in BAA91585 (PubMed:14702039).Curated
Sequence conflicti552 – 5521L → Q in BAB55355 (PubMed:14702039).Curated
Sequence conflicti570 – 5701D → G in CAE46035 (PubMed:17974005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195417 mRNA. Translation: AAF04150.1.
AK001255 mRNA. Translation: BAA91585.1.
AK027768 mRNA. Translation: BAB55355.1.
AK315491 mRNA. Translation: BAG37875.1.
CH471195 Genomic DNA. Translation: EAW84981.1.
BC015476 mRNA. Translation: AAH15476.1.
AL137455 mRNA. Translation: CAB70746.1.
BX641072 mRNA. Translation: CAE46035.1. Sequence problems.
CCDSiCCDS4427.1.
PIRiT46269.
RefSeqiNP_057306.2. NM_016222.3.
UniGeneiHs.484288.

Genome annotation databases

EnsembliENST00000507955; ENSP00000422753; ENSG00000183258.
GeneIDi51428.
KEGGihsa:51428.
UCSCiuc003mho.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195417 mRNA. Translation: AAF04150.1.
AK001255 mRNA. Translation: BAA91585.1.
AK027768 mRNA. Translation: BAB55355.1.
AK315491 mRNA. Translation: BAG37875.1.
CH471195 Genomic DNA. Translation: EAW84981.1.
BC015476 mRNA. Translation: AAH15476.1.
AL137455 mRNA. Translation: CAB70746.1.
BX641072 mRNA. Translation: CAE46035.1. Sequence problems.
CCDSiCCDS4427.1.
PIRiT46269.
RefSeqiNP_057306.2. NM_016222.3.
UniGeneiHs.484288.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P6NX-ray2.60A/B402-569[»]
ProteinModelPortaliQ9UJV9.
SMRiQ9UJV9. Positions 161-566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119534. 31 interactions.
IntActiQ9UJV9. 157 interactions.
MINTiMINT-3081244.
STRINGi9606.ENSP00000422753.

PTM databases

iPTMnetiQ9UJV9.
PhosphoSiteiQ9UJV9.

Polymorphism and mutation databases

BioMutaiDDX41.
DMDMi20532370.

Proteomic databases

EPDiQ9UJV9.
MaxQBiQ9UJV9.
PaxDbiQ9UJV9.
PeptideAtlasiQ9UJV9.
PRIDEiQ9UJV9.

Protocols and materials databases

DNASUi51428.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000507955; ENSP00000422753; ENSG00000183258.
GeneIDi51428.
KEGGihsa:51428.
UCSCiuc003mho.4. human.

Organism-specific databases

CTDi51428.
GeneCardsiDDX41.
HGNCiHGNC:18674. DDX41.
HPAiHPA017911.
HPA048803.
MIMi608170. gene.
neXtProtiNX_Q9UJV9.
PharmGKBiPA134908862.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0341. Eukaryota.
ENOG410XQQC. LUCA.
GeneTreeiENSGT00820000127023.
HOGENOMiHOG000268792.
HOVERGENiHBG015893.
InParanoidiQ9UJV9.
KOiK13116.
PhylomeDBiQ9UJV9.
TreeFamiTF300340.

Enzyme and pathway databases

ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
SignaLinkiQ9UJV9.

Miscellaneous databases

ChiTaRSiDDX41. human.
EvolutionaryTraceiQ9UJV9.
GeneWikiiDDX41.
GenomeRNAii51428.
PROiQ9UJV9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJV9.
CleanExiHS_DDX41.
ExpressionAtlasiQ9UJV9. baseline and differential.
GenevisibleiQ9UJV9. HS.

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.
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. 2 hits.
PROSITEiPS51192. 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. "Developmental and cell biological functions of the Drosophila DEAD-box protein abstrakt."
    Irion U., Leptin M.
    Curr. Biol. 9:1373-1381(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Skin.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-622.
    Tissue: Amygdala.
  6. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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 SER-21 AND SER-23, 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 SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [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. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 402-569.

Entry informationi

Entry nameiDDX41_HUMAN
AccessioniPrimary (citable) accession number: Q9UJV9
Secondary accession number(s): B2RDC8
, Q96BK6, Q96K05, Q9NT96, Q9NW04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2002
Last modified: June 8, 2016
This is version 168 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.