Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-5A-dependent ribonuclease

Gene

RNASEL

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

Functioni

Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis (PubMed:26263979). Might play a central role in the regulation of mRNA turnover (PubMed:11585831).2 Publications

Catalytic activityi

Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.

Cofactori

Mn2+, Mg2+Note: Manganese or magnesium. Required for optimal RNA cleavage rates.

Enzyme regulationi

After binding to 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) the homodimerization and subsequent activation occurs. Inhibited by RNASEL inhibitor ABCE1/RLI, a cytoplasmic member of the ATP-binding cassette (ABC) transporter family.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri395 – 444C6-type; atypicalAdd BLAST50

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • endoribonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: InterPro
  • ribonucleoprotein complex binding Source: Ensembl
  • RNA binding Source: UniProtKB
  • rRNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Antiviral defense

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS06069-MONOMER.
ZFISH:HS06069-MONOMER.
ReactomeiR-HSA-382556. ABC-family proteins mediated transport.
R-HSA-909733. Interferon alpha/beta signaling.
SignaLinkiQ05823.

Names & Taxonomyi

Protein namesi
Recommended name:
2-5A-dependent ribonuclease (EC:3.1.26.-)
Short name:
2-5A-dependent RNase
Alternative name(s):
Ribonuclease 4
Ribonuclease L
Short name:
RNase L
Gene namesi
Name:RNASEL
Synonyms:RNS4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10050. RNASEL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Prostate cancer, hereditary, 1 (HPC1)
Disease susceptibility is associated with variations affecting the gene represented in this entry.4 Publications
Disease descriptionA condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
See also OMIM:601518

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi240K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-274. 1 Publication1
Mutagenesisi274K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-240. 1 Publication1
Mutagenesisi392K → R: Complete loss of enzymatic activity and enzyme dimerization. No change in binding to 2-5A and RNA. 1 Publication1
Mutagenesisi583H → A: No change in enzymatic activity. 1 Publication1
Mutagenesisi584P → A: No change in enzymatic activity. 1 Publication1
Mutagenesisi632W → A: No change in enzymatic activity. 1 Publication1
Mutagenesisi661D → A: Complete loss of enzymatic activity. 1 Publication1
Mutagenesisi667R → A: Complete loss of enzymatic activity. No change in 2-5A binding and enzyme dimerization. 1 Publication1
Mutagenesisi672H → A: Complete loss of enzymatic activity. No change in 2-5A binding activity and enzyme dimerization. 1 Publication1

Organism-specific databases

DisGeNETi6041.
MalaCardsiRNASEL.
MIMi176807. phenotype.
601518. phenotype.
OpenTargetsiENSG00000135828.
Orphaneti1331. Familial prostate cancer.
PharmGKBiPA34418.

Chemistry databases

ChEMBLiCHEMBL3575.

Polymorphism and mutation databases

BioMutaiRNASEL.
DMDMi1350802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670511 – 7412-5A-dependent ribonucleaseAdd BLAST741

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei684N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ05823.
PaxDbiQ05823.
PeptideAtlasiQ05823.
PRIDEiQ05823.

PTM databases

iPTMnetiQ05823.
PhosphoSitePlusiQ05823.

Miscellaneous databases

PMAP-CutDBQ05823.

Expressioni

Tissue specificityi

Highly expressed in spleen and thymus followed by prostate, testis, uterus, small intestine, colon and peripheral blood leukocytes.

Inductioni

By interferons. Virus replication in higher vertebrates is restrained by IFNs that cause cells to transcribe genes encoding antiviral proteins, such as 2'-5' oligoadenylate synthetases (OASs). oligoadenylate synthetase is stimulated by dsRNA to produce 5'-phosphorylated, 2'-5'-linked oligoadenylates (2-5A), whose function is to activate RNASEL.

Gene expression databases

BgeeiENSG00000135828.
CleanExiHS_RNASEL.
GenevisibleiQ05823. HS.

Organism-specific databases

HPAiCAB010906.
HPA002633.

Interactioni

Subunit structurei

Monomer (inactive form) or homodimer. Interacts with ABCE1; this interaction inhibits the RNASEL.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IQGAP1P469402EBI-8390477,EBI-297509

Protein-protein interaction databases

BioGridi111969. 11 interactors.
DIPiDIP-61367N.
IntActiQ05823. 4 interactors.
MINTiMINT-7990548.
STRINGi9606.ENSP00000356530.

Chemistry databases

BindingDBiQ05823.

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 34Combined sources13
Helixi38 – 46Combined sources9
Turni56 – 58Combined sources3
Helixi62 – 68Combined sources7
Helixi72 – 80Combined sources9
Helixi95 – 102Combined sources8
Helixi105 – 113Combined sources9
Helixi128 – 134Combined sources7
Helixi138 – 146Combined sources9
Helixi159 – 163Combined sources5
Helixi171 – 178Combined sources8
Helixi181 – 189Combined sources9
Helixi205 – 211Combined sources7
Turni215 – 217Combined sources3
Helixi218 – 227Combined sources10
Helixi237 – 239Combined sources3
Helixi242 – 248Combined sources7
Helixi252 – 260Combined sources9
Beta strandi261 – 263Combined sources3
Helixi276 – 282Combined sources7
Helixi286 – 295Combined sources10
Beta strandi301 – 303Combined sources3
Helixi304 – 310Combined sources7
Helixi314 – 322Combined sources9
Beta strandi341 – 344Combined sources4
Helixi345 – 352Combined sources8
Beta strandi361 – 363Combined sources3
Helixi367 – 369Combined sources3
Beta strandi370 – 374Combined sources5
Beta strandi377 – 395Combined sources19
Helixi399 – 409Combined sources11
Beta strandi420 – 425Combined sources6
Beta strandi427 – 435Combined sources9
Beta strandi438 – 440Combined sources3
Helixi441 – 445Combined sources5
Helixi459 – 477Combined sources19
Helixi488 – 490Combined sources3
Beta strandi491 – 493Combined sources3
Beta strandi495 – 497Combined sources3
Beta strandi499 – 501Combined sources3
Helixi514 – 532Combined sources19
Turni533 – 535Combined sources3
Helixi539 – 544Combined sources6
Helixi547 – 551Combined sources5
Helixi557 – 567Combined sources11
Helixi576 – 580Combined sources5
Helixi584 – 586Combined sources3
Helixi589 – 600Combined sources12
Helixi603 – 606Combined sources4
Helixi613 – 618Combined sources6
Turni628 – 631Combined sources4
Helixi632 – 634Combined sources3
Helixi638 – 645Combined sources8
Helixi646 – 648Combined sources3
Turni649 – 652Combined sources4
Helixi659 – 672Combined sources14
Helixi681 – 685Combined sources5
Helixi688 – 695Combined sources8
Helixi699 – 707Combined sources9
Helixi711 – 715Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WDYX-ray1.80A21-305[»]
4G8KX-ray2.40A/B1-337[»]
4G8LX-ray2.80A/B/C/D1-337[»]
4OAUX-ray2.60C21-719[»]
4OAVX-ray2.10B/D21-719[»]
ProteinModelPortaliQ05823.
SMRiQ05823.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05823.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati24 – 53ANK 1Add BLAST30
Repeati58 – 87ANK 2Add BLAST30
Repeati91 – 120ANK 3Add BLAST30
Repeati124 – 153ANK 4Add BLAST30
Repeati167 – 197ANK 5Add BLAST31
Repeati201 – 234ANK 6Add BLAST34
Repeati238 – 268ANK 7Add BLAST31
Repeati272 – 301ANK 8Add BLAST30
Repeati303 – 329ANK 9Add BLAST27
Domaini365 – 586Protein kinasePROSITE-ProRule annotationAdd BLAST222
Domaini589 – 723KENPROSITE-ProRule annotationAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 2422-5A binding (P-loop) 1Add BLAST14
Regioni253 – 2752-5A binding (P-loop) 2Add BLAST23

Domaini

The nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain.
The protein kinase domain is predicted to be catalytically inactive. It allows the homodimerization.
The ribonuclease domain is located in the C-terminus. A single active nuclease domain in a dimer is sufficient for ribonuclease activity (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily.Curated
Contains 9 ANK repeats.PROSITE-ProRule annotation
Contains 1 KEN domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri395 – 444C6-type; atypicalAdd BLAST50

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1027. Eukaryota.
KOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129724.
HOGENOMiHOG000276879.
HOVERGENiHBG012673.
InParanoidiQ05823.
KOiK01165.
OMAiDCGDLVM.
OrthoDBiEOG091G03H3.
PhylomeDBiQ05823.
TreeFamiTF344032.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010513. KEN_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR018997. PUB_domain.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 8 hits.
SM00580. PUG. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51392. KEN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q05823-1) [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
MESRDHNNPQ EGPTSSSGRR AAVEDNHLLI KAVQNEDVDL VQQLLEGGAN
60 70 80 90 100
VNFQEEEGGW TPLHNAVQMS REDIVELLLR HGADPVLRKK NGATPFILAA
110 120 130 140 150
IAGSVKLLKL FLSKGADVNE CDFYGFTAFM EAAVYGKVKA LKFLYKRGAN
160 170 180 190 200
VNLRRKTKED QERLRKGGAT ALMDAAEKGH VEVLKILLDE MGADVNACDN
210 220 230 240 250
MGRNALIHAL LSSDDSDVEA ITHLLLDHGA DVNVRGERGK TPLILAVEKK
260 270 280 290 300
HLGLVQRLLE QEHIEINDTD SDGKTALLLA VELKLKKIAE LLCKRGASTD
310 320 330 340 350
CGDLVMTARR NYDHSLVKVL LSHGAKEDFH PPAEDWKPQS SHWGAALKDL
360 370 380 390 400
HRIYRPMIGK LKFFIDEKYK IADTSEGGIY LGFYEKQEVA VKTFCEGSPR
410 420 430 440 450
AQREVSCLQS SRENSHLVTF YGSESHRGHL FVCVTLCEQT LEACLDVHRG
460 470 480 490 500
EDVENEEDEF ARNVLSSIFK AVQELHLSCG YTHQDLQPQN ILIDSKKAAH
510 520 530 540 550
LADFDKSIKW AGDPQEVKRD LEDLGRLVLY VVKKGSISFE DLKAQSNEEV
560 570 580 590 600
VQLSPDEETK DLIHRLFHPG EHVRDCLSDL LGHPFFWTWE SRYRTLRNVG
610 620 630 640 650
NESDIKTRKS ESEILRLLQP GPSEHSKSFD KWTTKINECV MKKMNKFYEK
660 670 680 690 700
RGNFYQNTVG DLLKFIRNLG EHIDEEKHKK MKLKIGDPSL YFQKTFPDLV
710 720 730 740
IYVYTKLQNT EYRKHFPQTH SPNKPQCDGA GGASGLASPG C
Length:741
Mass (Da):83,533
Last modified:February 1, 1996 - v2
Checksum:i91385EA307E3CE1D
GO
Isoform 2 (identifier: Q05823-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     636-652: INECVMKKMNKFYEKRG → MSKLRHRQIIFPTTQNQ
     653-741: Missing.

Show »
Length:652
Mass (Da):73,416
Checksum:i4F39B25B82F07216
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01350959G → S.2 PublicationsCorresponds to variant rs151296858dbSNPEnsembl.1
Natural variantiVAR_04235897I → L.1 PublicationCorresponds to variant rs56250729dbSNPEnsembl.1
Natural variantiVAR_042359289A → T.1 PublicationCorresponds to variant rs35553278dbSNPEnsembl.1
Natural variantiVAR_013510406S → F.1 PublicationCorresponds to variant rs145787003dbSNPEnsembl.1
Natural variantiVAR_012056462R → Q Risk factor for prostate cancer; reduced enzymatic activity. 4 PublicationsCorresponds to variant rs486907dbSNPEnsembl.1
Natural variantiVAR_012057541D → E No change in enzymatic activity. 4 PublicationsCorresponds to variant rs627928dbSNPEnsembl.1
Natural variantiVAR_042360592R → H.1 PublicationCorresponds to variant rs35896902dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056272636 – 652INECV…YEKRG → MSKLRHRQIIFPTTQNQ in isoform 2. 2 PublicationsAdd BLAST17
Alternative sequenceiVSP_056273653 – 741Missing in isoform 2. 2 PublicationsAdd BLAST89

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10381 Genomic DNA. Translation: AAA18032.1.
CR627369 mRNA. Translation: CAH10468.1.
AL138776 Genomic DNA. Translation: CAH71322.1.
CH471067 Genomic DNA. Translation: EAW91128.1.
BC090934 mRNA. Translation: AAH90934.1.
BC114433 mRNA. Translation: AAI14434.1.
CCDSiCCDS1347.1. [Q05823-1]
PIRiA45771.
RefSeqiNP_066956.1. NM_021133.3. [Q05823-1]
UniGeneiHs.518545.

Genome annotation databases

EnsembliENST00000367559; ENSP00000356530; ENSG00000135828. [Q05823-1]
ENST00000539397; ENSP00000440844; ENSG00000135828. [Q05823-2]
GeneIDi6041.
KEGGihsa:6041.
UCSCiuc001gpk.4. human. [Q05823-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10381 Genomic DNA. Translation: AAA18032.1.
CR627369 mRNA. Translation: CAH10468.1.
AL138776 Genomic DNA. Translation: CAH71322.1.
CH471067 Genomic DNA. Translation: EAW91128.1.
BC090934 mRNA. Translation: AAH90934.1.
BC114433 mRNA. Translation: AAI14434.1.
CCDSiCCDS1347.1. [Q05823-1]
PIRiA45771.
RefSeqiNP_066956.1. NM_021133.3. [Q05823-1]
UniGeneiHs.518545.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WDYX-ray1.80A21-305[»]
4G8KX-ray2.40A/B1-337[»]
4G8LX-ray2.80A/B/C/D1-337[»]
4OAUX-ray2.60C21-719[»]
4OAVX-ray2.10B/D21-719[»]
ProteinModelPortaliQ05823.
SMRiQ05823.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111969. 11 interactors.
DIPiDIP-61367N.
IntActiQ05823. 4 interactors.
MINTiMINT-7990548.
STRINGi9606.ENSP00000356530.

Chemistry databases

BindingDBiQ05823.
ChEMBLiCHEMBL3575.

PTM databases

iPTMnetiQ05823.
PhosphoSitePlusiQ05823.

Polymorphism and mutation databases

BioMutaiRNASEL.
DMDMi1350802.

Proteomic databases

EPDiQ05823.
PaxDbiQ05823.
PeptideAtlasiQ05823.
PRIDEiQ05823.

Protocols and materials databases

DNASUi6041.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367559; ENSP00000356530; ENSG00000135828. [Q05823-1]
ENST00000539397; ENSP00000440844; ENSG00000135828. [Q05823-2]
GeneIDi6041.
KEGGihsa:6041.
UCSCiuc001gpk.4. human. [Q05823-1]

Organism-specific databases

CTDi6041.
DisGeNETi6041.
GeneCardsiRNASEL.
HGNCiHGNC:10050. RNASEL.
HPAiCAB010906.
HPA002633.
MalaCardsiRNASEL.
MIMi176807. phenotype.
180435. gene.
601518. phenotype.
neXtProtiNX_Q05823.
OpenTargetsiENSG00000135828.
Orphaneti1331. Familial prostate cancer.
PharmGKBiPA34418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1027. Eukaryota.
KOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129724.
HOGENOMiHOG000276879.
HOVERGENiHBG012673.
InParanoidiQ05823.
KOiK01165.
OMAiDCGDLVM.
OrthoDBiEOG091G03H3.
PhylomeDBiQ05823.
TreeFamiTF344032.

Enzyme and pathway databases

BioCyciMetaCyc:HS06069-MONOMER.
ZFISH:HS06069-MONOMER.
ReactomeiR-HSA-382556. ABC-family proteins mediated transport.
R-HSA-909733. Interferon alpha/beta signaling.
SignaLinkiQ05823.

Miscellaneous databases

EvolutionaryTraceiQ05823.
GeneWikiiRibonuclease_L.
RNASEL.
GenomeRNAii6041.
PMAP-CutDBQ05823.
PROiQ05823.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135828.
CleanExiHS_RNASEL.
GenevisibleiQ05823. HS.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010513. KEN_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR018997. PUB_domain.
[Graphical view]
PfamiPF12796. Ank_2. 3 hits.
PF00069. Pkinase. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 8 hits.
SM00580. PUG. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51392. KEN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRN5A_HUMAN
AccessioniPrimary (citable) accession number: Q05823
Secondary accession number(s): Q5W0L2, Q6AI46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 167 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 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.