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Protein

RanBP-type and C3HC4-type zinc finger-containing protein 1

Gene

RBCK1

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

Functioni

E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.9 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri193 – 222RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri282 – 327RING-type 1PROSITE-ProRule annotationAdd BLAST46
Zinc fingeri362 – 411IBR-typeAdd BLAST50
Zinc fingeri437 – 463RING-type 2PROSITE-ProRule annotationAdd BLAST27

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125826-MONOMER.
ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ9BYM8.

Names & Taxonomyi

Protein namesi
Recommended name:
RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC:6.3.2.-)
Alternative name(s):
HBV-associated factor 4
Heme-oxidized IRP2 ubiquitin ligase 1
Short name:
HOIL-1
Hepatitis B virus X-associated protein 4
RING finger protein 54
Ubiquitin-conjugating enzyme 7-interacting protein 3
Gene namesi
Name:RBCK1
Synonyms:C20orf18, RNF54, UBCE7IP3, XAP3, XAP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15864. RBCK1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • LUBAC complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Polyglucosan body myopathy 1 with or without immunodeficiency (PGBM1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by polyglucosan storage myopathy associated with early-onset progressive muscle weakness and progressive dilated cardiomyopathy, which may necessitate cardiac transplant in severe cases. Some patients present with severe immunodeficiency, invasive bacterial infections and chronic autoinflammation.
See also OMIM:615895
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07138518A → P in PGBM1. 1 Publication1
Natural variantiVAR_071386387N → S in PGBM1. 1 PublicationCorresponds to variant rs566912235dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi282C → S: Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-285. 1 Publication1
Mutagenesisi285C → S: Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-282. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10616.
MalaCardsiRBCK1.
MIMi615895. phenotype.
OpenTargetsiENSG00000125826.
Orphaneti329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
397937. Polyglucosan body myopathy.
PharmGKBiPA25723.

Polymorphism and mutation databases

BioMutaiRBCK1.
DMDMi166214993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000562951 – 510RanBP-type and C3HC4-type zinc finger-containing protein 1Add BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei50PhosphoserineCombined sources1
Modified residuei330PhosphotyrosineCombined sources1

Post-translational modificationi

Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome (By similarity).By similarity
Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BYM8.
MaxQBiQ9BYM8.
PaxDbiQ9BYM8.
PeptideAtlasiQ9BYM8.
PRIDEiQ9BYM8.

PTM databases

iPTMnetiQ9BYM8.
PhosphoSitePlusiQ9BYM8.

Expressioni

Inductioni

By viral transfection.1 Publication

Gene expression databases

BgeeiENSG00000125826.
CleanExiHS_RBCK1.
ExpressionAtlasiQ9BYM8. baseline and differential.
GenevisibleiQ9BYM8. HS.

Organism-specific databases

HPAiHPA024185.

Interactioni

Subunit structurei

Forms homodimers in vitro (By similarity). Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Interacts with beta-I-type (PRKCB1) and zeta-type protein kinase C (PRKCZ) and with UBE2L3. Interacts with PRKCH. Interacts with the HBV pX/HBx protein, which is required to activate transcription of the viral genome. Isoform 1 and isoform 2 interact with IREB2 only in iron-rich conditions. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Interacts with EYA1, TAB2, TAB3, MAP3K7 TRAF6 and RIPK1. Interacts with IRF3.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hoxa1P090223EBI-2340624,EBI-3957603From a different organism.
IKBKGQ9Y6K94EBI-2340624,EBI-81279
NAA10P412273EBI-2340624,EBI-747693
NDUFAF3Q9BU613EBI-2340624,EBI-2114801
NDUFAF3Q9BU61-23EBI-2340624,EBI-10298649
RNF31Q96EP020EBI-2340624,EBI-948111
Socs6Q9JLY05EBI-2340624,EBI-8500205From a different organism.
SYCE1Q8N0S23EBI-2340624,EBI-6872807
Traf1Q4VA122EBI-2340624,EBI-6116765From a different organism.
TSSK3Q96PN85EBI-2340624,EBI-3918381
UBE2L3P680363EBI-2340624,EBI-711173
UBE2L6O149336EBI-2340624,EBI-2129974
UBE2NP610882EBI-2340624,EBI-1052908

GO - Molecular functioni

  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115862. 83 interactors.
DIPiDIP-47737N.
IntActiQ9BYM8. 51 interactors.
MINTiMINT-6768751.
STRINGi9606.ENSP00000348632.

Structurei

Secondary structure

1510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi55 – 66Combined sources12
Beta strandi69 – 75Combined sources7
Helixi81 – 92Combined sources12
Helixi96 – 98Combined sources3
Beta strandi99 – 103Combined sources5
Beta strandi106 – 108Combined sources3
Helixi115 – 117Combined sources3
Beta strandi125 – 130Combined sources6
Beta strandi194 – 197Combined sources4
Turni200 – 202Combined sources3
Beta strandi214 – 216Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CRCNMR-A194-232[»]
2LGYNMR-A51-139[»]
4DBGX-ray2.71A37-137[»]
ProteinModelPortaliQ9BYM8.
SMRiQ9BYM8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYM8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 119Ubiquitin-likePROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 270Interaction with TAB21 PublicationAdd BLAST270
Regioni1 – 220Interaction with IRF31 PublicationAdd BLAST220
Regioni69 – 131Interaction with RNF311 PublicationAdd BLAST63

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili233 – 261Sequence analysisAdd BLAST29

Domaini

The RanBP2-type zinc finger, also called Npl4 zinc finger (NZF), mediates binding to 'Met-1'-linked polyubiquitins.By similarity
The UBL domain mediates association with RNF31 via interaction with its UBA domain.1 Publication

Sequence similaritiesi

Contains 1 IBR-type zinc finger.Curated
Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri193 – 222RanBP2-typePROSITE-ProRule annotationAdd BLAST30
Zinc fingeri282 – 327RING-type 1PROSITE-ProRule annotationAdd BLAST46
Zinc fingeri362 – 411IBR-typeAdd BLAST50
Zinc fingeri437 – 463RING-type 2PROSITE-ProRule annotationAdd BLAST27

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00530000063620.
HOVERGENiHBG061515.
InParanoidiQ9BYM8.
KOiK10630.
OMAiINCLLCK.
OrthoDBiEOG091G04QK.
PhylomeDBiQ9BYM8.
TreeFamiTF323486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR002867. IBR_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
IPR027370. Znf-RING_LisH.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF01485. IBR. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF90209. SSF90209. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q9BYM8-1) [UniParc]FASTAAdd to basket
Also known as: HOIL-1L

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
MDEKTKKAEE MALSLTRAVA GGDEQVAMKC AIWLAEQRVP LSVQLKPEVS
60 70 80 90 100
PTQDIRLWVS VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPVLQQ
110 120 130 140 150
WVIGQRLARD QETLHSHGVR QNGDSAYLYL LSARNTSLNP QELQRERQLR
160 170 180 190 200
MLEDLGFKDL TLQPRGPLEP GPPKPGVPQE PGRGQPDAVP EPPPVGWQCP
210 220 230 240 250
GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL AGEEEALRQY
260 270 280 290 300
QQRKQQQQEG NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC
310 320 330 340 350
LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IKALLTPEDY
360 370 380 390 400
QRFLDLGISI AENRSAFSYH CKTPDCKGWC FFEDDVNEFT CPVCFHVNCL
410 420 430 440 450
LCKAIHEQMN CKEYQEDLAL RAQNDVAARQ TTEMLKVMLQ QGEAMRCPQC
460 470 480 490 500
QIVVQKKDGC DWIRCTVCHT EICWVTKGPR WGPGGPGDTS GGCRCRVNGI
510
PCHPSCQNCH
Length:510
Mass (Da):57,572
Last modified:January 15, 2008 - v2
Checksum:iC6EF957B1F152FF2
GO
Isoform 2 (identifier: Q9BYM8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE

Show »
Length:468
Mass (Da):52,936
Checksum:i5B4420D28508EE16
GO
Isoform 3 (identifier: Q9BYM8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE
     253-272: RKQQQQEGNYLQHVQLDQRS → GVPAGHHPQQPGGGGLLPLH
     273-510: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:230
Mass (Da):25,654
Checksum:i8EDB1C28B96BF8D4
GO

Sequence cautioni

The sequence AAH15219 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti236E → D in BAC75409 (PubMed:12629548).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07138518A → P in PGBM1. 1 Publication1
Natural variantiVAR_071386387N → S in PGBM1. 1 PublicationCorresponds to variant rs566912235dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0057661 – 55MDEKT…PTQDI → MGTATPDGREDQE in isoform 2 and isoform 3. 3 PublicationsAdd BLAST55
Alternative sequenceiVSP_005767253 – 272RKQQQ…LDQRS → GVPAGHHPQQPGGGGLLPLH in isoform 3. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_005768273 – 510Missing in isoform 3. 1 PublicationAdd BLAST238

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67322 mRNA. Translation: AAD00162.1.
AB107766 mRNA. Translation: BAC75409.1.
AL121747 Genomic DNA. Translation: CAC17516.1.
AL121747 Genomic DNA. Translation: CAC28312.2.
BC000983 mRNA. No translation available.
BC015219 mRNA. Translation: AAH15219.2. Different initiation.
CCDSiCCDS12998.1. [Q9BYM8-3]
CCDS13000.2. [Q9BYM8-1]
RefSeqiNP_006453.1. NM_006462.5. [Q9BYM8-3]
NP_112506.2. NM_031229.3. [Q9BYM8-1]
UniGeneiHs.247280.
Hs.29546.

Genome annotation databases

EnsembliENST00000353660; ENSP00000254960; ENSG00000125826. [Q9BYM8-3]
ENST00000356286; ENSP00000348632; ENSG00000125826. [Q9BYM8-1]
GeneIDi10616.
KEGGihsa:10616.
UCSCiuc002wdp.5. human. [Q9BYM8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67322 mRNA. Translation: AAD00162.1.
AB107766 mRNA. Translation: BAC75409.1.
AL121747 Genomic DNA. Translation: CAC17516.1.
AL121747 Genomic DNA. Translation: CAC28312.2.
BC000983 mRNA. No translation available.
BC015219 mRNA. Translation: AAH15219.2. Different initiation.
CCDSiCCDS12998.1. [Q9BYM8-3]
CCDS13000.2. [Q9BYM8-1]
RefSeqiNP_006453.1. NM_006462.5. [Q9BYM8-3]
NP_112506.2. NM_031229.3. [Q9BYM8-1]
UniGeneiHs.247280.
Hs.29546.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CRCNMR-A194-232[»]
2LGYNMR-A51-139[»]
4DBGX-ray2.71A37-137[»]
ProteinModelPortaliQ9BYM8.
SMRiQ9BYM8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115862. 83 interactors.
DIPiDIP-47737N.
IntActiQ9BYM8. 51 interactors.
MINTiMINT-6768751.
STRINGi9606.ENSP00000348632.

PTM databases

iPTMnetiQ9BYM8.
PhosphoSitePlusiQ9BYM8.

Polymorphism and mutation databases

BioMutaiRBCK1.
DMDMi166214993.

Proteomic databases

EPDiQ9BYM8.
MaxQBiQ9BYM8.
PaxDbiQ9BYM8.
PeptideAtlasiQ9BYM8.
PRIDEiQ9BYM8.

Protocols and materials databases

DNASUi10616.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353660; ENSP00000254960; ENSG00000125826. [Q9BYM8-3]
ENST00000356286; ENSP00000348632; ENSG00000125826. [Q9BYM8-1]
GeneIDi10616.
KEGGihsa:10616.
UCSCiuc002wdp.5. human. [Q9BYM8-1]

Organism-specific databases

CTDi10616.
DisGeNETi10616.
GeneCardsiRBCK1.
HGNCiHGNC:15864. RBCK1.
HPAiHPA024185.
MalaCardsiRBCK1.
MIMi610924. gene.
615895. phenotype.
neXtProtiNX_Q9BYM8.
OpenTargetsiENSG00000125826.
Orphaneti329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
397937. Polyglucosan body myopathy.
PharmGKBiPA25723.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00530000063620.
HOVERGENiHBG061515.
InParanoidiQ9BYM8.
KOiK10630.
OMAiINCLLCK.
OrthoDBiEOG091G04QK.
PhylomeDBiQ9BYM8.
TreeFamiTF323486.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000125826-MONOMER.
ReactomeiR-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiQ9BYM8.

Miscellaneous databases

ChiTaRSiRBCK1. human.
EvolutionaryTraceiQ9BYM8.
GeneWikiiRBCK1.
GenomeRNAii10616.
PROiQ9BYM8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000125826.
CleanExiHS_RBCK1.
ExpressionAtlasiQ9BYM8. baseline and differential.
GenevisibleiQ9BYM8. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR002867. IBR_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
IPR027370. Znf-RING_LisH.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF01485. IBR. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF90209. SSF90209. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHOIL1_HUMAN
AccessioniPrimary (citable) accession number: Q9BYM8
Secondary accession number(s): O95623
, Q86SL2, Q96BS3, Q9BYM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 15, 2008
Last modified: November 30, 2016
This is version 161 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 20
    Human chromosome 20: 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. 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.