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Protein

Ubiquilin-2

Gene

UBQLN2

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

Functioni

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:10983987). Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:24215460, PubMed:18307982). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:19148225, PubMed:20529957). Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs) (PubMed:18199683).6 Publications

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of clathrin-dependent endocytosis Source: UniProtKB
  • negative regulation of G-protein coupled receptor internalization Source: UniProtKB
  • positive regulation of ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • regulation of autophagosome assembly Source: UniProtKB
  • regulation of macroautophagy Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

BioCyciZFISH:G66-31945-MONOMER.
ReactomeiR-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquilin-2
Alternative name(s):
Chap1
DSK2 homolog
Protein linking IAP with cytoskeleton 2
Short name:
PLIC-2
Short name:
hPLIC-2
Ubiquitin-like product Chap1/Dsk2
Gene namesi
Name:UBQLN2
Synonyms:N4BP4, PLIC2
ORF Names:HRIHFB2157
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12509. UBQLN2.

Subcellular locationi

GO - Cellular componenti

  • autophagosome Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: UniProtKB-KW
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS15 may develop frontotemporal dementia.
See also OMIM:300857
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068892155S → N in ALS15; uncertain pathological significance. 1 PublicationCorresponds to variant rs374522677dbSNPEnsembl.1
Natural variantiVAR_068893189P → T in ALS15; uncertain pathological significance. 1 Publication1
Natural variantiVAR_068895283A → T in ALS15. 1 PublicationCorresponds to variant rs749463696dbSNPEnsembl.1
Natural variantiVAR_068896425Q → R in ALS15. 1 Publication1
Natural variantiVAR_068897487T → I in ALS15. 1 Publication1
Natural variantiVAR_066562497P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1 and FAF2; increases translocation of HNRNPA1 to the cytoplasm; adversely affects ERAD. 3 PublicationsCorresponds to variant rs387906709dbSNPEnsembl.1
Natural variantiVAR_066563497P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs387906710dbSNPEnsembl.1
Natural variantiVAR_066564506P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs387906711dbSNPEnsembl.1
Natural variantiVAR_066565509P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs387906712dbSNPEnsembl.1
Natural variantiVAR_066566525P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs369947678dbSNPEnsembl.1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi29978.
MalaCardsiUBQLN2.
MIMi300857. phenotype.
OpenTargetsiENSG00000188021.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA37156.

Polymorphism and mutation databases

BioMutaiUBQLN2.
DMDMi124056593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002110112 – 624Ubiquilin-2Add BLAST623

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Post-translational modificationi

Degraded during macroautophagy.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9UHD9.
MaxQBiQ9UHD9.
PaxDbiQ9UHD9.
PeptideAtlasiQ9UHD9.
PRIDEiQ9UHD9.

PTM databases

iPTMnetiQ9UHD9.
PhosphoSitePlusiQ9UHD9.

Expressioni

Inductioni

Highly expressed in mitotic cells from metaphase to telophase. Expression in non-mitotic cells is very low.

Gene expression databases

BgeeiENSG00000188021.
CleanExiHS_UBQLN2.
GenevisibleiQ9UHD9. HS.

Organism-specific databases

HPAiCAB013481.
HPA006431.

Interactioni

Subunit structurei

Homodimer. Forms heterodimer with UBQLN1. Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72. Interacts with HNRNPA1 and HNRNPU. Found in a complex with UBQLN1 and MAP1LC3A/B/C. Interacts with EPS15, EPN1 and EPN2. Interacts with HERPUD1. Interacts with RAD23A. Interacts with TARDBP. Interacts (via C-terminus) with FAF2 (via N-terminus). Interacts with UBQLN4. Binds CD47 (By similarity).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161864EBI-947187,EBI-954387
AGR2O959944EBI-947187,EBI-712648
C1QAP027453EBI-947187,EBI-1220209
CTAG1BP783586EBI-947187,EBI-1188472
DAZAP2Q150384EBI-947187,EBI-724310
FAM127AA6ZKI34EBI-947187,EBI-10174072
HNRNPA1P096512EBI-947187,EBI-352662
HNRNPA1P09651-24EBI-947187,EBI-352677
HNRNPUQ008393EBI-947187,EBI-351126
PSMD4P550363EBI-947187,EBI-359318
RAD23AP547255EBI-947187,EBI-746453
RPN13O487264EBI-947187,EBI-7710745From a different organism.
TRIM32Q130494EBI-947187,EBI-742790

Protein-protein interaction databases

BioGridi119006. 81 interactors.
DIPiDIP-42116N.
IntActiQ9UHD9. 209 interactors.
MINTiMINT-1192483.
STRINGi9606.ENSP00000345195.

Structurei

Secondary structure

1624
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 25Combined sources3
Beta strandi33 – 38Combined sources6
Beta strandi43 – 48Combined sources6
Helixi54 – 65Combined sources12
Beta strandi69 – 76Combined sources8
Beta strandi79 – 82Combined sources4
Helixi87 – 91Combined sources5
Beta strandi93 – 102Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J8CNMR-A1-103[»]
2NBVNMR-B26-103[»]
ProteinModelPortaliQ9UHD9.
SMRiQ9UHD9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHD9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 107Ubiquitin-likePROSITE-ProRule annotationAdd BLAST75
Domaini178 – 206STI1 1Sequence analysisAdd BLAST29
Domaini208 – 247STI1 2Sequence analysisAdd BLAST40
Domaini379 – 426STI1 3Sequence analysisAdd BLAST48
Domaini430 – 462STI1 4Sequence analysisAdd BLAST33
Repeati491 – 49313
Repeati494 – 49623
Repeati497 – 49933
Repeati500 – 50243
Repeati503 – 50553
Repeati506 – 50863
Repeati509 – 51173
Repeati512 – 51483
Repeati515 – 51793
Repeati518 – 520103
Repeati521 – 523113
Repeati524 – 526123
Domaini581 – 621UBAPROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni491 – 52612 X 3 AA tandem repeats of P-X-XAdd BLAST36

Domaini

The ubiquitin-like domain is essential for its inhibitory effect on GPCR endocytosis. Mediates its association with the subunits of the proteasome.1 Publication1 Publication
The UBA domain is essential for its association with microtubule-associated protein 1 light chain 3 (MAP1LC3). Mediates its association with ubiquitinated substrates.1 Publication1 Publication
Dimerization is dependent upon the central region of the protein containing the STI1 domains and is independent of its ubiquitin-like and UBA domains.1 Publication

Sequence similaritiesi

Contains 4 STI1 domains.Sequence analysis
Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0010. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ9UHD9.
KOiK04523.
OMAiNRPQGQS.
OrthoDBiEOG091G08WB.
PhylomeDBiQ9UHD9.
TreeFamiTF314412.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR015496. Ubiquilin.
IPR028430. Ubiquilin-1/2.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 2 hits.
PTHR10677:SF5. PTHR10677:SF5. 2 hits.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UHD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENGESSGP PRPSRGPAAA QGSAAAPAEP KIIKVTVKTP KEKEEFAVPE
60 70 80 90 100
NSSVQQFKEA ISKRFKSQTD QLVLIFAGKI LKDQDTLIQH GIHDGLTVHL
110 120 130 140 150
VIKSQNRPQG QSTQPSNAAG TNTTSASTPR SNSTPISTNS NPFGLGSLGG
160 170 180 190 200
LAGLSSLGLS STNFSELQSQ MQQQLMASPE MMIQIMENPF VQSMLSNPDL
210 220 230 240 250
MRQLIMANPQ MQQLIQRNPE ISHLLNNPDI MRQTLEIARN PAMMQEMMRN
260 270 280 290 300
QDLALSNLES IPGGYNALRR MYTDIQEPML NAAQEQFGGN PFASVGSSSS
310 320 330 340 350
SGEGTQPSRT ENRDPLPNPW APPPATQSSA TTSTTTSTGS GSGNSSSNAT
360 370 380 390 400
GNTVAAANYV ASIFSTPGMQ SLLQQITENP QLIQNMLSAP YMRSMMQSLS
410 420 430 440 450
QNPDLAAQMM LNSPLFTANP QLQEQMRPQL PAFLQQMQNP DTLSAMSNPR
460 470 480 490 500
AMQALMQIQQ GLQTLATEAP GLIPSFTPGV GVGVLGTAIG PVGPVTPIGP
510 520 530 540 550
IGPIVPFTPI GPIGPIGPTG PAAPPGSTGS GGPTGPTVSS AAPSETTSPT
560 570 580 590 600
SESGPNQQFI QQMVQALAGA NAPQLPNPEV RFQQQLEQLN AMGFLNREAN
610 620
LQALIATGGD INAAIERLLG SQPS
Length:624
Mass (Da):65,696
Last modified:January 23, 2007 - v2
Checksum:iDF7DF8C4D7B71AC3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti544S → R in AAF17237 (PubMed:10675567).Curated1
Sequence conflicti544S → R in BAA34801 (PubMed:9853615).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068892155S → N in ALS15; uncertain pathological significance. 1 PublicationCorresponds to variant rs374522677dbSNPEnsembl.1
Natural variantiVAR_068893189P → T in ALS15; uncertain pathological significance. 1 Publication1
Natural variantiVAR_052680235L → H.Corresponds to variant rs17002693dbSNPEnsembl.1
Natural variantiVAR_068894282A → V Probable disease-associated mutation found in a patient with frontotemporal dementia. 1 Publication1
Natural variantiVAR_068895283A → T in ALS15. 1 PublicationCorresponds to variant rs749463696dbSNPEnsembl.1
Natural variantiVAR_068896425Q → R in ALS15. 1 Publication1
Natural variantiVAR_068897487T → I in ALS15. 1 Publication1
Natural variantiVAR_066562497P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1 and FAF2; increases translocation of HNRNPA1 to the cytoplasm; adversely affects ERAD. 3 PublicationsCorresponds to variant rs387906709dbSNPEnsembl.1
Natural variantiVAR_066563497P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs387906710dbSNPEnsembl.1
Natural variantiVAR_066564506P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs387906711dbSNPEnsembl.1
Natural variantiVAR_066565509P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs387906712dbSNPEnsembl.1
Natural variantiVAR_066566525P → S in ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm. 2 PublicationsCorresponds to variant rs369947678dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF189009 mRNA. Translation: AAF17237.1.
AF293385 mRNA. Translation: AAG02474.1.
AL354793 Genomic DNA. Translation: CAD13519.1.
CH471154 Genomic DNA. Translation: EAW93233.1.
BC069237 mRNA. Translation: AAH69237.1.
AL442081 mRNA. Translation: CAC09446.1.
AB015344 mRNA. Translation: BAA34801.1.
CCDSiCCDS14374.1.
RefSeqiNP_038472.2. NM_013444.3.
UniGeneiHs.179309.

Genome annotation databases

EnsembliENST00000338222; ENSP00000345195; ENSG00000188021.
GeneIDi29978.
KEGGihsa:29978.
UCSCiuc004dus.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF189009 mRNA. Translation: AAF17237.1.
AF293385 mRNA. Translation: AAG02474.1.
AL354793 Genomic DNA. Translation: CAD13519.1.
CH471154 Genomic DNA. Translation: EAW93233.1.
BC069237 mRNA. Translation: AAH69237.1.
AL442081 mRNA. Translation: CAC09446.1.
AB015344 mRNA. Translation: BAA34801.1.
CCDSiCCDS14374.1.
RefSeqiNP_038472.2. NM_013444.3.
UniGeneiHs.179309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J8CNMR-A1-103[»]
2NBVNMR-B26-103[»]
ProteinModelPortaliQ9UHD9.
SMRiQ9UHD9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119006. 81 interactors.
DIPiDIP-42116N.
IntActiQ9UHD9. 209 interactors.
MINTiMINT-1192483.
STRINGi9606.ENSP00000345195.

PTM databases

iPTMnetiQ9UHD9.
PhosphoSitePlusiQ9UHD9.

Polymorphism and mutation databases

BioMutaiUBQLN2.
DMDMi124056593.

Proteomic databases

EPDiQ9UHD9.
MaxQBiQ9UHD9.
PaxDbiQ9UHD9.
PeptideAtlasiQ9UHD9.
PRIDEiQ9UHD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338222; ENSP00000345195; ENSG00000188021.
GeneIDi29978.
KEGGihsa:29978.
UCSCiuc004dus.4. human.

Organism-specific databases

CTDi29978.
DisGeNETi29978.
GeneCardsiUBQLN2.
GeneReviewsiUBQLN2.
HGNCiHGNC:12509. UBQLN2.
HPAiCAB013481.
HPA006431.
MalaCardsiUBQLN2.
MIMi300264. gene.
300857. phenotype.
neXtProtiNX_Q9UHD9.
OpenTargetsiENSG00000188021.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA37156.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0010. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00390000005720.
HOGENOMiHOG000234878.
HOVERGENiHBG064537.
InParanoidiQ9UHD9.
KOiK04523.
OMAiNRPQGQS.
OrthoDBiEOG091G08WB.
PhylomeDBiQ9UHD9.
TreeFamiTF314412.

Enzyme and pathway databases

BioCyciZFISH:G66-31945-MONOMER.
ReactomeiR-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.

Miscellaneous databases

ChiTaRSiUBQLN2. human.
EvolutionaryTraceiQ9UHD9.
GeneWikiiUBQLN2.
GenomeRNAii29978.
PROiQ9UHD9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000188021.
CleanExiHS_UBQLN2.
GenevisibleiQ9UHD9. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR015496. Ubiquilin.
IPR028430. Ubiquilin-1/2.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 2 hits.
PTHR10677:SF5. PTHR10677:SF5. 2 hits.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 4 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF48371. SSF48371. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBQL2_HUMAN
AccessioniPrimary (citable) accession number: Q9UHD9
Secondary accession number(s): O94798
, Q5D027, Q9H3W6, Q9HAZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 144 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 X
    Human chromosome X: 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.