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Protein

Proteasome inhibitor PI31 subunit

Gene

PSMF1

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 control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.1 Publication

GO - Molecular functioni

  • endopeptidase inhibitor activity Source: UniProtKB
  • proteasome binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome inhibitor PI31 subunit
Short name:
hPI31
Gene namesi
Name:PSMF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9571. PSMF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: Reactome
  • proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61V → R: Abolishes homodimerization. 1 Publication
Mutagenesisi83 – 831I → E: Abolishes interaction with FBXO7, but has no effect on homodimerization; when associated with E-90. 1 Publication
Mutagenesisi90 – 901I → E: Abolishes interaction with FBXO7, but has no effect on homodimerization; when associated with E-83. 1 Publication

Organism-specific databases

PharmGKBiPA33917.

Polymorphism and mutation databases

BioMutaiPSMF1.
DMDMi134047876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 271270Proteasome inhibitor PI31 subunitPRO_0000220920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei252 – 2521Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92530.
PaxDbiQ92530.
PRIDEiQ92530.

PTM databases

PhosphoSiteiQ92530.

Expressioni

Gene expression databases

BgeeiQ92530.
CleanExiHS_PSMF1.
ExpressionAtlasiQ92530. baseline and differential.
GenevisibleiQ92530. HS.

Organism-specific databases

HPAiHPA041122.
HPA041300.

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with FBXO7. Interacts with the 20S proteasome.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FBXO7Q9Y3I13EBI-945916,EBI-1161222
RBFOX1Q9NWB12EBI-945916,EBI-945906

Protein-protein interaction databases

BioGridi114872. 41 interactions.
IntActiQ92530. 14 interactions.
MINTiMINT-1633308.
STRINGi9606.ENSP00000327704.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Helixi12 – 143Combined sources
Helixi18 – 3114Combined sources
Turni32 – 343Combined sources
Beta strandi35 – 439Combined sources
Beta strandi51 – 533Combined sources
Turni56 – 594Combined sources
Beta strandi62 – 7312Combined sources
Beta strandi77 – 859Combined sources
Beta strandi88 – 947Combined sources
Turni96 – 994Combined sources
Beta strandi101 – 1077Combined sources
Helixi108 – 1114Combined sources
Turni115 – 1184Combined sources
Helixi120 – 1234Combined sources
Beta strandi124 – 1263Combined sources
Helixi127 – 13711Combined sources
Helixi139 – 14911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VT8X-ray2.60A/B1-151[»]
4OUHX-ray2.00A/B/C/D1-158[»]
ProteinModelPortaliQ92530.
SMRiQ92530. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92530.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 150149Important for homodimerization and interaction with FBXO7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi154 – 271118Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome inhibitor PI31 family.Curated

Phylogenomic databases

eggNOGiNOG255866.
GeneTreeiENSGT00390000012257.
HOGENOMiHOG000231957.
HOVERGENiHBG053746.
InParanoidiQ92530.
KOiK06700.
OMAiLRYEYKD.
PhylomeDBiQ92530.
TreeFamiTF106238.

Family and domain databases

InterProiIPR021625. FP_dom.
IPR013886. PI31_Prot_Reg.
[Graphical view]
PfamiPF08577. PI31_Prot_C. 1 hit.
PF11566. PI31_Prot_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q92530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYFGLGV GDQPGPNDKK
60 70 80 90 100
SELLPAGWNN NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ
110 120 130 140 150
VADLTLNLDD YIDAEHLGDF HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN
160 170 180 190 200
VSSPHREFPP ATAREVDPLR IPPHHPHTSR QPPWCDPLGP FVVGGEDLDP
210 220 230 240 250
FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG ARFDPFGPIG
260 270
TSPPGPNPDH LPPPGYDDMY L
Length:271
Mass (Da):29,817
Last modified:March 20, 2007 - v2
Checksum:iC669F8210AFAD727
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361F → C.3 Publications
Corresponds to variant rs1803415 [ dbSNP | Ensembl ].
VAR_024564
Natural varianti174 – 1741H → R.
Corresponds to variant rs2235587 [ dbSNP | Ensembl ].
VAR_022153

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88378 mRNA. Translation: BAA13603.1.
AL031665 Genomic DNA. Translation: CAC10383.1.
CH471133 Genomic DNA. Translation: EAX10650.1.
CH471133 Genomic DNA. Translation: EAX10651.1.
BC126462 mRNA. Translation: AAI26463.1.
CCDSiCCDS13010.1.
RefSeqiNP_006805.2. NM_006814.3.
NP_848693.2. NM_178578.2.
UniGeneiHs.471917.

Genome annotation databases

EnsembliENST00000333082; ENSP00000327704; ENSG00000125818.
ENST00000335877; ENSP00000338039; ENSG00000125818.
GeneIDi9491.
KEGGihsa:9491.
UCSCiuc002wel.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88378 mRNA. Translation: BAA13603.1.
AL031665 Genomic DNA. Translation: CAC10383.1.
CH471133 Genomic DNA. Translation: EAX10650.1.
CH471133 Genomic DNA. Translation: EAX10651.1.
BC126462 mRNA. Translation: AAI26463.1.
CCDSiCCDS13010.1.
RefSeqiNP_006805.2. NM_006814.3.
NP_848693.2. NM_178578.2.
UniGeneiHs.471917.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VT8X-ray2.60A/B1-151[»]
4OUHX-ray2.00A/B/C/D1-158[»]
ProteinModelPortaliQ92530.
SMRiQ92530. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114872. 41 interactions.
IntActiQ92530. 14 interactions.
MINTiMINT-1633308.
STRINGi9606.ENSP00000327704.

PTM databases

PhosphoSiteiQ92530.

Polymorphism and mutation databases

BioMutaiPSMF1.
DMDMi134047876.

Proteomic databases

MaxQBiQ92530.
PaxDbiQ92530.
PRIDEiQ92530.

Protocols and materials databases

DNASUi9491.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333082; ENSP00000327704; ENSG00000125818.
ENST00000335877; ENSP00000338039; ENSG00000125818.
GeneIDi9491.
KEGGihsa:9491.
UCSCiuc002wel.4. human.

Organism-specific databases

CTDi9491.
GeneCardsiGC20P001094.
HGNCiHGNC:9571. PSMF1.
HPAiHPA041122.
HPA041300.
neXtProtiNX_Q92530.
PharmGKBiPA33917.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255866.
GeneTreeiENSGT00390000012257.
HOGENOMiHOG000231957.
HOVERGENiHBG053746.
InParanoidiQ92530.
KOiK06700.
OMAiLRYEYKD.
PhylomeDBiQ92530.
TreeFamiTF106238.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSiPSMF1. human.
EvolutionaryTraceiQ92530.
GeneWikiiPSMF1.
GenomeRNAii9491.
NextBioi35560.
PROiQ92530.

Gene expression databases

BgeeiQ92530.
CleanExiHS_PSMF1.
ExpressionAtlasiQ92530. baseline and differential.
GenevisibleiQ92530. HS.

Family and domain databases

InterProiIPR021625. FP_dom.
IPR013886. PI31_Prot_Reg.
[Graphical view]
PfamiPF08577. PI31_Prot_C. 1 hit.
PF11566. PI31_Prot_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome."
    McCutchen-Maloney S.L., Matsuda K., Shimbara N., Binns D.D., Tanaka K., Slaughter C.A., DeMartino G.N.
    J. Biol. Chem. 275:18557-18565(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-36, FUNCTION, SUBUNIT.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT CYS-36.
  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], VARIANT CYS-36.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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.
  12. "Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor."
    Kirk R., Laman H., Knowles P.P., Murray-Rust J., Lomonosov M., Meziane E.K., McDonald N.Q.
    J. Biol. Chem. 283:22325-22335(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-151, INTERACTION WITH FBXO7, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF VAL-6; ILE-83 AND ILE-90.

Entry informationi

Entry nameiPSMF1_HUMAN
AccessioniPrimary (citable) accession number: Q92530
Secondary accession number(s): A0AVQ9, D3DVW3, Q9H4I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 20, 2007
Last modified: June 24, 2015
This is version 134 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.