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

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene

Fkbp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.3 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by FK506.By similarity

GO - Molecular functioni

  • ATP binding Source: MGI
  • FK506 binding Source: GO_Central
  • glucocorticoid receptor binding Source: MGI
  • GTP binding Source: MGI
  • heat shock protein binding Source: MGI
  • peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  • phosphoprotein binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

  • androgen receptor signaling pathway Source: MGI
  • chaperone-mediated protein folding Source: UniProtKB
  • copper ion transport Source: Ensembl
  • embryo implantation Source: MGI
  • male sex differentiation Source: MGI
  • negative regulation of microtubule polymerization Source: Ensembl
  • negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
  • negative regulation of neuron projection development Source: UniProtKB
  • prostate gland development Source: MGI
  • protein complex localization Source: MGI
  • reproductive structure development Source: MGI
  • steroid hormone receptor complex assembly Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiR-MMU-3371568. Attenuation phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP4 (EC:5.2.1.8)
Short name:
PPIase FKBP4
Alternative name(s):
52 kDa FK506-binding protein
Short name:
52 kDa FKBP
Short name:
FKBP-52
59 kDa immunophilin
Short name:
p59
FK506-binding protein 4
Short name:
FKBP-4
FKBP59
HSP-binding immunophilin
Short name:
HBI
Immunophilin FKBP52
Rotamase
Cleaved into the following chain:
Gene namesi
Name:Fkbp4
Synonyms:Fkpb52
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:95543. Fkbp4.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication
  • Mitochondrion By similarity
  • Nucleus 2 Publications
  • Cytoplasmcytoskeleton By similarity

  • Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor. Colocalized with MAPT/TAU in the distal part of the primary cortical neurons.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Peptidyl-prolyl cis-trans isomerase FKBP4PRO_0000391469Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 458457Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processedPRO_0000075319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternateBy similarity
Modified residuei2 – 21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partialBy similarity
Modified residuei143 – 1431Phosphothreonine; by CK2By similarity
Modified residuei220 – 2201PhosphotyrosineBy similarity
Modified residuei282 – 2821N6-acetyllysineBy similarity
Modified residuei436 – 4361PhosphothreonineBy similarity
Cross-linki441 – 441Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei452 – 4521PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by CK2 results in loss of HSP90 binding activity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP30416.
MaxQBiP30416.
PaxDbiP30416.
PeptideAtlasiP30416.
PRIDEiP30416.

2D gel databases

REPRODUCTION-2DPAGEP30416.

PTM databases

iPTMnetiP30416.
PhosphoSiteiP30416.
SwissPalmiP30416.

Expressioni

Gene expression databases

BgeeiP30416.
CleanExiMM_FKBP4.
ExpressionAtlasiP30416. baseline and differential.
GenevisibleiP30416. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Associates with HSP90AA1 and HSPA1A/HSPA1B in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU. Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the interaction is Ca2+ dependent. Interaction with S100A1 and S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90 interaction. Interacts with dynein; contributes to NR3C1 transport to the nucleus.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nr3c1P065373EBI-492746,EBI-492753

GO - Molecular functioni

  • glucocorticoid receptor binding Source: MGI
  • heat shock protein binding Source: MGI
  • phosphoprotein binding Source: MGI

Protein-protein interaction databases

BioGridi199685. 2 interactions.
IntActiP30416. 4 interactions.
MINTiMINT-1869690.
STRINGi10090.ENSMUSP00000032508.

Structurei

3D structure databases

ProteinModelPortaliP30416.
SMRiP30416. Positions 21-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 13889PPIase FKBP-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini167 – 25387PPIase FKBP-type 2PROSITE-ProRule annotationAdd
BLAST
Repeati270 – 30334TPR 1Add
BLAST
Repeati319 – 35234TPR 2Add
BLAST
Repeati353 – 38634TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 400134Interaction with tubulinBy similarityAdd
BLAST

Domaini

The PPIase activity is mainly due to the fisrt PPIase FKBP-type domain (1-138 AA).By similarity
The C-terminal region (AA 375-458) is required to prevent tubulin polymerization.By similarity
The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400.By similarity
The TPR repeats mediate mitochondrial localization.By similarity

Sequence similaritiesi

Contains 2 PPIase FKBP-type domains.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0543. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000256916.
HOVERGENiHBG051624.
InParanoidiP30416.
KOiK09571.
OMAiHPTDTEM.
PhylomeDBiP30416.
TreeFamiTF354214.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR031212. FKBP4.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PTHR10516:SF25. PTHR10516:SF25. 2 hits.
PfamiPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30416-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAEEMKAAE NGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETPMIG
60 70 80 90 100
DRVFVHYTGW LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG
110 120 130 140 150
EVCHITCKPE YAYGAAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI
160 170 180 190 200
IRRIRTRGEG YARPNDGAMV EVALEGYHKD RLFDQRELCF EVGEGESLDL
210 220 230 240 250
PCGLEEAIQR MEKGEHSIVY LKPSYAFGSV GKERFQIPPH AELRYEVRLK
260 270 280 290 300
SFEKAKESWE MSSAEKLEQS NIVKERGTAY FKEGKYKQAL LQYKKIVSWL
310 320 330 340 350
EYESSFSGEE MQKVHALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS
360 370 380 390 400
NNEKGLFRRG EAHLAVNDFD LARADFQKVL QLYPSNKAAK TQLAVCQQRT
410 420 430 440 450
RRQLAREKKL YANMFERLAE EEHKVKAEVA AGDHPTDAEM KGERNNVAEN

QSRVETEA
Length:458
Mass (Da):51,572
Last modified:January 23, 2007 - v5
Checksum:iCFB2ED49E9B6BA7A
GO

Sequence cautioni

The sequence CAA34914.1 differs from that shown. Reason: Frameshift at positions 16, 156, 204 and 265. Curated
The sequence CAA34914.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72MK → HE in CAC39452 (PubMed:8341706).Curated
Sequence conflicti156 – 1638TRGEGYAR → LGVKAMQG in CAC39452 (PubMed:8341706).Curated
Sequence conflicti203 – 24038GLEEA…QIPPH → AWRRPFSAWRKESIPSCTSN LAMLLAVWGRRGSRSHRT in CAC39452 (PubMed:8341706).CuratedAdd
BLAST
Sequence conflicti203 – 24038GLEEA…QIPPH → AWRRPFSAWRKESIPSCTSN LAMLLAVWGRRGSRSHRT in CAA34914 (PubMed:8341706).CuratedAdd
BLAST
Sequence conflicti265 – 2728EKLEQSNI → RSWSRATY in CAC39452 (PubMed:8341706).Curated
Sequence conflicti315 – 3151H → R in AAH03447 (PubMed:15489334).Curated
Sequence conflicti360 – 3601G → R in BAE35690 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70887 mRNA. Translation: CAA50231.1.
AK083912 mRNA. Translation: BAC39057.1.
AK160202 mRNA. Translation: BAE35690.1.
BC003447 mRNA. Translation: AAH03447.1.
X17069 mRNA. Translation: CAC39452.1.
X17068 mRNA. Translation: CAA34914.1. Sequence problems.
CCDSiCCDS20573.1.
PIRiJN0873.
RefSeqiNP_034349.1. NM_010219.3.
UniGeneiMm.12758.

Genome annotation databases

EnsembliENSMUST00000032508; ENSMUSP00000032508; ENSMUSG00000030357.
GeneIDi14228.
KEGGimmu:14228.
UCSCiuc009edr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70887 mRNA. Translation: CAA50231.1.
AK083912 mRNA. Translation: BAC39057.1.
AK160202 mRNA. Translation: BAE35690.1.
BC003447 mRNA. Translation: AAH03447.1.
X17069 mRNA. Translation: CAC39452.1.
X17068 mRNA. Translation: CAA34914.1. Sequence problems.
CCDSiCCDS20573.1.
PIRiJN0873.
RefSeqiNP_034349.1. NM_010219.3.
UniGeneiMm.12758.

3D structure databases

ProteinModelPortaliP30416.
SMRiP30416. Positions 21-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199685. 2 interactions.
IntActiP30416. 4 interactions.
MINTiMINT-1869690.
STRINGi10090.ENSMUSP00000032508.

PTM databases

iPTMnetiP30416.
PhosphoSiteiP30416.
SwissPalmiP30416.

2D gel databases

REPRODUCTION-2DPAGEP30416.

Proteomic databases

EPDiP30416.
MaxQBiP30416.
PaxDbiP30416.
PeptideAtlasiP30416.
PRIDEiP30416.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032508; ENSMUSP00000032508; ENSMUSG00000030357.
GeneIDi14228.
KEGGimmu:14228.
UCSCiuc009edr.1. mouse.

Organism-specific databases

CTDi2288.
MGIiMGI:95543. Fkbp4.

Phylogenomic databases

eggNOGiKOG0543. Eukaryota.
COG0545. LUCA.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000256916.
HOVERGENiHBG051624.
InParanoidiP30416.
KOiK09571.
OMAiHPTDTEM.
PhylomeDBiP30416.
TreeFamiTF354214.

Enzyme and pathway databases

ReactomeiR-MMU-3371568. Attenuation phase.

Miscellaneous databases

ChiTaRSiFkbp4. mouse.
PROiP30416.
SOURCEiSearch...

Gene expression databases

BgeeiP30416.
CleanExiMM_FKBP4.
ExpressionAtlasiP30416. baseline and differential.
GenevisibleiP30416. MM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR031212. FKBP4.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PTHR10516:SF25. PTHR10516:SF25. 2 hits.
PfamiPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a mouse cDNA encoding p59, an immunophilin that associates with the glucocorticoid receptor."
    Schmitt J., Stunnenberg H.G.
    Gene 132:267-271(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Spinal ganglion.
  3. "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: Lung tumor.
  4. "Overexpression, characterization, and purification of a recombinant mouse immunophilin FKBP-52 and identification of an associated phosphoprotein."
    Alnemri E.S., Fernandes-Alnemri T., Nelki D.S., Dudley K., Dubois G.C., Litwack G.
    Proc. Natl. Acad. Sci. U.S.A. 90:6839-6843(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-458, PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Testis.
  5. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
    Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
    J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND HSP90AA1.
  6. "Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus."
    Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.
    J. Biol. Chem. 276:14884-14889(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTRACELLULAR TRAFFICKING, IDENTIFICATION IN A COMPLEX WITH HSP90AA1 AND NR3C1, INTERACTION WITH DYNEIN.
  7. "A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins."
    Davies T.H., Ning Y.M., Sanchez E.R.
    J. Biol. Chem. 277:4597-4600(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTRACELLULAR TRAFFICKING, IDENTIFICATION IN A COMPLEX WITH HSP90AA1 AND NR3C1, SUBCELLULAR LOCATION, INTERACTION WITH DYNEIN.
  8. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 235-244.
    Tissue: Brain.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiFKBP4_MOUSE
AccessioniPrimary (citable) accession number: P30416
Secondary accession number(s): Q3TVC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 166 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.