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Protein

Serine/threonine-protein phosphatase 5

Gene

Ppp5c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2.5 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Cofactori

Mg2+2 Publications, Mn2+2 PublicationsNote: Binds 2 magnesium or manganese ions per subunit.2 Publications

Enzyme regulationi

Autoinhibited. In the autoinhibited state, the TPR domain interacts with the catalytic region and prevents substrate access to the catalytic pocket. Allosterically activated by various polyunsaturated fatty acids, free long-chain fatty-acids and long-chain fatty acyl-CoA esters, arachidonic acid being the most effective activator. HSP90A and probably RAC1, GNA12 and GNA13 can also release the autoinhibition by the TPR repeat. Activation by RAC1, GNA12 and GNA13 is synergistic with the one produced by fatty acids binding. Inhibited by okadaic acid.3 Publications

Kineticsi

  1. KM=12.1 µM for MAPT/TAU (at pH 7.4 and 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi242 – 2421Magnesium or manganese 11 Publication
    Metal bindingi244 – 2441Magnesium or manganese 11 Publication
    Binding sitei244 – 2441SubstrateBy similarity
    Metal bindingi271 – 2711Magnesium or manganese 11 Publication
    Metal bindingi271 – 2711Magnesium or manganese 21 Publication
    Binding sitei275 – 2751SubstrateBy similarity
    Metal bindingi303 – 3031Magnesium or manganese 21 Publication
    Active sitei304 – 3041Proton donor/acceptorBy similarity
    Metal bindingi352 – 3521Magnesium or manganese 21 Publication
    Binding sitei400 – 4001SubstrateBy similarity
    Metal bindingi427 – 4271Magnesium or manganese 21 Publication
    Binding sitei427 – 4271SubstrateBy similarity

    GO - Molecular functioni

    • G-protein alpha-subunit binding Source: RGD
    • heat shock protein binding Source: RGD
    • metal ion binding Source: UniProtKB-KW
    • microtubule binding Source: RGD
    • phosphoprotein phosphatase activity Source: UniProtKB
    • RNA binding Source: Ensembl
    • signal transducer activity Source: Ensembl

    GO - Biological processi

    • cellular response to cadmium ion Source: RGD
    • cellular response to hydrogen peroxide Source: RGD
    • histone dephosphorylation Source: RGD
    • negative regulation of cell death Source: RGD
    • negative regulation of neuron death Source: RGD
    • negative regulation of protein phosphorylation Source: RGD
    • positive regulation of glucocorticoid receptor signaling pathway Source: RGD
    • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    • protein dephosphorylation Source: RGD
    • protein heterooligomerization Source: RGD
    • protein oligomerization Source: RGD
    • response to lead ion Source: RGD
    • response to morphine Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.16. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 5 (EC:3.1.3.16)
    Short name:
    PP5
    Alternative name(s):
    Protein phosphatase T
    Short name:
    PPT
    Gene namesi
    Name:Ppp5c
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi68415. Ppp5c.

    Subcellular locationi

    • Nucleus 1 Publication
    • Cytoplasm 1 Publication
    • Membrane By similarity

    • Note: Predominantly nuclear. But also present in the cytoplasm.

    GO - Cellular componenti

    • cell periphery Source: RGD
    • cytoplasm Source: RGD
    • cytosol Source: RGD
    • membrane Source: UniProtKB-SubCell
    • neuronal cell body Source: RGD
    • neuron projection Source: RGD
    • nucleoplasm Source: Ensembl
    • nucleus Source: RGD
    • perikaryon Source: RGD
    • proximal dendrite Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291E → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi32 – 321K → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi40 – 401K → A: Slightly reduces activation by arachidonic acid.
    Mutagenesisi56 – 561E → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi63 – 631I → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi74 – 741R → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi76 – 761E → A: Increases basal phosphatase activity. 1 Publication
    Mutagenesisi77 – 771C → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi80 – 801Y → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi93 – 931K → E: Loss of inhibition of KCNH2 channel stimulation. 1 Publication
    Mutagenesisi97 – 971K → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi101 – 1011R → A: No effect on phosphatase activity. 1 Publication
    Mutagenesisi126 – 1261K → A: Loss of inhibition of KCNH2 channel stimulation. 1 Publication
    Mutagenesisi451 – 4511Y → A: Insensitive to okadaic acid. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 499498Serine/threonine-protein phosphatase 5PRO_0000058897Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Post-translational modificationi

    Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP53042.

    Expressioni

    Tissue specificityi

    Predominantly found in brain and, in lower levels, in testis, but was nearly undetectable in spleen, lung, skeletal muscle, kidney and liver.1 Publication

    Gene expression databases

    ExpressionAtlasiP53042. baseline.
    GenevisibleiP53042. RN.

    Interactioni

    Subunit structurei

    Part of a complex with HSP90/HSP90AA1 and steroid receptors. Interacts with CDC16, CDC27. Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the phosphatase activity on MAP3K5. Interacts (via TPR repeats) with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the interaction is direct and activates the phosphatase activity. Dissociates from HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid. Interacts with ATM and ATR; both interactions are induced by DNA damage and enhance ATM and ATR kinase activity. Interacts with RAD17; reduced by DNA damage. Interacts with nuclear receptors such as NR3C1/GCR and PPARG (activated by agonist); regulates their transactivation activities. Interacts (via TPR repeats) with S100 proteins S100A1, S100A2, S100A6, S100B and S100P; the interactions are calcium-dependent, strongly activate PPP5C phosphatase activity and compete with HSP90AA1 and MAP3K5 interactions. Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3 phosphorylation and protein levels. Interacts (via TPR repeats) with CRY1 and CRY2; the interaction with CRY2 downregulates the phosphatase activity on CSNK1E. Interacts (via TPR repeats) with the active form of RAC1, GNA12 or GNA13; these interactions activate the phosphatase activity and translocate PPP5C to the cell membrane.4 Publications

    Protein-protein interaction databases

    DIPiDIP-61212N.
    STRINGi10116.ENSRNOP00000023078.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 4017Combined sources
    Helixi44 – 5714Combined sources
    Helixi62 – 7413Combined sources
    Helixi78 – 9114Combined sources
    Helixi96 – 10813Combined sources
    Helixi112 – 12514Combined sources
    Helixi130 – 14819Combined sources
    Helixi161 – 1644Combined sources
    Helixi167 – 1693Combined sources
    Helixi188 – 19912Combined sources
    Helixi206 – 22116Combined sources
    Beta strandi225 – 2295Combined sources
    Beta strandi236 – 2405Combined sources
    Helixi247 – 25711Combined sources
    Beta strandi262 – 2643Combined sources
    Beta strandi266 – 2705Combined sources
    Beta strandi273 – 2764Combined sources
    Helixi279 – 29214Combined sources
    Turni294 – 2963Combined sources
    Beta strandi297 – 3004Combined sources
    Helixi307 – 3137Combined sources
    Helixi315 – 3228Combined sources
    Helixi325 – 33511Combined sources
    Beta strandi340 – 3445Combined sources
    Turni345 – 3473Combined sources
    Beta strandi348 – 3536Combined sources
    Beta strandi357 – 3593Combined sources
    Helixi363 – 3675Combined sources
    Beta strandi372 – 3743Combined sources
    Beta strandi377 – 3793Combined sources
    Helixi380 – 3867Combined sources
    Beta strandi391 – 3977Combined sources
    Beta strandi401 – 4066Combined sources
    Helixi408 – 41811Combined sources
    Beta strandi422 – 4254Combined sources
    Beta strandi433 – 4375Combined sources
    Helixi438 – 4403Combined sources
    Beta strandi442 – 4454Combined sources
    Helixi451 – 4533Combined sources
    Beta strandi459 – 4657Combined sources
    Beta strandi468 – 4769Combined sources
    Turni486 – 4894Combined sources
    Helixi492 – 4943Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JA7X-ray2.00A16-499[»]
    4JA9X-ray2.30A16-499[»]
    ProteinModelPortaliP53042.
    SMRiP53042. Positions 23-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati28 – 6134TPR 1Add
    BLAST
    Repeati62 – 9534TPR 2Add
    BLAST
    Repeati96 – 12934TPR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 499300CatalyticAdd
    BLAST
    Regioni303 – 3042Substrate bindingBy similarity
    Regioni495 – 4995Required for autoinhibition

    Sequence similaritiesi

    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000063173.
    HOGENOMiHOG000172698.
    HOVERGENiHBG000216.
    InParanoidiP53042.
    KOiK04460.
    OMAiMNRVYGF.
    OrthoDBiEOG7V49Z3.
    PhylomeDBiP53042.
    TreeFamiTF105562.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR013235. PPP_dom.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR011236. Ser/Thr_PPase_5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical_dom.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF12. PTHR11668:SF12. 1 hit.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P53042-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAMAEGERTE CAEPPRDEPP AEGTLKRAEE LKTQANDYFK AKDYENAIKF
    60 70 80 90 100
    YSQAIELNPS NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY
    110 120 130 140 150
    RRAASNMALG KFRAALRDYE TVVKVKPNDK DAKMKYQECS KIVKQKAFER
    160 170 180 190 200
    AIAGDEHRRS VVDSLDIESM TIEDEYSGPK LEDGKVTITF MKDLMQWYKD
    210 220 230 240 250
    QKKLHRKCAY QILVQVKEVL CKLSTLVETT LKETEKITVC GDTHGQFYDL
    260 270 280 290 300
    LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
    310 320 330 340 350
    RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI
    360 370 380 390 400
    MHGGLFSEDG VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSVSKR
    410 420 430 440 450
    GVSCQFGPDV TKAFLEENQL DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN
    460 470 480 490
    YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP HPNVKPMAYA NTLLQLGMM
    Length:499
    Mass (Da):56,917
    Last modified:October 1, 1996 - v1
    Checksum:i720A7FB7AFC701D2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X77237 mRNA. Translation: CAA54454.1.
    PIRiA55346.
    RefSeqiNP_113917.1. NM_031729.1.
    UniGeneiRn.6107.

    Genome annotation databases

    EnsembliENSRNOT00000023078; ENSRNOP00000023078; ENSRNOG00000016907.
    GeneIDi65179.
    KEGGirno:65179.
    UCSCiRGD:68415. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X77237 mRNA. Translation: CAA54454.1.
    PIRiA55346.
    RefSeqiNP_113917.1. NM_031729.1.
    UniGeneiRn.6107.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4JA7X-ray2.00A16-499[»]
    4JA9X-ray2.30A16-499[»]
    ProteinModelPortaliP53042.
    SMRiP53042. Positions 23-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-61212N.
    STRINGi10116.ENSRNOP00000023078.

    Proteomic databases

    PRIDEiP53042.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000023078; ENSRNOP00000023078; ENSRNOG00000016907.
    GeneIDi65179.
    KEGGirno:65179.
    UCSCiRGD:68415. rat.

    Organism-specific databases

    CTDi5536.
    RGDi68415. Ppp5c.

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000063173.
    HOGENOMiHOG000172698.
    HOVERGENiHBG000216.
    InParanoidiP53042.
    KOiK04460.
    OMAiMNRVYGF.
    OrthoDBiEOG7V49Z3.
    PhylomeDBiP53042.
    TreeFamiTF105562.

    Enzyme and pathway databases

    BRENDAi3.1.3.16. 5301.

    Miscellaneous databases

    NextBioi614076.
    PROiP53042.

    Gene expression databases

    ExpressionAtlasiP53042. baseline.
    GenevisibleiP53042. RN.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR013235. PPP_dom.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    IPR011236. Ser/Thr_PPase_5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical_dom.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR11668:SF12. PTHR11668:SF12. 1 hit.
    PfamiPF00149. Metallophos. 1 hit.
    PF08321. PPP5. 1 hit.
    PF00515. TPR_1. 2 hits.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    SM00028. TPR. 3 hits.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
      Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
      J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Testis.
    2. "Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation."
      Kang H., Sayner S.L., Gross K.L., Russell L.C., Chinkers M.
      Biochemistry 40:10485-10490(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PHOSPHATASE, ENZYME REGULATION, MUTAGENESIS OF GLU-29; LYS-32; GLU-56; ILE-63; ARG-74; GLU-76; CYS-77; TYR-80; LYS-97 AND ARG-101.
    3. "Identification of potential physiological activators of protein phosphatase 5."
      Ramsey A.J., Chinkers M.
      Biochemistry 41:5625-5632(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, ENZYME REGULATION, CATALYTIC ACTIVITY.
    4. "Galpha(12) and Galpha(13) interact with Ser/Thr protein phosphatase type 5 and stimulate its phosphatase activity."
      Yamaguchi Y., Katoh H., Mori K., Negishi M.
      Curr. Biol. 12:1353-1358(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PHOSPHATASE, INTERACTION WITH GNA12 AND GNA13, SUBCELLULAR LOCATION.
    5. "Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer's disease."
      Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.
      J. Biol. Chem. 280:1790-1796(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATING MAPT, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    6. "Regulation of the Raf-MEK-ERK pathway by protein phosphatase 5."
      von Kriegsheim A., Pitt A., Grindlay G.J., Kolch W., Dhillon A.S.
      Nat. Cell Biol. 8:1011-1016(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAPK SIGNALING.
    7. Cited for: FUNCTION IN RAC1 SIGNALING, ENZYME REGULATION, INTERACTION WITH RAC1, MUTAGENESIS OF LYS-93; LYS-126 AND TYR-451.
    8. "Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5."
      Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRY1 AND CRY2.
    9. "Selective targeting of the autoinhibition of PP5 reduces tau phosphorylation in mouse."
      Haslbeck V., Helmuth M., Alte F., Popowicz G., Schmidt W., Weiwad M., Fischer G., Gemmecker G., Sattler M., Striggow F., Groll M., Richter K.
      Submitted (FEB-2013) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 16-499 IN COMPLEX WITH MAGNESIUM, COFACTOR.

    Entry informationi

    Entry nameiPPP5_RAT
    AccessioniPrimary (citable) accession number: P53042
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: July 22, 2015
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.