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Protein

Ubiquitin thioesterase otulin

Gene

OTULIN

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

Functioni

Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Associates with the LUBAC complex via direct interaction with RNF31 and counteracts its action by cleaving linear polyubiquitin chains to substrates. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by counteracting activity of the LUBAC complex. Plays a key role in innate immune response: required to restrict linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation, probably to limit NOD2-dependent proinflammatory signaling.4 Publications

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).2 Publications

Kineticsi

Kcat is 6.3 sec(-1) with linear diubiquitin as substrate.

  1. KM=7.98 µM for linear diubiquitin1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei126 – 1261By similarity
    Active sitei129 – 1291Nucleophile
    Binding sitei314 – 3141Linear diubiquitin2 Publications
    Active sitei339 – 3391

    GO - Molecular functioni

    • cysteine-type peptidase activity Source: UniProtKB
    • ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    • canonical Wnt signaling pathway Source: UniProtKB
    • innate immune response Source: UniProtKB
    • negative regulation of inflammatory response Source: UniProtKB
    • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    • nucleotide-binding oligomerization domain containing 2 signaling pathway Source: UniProtKB
    • protein linear deubiquitination Source: UniProtKB
    • sprouting angiogenesis Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Angiogenesis, Immunity, Innate immunity, Ubl conjugation pathway, Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin thioesterase otulin (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme otulin
    OTU domain-containing deubiquitinase with linear linkage specificity
    Ubiquitin thioesterase Gumby
    Gene namesi
    Name:OTULIN
    Synonyms:FAM105B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:25118. OTULIN.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • LUBAC complex Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911Y → F: Results in strong reduction of kcat while not affecting KM. 1 Publication
    Mutagenesisi96 – 961W → A: Decreased activity toward linear ubiquitin. 2 Publications
    Mutagenesisi100 – 1023TQK → AAA: Decreased activity toward linear ubiquitin. 1 Publication
    Mutagenesisi129 – 1291C → A: Abolishes deubiquitinase activity. 3 Publications
    Mutagenesisi259 – 2591L → E: Decreased affinity for linear diubiquitin. 1 Publication
    Mutagenesisi314 – 3141E → R: Decreased affinity for linear diubiquitin. 1 Publication
    Mutagenesisi336 – 3361D → A: Stabilizes H-339 in the active conformation, generating a more reactive enzyme. 1 Publication
    Mutagenesisi339 – 3391H → A: Impaired deubiquitinase activity. 1 Publication
    Mutagenesisi341 – 3411N → A: Abolishes deubiquitinase activity. 1 Publication
    Mutagenesisi341 – 3411N → D: Stabilizes H-339 in the active conformation, generating a more reactive enzyme. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671789.

    Polymorphism and mutation databases

    BioMutaiFAM105B.
    DMDMi118572305.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Ubiquitin thioesterase otulinPRO_0000261637Add
    BLAST

    Post-translational modificationi

    Ubiquitinated.1 Publication
    Acetylated.1 Publication
    Phosphorylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96BN8.
    PaxDbiQ96BN8.
    PeptideAtlasiQ96BN8.
    PRIDEiQ96BN8.

    PTM databases

    PhosphoSiteiQ96BN8.

    Expressioni

    Gene expression databases

    BgeeiQ96BN8.
    CleanExiHS_FAM105B.
    ExpressionAtlasiQ96BN8. baseline and differential.
    GenevisibleiQ96BN8. HS.

    Organism-specific databases

    HPAiHPA051074.

    Interactioni

    Subunit structurei

    Interacts with RNF31; the interaction is direct.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAZAP2Q150383EBI-750730,EBI-724310
    FAM168AQ925673EBI-750730,EBI-7957930

    Protein-protein interaction databases

    BioGridi124684. 15 interactions.
    IntActiQ96BN8. 4 interactions.
    MINTiMINT-7944191.
    STRINGi9606.ENSP00000284274.

    Structurei

    Secondary structure

    1
    352
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi55 – 573Combined sources
    Helixi59 – 635Combined sources
    Helixi88 – 958Combined sources
    Helixi101 – 11414Combined sources
    Beta strandi118 – 1214Combined sources
    Helixi129 – 14012Combined sources
    Helixi147 – 1504Combined sources
    Helixi153 – 16412Combined sources
    Helixi166 – 1705Combined sources
    Helixi184 – 20421Combined sources
    Helixi208 – 21811Combined sources
    Beta strandi220 – 2223Combined sources
    Helixi223 – 24826Combined sources
    Helixi255 – 2628Combined sources
    Beta strandi263 – 2653Combined sources
    Helixi269 – 2757Combined sources
    Helixi277 – 2793Combined sources
    Turni280 – 2823Combined sources
    Helixi288 – 29811Combined sources
    Beta strandi301 – 3066Combined sources
    Helixi307 – 3093Combined sources
    Helixi313 – 3153Combined sources
    Beta strandi316 – 3227Combined sources
    Beta strandi329 – 3368Combined sources
    Beta strandi339 – 3446Combined sources
    Helixi346 – 3483Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZNVX-ray1.30A80-352[»]
    3ZNXX-ray1.35A80-352[»]
    3ZNZX-ray1.90A80-352[»]
    4KSJX-ray1.60A79-352[»]
    4KSKX-ray2.40A/B55-352[»]
    4KSLX-ray2.83A/B/E/G/I/K/M/O/Q/S/U/W79-352[»]
    4OYKX-ray2.00C/D49-67[»]
    4P0BX-ray2.70B/D52-61[»]
    ProteinModelPortaliQ96BN8.
    SMRiQ96BN8. Positions 80-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini118 – 346229OTUAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni95 – 962Linear diubiquitin binding
    Regioni124 – 1263Linear diubiquitin binding
    Regioni255 – 2595Linear diubiquitin binding
    Regioni283 – 2897Linear diubiquitin binding
    Regioni336 – 3383Linear diubiquitin binding

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili49 – 7325Sequence AnalysisAdd
    BLAST

    Domaini

    The specificity for linear polyubiquitin is given by the 'Glu-16' residue in ubiquitin chain.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C65 family. Otulin subfamily.Curated
    Contains 1 OTU domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG47891.
    GeneTreeiENSGT00390000009802.
    HOGENOMiHOG000294085.
    HOVERGENiHBG104927.
    InParanoidiQ96BN8.
    KOiK18343.
    OMAiKYNTEEF.
    PhylomeDBiQ96BN8.
    TreeFamiTF328709.

    Family and domain databases

    InterProiIPR023235. FAM105.
    IPR023237. FAM105B.
    [Graphical view]
    PRINTSiPR02055. PROTEINF105.
    PR02057. PROTEINF105B.

    Sequencei

    Sequence statusi: Complete.

    Q96BN8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSRGTMPQPE AWPGASCAET PAREAAATAR DGGKAAASGQ PRPEMQCPAE
    60 70 80 90 100
    HEEDMYRAAD EIEKEKELLI HERGASEPRL SVAPEMDIMD YCKKEWRGNT
    110 120 130 140 150
    QKATCMKMGY EEVSQKFTSI RRVRGDNYCA LRATLFQAMS QAVGLPPWLQ
    160 170 180 190 200
    DPELMLLPEK LISKYNWIKQ WKLGLKFDGK NEDLVDKIKE SLTLLRKKWA
    210 220 230 240 250
    GLAEMRTAEA RQIACDELFT NEAEEYSLYE AVKFLMLNRA IELYNDKEKG
    260 270 280 290 300
    KEVPFFSVLL FARDTSNDPG QLLRNHLNQV GHTGGLEQVE MFLLAYAVRH
    310 320 330 340 350
    TIQVYRLSKY NTEEFITVYP TDPPKDWPVV TLIAEDDRHY NIPVRVCEET

    SL
    Length:352
    Mass (Da):40,263
    Last modified:November 28, 2006 - v3
    Checksum:i65071FF7B427C2FA
    GO

    Sequence cautioni

    The sequence AAH07706.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAH15392.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC03828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti211 – 2111R → G in BAC03828 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551M → L.
    Corresponds to variant rs11953822 [ dbSNP | Ensembl ].
    VAR_053819
    Natural varianti227 – 2271S → N.
    Corresponds to variant rs9312870 [ dbSNP | Ensembl ].
    VAR_029469
    Natural varianti311 – 3111N → S.
    Corresponds to variant rs9312870 [ dbSNP | Ensembl ].
    VAR_053820

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC010491 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08038.1.
    CH471102 Genomic DNA. Translation: EAX08039.1.
    BC007706 mRNA. Translation: AAH07706.3. Different initiation.
    BC015392 mRNA. Translation: AAH15392.2. Different initiation.
    AK092203 mRNA. Translation: BAC03828.1. Different initiation.
    CCDSiCCDS43302.1.
    RefSeqiNP_612357.4. NM_138348.4.
    UniGeneiHs.406335.

    Genome annotation databases

    EnsembliENST00000284274; ENSP00000284274; ENSG00000154124.
    GeneIDi90268.
    KEGGihsa:90268.
    UCSCiuc003jfk.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC010491 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08038.1.
    CH471102 Genomic DNA. Translation: EAX08039.1.
    BC007706 mRNA. Translation: AAH07706.3. Different initiation.
    BC015392 mRNA. Translation: AAH15392.2. Different initiation.
    AK092203 mRNA. Translation: BAC03828.1. Different initiation.
    CCDSiCCDS43302.1.
    RefSeqiNP_612357.4. NM_138348.4.
    UniGeneiHs.406335.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZNVX-ray1.30A80-352[»]
    3ZNXX-ray1.35A80-352[»]
    3ZNZX-ray1.90A80-352[»]
    4KSJX-ray1.60A79-352[»]
    4KSKX-ray2.40A/B55-352[»]
    4KSLX-ray2.83A/B/E/G/I/K/M/O/Q/S/U/W79-352[»]
    4OYKX-ray2.00C/D49-67[»]
    4P0BX-ray2.70B/D52-61[»]
    ProteinModelPortaliQ96BN8.
    SMRiQ96BN8. Positions 80-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi124684. 15 interactions.
    IntActiQ96BN8. 4 interactions.
    MINTiMINT-7944191.
    STRINGi9606.ENSP00000284274.

    PTM databases

    PhosphoSiteiQ96BN8.

    Polymorphism and mutation databases

    BioMutaiFAM105B.
    DMDMi118572305.

    Proteomic databases

    MaxQBiQ96BN8.
    PaxDbiQ96BN8.
    PeptideAtlasiQ96BN8.
    PRIDEiQ96BN8.

    Protocols and materials databases

    DNASUi90268.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000284274; ENSP00000284274; ENSG00000154124.
    GeneIDi90268.
    KEGGihsa:90268.
    UCSCiuc003jfk.3. human.

    Organism-specific databases

    CTDi90268.
    GeneCardsiGC05P014667.
    HGNCiHGNC:25118. OTULIN.
    HPAiHPA051074.
    neXtProtiNX_Q96BN8.
    PharmGKBiPA142671789.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG47891.
    GeneTreeiENSGT00390000009802.
    HOGENOMiHOG000294085.
    HOVERGENiHBG104927.
    InParanoidiQ96BN8.
    KOiK18343.
    OMAiKYNTEEF.
    PhylomeDBiQ96BN8.
    TreeFamiTF328709.

    Miscellaneous databases

    GenomeRNAii90268.
    NextBioi76620.
    PROiQ96BN8.

    Gene expression databases

    BgeeiQ96BN8.
    CleanExiHS_FAM105B.
    ExpressionAtlasiQ96BN8. baseline and differential.
    GenevisibleiQ96BN8. HS.

    Family and domain databases

    InterProiIPR023235. FAM105.
    IPR023237. FAM105B.
    [Graphical view]
    PRINTSiPR02055. PROTEINF105.
    PR02057. PROTEINF105B.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Ovary and Prostate.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-298.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
      Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
      Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    7. Cited for: FUNCTION, MUTAGENESIS OF TRP-96 AND CYS-129.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF MUTANT ASP-336, X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH LINEAR DIUBIQUITIN, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, ACETYLATION, MUTAGENESIS OF TYR-91; TRP-96; 100-THR--LYS-102; CYS-129; LEU-259; GLU-314; ASP-336; HIS-339 AND ASN-341.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 79-352 OF MUTANT CYS-129, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 79-352 OF MUTANT CYS-129 IN COMPLEX WITH LINEAR DIUBIQUITIN, FUNCTION, INTERACTION WITH RNF31 AND DVL2, MUTAGENESIS OF CYS-129.

    Entry informationi

    Entry nameiOTUL_HUMAN
    AccessioniPrimary (citable) accession number: Q96BN8
    Secondary accession number(s): D3DTD3, Q8NAS0, Q96IA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: June 24, 2015
    This is version 83 of the entry and version 3 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 5
      Human chromosome 5: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. 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.