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Protein

Phosphomannomutase 1

Gene

PMM1

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

Functioni

Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.1 Publication

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Cofactori

Mg2+1 Publication

Enzyme regulationi

IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity.By similarity

Kineticsi

  1. KM=54 µM for alpha-D-mannose 1-phosphate1 Publication
  2. KM=7.5 µM for alpha-D-glucose 1-phosphate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei19 – 191Nucleophile1 Publication
    Metal bindingi19 – 191Magnesium
    Active sitei21 – 211Proton donor/acceptorSequence Analysis
    Metal bindingi21 – 211Magnesium; via carbonyl oxygen
    Binding sitei28 – 281Substrate
    Binding sitei132 – 1321Substrate
    Binding sitei143 – 1431Substrate
    Binding sitei150 – 1501Substrate
    Binding sitei186 – 1861Substrate; via amide nitrogen
    Binding sitei188 – 1881Substrate
    Binding sitei190 – 1901Substrate
    Metal bindingi218 – 2181Magnesium

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • phosphomannomutase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi5.4.2.8. 2681.
    ReactomeiREACT_22423. Synthesis of GDP-mannose.
    UniPathwayiUPA00126; UER00424.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphomannomutase 1 (EC:5.4.2.8)
    Short name:
    PMM 1
    Alternative name(s):
    PMMH-22
    Gene namesi
    Name:PMM1
    Synonyms:PMMH22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9114. PMM1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33440.

    Polymorphism and mutation databases

    BioMutaiPMM1.
    DMDMi2499519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 262261Phosphomannomutase 1PRO_0000199692Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei158 – 1581N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ92871.
    PaxDbiQ92871.
    PRIDEiQ92871.

    PTM databases

    DEPODiQ92871.
    PhosphoSiteiQ92871.

    Expressioni

    Tissue specificityi

    Strong expression in liver, heart, brain, and pancreas; lower expression in skeletal muscle.

    Gene expression databases

    BgeeiQ92871.
    CleanExiHS_PMM1.
    ExpressionAtlasiQ92871. baseline and differential.
    GenevestigatoriQ92871.

    Organism-specific databases

    HPAiHPA030712.
    HPA056509.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAB6AP203404EBI-746784,EBI-1052826

    Protein-protein interaction databases

    BioGridi111385. 11 interactions.
    IntActiQ92871. 4 interactions.
    MINTiMINT-1482037.
    STRINGi9606.ENSP00000216259.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 218Combined sources
    Turni22 – 243Combined sources
    Helixi33 – 4210Combined sources
    Turni43 – 453Combined sources
    Beta strandi46 – 516Combined sources
    Helixi56 – 638Combined sources
    Turni66 – 683Combined sources
    Helixi69 – 724Combined sources
    Beta strandi74 – 785Combined sources
    Helixi79 – 813Combined sources
    Beta strandi83 – 864Combined sources
    Beta strandi89 – 913Combined sources
    Helixi96 – 1005Combined sources
    Helixi102 – 11716Combined sources
    Beta strandi128 – 1314Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi147 – 16014Combined sources
    Helixi162 – 17312Combined sources
    Turni174 – 1763Combined sources
    Beta strandi179 – 1824Combined sources
    Beta strandi185 – 1873Combined sources
    Beta strandi189 – 1935Combined sources
    Helixi198 – 2014Combined sources
    Helixi202 – 2054Combined sources
    Turni206 – 2094Combined sources
    Beta strandi211 – 2188Combined sources
    Helixi227 – 2315Combined sources
    Beta strandi235 – 2395Combined sources
    Helixi243 – 25412Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FUCX-ray2.10A1-262[»]
    2FUEX-ray1.75A1-262[»]
    ProteinModelPortaliQ92871.
    SMRiQ92871. Positions 13-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92871.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic PMM family.Curated

    Phylogenomic databases

    eggNOGiCOG0561.
    GeneTreeiENSGT00390000002918.
    HOGENOMiHOG000181843.
    HOVERGENiHBG009971.
    InParanoidiQ92871.
    KOiK17497.
    OMAiNDYEIYD.
    OrthoDBiEOG773XH0.
    PhylomeDBiQ92871.
    TreeFamiTF300874.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view]
    PANTHERiPTHR10466. PTHR10466. 1 hit.
    PfamiPF03332. PMM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q92871-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV
    60 70 80 90 100
    VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL
    110 120 130 140 150
    GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER
    160 170 180 190 200
    IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY
    210 220 230 240 250
    CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC
    260
    REIFFPETAH EA
    Length:262
    Mass (Da):29,747
    Last modified:November 1, 1997 - v2
    Checksum:i1FBA7BFC9C3BB0BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111K → R in AAC51117 (PubMed:9070917).Curated
    Sequence conflicti169 – 1691A → D in AAC51117 (PubMed:9070917).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U62526 mRNA. Translation: AAC51117.1.
    D87810 mRNA. Translation: BAA13460.1.
    U86070 mRNA. Translation: AAC00023.1.
    CR456544 mRNA. Translation: CAG30430.1.
    AK289368 mRNA. Translation: BAF82057.1.
    AK316580 mRNA. Translation: BAG38168.1.
    AL023553 Genomic DNA. Translation: CAB46025.1.
    CH471095 Genomic DNA. Translation: EAW60443.1.
    BC010855 mRNA. Translation: AAH10855.1.
    BC016818 mRNA. Translation: AAH16818.1.
    CCDSiCCDS14020.1.
    RefSeqiNP_002667.2. NM_002676.2.
    UniGeneiHs.75835.

    Genome annotation databases

    EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
    GeneIDi5372.
    KEGGihsa:5372.
    UCSCiuc003bal.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U62526 mRNA. Translation: AAC51117.1.
    D87810 mRNA. Translation: BAA13460.1.
    U86070 mRNA. Translation: AAC00023.1.
    CR456544 mRNA. Translation: CAG30430.1.
    AK289368 mRNA. Translation: BAF82057.1.
    AK316580 mRNA. Translation: BAG38168.1.
    AL023553 Genomic DNA. Translation: CAB46025.1.
    CH471095 Genomic DNA. Translation: EAW60443.1.
    BC010855 mRNA. Translation: AAH10855.1.
    BC016818 mRNA. Translation: AAH16818.1.
    CCDSiCCDS14020.1.
    RefSeqiNP_002667.2. NM_002676.2.
    UniGeneiHs.75835.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FUCX-ray2.10A1-262[»]
    2FUEX-ray1.75A1-262[»]
    ProteinModelPortaliQ92871.
    SMRiQ92871. Positions 13-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111385. 11 interactions.
    IntActiQ92871. 4 interactions.
    MINTiMINT-1482037.
    STRINGi9606.ENSP00000216259.

    PTM databases

    DEPODiQ92871.
    PhosphoSiteiQ92871.

    Polymorphism and mutation databases

    BioMutaiPMM1.
    DMDMi2499519.

    Proteomic databases

    MaxQBiQ92871.
    PaxDbiQ92871.
    PRIDEiQ92871.

    Protocols and materials databases

    DNASUi5372.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000216259; ENSP00000216259; ENSG00000100417.
    GeneIDi5372.
    KEGGihsa:5372.
    UCSCiuc003bal.2. human.

    Organism-specific databases

    CTDi5372.
    GeneCardsiGC22M041972.
    HGNCiHGNC:9114. PMM1.
    HPAiHPA030712.
    HPA056509.
    MIMi601786. gene.
    neXtProtiNX_Q92871.
    PharmGKBiPA33440.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0561.
    GeneTreeiENSGT00390000002918.
    HOGENOMiHOG000181843.
    HOVERGENiHBG009971.
    InParanoidiQ92871.
    KOiK17497.
    OMAiNDYEIYD.
    OrthoDBiEOG773XH0.
    PhylomeDBiQ92871.
    TreeFamiTF300874.

    Enzyme and pathway databases

    UniPathwayiUPA00126; UER00424.
    BRENDAi5.4.2.8. 2681.
    ReactomeiREACT_22423. Synthesis of GDP-mannose.

    Miscellaneous databases

    EvolutionaryTraceiQ92871.
    GeneWikiiPMM1.
    GenomeRNAii5372.
    NextBioi20842.
    PROiQ92871.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ92871.
    CleanExiHS_PMM1.
    ExpressionAtlasiQ92871. baseline and differential.
    GenevestigatoriQ92871.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view]
    PANTHERiPTHR10466. PTHR10466. 1 hit.
    PfamiPF03332. PMM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13."
      Matthijs G., Schollen E., Pirard M., Budarf M.L., van Schaftingen E., Cassiman J.-J.
      Genomics 40:41-47(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13."
      Wada Y., Sakamoto M.
      Genomics 39:416-417(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Hansen S.H., Frank S.R., Casanova J.E.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
      Tissue: Skeletal muscle.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Brain and Pancreas.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a."
      Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N.
      J. Biol. Chem. 281:14918-14926(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND MANNOSE 1-PHOSPHATE, FUNCTION, ACTIVE SITE, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiPMM1_HUMAN
    AccessioniPrimary (citable) accession number: Q92871
    Secondary accession number(s): A8K003, Q92586
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: April 29, 2015
    This is version 142 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 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.