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Q9UKG1

- DP13A_HUMAN

UniProt

Q9UKG1 - DP13A_HUMAN

Protein

DCC-interacting protein 13-alpha

Gene

APPL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction.2 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB
    3. protein kinase B binding Source: BHF-UCL

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cell cycle Source: UniProtKB-KW
    3. cell proliferation Source: UniProtKB
    4. insulin receptor signaling pathway Source: BHF-UCL
    5. positive regulation of apoptotic process Source: Reactome
    6. regulation of apoptotic process Source: Reactome
    7. regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
    8. regulation of glucose import Source: BHF-UCL
    9. signal transduction Source: UniProtKB

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    ReactomeiREACT_22128. Role of DCC in regulating apoptosis.
    SignaLinkiQ9UKG1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DCC-interacting protein 13-alpha
    Short name:
    Dip13-alpha
    Alternative name(s):
    Adapter protein containing PH domain, PTB domain and leucine zipper motif 1
    Gene namesi
    Name:APPL1
    Synonyms:APPLImported, DIP13A, KIAA1428Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:24035. APPL1.

    Subcellular locationi

    Early endosome membrane; Peripheral membrane protein. Nucleus
    Note: Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: BHF-UCL
    3. early endosome membrane Source: UniProtKB-SubCell
    4. endosome membrane Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. nucleus Source: UniProtKB
    7. vesicle membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162376755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 709709DCC-interacting protein 13-alphaPRO_0000079985Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei399 – 3991Phosphothreonine1 Publication
    Modified residuei401 – 4011Phosphoserine1 Publication
    Modified residuei410 – 4101Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Phosophorylation at Ser-410 by PKA severely impairs binding to OCRL.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKG1.
    PaxDbiQ9UKG1.
    PeptideAtlasiQ9UKG1.
    PRIDEiQ9UKG1.

    PTM databases

    PhosphoSiteiQ9UKG1.

    Expressioni

    Tissue specificityi

    High levels in heart, ovary, pancreas and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9UKG1.
    BgeeiQ9UKG1.
    CleanExiHS_APPL1.
    GenevestigatoriQ9UKG1.

    Organism-specific databases

    HPAiHPA011138.

    Interactioni

    Subunit structurei

    Binds RAB5A/Rab5 through an N-terminal domain. This interaction is essential for its recruitment to endosomal membranes as well as its role in cell proliferation. Binds DCC and the catalytic domain of the inactive form of AKT2 through its PID domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex. Interacts with OCRL and INPP5B.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-741243,EBI-741243
    ACTN2P356092EBI-741243,EBI-77797
    ADIPOR1Q96A546EBI-741243,EBI-1632076
    Adipor1Q91VH13EBI-741243,EBI-992398From a different organism.
    ADIPOR2Q86V243EBI-741243,EBI-1769445
    DSTQ030013EBI-741243,EBI-310758
    DYSFO759232EBI-741243,EBI-2799016
    EGFRP005332EBI-741243,EBI-297353
    HDAC1Q135472EBI-741243,EBI-301834
    HDAC3O153792EBI-741243,EBI-607682
    RAB21Q9UL2510EBI-741243,EBI-1056039
    RAB5AP2033917EBI-741243,EBI-399437
    SYNE2Q8WXH03EBI-741243,EBI-2372294
    TRAF2Q129332EBI-741243,EBI-355744

    Protein-protein interaction databases

    BioGridi117522. 33 interactions.
    DIPiDIP-29322N.
    IntActiQ9UKG1. 50 interactions.
    MINTiMINT-1177965.
    STRINGi9606.ENSP00000288266.

    Structurei

    Secondary structure

    1
    709
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Turni12 – 143
    Helixi16 – 6651
    Helixi67 – 704
    Helixi81 – 11030
    Helixi112 – 1209
    Helixi122 – 15130
    Beta strandi152 – 1543
    Helixi157 – 21761
    Helixi220 – 25738
    Helixi259 – 2613
    Beta strandi262 – 2654
    Turni268 – 2703
    Beta strandi281 – 2866
    Beta strandi298 – 3058
    Beta strandi308 – 3125
    Beta strandi320 – 3245
    Beta strandi329 – 3335
    Beta strandi339 – 3457
    Beta strandi348 – 3503
    Helixi360 – 37415
    Beta strandi499 – 51214
    Helixi519 – 53416
    Beta strandi542 – 55514
    Turni557 – 5593
    Beta strandi562 – 5676
    Helixi568 – 5703
    Beta strandi571 – 5777
    Beta strandi580 – 59011
    Beta strandi600 – 61011
    Helixi612 – 62918

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EJ8X-ray1.84A/B492-644[»]
    2ELAX-ray2.00A/B493-646[»]
    2ELBX-ray2.60A1-376[»]
    2Q12X-ray1.79A5-265[»]
    2Q13X-ray2.05A5-385[»]
    2Z0NX-ray1.95A1-275[»]
    2Z0OX-ray2.58A1-385[»]
    ProteinModelPortaliQ9UKG1.
    SMRiQ9UKG1. Positions 4-378, 499-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKG1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini277 – 37599PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini496 – 656161PIDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 428428Required for RAB5A bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili215 – 25945Sequence AnalysisAdd
    BLAST
    Coiled coili621 – 67353Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi403 – 41412F&HAdd
    BLAST

    Domaini

    Overexpression of an N-terminal domain (residues 1-319) or a C-terminal region (residues 273-709) has a proapoptotic effect.1 Publication
    The F&H motif, an approximately 12-13 amino-acid sequence centered around Phe and His residues, is essential for binding to OCRL and INPP5B.1 Publication

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 PID domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG69757.
    HOGENOMiHOG000285988.
    HOVERGENiHBG051394.
    InParanoidiQ9UKG1.
    KOiK08733.
    OMAiSDVETMQ.
    OrthoDBiEOG79PJPK.
    PhylomeDBiQ9UKG1.
    TreeFamiTF328669.

    Family and domain databases

    Gene3Di1.20.1270.60. 1 hit.
    2.30.29.30. 2 hits.
    InterProiIPR027267. AH/BAR-dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view]
    PfamiPF00640. PID. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS01179. PID. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UKG1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA    50
    QNELSAATHL TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH 100
    AVLSTQLADA MMFPITQFKE RDLKEILTLK EVFQIASNDH DAAINRYSRL 150
    SKKRENDKVK YEVTEDVYTS RKKQHQTMMH YFCALNTLQY KKKIALLEPL 200
    LGYMQAQISF FKMGSENLNE QLEEFLANIG TSVQNVRREM DSDIETMQQT 250
    IEDLEVASDP LYVPDPDPTK FPVNRNLTRK AGYLNARNKT GLVSSTWDRQ 300
    FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK 350
    KSSILQAESK KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP 400
    SPSFQQRHES LRPAAGQSRP PTARTSSSGS LGSESTNLAA LSLDSLVAPD 450
    TPIQFDIISP VCEDQPGQAK AFGQGGRRTN PFGESGGSTK SETEDSILHQ 500
    LFIVRFLGSM EVKSDDHPDV VYETMRQILA ARAIHNIFRM TESHLLVTCD 550
    CLKLIDPQTQ VTRLTFPLPC VVLYATHQEN KRLFGFVLRT SSGRSESNLS 600
    SVCYIFESNN EGEKICDSVG LAKQIALHAE LDRRASEKQK EIERVKEKQQ 650
    KELNKQKQIE KDLEEQSRLI AASSRPNQAS SEGQFVVLSS SQSEESDLGE 700
    GGKKRESEA 709
    Length:709
    Mass (Da):79,663
    Last modified:May 1, 2000 - v1
    Checksum:i4CABECFCF4BB110D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti108 – 1081A → V.
    Corresponds to variant rs4381906 [ dbSNP | Ensembl ].
    VAR_050958
    Natural varianti643 – 6431E → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035909
    Natural varianti700 – 7001E → G.
    Corresponds to variant rs11544593 [ dbSNP | Ensembl ].
    VAR_050959

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169797 mRNA. Translation: AAF04012.1.
    AF424738 mRNA. Translation: AAL17835.1.
    AB037849 mRNA. Translation: BAA92666.2.
    BC028599 mRNA. Translation: AAH28599.1.
    CCDSiCCDS2882.1.
    RefSeqiNP_036228.1. NM_012096.2.
    UniGeneiHs.476415.

    Genome annotation databases

    EnsembliENST00000288266; ENSP00000288266; ENSG00000157500.
    GeneIDi26060.
    KEGGihsa:26060.
    UCSCiuc003dio.3. human.

    Polymorphism databases

    DMDMi61213025.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169797 mRNA. Translation: AAF04012.1 .
    AF424738 mRNA. Translation: AAL17835.1 .
    AB037849 mRNA. Translation: BAA92666.2 .
    BC028599 mRNA. Translation: AAH28599.1 .
    CCDSi CCDS2882.1.
    RefSeqi NP_036228.1. NM_012096.2.
    UniGenei Hs.476415.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EJ8 X-ray 1.84 A/B 492-644 [» ]
    2ELA X-ray 2.00 A/B 493-646 [» ]
    2ELB X-ray 2.60 A 1-376 [» ]
    2Q12 X-ray 1.79 A 5-265 [» ]
    2Q13 X-ray 2.05 A 5-385 [» ]
    2Z0N X-ray 1.95 A 1-275 [» ]
    2Z0O X-ray 2.58 A 1-385 [» ]
    ProteinModelPortali Q9UKG1.
    SMRi Q9UKG1. Positions 4-378, 499-645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117522. 33 interactions.
    DIPi DIP-29322N.
    IntActi Q9UKG1. 50 interactions.
    MINTi MINT-1177965.
    STRINGi 9606.ENSP00000288266.

    PTM databases

    PhosphoSitei Q9UKG1.

    Polymorphism databases

    DMDMi 61213025.

    Proteomic databases

    MaxQBi Q9UKG1.
    PaxDbi Q9UKG1.
    PeptideAtlasi Q9UKG1.
    PRIDEi Q9UKG1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288266 ; ENSP00000288266 ; ENSG00000157500 .
    GeneIDi 26060.
    KEGGi hsa:26060.
    UCSCi uc003dio.3. human.

    Organism-specific databases

    CTDi 26060.
    GeneCardsi GC03P057237.
    HGNCi HGNC:24035. APPL1.
    HPAi HPA011138.
    MIMi 604299. gene.
    neXtProti NX_Q9UKG1.
    PharmGKBi PA162376755.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69757.
    HOGENOMi HOG000285988.
    HOVERGENi HBG051394.
    InParanoidi Q9UKG1.
    KOi K08733.
    OMAi SDVETMQ.
    OrthoDBi EOG79PJPK.
    PhylomeDBi Q9UKG1.
    TreeFami TF328669.

    Enzyme and pathway databases

    Reactomei REACT_22128. Role of DCC in regulating apoptosis.
    SignaLinki Q9UKG1.

    Miscellaneous databases

    ChiTaRSi APPL1. human.
    EvolutionaryTracei Q9UKG1.
    GeneWikii APPL1.
    GenomeRNAii 26060.
    NextBioi 47954.
    PROi Q9UKG1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKG1.
    Bgeei Q9UKG1.
    CleanExi HS_APPL1.
    Genevestigatori Q9UKG1.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    2.30.29.30. 2 hits.
    InterProi IPR027267. AH/BAR-dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view ]
    Pfami PF00640. PID. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS01179. PID. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2."
      Mitsuuchi Y., Johnson S.W., Sonoda G., Tanno S., Golemis E.A., Testa J.R.
      Oncogene 18:4891-4898(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH AKT2 AND PIK3CA.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DCC.
    3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: BrainImported.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "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: TestisImported.
    6. "APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment."
      Miaczynska M., Christoforidis S., Giner A., Shevchenko A., Uttenweiler-Joseph S., Habermann B., Wilm M., Parton R.G., Zerial M.
      Cell 116:445-456(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND NURD/MECP1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway."
      Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S., Modregger J., Biemesderfer D., Toomre D., De Camilli P.
      Dev. Cell 13:377-390(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OCRL, F&H MOTIF, PHOSPHORYLATION AT SER-410.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1."
      Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.
      Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OCRL, SUBCELLULAR LOCATION.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway."
      Noakes C.J., Lee G., Lowe M.
      Mol. Biol. Cell 22:606-623(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OCRL.
    15. "Recognition of the F&H motif by the Lowe syndrome protein OCRL."
      Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.
      Nat. Struct. Mol. Biol. 18:789-795(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OCRL, F&H MOTIF.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-643.

    Entry informationi

    Entry nameiDP13A_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKG1
    Secondary accession number(s): Q9P2B9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 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 3
      Human chromosome 3: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3