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P56282

- DPOE2_HUMAN

UniProt

P56282 - DPOE2_HUMAN

Protein

DNA polymerase epsilon subunit 2

Gene

POLE2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Participates in DNA repair and in chromosomal DNA replication.

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA-directed DNA polymerase activity Source: ProtInc

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. DNA replication Source: ProtInc
    3. DNA replication initiation Source: Reactome
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. nucleotide-excision repair Source: Reactome
    7. nucleotide-excision repair, DNA gap filling Source: Reactome
    8. telomere maintenance Source: Reactome
    9. telomere maintenance via recombination Source: Reactome
    10. telomere maintenance via semi-conservative replication Source: Reactome
    11. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2244. DNA replication initiation.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_7993. Telomere C-strand synthesis initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase epsilon subunit 2 (EC:2.7.7.7)
    Alternative name(s):
    DNA polymerase II subunit 2
    DNA polymerase epsilon subunit B
    Gene namesi
    Name:POLE2
    Synonyms:DPE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9178. POLE2.

    Subcellular locationi

    GO - Cellular componenti

    1. epsilon DNA polymerase complex Source: UniProtKB
    2. intracellular membrane-bounded organelle Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA278.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 527527DNA polymerase epsilon subunit 2PRO_0000071562Add
    BLAST

    Proteomic databases

    MaxQBiP56282.
    PaxDbiP56282.
    PRIDEiP56282.

    PTM databases

    PhosphoSiteiP56282.

    Expressioni

    Gene expression databases

    ArrayExpressiP56282.
    BgeeiP56282.
    CleanExiHS_POLE2.
    GenevestigatoriP56282.

    Organism-specific databases

    HPAiHPA027555.

    Interactioni

    Subunit structurei

    Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4.1 Publication

    Protein-protein interaction databases

    BioGridi111423. 12 interactions.
    IntActiP56282. 7 interactions.
    MINTiMINT-1377461.
    STRINGi9606.ENSP00000216367.

    Structurei

    Secondary structure

    1
    527
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi23 – 3210
    Turni33 – 353
    Turni38 – 403
    Helixi41 – 5212
    Beta strandi58 – 625
    Helixi64 – 7310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V6ZNMR-M1-73[»]
    ProteinModelPortaliP56282.
    SMRiP56282. Positions 1-75.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56282.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG311342.
    HOGENOMiHOG000265254.
    HOVERGENiHBG061290.
    InParanoidiP56282.
    KOiK02325.
    OMAiILQQRTH.
    OrthoDBiEOG725DH7.
    PhylomeDBiP56282.
    TreeFamiTF103007.

    Family and domain databases

    InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
    IPR016266. DNA_pol_e_bsu.
    IPR024639. DNA_pol_e_bsu_N.
    [Graphical view]
    PfamiPF04042. DNA_pol_E_B. 1 hit.
    PF12213. Dpoe2NT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000799. DNA_pol_eps_2. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P56282-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAPERLRSRA LSAFKLRGLL LRGEAIKYLT EALQSISELE LEDKLEKIIN    50
    AVEKQPLSSN MIERSVVEAA VQECSQSVDE TIEHVFNIIG AFDIPRFVYN 100
    SERKKFLPLL MTNHPAPNLF GTPRDKAEMF RERYTILHQR THRHELFTPP 150
    VIGSHPDESG SKFQLKTIET LLGSTTKIGD AIVLGMITQL KEGKFFLEDP 200
    TGTVQLDLSK AQFHSGLYTE ACFVLAEGWF EDQVFHVNAF GFPPTEPSST 250
    TRAYYGNINF FGGPSNTSVK TSAKLKQLEE ENKDAMFVFL SDVWLDQVEV 300
    LEKLRIMFAG YSPAPPTCFI LCGNFSSAPY GKNQVQALKD SLKTLADIIC 350
    EYPDIHQSSR FVFVPGPEDP GFGSILPRPP LAESITNEFR QRVPFSVFTT 400
    NPCRIQYCTQ EITVFREDLV NKMCRNCVRF PSSNLAIPNH FVKTILSQGH 450
    LTPLPLYVCP VYWAYDYALR VYPVPDLLVI ADKYDPFTTT NTECLCINPG 500
    SFPRSGFSFK VFYPSNKTVE DSKLQGF 527
    Length:527
    Mass (Da):59,537
    Last modified:December 15, 1998 - v2
    Checksum:iAFA7AF7C2C0BFF15
    GO
    Isoform 2 (identifier: P56282-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         83-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:501
    Mass (Da):56,418
    Checksum:iECB4BFD1E2FDAE1C
    GO
    Isoform 3 (identifier: P56282-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         500-527: GSFPRSGFSFKVFYPSNKTVEDSKLQGF → VRM

    Show »
    Length:502
    Mass (Da):56,784
    Checksum:i0F3391E93AB14483
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111L → P in AAC51920. (PubMed:9405441)Curated
    Sequence conflicti359 – 3591Missing in AAC51920. (PubMed:9405441)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti84 – 841H → P.1 Publication
    Corresponds to variant rs34857719 [ dbSNP | Ensembl ].
    VAR_044379
    Natural varianti456 – 4561L → V.
    Corresponds to variant rs34574266 [ dbSNP | Ensembl ].
    VAR_044380
    Natural varianti514 – 5141P → L.1 Publication
    Corresponds to variant rs45515094 [ dbSNP | Ensembl ].
    VAR_044381

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei83 – 10826Missing in isoform 2. 1 PublicationVSP_042551Add
    BLAST
    Alternative sequencei500 – 52728GSFPR…KLQGF → VRM in isoform 3. 1 PublicationVSP_043796Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF025840 mRNA. Translation: AAC51920.1.
    AF036899 mRNA. Translation: AAC39610.1.
    AF387034
    , AF387021, AF387022, AF387023, AF387024, AF387025, AF387026, AF387027, AF387028, AF387029, AF387030, AF387031, AF387032, AF387033 Genomic DNA. Translation: AAK72254.1.
    EF506887 Genomic DNA. Translation: ABO43040.1.
    AK293163 mRNA. Translation: BAG56707.1.
    AL139099 Genomic DNA. No translation available.
    AL591767 Genomic DNA. No translation available.
    BC112962 mRNA. Translation: AAI12963.1.
    BC126218 mRNA. Translation: AAI26219.1.
    BC126220 mRNA. Translation: AAI26221.1.
    CCDSiCCDS32073.1. [P56282-1]
    CCDS55914.1. [P56282-2]
    CCDS55915.1. [P56282-3]
    RefSeqiNP_001184259.1. NM_001197330.1. [P56282-2]
    NP_001184260.1. NM_001197331.1. [P56282-3]
    NP_002683.2. NM_002692.3. [P56282-1]
    UniGeneiHs.162777.

    Genome annotation databases

    EnsembliENST00000216367; ENSP00000216367; ENSG00000100479. [P56282-1]
    ENST00000539565; ENSP00000446313; ENSG00000100479. [P56282-2]
    ENST00000554396; ENSP00000451621; ENSG00000100479. [P56282-3]
    GeneIDi5427.
    KEGGihsa:5427.
    UCSCiuc001wwu.3. human. [P56282-1]
    uc010ano.3. human. [P56282-3]
    uc021rsr.1. human. [P56282-2]

    Polymorphism databases

    DMDMi3915676.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF025840 mRNA. Translation: AAC51920.1 .
    AF036899 mRNA. Translation: AAC39610.1 .
    AF387034
    , AF387021 , AF387022 , AF387023 , AF387024 , AF387025 , AF387026 , AF387027 , AF387028 , AF387029 , AF387030 , AF387031 , AF387032 , AF387033 Genomic DNA. Translation: AAK72254.1 .
    EF506887 Genomic DNA. Translation: ABO43040.1 .
    AK293163 mRNA. Translation: BAG56707.1 .
    AL139099 Genomic DNA. No translation available.
    AL591767 Genomic DNA. No translation available.
    BC112962 mRNA. Translation: AAI12963.1 .
    BC126218 mRNA. Translation: AAI26219.1 .
    BC126220 mRNA. Translation: AAI26221.1 .
    CCDSi CCDS32073.1. [P56282-1 ]
    CCDS55914.1. [P56282-2 ]
    CCDS55915.1. [P56282-3 ]
    RefSeqi NP_001184259.1. NM_001197330.1. [P56282-2 ]
    NP_001184260.1. NM_001197331.1. [P56282-3 ]
    NP_002683.2. NM_002692.3. [P56282-1 ]
    UniGenei Hs.162777.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V6Z NMR - M 1-73 [» ]
    ProteinModelPortali P56282.
    SMRi P56282. Positions 1-75.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111423. 12 interactions.
    IntActi P56282. 7 interactions.
    MINTi MINT-1377461.
    STRINGi 9606.ENSP00000216367.

    PTM databases

    PhosphoSitei P56282.

    Polymorphism databases

    DMDMi 3915676.

    Proteomic databases

    MaxQBi P56282.
    PaxDbi P56282.
    PRIDEi P56282.

    Protocols and materials databases

    DNASUi 5427.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216367 ; ENSP00000216367 ; ENSG00000100479 . [P56282-1 ]
    ENST00000539565 ; ENSP00000446313 ; ENSG00000100479 . [P56282-2 ]
    ENST00000554396 ; ENSP00000451621 ; ENSG00000100479 . [P56282-3 ]
    GeneIDi 5427.
    KEGGi hsa:5427.
    UCSCi uc001wwu.3. human. [P56282-1 ]
    uc010ano.3. human. [P56282-3 ]
    uc021rsr.1. human. [P56282-2 ]

    Organism-specific databases

    CTDi 5427.
    GeneCardsi GC14M050110.
    HGNCi HGNC:9178. POLE2.
    HPAi HPA027555.
    MIMi 602670. gene.
    neXtProti NX_P56282.
    PharmGKBi PA278.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311342.
    HOGENOMi HOG000265254.
    HOVERGENi HBG061290.
    InParanoidi P56282.
    KOi K02325.
    OMAi ILQQRTH.
    OrthoDBi EOG725DH7.
    PhylomeDBi P56282.
    TreeFami TF103007.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_2244. DNA replication initiation.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_7993. Telomere C-strand synthesis initiation.

    Miscellaneous databases

    EvolutionaryTracei P56282.
    GeneWikii POLE2.
    GenomeRNAii 5427.
    NextBioi 20997.
    PROi P56282.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56282.
    Bgeei P56282.
    CleanExi HS_POLE2.
    Genevestigatori P56282.

    Family and domain databases

    InterProi IPR007185. DNA_pol_alpha/epsilon_bsu.
    IPR016266. DNA_pol_e_bsu.
    IPR024639. DNA_pol_e_bsu_N.
    [Graphical view ]
    Pfami PF04042. DNA_pol_E_B. 1 hit.
    PF12213. Dpoe2NT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000799. DNA_pol_eps_2. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Purification, cDNA cloning, and gene mapping of the small subunit of human DNA polymerase epsilon."
      Li Y., Asahara H., Patel V.S., Zhou S., Linn S.
      J. Biol. Chem. 272:32337-32344(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The small subunits of human and mouse DNA polymerase epsilon are homologous to the second largest subunit of the yeast Saccharomyces cerevisiae DNA polymerase epsilon."
      Jokela M., Makiniemi M., Lehtonen S., Szpirer C., Hellman U., Syvaeoja J.E.
      Nucleic Acids Res. 26:730-734(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "E2F mediates induction of the Sp1-controlled promoter of the human DNA polymerase varepsilon B-subunit gene POLE2."
      Huang D., Jokela M., Tuusa J., Skog S., Poikonen K., Syvaoja J.E.
      Nucleic Acids Res. 29:2810-2821(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIEHS SNPs program
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-84 AND LEU-514.
    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] (ISOFORM 2).
    6. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1 AND 3).
      Tissue: Embryonic stem cell.
    8. "Identification and cloning of two histone fold motif-containing subunits of HeLa DNA polymerase epsilon."
      Li Y., Pursell Z.F., Linn S.
      J. Biol. Chem. 275:23247-23252(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX.
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiDPOE2_HUMAN
    AccessioniPrimary (citable) accession number: P56282
    Secondary accession number(s): A0AV55
    , A4FU92, A4LBB7, A6NH58, B4DDE6, O43560
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 122 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

    Miscellaneous

    In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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