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P55010

- IF5_HUMAN

UniProt

P55010 - IF5_HUMAN

Protein

Eukaryotic translation initiation factor 5

Gene

EIF5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (10 Jan 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 348GTPSequence Analysis

    GO - Molecular functioni

    1. GTPase activity Source: ProtInc
    2. GTP binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. translation factor activity, nucleic acid binding Source: ProtInc
    5. translation initiation factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. GTP catabolic process Source: GOC
    4. regulation of translational initiation Source: ProtInc
    5. translation Source: Reactome
    6. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_931. Ribosomal scanning and start codon recognition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 5
    Short name:
    eIF-5
    Gene namesi
    Name:EIF5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:3299. EIF5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. plasma membrane Source: HPA

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Eukaryotic translation initiation factor 5PRO_0000212516Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine2 Publications
    Modified residuei229 – 2291Phosphoserine1 Publication
    Modified residuei389 – 3891Phosphoserine4 Publications
    Modified residuei390 – 3901Phosphoserine4 Publications
    Modified residuei419 – 4191Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP55010.
    PaxDbiP55010.
    PeptideAtlasiP55010.
    PRIDEiP55010.

    PTM databases

    PhosphoSiteiP55010.

    Expressioni

    Gene expression databases

    ArrayExpressiP55010.
    BgeeiP55010.
    CleanExiHS_EIF5.
    GenevestigatoriP55010.

    Organism-specific databases

    HPAiCAB004226.
    HPA000867.

    Interactioni

    Protein-protein interaction databases

    BioGridi108298. 39 interactions.
    IntActiP55010. 5 interactions.
    MINTiMINT-5004352.
    STRINGi9606.ENSP00000216554.

    Structurei

    Secondary structure

    1
    431
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Beta strandi17 – 193
    Beta strandi23 – 253
    Beta strandi27 – 315
    Beta strandi33 – 364
    Helixi39 – 457
    Helixi51 – 6111
    Beta strandi65 – 684
    Turni69 – 724
    Beta strandi73 – 786
    Helixi82 – 9514
    Turni100 – 1023
    Beta strandi103 – 1053
    Beta strandi108 – 1125
    Turni113 – 1164
    Beta strandi117 – 1215
    Beta strandi123 – 1253
    Beta strandi128 – 1303
    Beta strandi133 – 1364
    Helixi137 – 1437
    Helixi236 – 25217
    Helixi256 – 2583
    Helixi260 – 26910
    Helixi273 – 2753
    Helixi276 – 2849
    Helixi289 – 2957
    Helixi297 – 3048
    Helixi308 – 32417
    Helixi326 – 3294
    Helixi330 – 3323
    Helixi333 – 34210
    Helixi348 – 3569
    Beta strandi361 – 3633
    Helixi365 – 38319
    Helixi400 – 4089

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E9HNMR-A1-150[»]
    2G2KNMR-A2-170[»]
    2IU1X-ray1.80A232-431[»]
    ProteinModelPortaliP55010.
    SMRiP55010. Positions 3-150, 232-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55010.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini233 – 392160W2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi196 – 2027Asp/Glu-rich (highly acidic)
    Compositional biasi384 – 40219Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi423 – 4297Asp-rich (acidic)

    Sequence similaritiesi

    Belongs to the eIF-2-beta/eIF-5 family.Curated
    Contains 1 W2 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1601.
    HOGENOMiHOG000214327.
    HOVERGENiHBG006132.
    InParanoidiP55010.
    KOiK03262.
    OMAiMHQAQLL.
    OrthoDBiEOG7FV3QF.
    PhylomeDBiP55010.
    TreeFamiTF101533.

    Family and domain databases

    Gene3Di1.25.40.180. 1 hit.
    3.30.30.50. 1 hit.
    InterProiIPR016024. ARM-type_fold.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR002735. Transl_init_fac_IF2/IF5.
    IPR016189. Transl_init_fac_IF2/IF5_N.
    IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
    IPR003307. W2_domain.
    [Graphical view]
    PfamiPF01873. eIF-5_eIF-2B. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view]
    SMARTiSM00653. eIF2B_5. 1 hit.
    SM00515. eIF5C. 1 hit.
    [Graphical view]
    SUPFAMiSSF100966. SSF100966. 1 hit.
    SSF48371. SSF48371. 1 hit.
    SSF75689. SSF75689. 1 hit.
    PROSITEiPS51363. W2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P55010-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP    50
    TYPTKYFGCE LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP 100
    ECENPETDLH VNPKKQTIGN SCKACGYRGM LDTHHKLCTF ILKNPPENSD 150
    SGTGKKEKEK KNRKGKDKEN GSVSSSETPP PPPPPNEINP PPHTMEEEED 200
    DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV NILFDFVKKK 250
    KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF 300
    LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV 350
    IISWSEKASK KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN 400
    IEVVYSKAAS VPKVETVKSD NKDDDIDIDA I 431
    Length:431
    Mass (Da):49,223
    Last modified:January 10, 2003 - v2
    Checksum:iC6CCC3A255F9B9BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601E → G in CAB45711. (PubMed:11230166)Curated
    Sequence conflicti203 – 2031W → S in AAC50572. (PubMed:8663286)Curated
    Sequence conflicti295 – 2951K → E in CAB45711. (PubMed:11230166)Curated
    Sequence conflicti311 – 3111Q → K in AAH32866. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti418 – 4181K → M in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036467

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49436 mRNA. Translation: AAC50572.1.
    AL080102 mRNA. Translation: CAB45711.1.
    AK026933 mRNA. Translation: BAB15593.1.
    BX537367 mRNA. Translation: CAD97610.1.
    CH471061 Genomic DNA. Translation: EAW81809.1.
    BC007728 mRNA. Translation: AAH07728.1.
    BC032866 mRNA. Translation: AAH32866.1.
    CCDSiCCDS9980.1.
    PIRiT12450.
    RefSeqiNP_001960.2. NM_001969.4.
    NP_892116.2. NM_183004.4.
    UniGeneiHs.433702.
    Hs.741278.

    Genome annotation databases

    EnsembliENST00000216554; ENSP00000216554; ENSG00000100664.
    ENST00000392715; ENSP00000376477; ENSG00000100664.
    ENST00000558506; ENSP00000453743; ENSG00000100664.
    GeneIDi1983.
    KEGGihsa:1983.
    UCSCiuc001ymq.4. human.

    Polymorphism databases

    DMDMi27735202.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49436 mRNA. Translation: AAC50572.1 .
    AL080102 mRNA. Translation: CAB45711.1 .
    AK026933 mRNA. Translation: BAB15593.1 .
    BX537367 mRNA. Translation: CAD97610.1 .
    CH471061 Genomic DNA. Translation: EAW81809.1 .
    BC007728 mRNA. Translation: AAH07728.1 .
    BC032866 mRNA. Translation: AAH32866.1 .
    CCDSi CCDS9980.1.
    PIRi T12450.
    RefSeqi NP_001960.2. NM_001969.4.
    NP_892116.2. NM_183004.4.
    UniGenei Hs.433702.
    Hs.741278.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E9H NMR - A 1-150 [» ]
    2G2K NMR - A 2-170 [» ]
    2IU1 X-ray 1.80 A 232-431 [» ]
    ProteinModelPortali P55010.
    SMRi P55010. Positions 3-150, 232-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108298. 39 interactions.
    IntActi P55010. 5 interactions.
    MINTi MINT-5004352.
    STRINGi 9606.ENSP00000216554.

    PTM databases

    PhosphoSitei P55010.

    Polymorphism databases

    DMDMi 27735202.

    Proteomic databases

    MaxQBi P55010.
    PaxDbi P55010.
    PeptideAtlasi P55010.
    PRIDEi P55010.

    Protocols and materials databases

    DNASUi 1983.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216554 ; ENSP00000216554 ; ENSG00000100664 .
    ENST00000392715 ; ENSP00000376477 ; ENSG00000100664 .
    ENST00000558506 ; ENSP00000453743 ; ENSG00000100664 .
    GeneIDi 1983.
    KEGGi hsa:1983.
    UCSCi uc001ymq.4. human.

    Organism-specific databases

    CTDi 1983.
    GeneCardsi GC14P103800.
    HGNCi HGNC:3299. EIF5.
    HPAi CAB004226.
    HPA000867.
    MIMi 601710. gene.
    neXtProti NX_P55010.
    PharmGKBi PA27725.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1601.
    HOGENOMi HOG000214327.
    HOVERGENi HBG006132.
    InParanoidi P55010.
    KOi K03262.
    OMAi MHQAQLL.
    OrthoDBi EOG7FV3QF.
    PhylomeDBi P55010.
    TreeFami TF101533.

    Enzyme and pathway databases

    Reactomei REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi eIF5. human.
    EvolutionaryTracei P55010.
    GeneWikii EIF5.
    GenomeRNAii 1983.
    NextBioi 8031.
    PROi P55010.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55010.
    Bgeei P55010.
    CleanExi HS_EIF5.
    Genevestigatori P55010.

    Family and domain databases

    Gene3Di 1.25.40.180. 1 hit.
    3.30.30.50. 1 hit.
    InterProi IPR016024. ARM-type_fold.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR002735. Transl_init_fac_IF2/IF5.
    IPR016189. Transl_init_fac_IF2/IF5_N.
    IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
    IPR003307. W2_domain.
    [Graphical view ]
    Pfami PF01873. eIF-5_eIF-2B. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view ]
    SMARTi SM00653. eIF2B_5. 1 hit.
    SM00515. eIF5C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100966. SSF100966. 1 hit.
    SSF48371. SSF48371. 1 hit.
    SSF75689. SSF75689. 1 hit.
    PROSITEi PS51363. W2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5)."
      Si K., Das K., Maitra U.
      J. Biol. Chem. 271:16934-16938(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 Uterus.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-229; SER-389; SER-390 AND SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-10; SER-389; SER-390 AND SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of the EIF-5_EIF-2B domain from human eukaryotic translation initiation factor 5."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-150.
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-418.

    Entry informationi

    Entry nameiIF5_HUMAN
    AccessioniPrimary (citable) accession number: P55010
    Secondary accession number(s): Q53XB3, Q9H5N2, Q9UG48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 10, 2003
    Last modified: October 1, 2014
    This is version 143 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 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. Translation initiation factors
      List of translation initiation factor entries
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3