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Q8IV48

- ERI1_HUMAN

UniProt

Q8IV48 - ERI1_HUMAN

Protein

3'-5' exoribonuclease 1

Gene

ERI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.2 Publications

    Cofactori

    Binds 2 magnesium ions per subunit.

    Enzyme regulationi

    Although it can bind simultaneously with SLBP to the 3'-end of histone mRNA, the presence of SLBP prevents the exonuclease activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi134 – 1341Magnesium 1
    Metal bindingi134 – 1341Magnesium 2
    Active sitei136 – 1361Proton acceptorSequence Analysis
    Metal bindingi136 – 1361Magnesium 1
    Binding sitei136 – 1361AMP1 Publication
    Binding sitei137 – 1371AMP; via amide nitrogen and carbonyl oxygen1 Publication
    Metal bindingi234 – 2341Magnesium 2
    Active sitei293 – 2931Proton acceptorSequence Analysis
    Binding sitei293 – 2931AMP1 Publication
    Metal bindingi298 – 2981Magnesium 1

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. histone pre-mRNA stem-loop binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. ribosome binding Source: UniProtKB
    5. rRNA binding Source: UniProtKB

    GO - Biological processi

    1. gene silencing by RNA Source: UniProtKB-KW
    2. nucleic acid phosphodiester bond hydrolysis Source: GOC
    3. rRNA 3'-end processing Source: UniProtKB

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    RNA-mediated gene silencing, rRNA processing

    Keywords - Ligandi

    Magnesium, Metal-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3'-5' exoribonuclease 1 (EC:3.1.-.-)
    Alternative name(s):
    3'-5' exonuclease ERI1
    Eri-1 homolog
    Histone mRNA 3'-end-specific exoribonuclease
    Histone mRNA 3'-exonuclease 1
    Protein 3'hExo
    Short name:
    HEXO
    Gene namesi
    Name:ERI1
    Synonyms:3'EXO, THEX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:23994. ERI1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone pre-mRNA 3'end processing complex Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921K → A: Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-104. 1 Publication
    Mutagenesisi96 – 961R → A: Does not inhibit RNA-binding to the stem-loop structure. 1 Publication
    Mutagenesisi99 – 991K → A: Reduces slightly RNA-binding to the stem-loop structure. 1 Publication
    Mutagenesisi104 – 1041K → A: Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-92. 1 Publication
    Mutagenesisi105 – 1051R → A: Inhibits RNA-binding to the stem-loop structure. 1 Publication
    Mutagenesisi109 – 1091Y → A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-110. 1 Publication
    Mutagenesisi110 – 1101Y → A: Reduces slightly RNA-binding to the stem-loop structure; when associated with A-109. 1 Publication
    Mutagenesisi111 – 1111K → A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-112. 1 Publication
    Mutagenesisi112 – 1121K → A: Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-111. 1 Publication
    Mutagenesisi234 – 2341D → A: Inhibits 3'-end histone mRNA exonuclease activity. 1 Publication
    Mutagenesisi235 – 2351M → A: Inhibits RNA-binding to the stem-loop structure and 3'-end histone mRNA exonuclease activity. 1 Publication
    Mutagenesisi298 – 2981D → A: Inhibits 3'-end histone mRNA exonuclease activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA164719226.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 3493483'-5' exoribonuclease 1PRO_0000187007Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IV48.
    PaxDbiQ8IV48.
    PeptideAtlasiQ8IV48.
    PRIDEiQ8IV48.

    PTM databases

    PhosphoSiteiQ8IV48.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IV48.
    BgeeiQ8IV48.
    CleanExiHS_ERI1.
    GenevestigatoriQ8IV48.

    Organism-specific databases

    HPAiCAB033838.

    Interactioni

    Subunit structurei

    Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts in a cooperative manner with SLBP to the mature 3'-end of histone mRNAs By similarity. Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes. Found in a ternary complex with SLBP and the stem-loop structure of the 3'-end of histone mRNAs.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi124718. 5 interactions.
    STRINGi9606.ENSP00000250263.

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 7714
    Helixi81 – 9010
    Helixi99 – 11416
    Beta strandi126 – 1327
    Beta strandi151 – 16010
    Turni161 – 1633
    Beta strandi165 – 17410
    Beta strandi177 – 1793
    Helixi184 – 1907
    Helixi194 – 1985
    Beta strandi200 – 2023
    Helixi203 – 21614
    Turni220 – 2223
    Beta strandi225 – 2317
    Turni232 – 2354
    Helixi236 – 24611
    Helixi252 – 2543
    Beta strandi255 – 2595
    Helixi260 – 2689
    Helixi272 – 2743
    Helixi277 – 2837
    Helixi295 – 31117
    Beta strandi320 – 32910
    Beta strandi332 – 3343

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W0HX-ray1.59A123-322[»]
    1ZBHX-ray3.00A/B/C/D51-349[»]
    1ZBUX-ray3.00A/B/C/D1-349[»]
    4L8RX-ray2.60B/E55-349[»]
    ProteinModelPortaliQ8IV48.
    SMRiQ8IV48. Positions 60-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IV48.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 11035SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini130 – 306177ExonucleaseAdd
    BLAST

    Domaini

    The SAP domain is necessary for binding to the stem-loop structure of histone mRNAs and to form the ternary complex with SLBP, but not for 3'-end histone mRNA exonuclease activity.

    Sequence similaritiesi

    Contains 1 exonuclease domain.Curated
    Contains 1 SAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5018.
    HOGENOMiHOG000006635.
    HOVERGENiHBG048925.
    InParanoidiQ8IV48.
    KOiK01175.
    OMAiFLNIQCR.
    OrthoDBiEOG7BGHM2.
    PhylomeDBiQ8IV48.
    TreeFamiTF313449.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR006055. Exonuclease.
    IPR013520. Exonuclease_RNaseT/DNA_pol3.
    IPR012337. RNaseH-like_dom.
    IPR003034. SAP_dom.
    [Graphical view]
    PfamiPF00929. RNase_T. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view]
    SMARTiSM00479. EXOIII. 1 hit.
    SM00513. SAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 1 hit.
    PROSITEiPS50800. SAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8IV48-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDPQSKEPA GEAVALALLE SPRPEGGEEP PRPSPEETQQ CKFDGQETKG    50
    SKFITSSASD FSDPVYKEIA ITNGCINRMS KEELRAKLSE FKLETRGVKD 100
    VLKKRLKNYY KKQKLMLKES NFADSYYDYI CIIDFEATCE EGNPPEFVHE 150
    IIEFPVVLLN THTLEIEDTF QQYVRPEINT QLSDFCISLT GITQDQVDRA 200
    DTFPQVLKKV IDWMKLKELG TKYKYSLLTD GSWDMSKFLN IQCQLSRLKY 250
    PPFAKKWINI RKSYGNFYKV PRSQTKLTIM LEKLGMDYDG RPHCGLDDSK 300
    NIARIAVRML QDGCELRINE KMHAGQLMSV SSSLPIEGTP PPQMPHFRK 349
    Length:349
    Mass (Da):40,064
    Last modified:January 23, 2007 - v3
    Checksum:iD5837AA05F09410C
    GO

    Sequence cautioni

    The sequence CAB70871.2 differs from that shown. Reason: Frameshift at position 117.
    The sequence CAB70871.2 differs from that shown. Reason: Erroneous termination at position 159. Translated as Leu.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161L → P.1 Publication
    Corresponds to variant rs2288672 [ dbSNP | Ensembl ].
    VAR_018107

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY310909 mRNA. Translation: AAQ21219.1.
    AK291062 mRNA. Translation: BAF83751.1.
    AL137679 mRNA. Translation: CAB70871.2. Sequence problems.
    BC035279 mRNA. Translation: AAH35279.1.
    CCDSiCCDS5972.1.
    PIRiT46432.
    RefSeqiNP_699163.2. NM_153332.3.
    XP_006716327.1. XM_006716264.1.
    UniGeneiHs.20000.

    Genome annotation databases

    EnsembliENST00000250263; ENSP00000250263; ENSG00000104626.
    ENST00000519292; ENSP00000430190; ENSG00000104626.
    ENST00000523898; ENSP00000429615; ENSG00000104626.
    GeneIDi90459.
    KEGGihsa:90459.
    UCSCiuc003wsk.2. human.

    Polymorphism databases

    DMDMi45476938.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY310909 mRNA. Translation: AAQ21219.1 .
    AK291062 mRNA. Translation: BAF83751.1 .
    AL137679 mRNA. Translation: CAB70871.2 . Sequence problems.
    BC035279 mRNA. Translation: AAH35279.1 .
    CCDSi CCDS5972.1.
    PIRi T46432.
    RefSeqi NP_699163.2. NM_153332.3.
    XP_006716327.1. XM_006716264.1.
    UniGenei Hs.20000.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W0H X-ray 1.59 A 123-322 [» ]
    1ZBH X-ray 3.00 A/B/C/D 51-349 [» ]
    1ZBU X-ray 3.00 A/B/C/D 1-349 [» ]
    4L8R X-ray 2.60 B/E 55-349 [» ]
    ProteinModelPortali Q8IV48.
    SMRi Q8IV48. Positions 60-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124718. 5 interactions.
    STRINGi 9606.ENSP00000250263.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    PTM databases

    PhosphoSitei Q8IV48.

    Polymorphism databases

    DMDMi 45476938.

    Proteomic databases

    MaxQBi Q8IV48.
    PaxDbi Q8IV48.
    PeptideAtlasi Q8IV48.
    PRIDEi Q8IV48.

    Protocols and materials databases

    DNASUi 90459.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250263 ; ENSP00000250263 ; ENSG00000104626 .
    ENST00000519292 ; ENSP00000430190 ; ENSG00000104626 .
    ENST00000523898 ; ENSP00000429615 ; ENSG00000104626 .
    GeneIDi 90459.
    KEGGi hsa:90459.
    UCSCi uc003wsk.2. human.

    Organism-specific databases

    CTDi 90459.
    GeneCardsi GC08P008900.
    HGNCi HGNC:23994. ERI1.
    HPAi CAB033838.
    MIMi 608739. gene.
    neXtProti NX_Q8IV48.
    PharmGKBi PA164719226.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5018.
    HOGENOMi HOG000006635.
    HOVERGENi HBG048925.
    InParanoidi Q8IV48.
    KOi K01175.
    OMAi FLNIQCR.
    OrthoDBi EOG7BGHM2.
    PhylomeDBi Q8IV48.
    TreeFami TF313449.

    Miscellaneous databases

    EvolutionaryTracei Q8IV48.
    GenomeRNAii 90459.
    NextBioi 76770.
    PROi Q8IV48.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IV48.
    Bgeei Q8IV48.
    CleanExi HS_ERI1.
    Genevestigatori Q8IV48.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR006055. Exonuclease.
    IPR013520. Exonuclease_RNaseT/DNA_pol3.
    IPR012337. RNaseH-like_dom.
    IPR003034. SAP_dom.
    [Graphical view ]
    Pfami PF00929. RNase_T. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view ]
    SMARTi SM00479. EXOIII. 1 hit.
    SM00513. SAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    PROSITEi PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A 3' exonuclease that specifically interacts with the 3' end of histone mRNA."
      Dominski Z., Yang X.-C., Kaygun H., Dadlez M., Marzluff W.F.
      Mol. Cell 12:295-305(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-23; 43-48; 53-67; 161-172; 200-208; 225-237; 263-269 AND 284-291, FUNCTION, ENZYME REGULATION, ENZYME ACTIVITY, RNA-BINDING.
    2. "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], VARIANT PRO-16.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    4. "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].
    5. "A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans."
      Kennedy S., Wang D., Ruvkun G.
      Nature 427:645-649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY IN VITRO.
    6. "Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA."
      Yang X.-C., Purdy M., Marzluff W.F., Dominski Z.
      J. Biol. Chem. 281:30447-30454(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A TERNARY COMPLEX, ENZYME ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-92; ARG-96; LYS-99; LYS-104; ARG-105; THY-109; THY-110; LYS-111; LYS-112; ASP-234; MET-235 AND ASP-298, RNA-BINDING.
    7. "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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh family member, bound to rAMP."
      Cheng Y., Patel D.J.
      J. Mol. Biol. 343:305-312(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 123-322 IN COMPLEX WITH MAGNESIUM IONS AND AMP.

    Entry informationi

    Entry nameiERI1_HUMAN
    AccessioniPrimary (citable) accession number: Q8IV48
    Secondary accession number(s): A8K4U7, Q9NSX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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