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Q9H9A7

- RMI1_HUMAN

UniProt

Q9H9A7 - RMI1_HUMAN

Protein

RecQ-mediated genome instability protein 1

Gene

RMI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
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    Functioni

    Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW

    Keywords - Biological processi

    DNA replication

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RecQ-mediated genome instability protein 1
    Alternative name(s):
    BLM-associated protein of 75 kDa
    Short name:
    BLAP75
    FAAP75
    Gene namesi
    Name:RMI1
    Synonyms:C9orf76
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:25764. RMI1.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Forms foci in response to DNA damage.

    GO - Cellular componenti

    1. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134939007.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 625625RecQ-mediated genome instability protein 1PRO_0000227546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei225 – 2251Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H9A7.
    PaxDbiQ9H9A7.
    PRIDEiQ9H9A7.

    PTM databases

    PhosphoSiteiQ9H9A7.

    Expressioni

    Gene expression databases

    BgeeiQ9H9A7.
    CleanExiHS_RMI1.
    GenevestigatoriQ9H9A7.

    Organism-specific databases

    HPAiCAB012247.
    HPA021661.
    HPA051592.

    Interactioni

    Subunit structurei

    Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM. Directly interacts with RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with BLM; the interaction is direct.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLMP5413210EBI-621339,EBI-621372

    Protein-protein interaction databases

    BioGridi123066. 20 interactions.
    DIPiDIP-33324N.
    IntActiQ9H9A7. 13 interactions.
    MINTiMINT-8048917.
    STRINGi9606.ENSP00000317039.

    Structurei

    Secondary structure

    1
    625
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1816
    Helixi24 – 3815
    Helixi45 – 5713
    Helixi61 – 644
    Turni71 – 755
    Beta strandi77 – 9519
    Helixi96 – 10813
    Helixi113 – 1153
    Helixi126 – 1294
    Beta strandi135 – 1439
    Beta strandi145 – 1506
    Beta strandi166 – 17611
    Beta strandi179 – 1824
    Helixi184 – 1863
    Beta strandi187 – 1915
    Helixi195 – 2017
    Helixi203 – 2108
    Helixi480 – 4823
    Helixi483 – 4875
    Helixi494 – 4996
    Beta strandi506 – 51712
    Helixi524 – 5263
    Beta strandi531 – 5355
    Beta strandi540 – 5456
    Helixi547 – 5548
    Helixi558 – 5647
    Helixi568 – 58720
    Beta strandi589 – 5979
    Turni598 – 6014
    Beta strandi602 – 6098
    Helixi613 – 62210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MXNX-ray1.55A473-625[»]
    3NBHX-ray2.00A475-625[»]
    3NBIX-ray2.00A2-213[»]
    4CGYX-ray2.85B1-219[»]
    4CHTX-ray3.25B1-219[»]
    4DAYX-ray3.30A473-625[»]
    ProteinModelPortaliQ9H9A7.
    SMRiQ9H9A7. Positions 2-216, 475-625.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RMI1 family.Curated

    Phylogenomic databases

    eggNOGiNOG261197.
    HOVERGENiHBG061190.
    InParanoidiQ9H9A7.
    KOiK10990.
    OMAiAMDLYSP.
    OrthoDBiEOG7F7W8R.
    PhylomeDBiQ9H9A7.
    TreeFamiTF316491.

    Family and domain databases

    InterProiIPR013894. DUF1767.
    [Graphical view]
    PfamiPF08585. DUF1767. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9H9A7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVTSIALRA ETWLLAAWHV KVPPMWLEAC INWIQEENNN VNLSQAQMNK    50
    QVFEQWLLTD LRDLEHPLLP DGILEIPKGE LNGFYALQIN SLVDVSQPAY 100
    SQIQKLRGKN TTNDLVTAEA QVTPKPWEAK PSRMLMLQLT DGIVQIQGME 150
    YQPIPILHSD LPPGTKILIY GNISFRLGVL LLKPENVKVL GGEVDALLEE 200
    YAQEKVLARL IGEPDLVVSV IPNNSNENIP RVTDVLDPAL GPSDEELLAS 250
    LDENDELTAN NDTSSERCFT TGSSSNTIPT RQSSFEPEFV ISPRPKEEPS 300
    NLSIHVMDGE LDDFSLEEAL LLEETVQKEQ METKELQPLT FNRNADRSIE 350
    RFSHNPNTTN NFSLTCKNGN NNWSEKNVSE QMTNEDKSFG CPSVRDQNRS 400
    IFSVHCNVPL AHDFTNKEKN LETDNKIKQT SSSDSHSLNN KILNREVVNY 450
    VQKRNSQISN ENDCNLQSCS LRSSENSINL SIAMDLYSPP FVYLSVLMAS 500
    KPKEVTTVKV KAFIVTLTGN LSSSGGIWSI TAKVSDGTAY LDVDFVDEIL 550
    TSLIGFSVPE MKQSKKDPLQ YQKFLEGLQK CQRDLIDLCC LMTISFNPSL 600
    SKAMVLALQD VNMEHLENLK KRLNK 625
    Length:625
    Mass (Da):70,144
    Last modified:February 8, 2011 - v3
    Checksum:i2BB449363DBF76B7
    GO

    Sequence cautioni

    The sequence AAH20606.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH32494.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH53549.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH39999.1 differs from that shown. Reason: Frameshift at position 375.
    The sequence AAH39999.1 differs from that shown. Reason: Frameshift at positions 377 and 444.
    The sequence AAH64937.1 differs from that shown. Reason: Frameshift at positions 444 and 615.
    The sequence AAH64937.1 differs from that shown. Reason: Frameshift at positions 377 and 444.
    The sequence CAI13575.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111E → G in BAB14325. (PubMed:14702039)Curated
    Sequence conflicti259 – 2591A → T in BAB14325. (PubMed:14702039)Curated
    Sequence conflicti318 – 3181E → D in AAH20606. (PubMed:15489334)Curated
    Sequence conflicti443 – 4431L → F in AAH39999. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001Y → H.1 Publication
    Corresponds to variant rs17855932 [ dbSNP | Ensembl ].
    VAR_025556
    Natural varianti455 – 4551N → S.2 Publications
    Corresponds to variant rs1982151 [ dbSNP | Ensembl ].
    VAR_025557

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022950 mRNA. Translation: BAB14325.1.
    AL732446 Genomic DNA. Translation: CAI13576.1.
    AL732446 Genomic DNA. Translation: CAI13575.1. Sequence problems.
    BC020606 mRNA. Translation: AAH20606.1. Sequence problems.
    BC032494 mRNA. Translation: AAH32494.1. Sequence problems.
    BC039999 mRNA. Translation: AAH39999.1. Frameshift.
    BC053549 mRNA. Translation: AAH53549.1. Sequence problems.
    BC064937 mRNA. Translation: AAH64937.1. Frameshift.
    CCDSiCCDS6669.1.
    RefSeqiNP_079221.2. NM_024945.2.
    XP_005252268.1. XM_005252211.1.
    XP_005252270.1. XM_005252213.1.
    UniGeneiHs.726327.

    Genome annotation databases

    EnsembliENST00000325875; ENSP00000317039; ENSG00000178966.
    GeneIDi80010.
    KEGGihsa:80010.
    UCSCiuc004anp.4. human.

    Polymorphism databases

    DMDMi322510109.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022950 mRNA. Translation: BAB14325.1 .
    AL732446 Genomic DNA. Translation: CAI13576.1 .
    AL732446 Genomic DNA. Translation: CAI13575.1 . Sequence problems.
    BC020606 mRNA. Translation: AAH20606.1 . Sequence problems.
    BC032494 mRNA. Translation: AAH32494.1 . Sequence problems.
    BC039999 mRNA. Translation: AAH39999.1 . Frameshift.
    BC053549 mRNA. Translation: AAH53549.1 . Sequence problems.
    BC064937 mRNA. Translation: AAH64937.1 . Frameshift.
    CCDSi CCDS6669.1.
    RefSeqi NP_079221.2. NM_024945.2.
    XP_005252268.1. XM_005252211.1.
    XP_005252270.1. XM_005252213.1.
    UniGenei Hs.726327.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MXN X-ray 1.55 A 473-625 [» ]
    3NBH X-ray 2.00 A 475-625 [» ]
    3NBI X-ray 2.00 A 2-213 [» ]
    4CGY X-ray 2.85 B 1-219 [» ]
    4CHT X-ray 3.25 B 1-219 [» ]
    4DAY X-ray 3.30 A 473-625 [» ]
    ProteinModelPortali Q9H9A7.
    SMRi Q9H9A7. Positions 2-216, 475-625.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123066. 20 interactions.
    DIPi DIP-33324N.
    IntActi Q9H9A7. 13 interactions.
    MINTi MINT-8048917.
    STRINGi 9606.ENSP00000317039.

    PTM databases

    PhosphoSitei Q9H9A7.

    Polymorphism databases

    DMDMi 322510109.

    Proteomic databases

    MaxQBi Q9H9A7.
    PaxDbi Q9H9A7.
    PRIDEi Q9H9A7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325875 ; ENSP00000317039 ; ENSG00000178966 .
    GeneIDi 80010.
    KEGGi hsa:80010.
    UCSCi uc004anp.4. human.

    Organism-specific databases

    CTDi 80010.
    GeneCardsi GC09P086595.
    H-InvDB HIX0008132.
    HGNCi HGNC:25764. RMI1.
    HPAi CAB012247.
    HPA021661.
    HPA051592.
    MIMi 610404. gene.
    neXtProti NX_Q9H9A7.
    PharmGKBi PA134939007.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261197.
    HOVERGENi HBG061190.
    InParanoidi Q9H9A7.
    KOi K10990.
    OMAi AMDLYSP.
    OrthoDBi EOG7F7W8R.
    PhylomeDBi Q9H9A7.
    TreeFami TF316491.

    Miscellaneous databases

    GeneWikii RMI1.
    GenomeRNAii 80010.
    NextBioi 70103.
    PROi Q9H9A7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H9A7.
    CleanExi HS_RMI1.
    Genevestigatori Q9H9A7.

    Family and domain databases

    InterProi IPR013894. DUF1767.
    [Graphical view ]
    Pfami PF08585. DUF1767. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 SER-455.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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], VARIANTS HIS-100 AND SER-455.
      Tissue: Brain, Skin, Testis and Uterus.
    4. "BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity."
      Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W.
      EMBO J. 24:1465-1476(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH BLM AND TOP3A, SUBCELLULAR LOCATION.
    5. "A double Holliday junction dissolvasome comprising BLM, topoisomerase III alpha, and BLAP75."
      Raynard S., Bussen W., Sung P.
      J. Biol. Chem. 281:13861-13864(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BLM AND TOP3A.
    6. "BLAP75/RMI1 promotes the BLM-dependent dissolution of homologous recombination intermediates."
      Wu L., Bachrati C.Z., Ou J., Xu C., Yin J., Chang M., Wang W., Li L., Brown G.W., Hickson I.D.
      Proc. Natl. Acad. Sci. U.S.A. 103:4068-4073(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BINDING TO DOUBLE HOLLIDAY JUNCTION, INTERACTION WITH TOP3A.
    7. "RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability."
      Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W., Hoatlin M.E., Hickson I.D., Wang W.
      Genes Dev. 22:2843-2855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RMI COMPLEX, INTERACTION WITH RMI2.
    8. "BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome."
      Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H., Andreassen P.R., Sung P., Meetei A.R.
      Genes Dev. 22:2856-2868(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RMI COMPLEX, INTERACTION WITH RMI2.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
      Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
      Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLM.

    Entry informationi

    Entry nameiRMI1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9A7
    Secondary accession number(s): Q05BX1
    , Q05CW3, Q5SQG8, Q5SQG9, Q6P1Q4, Q6PI89, Q7Z6L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 103 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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