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Q9NX24

- NHP2_HUMAN

UniProt

Q9NX24 - NHP2_HUMAN

Protein

H/ACA ribonucleoprotein complex subunit 2

Gene

NHP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.1 Publication

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. snoRNA binding Source: UniProtKB

    GO - Biological processi

    1. rRNA pseudouridine synthesis Source: UniProtKB

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_7974. Telomere Extension By Telomerase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    H/ACA ribonucleoprotein complex subunit 2
    Alternative name(s):
    Nucleolar protein family A member 2
    snoRNP protein NHP2
    Gene namesi
    Name:NHP2
    Synonyms:NOLA2
    ORF Names:HSPC286
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:14377. NHP2.

    Subcellular locationi

    Nucleusnucleolus. NucleusCajal body
    Note: Also localized to Cajal bodies (coiled bodies).

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. nucleus Source: HPA
    4. small nucleolar ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Dyskeratosis congenita, autosomal recessive, 2 (DKCB2) [MIM:613987]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti126 – 1261V → M in DKCB2. 1 Publication
    Corresponds to variant rs121908090 [ dbSNP | Ensembl ].
    VAR_065871
    Natural varianti139 – 1391Y → H in DKCB2. 1 Publication
    Corresponds to variant rs121908089 [ dbSNP | Ensembl ].
    VAR_065872

    Keywords - Diseasei

    Disease mutation, Dyskeratosis congenita

    Organism-specific databases

    MIMi613987. phenotype.
    Orphaneti1775. Dyskeratosis congenita.
    PharmGKBiPA164723898.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 153153H/ACA ribonucleoprotein complex subunit 2PRO_0000136763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei19 – 191Phosphoserine1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NX24.
    PaxDbiQ9NX24.
    PeptideAtlasiQ9NX24.
    PRIDEiQ9NX24.

    2D gel databases

    SWISS-2DPAGEQ9NX24.

    PTM databases

    PhosphoSiteiQ9NX24.

    Expressioni

    Tissue specificityi

    Expressed in brain, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus. Also expressed at lower levels in the liver.1 Publication

    Developmental stagei

    Transcript peaks at G1/S transition.1 Publication

    Gene expression databases

    ArrayExpressiQ9NX24.
    BgeeiQ9NX24.
    CleanExiHS_NHP2.
    GenevestigatoriQ9NX24.

    Organism-specific databases

    HPAiHPA044171.
    HPA050400.

    Interactioni

    Subunit structurei

    Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC).2 Publications

    Protein-protein interaction databases

    BioGridi120783. 24 interactions.
    IntActiQ9NX24. 9 interactions.
    MINTiMINT-3077751.
    STRINGi9606.ENSP00000274606.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NX24.
    SMRiQ9NX24. Positions 40-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L7Ae family.Curated

    Phylogenomic databases

    eggNOGiCOG1358.
    HOGENOMiHOG000055227.
    HOVERGENiHBG000328.
    InParanoidiQ9NX24.
    KOiK11129.
    OMAiPVDIMCH.
    OrthoDBiEOG7288T8.
    PhylomeDBiQ9NX24.
    TreeFamiTF105839.

    Family and domain databases

    Gene3Di3.30.1330.30. 1 hit.
    InterProiIPR002415. H/ACA_rnp_Nhp2_euk.
    IPR029064. L30e-like.
    IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
    IPR018492. Ribosomal_L7Ae/L8/Nhp2.
    [Graphical view]
    PfamiPF01248. Ribosomal_L7Ae. 1 hit.
    [Graphical view]
    PRINTSiPR00881. L7ARS6FAMILY.
    PR00883. NUCLEARHMG.
    SUPFAMiSSF55315. SSF55315. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9NX24-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC    50
    IKKAVKQKQI RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED 100
    RNLPYVYIPS KTDLGAAAGS KRPTCVIMVK PHEEYQEAYD ECLEEVQSLP 150
    LPL 153
    Length:153
    Mass (Da):17,201
    Last modified:October 1, 2000 - v1
    Checksum:i7658FDFF88AF3178
    GO

    Sequence cautioni

    The sequence AAF28964.1 differs from that shown. Reason: Frameshift at positions 37, 119 and 120.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181A → T.1 Publication
    Corresponds to variant rs139588879 [ dbSNP | Ensembl ].
    VAR_065870
    Natural varianti126 – 1261V → M in DKCB2. 1 Publication
    Corresponds to variant rs121908090 [ dbSNP | Ensembl ].
    VAR_065871
    Natural varianti139 – 1391Y → H in DKCB2. 1 Publication
    Corresponds to variant rs121908089 [ dbSNP | Ensembl ].
    VAR_065872

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293309 mRNA. Translation: CAC08452.1.
    AF401219 mRNA. Translation: AAL02175.1.
    AF161404 mRNA. Translation: AAF28964.1. Frameshift.
    AK000486 mRNA. Translation: BAA91198.1.
    CR457238 mRNA. Translation: CAG33519.1.
    AC136632 Genomic DNA. No translation available.
    BC000009 mRNA. Translation: AAH00009.1.
    BC006387 mRNA. Translation: AAH06387.1.
    CCDSiCCDS4432.1.
    RefSeqiNP_001030005.1. NM_001034833.1.
    NP_060308.1. NM_017838.3.
    UniGeneiHs.744074.

    Genome annotation databases

    EnsembliENST00000274606; ENSP00000274606; ENSG00000145912.
    GeneIDi55651.
    KEGGihsa:55651.
    UCSCiuc003mir.2. human.

    Polymorphism databases

    DMDMi68565945.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ293309 mRNA. Translation: CAC08452.1 .
    AF401219 mRNA. Translation: AAL02175.1 .
    AF161404 mRNA. Translation: AAF28964.1 . Frameshift.
    AK000486 mRNA. Translation: BAA91198.1 .
    CR457238 mRNA. Translation: CAG33519.1 .
    AC136632 Genomic DNA. No translation available.
    BC000009 mRNA. Translation: AAH00009.1 .
    BC006387 mRNA. Translation: AAH06387.1 .
    CCDSi CCDS4432.1.
    RefSeqi NP_001030005.1. NM_001034833.1.
    NP_060308.1. NM_017838.3.
    UniGenei Hs.744074.

    3D structure databases

    ProteinModelPortali Q9NX24.
    SMRi Q9NX24. Positions 40-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120783. 24 interactions.
    IntActi Q9NX24. 9 interactions.
    MINTi MINT-3077751.
    STRINGi 9606.ENSP00000274606.

    PTM databases

    PhosphoSitei Q9NX24.

    Polymorphism databases

    DMDMi 68565945.

    2D gel databases

    SWISS-2DPAGE Q9NX24.

    Proteomic databases

    MaxQBi Q9NX24.
    PaxDbi Q9NX24.
    PeptideAtlasi Q9NX24.
    PRIDEi Q9NX24.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274606 ; ENSP00000274606 ; ENSG00000145912 .
    GeneIDi 55651.
    KEGGi hsa:55651.
    UCSCi uc003mir.2. human.

    Organism-specific databases

    CTDi 55651.
    GeneCardsi GC05M177510.
    GeneReviewsi NHP2.
    HGNCi HGNC:14377. NHP2.
    HPAi HPA044171.
    HPA050400.
    MIMi 606470. gene.
    613987. phenotype.
    neXtProti NX_Q9NX24.
    Orphaneti 1775. Dyskeratosis congenita.
    PharmGKBi PA164723898.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1358.
    HOGENOMi HOG000055227.
    HOVERGENi HBG000328.
    InParanoidi Q9NX24.
    KOi K11129.
    OMAi PVDIMCH.
    OrthoDBi EOG7288T8.
    PhylomeDBi Q9NX24.
    TreeFami TF105839.

    Enzyme and pathway databases

    Reactomei REACT_7974. Telomere Extension By Telomerase.

    Miscellaneous databases

    ChiTaRSi NHP2. human.
    GeneWikii NOLA2.
    GenomeRNAii 55651.
    NextBioi 60350.
    PROi Q9NX24.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NX24.
    Bgeei Q9NX24.
    CleanExi HS_NHP2.
    Genevestigatori Q9NX24.

    Family and domain databases

    Gene3Di 3.30.1330.30. 1 hit.
    InterProi IPR002415. H/ACA_rnp_Nhp2_euk.
    IPR029064. L30e-like.
    IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
    IPR018492. Ribosomal_L7Ae/L8/Nhp2.
    [Graphical view ]
    Pfami PF01248. Ribosomal_L7Ae. 1 hit.
    [Graphical view ]
    PRINTSi PR00881. L7ARS6FAMILY.
    PR00883. NUCLEARHMG.
    SUPFAMi SSF55315. SSF55315. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human H/ACA small nucleolar RNPs and telomerase share evolutionarily conserved proteins NHP2 and NOP10."
      Pogacic V., Dragon F., Filipowicz W.
      Mol. Cell. Biol. 20:9028-9040(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GAR1; SMALL NUCLEOLAR RNAS AND TERC, SUBCELLULAR LOCATION.
    2. "Expression of the human homologue of the small nucleolar RNA-binding protein NHP2 gene during monocytic differentiation of U937 cells."
      Kang H.S., Jung H.M., Jun D., Huh T.L., Kim Y.H.
      Biochim. Biophys. Acta 1575:31-39(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    4. "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].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [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].
      Tissue: Muscle and Placenta.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins."
      Wang C., Meier U.T.
      EMBO J. 23:1857-1867(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
    11. "A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
      Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
      Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
    12. "A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58."
      Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E., Lamond A.I.
      Mol. Cell 39:618-631(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-5.
    13. "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-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Mutations in the telomerase component NHP2 cause the premature ageing syndrome dyskeratosis congenita."
      Vulliamy T., Beswick R., Kirwan M., Marrone A., Digweed M., Walne A., Dokal I.
      Proc. Natl. Acad. Sci. U.S.A. 105:8073-8078(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DKCB2 MET-126 AND HIS-139, VARIANT THR-118.

    Entry informationi

    Entry nameiNHP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NX24
    Secondary accession number(s): A6NKY8, Q9P095
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 128 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. Ribosomal proteins
      Ribosomal proteins families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3