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P35232

- PHB_HUMAN

UniProt

P35232 - PHB_HUMAN

Protein

Prohibitin

Gene

PHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Prohibitin inhibits DNA synthesis. It has a role in regulating proliferation. As yet it is unclear if the protein or the mRNA exhibits this effect. May play a role in regulating mitochondrial respiration activity and in aging.1 Publication

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. histone deacetylase binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
    5. transcription regulatory region DNA binding Source: BHF-UCL

    GO - Biological processi

    1. cellular response to interleukin-6 Source: BHF-UCL
    2. DNA biosynthetic process Source: Ensembl
    3. DNA replication Source: UniProtKB-KW
    4. histone deacetylation Source: UniProtKB
    5. negative regulation of androgen receptor signaling pathway Source: BHF-UCL
    6. negative regulation of cell growth Source: BHF-UCL
    7. negative regulation of cell proliferation Source: BHF-UCL
    8. negative regulation of glucocorticoid receptor signaling pathway Source: BHF-UCL
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. negative regulation of transcription by competitive promoter binding Source: BHF-UCL
    11. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    12. osteoblast differentiation Source: UniProt
    13. positive regulation of transcription, DNA-templated Source: UniProtKB
    14. progesterone receptor signaling pathway Source: BHF-UCL
    15. regulation of apoptotic process Source: UniProtKB
    16. regulation of transcription, DNA-templated Source: UniProtKB
    17. signal transduction Source: UniProtKB

    Keywords - Biological processi

    DNA synthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prohibitin
    Gene namesi
    Name:PHB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8912. PHB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: HGNC
    4. membrane Source: UniProtKB
    5. mitochondrial inner membrane Source: UniProtKB
    6. mitochondrion Source: LIFEdb
    7. nucleoplasm Source: UniProtKB
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA33251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 272272ProhibitinPRO_0000213878Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281N6-acetyllysineBy similarity
    Modified residuei186 – 1861N6-acetyllysineBy similarity
    Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
    Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
    Modified residuei249 – 2491PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP35232.
    PaxDbiP35232.
    PeptideAtlasiP35232.
    PRIDEiP35232.

    2D gel databases

    DOSAC-COBS-2DPAGEP35232.
    OGPiP35232.
    REPRODUCTION-2DPAGEIPI00017334.
    P35232.
    SWISS-2DPAGEP35232.
    UCD-2DPAGEP35232.

    PTM databases

    PhosphoSiteiP35232.

    Expressioni

    Tissue specificityi

    Widely expressed in different tissues.

    Developmental stagei

    Levels of expression in fibroblasts decrease heterogeneously during cellular aging.1 Publication

    Inductioni

    Expression increases approximately 3-fold upon entry into G1 phase compared with other phases of the cell cycle. Also induced following inhibition of mitochondrial protein synthesis by thiamphenicol.1 Publication

    Gene expression databases

    ArrayExpressiP35232.
    BgeeiP35232.
    CleanExiHS_PHB.
    GenevestigatoriP35232.

    Organism-specific databases

    HPAiHPA003280.

    Interactioni

    Subunit structurei

    Interacts with PHB2. Interacts with STOML2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LONRF3Q496Y02EBI-354213,EBI-2690768
    SKP2Q13309-22EBI-354213,EBI-7791408
    XPO1O149802EBI-354213,EBI-355867

    Protein-protein interaction databases

    BioGridi111264. 74 interactions.
    DIPiDIP-24248N.
    IntActiP35232. 59 interactions.
    MINTiMINT-1158239.
    STRINGi9606.ENSP00000300408.

    Structurei

    Secondary structure

    1
    272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 185
    Turni19 – 213
    Beta strandi22 – 276
    Beta strandi29 – 335
    Beta strandi50 – 523
    Beta strandi54 – 607
    Beta strandi65 – 673
    Turni87 – 893
    Helixi99 – 11012
    Helixi115 – 1184
    Helixi123 – 14422
    Helixi146 – 15510
    Beta strandi157 – 1593
    Beta strandi165 – 1673
    Helixi172 – 19120
    Helixi194 – 21118
    Helixi212 – 2143
    Turni217 – 2226
    Helixi224 – 24017
    Turni242 – 2465
    Helixi247 – 2526

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LU7model-A1-272[»]
    ProteinModelPortaliP35232.
    SMRiP35232. Positions 61-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili177 – 21135Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the prohibitin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0330.
    HOGENOMiHOG000205692.
    HOVERGENiHBG004457.
    InParanoidiP35232.
    KOiK17080.
    OMAiIIFDVRS.
    OrthoDBiEOG7V4B04.
    PhylomeDBiP35232.
    TreeFamiTF300095.

    Family and domain databases

    InterProiIPR001107. Band_7.
    IPR000163. Prohibitin.
    [Graphical view]
    PANTHERiPTHR23222. PTHR23222. 1 hit.
    PfamiPF01145. Band_7. 1 hit.
    [Graphical view]
    PRINTSiPR00679. PROHIBITIN.
    SMARTiSM00244. PHB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35232-1) [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

    MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV    50
    GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA 100
    SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV 150
    SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV 200
    EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ 250
    LSRSRNITYL PAGQSVLLQL PQ 272
    Length:272
    Mass (Da):29,804
    Last modified:February 1, 1994 - v1
    Checksum:i915494273E342C76
    GO
    Isoform 2 (identifier: P35232-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         140-256: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:155
    Mass (Da):17,018
    Checksum:iFDFDE03209523798
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881V → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_006479
    Natural varianti105 – 1051R → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_006480

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei140 – 256117Missing in isoform 2. 1 PublicationVSP_054922Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S85655 mRNA. Translation: AAB21614.1.
    L14272 Genomic DNA. Translation: AAO18340.1.
    BT007411 mRNA. Translation: AAP36079.1.
    AK302258 mRNA. Translation: BAG63609.1.
    AC091180 Genomic DNA. No translation available.
    BC013401 mRNA. Translation: AAH13401.1.
    BC095460 mRNA. Translation: AAH95460.1.
    CCDSiCCDS11548.1. [P35232-1]
    CCDS62244.1. [P35232-2]
    PIRiI52690.
    RefSeqiNP_001268425.1. NM_001281496.1. [P35232-1]
    NP_001268426.1. NM_001281497.1. [P35232-2]
    NP_001268644.1. NM_001281715.1. [P35232-1]
    NP_002625.1. NM_002634.3. [P35232-1]
    UniGeneiHs.514303.

    Genome annotation databases

    EnsembliENST00000300408; ENSP00000300408; ENSG00000167085. [P35232-1]
    ENST00000511832; ENSP00000425035; ENSG00000167085. [P35232-2]
    GeneIDi5245.
    KEGGihsa:5245.
    UCSCiuc002iox.1. human. [P35232-1]

    Polymorphism databases

    DMDMi464371.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S85655 mRNA. Translation: AAB21614.1 .
    L14272 Genomic DNA. Translation: AAO18340.1 .
    BT007411 mRNA. Translation: AAP36079.1 .
    AK302258 mRNA. Translation: BAG63609.1 .
    AC091180 Genomic DNA. No translation available.
    BC013401 mRNA. Translation: AAH13401.1 .
    BC095460 mRNA. Translation: AAH95460.1 .
    CCDSi CCDS11548.1. [P35232-1 ]
    CCDS62244.1. [P35232-2 ]
    PIRi I52690.
    RefSeqi NP_001268425.1. NM_001281496.1. [P35232-1 ]
    NP_001268426.1. NM_001281497.1. [P35232-2 ]
    NP_001268644.1. NM_001281715.1. [P35232-1 ]
    NP_002625.1. NM_002634.3. [P35232-1 ]
    UniGenei Hs.514303.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LU7 model - A 1-272 [» ]
    ProteinModelPortali P35232.
    SMRi P35232. Positions 61-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111264. 74 interactions.
    DIPi DIP-24248N.
    IntActi P35232. 59 interactions.
    MINTi MINT-1158239.
    STRINGi 9606.ENSP00000300408.

    PTM databases

    PhosphoSitei P35232.

    Polymorphism databases

    DMDMi 464371.

    2D gel databases

    DOSAC-COBS-2DPAGE P35232.
    OGPi P35232.
    REPRODUCTION-2DPAGE IPI00017334.
    P35232.
    SWISS-2DPAGE P35232.
    UCD-2DPAGE P35232.

    Proteomic databases

    MaxQBi P35232.
    PaxDbi P35232.
    PeptideAtlasi P35232.
    PRIDEi P35232.

    Protocols and materials databases

    DNASUi 5245.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300408 ; ENSP00000300408 ; ENSG00000167085 . [P35232-1 ]
    ENST00000511832 ; ENSP00000425035 ; ENSG00000167085 . [P35232-2 ]
    GeneIDi 5245.
    KEGGi hsa:5245.
    UCSCi uc002iox.1. human. [P35232-1 ]

    Organism-specific databases

    CTDi 5245.
    GeneCardsi GC17M047481.
    HGNCi HGNC:8912. PHB.
    HPAi HPA003280.
    MIMi 176705. gene.
    neXtProti NX_P35232.
    PharmGKBi PA33251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0330.
    HOGENOMi HOG000205692.
    HOVERGENi HBG004457.
    InParanoidi P35232.
    KOi K17080.
    OMAi IIFDVRS.
    OrthoDBi EOG7V4B04.
    PhylomeDBi P35232.
    TreeFami TF300095.

    Miscellaneous databases

    GeneWikii Prohibitin.
    GenomeRNAii 5245.
    NextBioi 20266.
    PROi P35232.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35232.
    Bgeei P35232.
    CleanExi HS_PHB.
    Genevestigatori P35232.

    Family and domain databases

    InterProi IPR001107. Band_7.
    IPR000163. Prohibitin.
    [Graphical view ]
    PANTHERi PTHR23222. PTHR23222. 1 hit.
    Pfami PF01145. Band_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00679. PROHIBITIN.
    SMARTi SM00244. PHB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human prohibitin gene located on chromosome 17q21 is mutated in sporadic breast cancer."
      Sato T., Saito H., Swensen J., Olifant A., Wood C., Danner D., Sakamoto T., Takita K., Kasumi F., Miki Y., Skolnick M., Nakamura Y.
      Cancer Res. 52:1643-1646(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-88 AND HIS-105.
      Tissue: Mammary gland.
    2. "The human prohibitin (PHB) gene family and its somatic mutations in human tumors."
      Sato T., Sakamoto T., Takita K., Saito H., Okui K., Nakamura Y.
      Genomics 17:762-764(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 2).
      Tissue: Testis.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Lung and Muscle.
    7. Bienvenut W.V.
      Submitted (MAR-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 5-11; 84-93; 106-128; 134-143; 178-186 AND 209-219, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 75-83; 94-117; 134-143; 158-177; 220-253 AND 256-272, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence."
      Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H., Hall P.A., Wright E.G.
      Exp. Cell Res. 265:262-273(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PHB2, DEVELOPMENTAL STAGE, INDUCTION.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
      Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.
      Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STOML2.

    Entry informationi

    Entry nameiPHB_HUMAN
    AccessioniPrimary (citable) accession number: P35232
    Secondary accession number(s): B4DY47, Q4VBQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 144 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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