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Q9NZL4

- HPBP1_HUMAN

UniProt

Q9NZL4 - HPBP1_HUMAN

Protein

Hsp70-binding protein 1

Gene

HSPBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.4 Publications

    GO - Molecular functioni

    1. enzyme inhibitor activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. negative regulation of catalytic activity Source: GOC
    2. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
    3. positive regulation of protein ubiquitination Source: BHF-UCL
    4. protein folding Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hsp70-binding protein 1
    Short name:
    HspBP1
    Alternative name(s):
    Heat shock protein-binding protein 1
    Hsp70-binding protein 2
    Short name:
    HspBP2
    Hsp70-interacting protein 1
    Hsp70-interacting protein 2
    Gene namesi
    Name:HSPBP1
    Synonyms:HSPBP
    ORF Names:PP1845
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:24989. HSPBP1.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164720725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Hsp70-binding protein 1PRO_0000084035Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei354 – 3541Phosphoserine1 Publication
    Modified residuei359 – 3591Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NZL4.
    PaxDbiQ9NZL4.
    PRIDEiQ9NZL4.

    PTM databases

    PhosphoSiteiQ9NZL4.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9NZL4.
    BgeeiQ9NZL4.
    GenevestigatoriQ9NZL4.

    Organism-specific databases

    HPAiCAB005865.

    Interactioni

    Subunit structurei

    Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSPA2P546523EBI-356763,EBI-356991

    Protein-protein interaction databases

    BioGridi117168. 37 interactions.
    IntActiQ9NZL4. 11 interactions.
    MINTiMINT-1158196.
    STRINGi9606.ENSP00000255631.

    Structurei

    Secondary structure

    1
    362
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi90 – 10415
    Helixi113 – 13422
    Helixi137 – 1459
    Helixi148 – 1547
    Turni155 – 1584
    Helixi162 – 17615
    Helixi180 – 1889
    Helixi191 – 20111
    Helixi205 – 21915
    Helixi223 – 2319
    Helixi234 – 24310
    Helixi247 – 26317
    Helixi265 – 2673
    Helixi268 – 2736
    Helixi276 – 2849
    Helixi291 – 30313
    Helixi307 – 3148
    Helixi316 – 3183
    Helixi320 – 33112
    Helixi335 – 3373
    Helixi338 – 35114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XQRX-ray2.10A/B87-362[»]
    1XQSX-ray2.90A/B87-362[»]
    ProteinModelPortaliQ9NZL4.
    SMRiQ9NZL4. Positions 87-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZL4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati135 – 17743ARM 1Add
    BLAST
    Repeati180 – 22041ARM 2Add
    BLAST
    Repeati223 – 26240ARM 3Add
    BLAST
    Repeati265 – 30440ARM 4Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi21 – 4020Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 4 ARM repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG235694.
    HOVERGENiHBG053282.
    InParanoidiQ9NZL4.
    KOiK09562.
    OrthoDBiEOG7N37D8.
    PhylomeDBiQ9NZL4.
    TreeFamiTF324307.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZL4-1) [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

    MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG    50
    LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL 100
    RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH 150
    LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD 200
    RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK 250
    VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC 300
    SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT 350
    CFSSPADDSM DR 362
    Length:362
    Mass (Da):39,474
    Last modified:October 1, 2000 - v1
    Checksum:i2B6AAB4161D5A326
    GO
    Isoform 2 (identifier: Q9NZL4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         207-309: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:259
    Mass (Da):28,024
    Checksum:i50A959E12693AF09
    GO
    Isoform 3 (identifier: Q9NZL4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGGRRAPLKRRLLSRPSRIDPSGRQSCFSGDHLLPLTHSSLLHKRPM
         25-28: GGGG → V

    Note: No experimental confirmation available.

    Show »
    Length:405
    Mass (Da):44,516
    Checksum:iAF3566553A8B3EB3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti276 – 2761M → V in BAG57622. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 273Missing.4 Publications
    VAR_023645

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGGRRAPLKRRLLSRPSRID PSGRQSCFSGDHLLPLTHSS LLHKRPM in isoform 3. 1 PublicationVSP_053681
    Alternative sequencei25 – 284GGGG → V in isoform 3. 1 PublicationVSP_053682
    Alternative sequencei207 – 309103Missing in isoform 2. 1 PublicationVSP_015945Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF093420 mRNA. Translation: AAC79703.1.
    AF187859 mRNA. Translation: AAF35833.1.
    AB020592 mRNA. Translation: BAB18742.1.
    AF217996 mRNA. Translation: AAG17238.1.
    AK130636 mRNA. Translation: BAC85399.1.
    AK294358 mRNA. Translation: BAG57622.1.
    CR457118 mRNA. Translation: CAG33399.1.
    AK075293 mRNA. Translation: BAG52102.1.
    BC001236 mRNA. Translation: AAH01236.1.
    BC002373 mRNA. Translation: AAH02373.1.
    RefSeqiNP_001123578.1. NM_001130106.1.
    NP_036399.3. NM_012267.4.
    UniGeneiHs.53066.

    Genome annotation databases

    EnsembliENST00000255631; ENSP00000255631; ENSG00000133265.
    ENST00000433386; ENSP00000398244; ENSG00000133265.
    ENST00000587922; ENSP00000467574; ENSG00000133265.
    GeneIDi23640.
    KEGGihsa:23640.
    UCSCiuc002qkc.3. human. [Q9NZL4-1]

    Polymorphism databases

    DMDMi74734730.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF093420 mRNA. Translation: AAC79703.1 .
    AF187859 mRNA. Translation: AAF35833.1 .
    AB020592 mRNA. Translation: BAB18742.1 .
    AF217996 mRNA. Translation: AAG17238.1 .
    AK130636 mRNA. Translation: BAC85399.1 .
    AK294358 mRNA. Translation: BAG57622.1 .
    CR457118 mRNA. Translation: CAG33399.1 .
    AK075293 mRNA. Translation: BAG52102.1 .
    BC001236 mRNA. Translation: AAH01236.1 .
    BC002373 mRNA. Translation: AAH02373.1 .
    RefSeqi NP_001123578.1. NM_001130106.1.
    NP_036399.3. NM_012267.4.
    UniGenei Hs.53066.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XQR X-ray 2.10 A/B 87-362 [» ]
    1XQS X-ray 2.90 A/B 87-362 [» ]
    ProteinModelPortali Q9NZL4.
    SMRi Q9NZL4. Positions 87-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117168. 37 interactions.
    IntActi Q9NZL4. 11 interactions.
    MINTi MINT-1158196.
    STRINGi 9606.ENSP00000255631.

    PTM databases

    PhosphoSitei Q9NZL4.

    Polymorphism databases

    DMDMi 74734730.

    Proteomic databases

    MaxQBi Q9NZL4.
    PaxDbi Q9NZL4.
    PRIDEi Q9NZL4.

    Protocols and materials databases

    DNASUi 23640.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255631 ; ENSP00000255631 ; ENSG00000133265 .
    ENST00000433386 ; ENSP00000398244 ; ENSG00000133265 .
    ENST00000587922 ; ENSP00000467574 ; ENSG00000133265 .
    GeneIDi 23640.
    KEGGi hsa:23640.
    UCSCi uc002qkc.3. human. [Q9NZL4-1 ]

    Organism-specific databases

    CTDi 23640.
    GeneCardsi GC19M055773.
    H-InvDB HIX0015460.
    HGNCi HGNC:24989. HSPBP1.
    HPAi CAB005865.
    MIMi 612939. gene.
    neXtProti NX_Q9NZL4.
    PharmGKBi PA164720725.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235694.
    HOVERGENi HBG053282.
    InParanoidi Q9NZL4.
    KOi K09562.
    OrthoDBi EOG7N37D8.
    PhylomeDBi Q9NZL4.
    TreeFami TF324307.

    Miscellaneous databases

    ChiTaRSi HSPBP1. human.
    EvolutionaryTracei Q9NZL4.
    GeneWikii HSPBP1.
    GenomeRNAii 23640.
    NextBioi 35471637.
    PROi Q9NZL4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZL4.
    Bgeei Q9NZL4.
    Genevestigatori Q9NZL4.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein."
      Raynes D.A., Guerriero V. Jr.
      J. Biol. Chem. 273:32883-32888(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL, FUNCTION, INTERACTION WITH HSPA1A, TISSUE SPECIFICITY.
      Tissue: Heart.
    2. "Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70."
      Guerriero V. Jr., Raynes D.A.
      Biochim. Biophys. Acta 1490:203-207(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, POLYMORPHISM OF POLY-GLY REGION.
      Tissue: Heart.
    3. Tanimura S., Tsujimoto M., Kohno M.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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] (ISOFORMS 2 AND 3).
      Tissue: Amygdala and Spleen.
    6. "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] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL.
    7. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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), VARIANT 25-GLY--GLY-27 DEL.
      Tissue: Lung and Placenta.
    9. "HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain."
      McLellan C.A., Raynes D.A., Guerriero V. Jr.
      J. Biol. Chem. 278:19017-19022(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSPA1A.
    10. "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator."
      Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.
      Mol. Biol. Cell 15:4003-4010(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSPA1A AND STUB1.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange."
      Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C., Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.
      Mol. Cell 17:367-379(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-362 IN COMPLEX WITH HSPA1A.

    Entry informationi

    Entry nameiHPBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZL4
    Secondary accession number(s): B3KQP0
    , B4DG11, O95351, Q6ZNU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 105 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, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3