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P01213

- PDYN_HUMAN

UniProt

P01213 - PDYN_HUMAN

Protein

Proenkephalin-B

Gene

PDYN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress By similarity.By similarity
    Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin By similarity.By similarity
    Leumorphin has a typical opiod activity and may have anti-apoptotic effect.By similarity

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. neuropeptide signaling pathway Source: UniProtKB-KW
    3. synaptic transmission Source: UniProtKB-KW

    Keywords - Molecular functioni

    Endorphin, Neuropeptide, Neurotransmitter, Opioid peptide

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_15295. Opioid Signalling.
    REACT_15457. G-protein activation.
    REACT_19231. G alpha (i) signalling events.

    Protein family/group databases

    TCDBi1.C.89.1.1. the dynorphin channel-forming neuropeptide (dynorphin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proenkephalin-B
    Alternative name(s):
    Beta-neoendorphin-dynorphin
    Preprodynorphin
    Cleaved into the following 9 chains:
    Big dynorphin
    Short name:
    Big Dyn
    Dynorphin A(1-17)
    Short name:
    Dyn-A17
    Short name:
    Dynorphin A
    Alternative name(s):
    Dynorphin B
    Short name:
    Dyn-B
    Dynorphin B(1-13)
    Alternative name(s):
    Dynorphin B-29
    Gene namesi
    Name:PDYN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:8820. PDYN.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia 23 (SCA23) [MIM:610245]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA23 is an adult-onset autosomal dominant form characterized by slowly progressive gait and limb ataxia, with variable additional features, including peripheral neuropathy and dysarthria.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381R → S in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue. 1 Publication
    VAR_064913
    Natural varianti211 – 2111L → S in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons. 1 Publication
    VAR_064914
    Natural varianti212 – 2121R → W in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect. 1 Publication
    Corresponds to variant rs201486601 [ dbSNP | Ensembl ].
    VAR_064915
    Natural varianti215 – 2151R → C in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect. 1 Publication
    VAR_064916

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi610245. phenotype.
    Orphaneti101108. Spinocerebellar ataxia type 23.
    PharmGKBiPA33163.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Propeptidei21 – 172152PRO_0000008176Add
    BLAST
    Peptidei175 – 18410Alpha-neoendorphinPRO_0000306347
    Peptidei175 – 1839Beta-neoendorphinPRO_0000008177
    Peptidei175 – 1795Leu-enkephalinBy similarityPRO_0000306348
    Propeptidei186 – 20419PRO_0000008178Add
    BLAST
    Peptidei207 – 23832Big dynorphinPRO_0000306349Add
    BLAST
    Peptidei207 – 22317Dynorphin A(1-17)PRO_0000008179Add
    BLAST
    Peptidei207 – 21913Dynorphin A(1-13)By similarityPRO_0000306350Add
    BLAST
    Peptidei207 – 2148Dynorphin A(1-8)By similarityPRO_0000306351
    Peptidei207 – 2115Leu-enkephalinBy similarityPRO_0000306352
    Peptidei226 – 25429LeumorphinPRO_0000008180Add
    BLAST
    Peptidei226 – 23813RimorphinPRO_0000008181Add
    BLAST
    Peptidei226 – 2305Leu-enkephalinPRO_0000008182

    Post-translational modificationi

    The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiP01213.
    PeptideAtlasiP01213.
    PRIDEiP01213.

    PTM databases

    PhosphoSiteiP01213.

    Miscellaneous databases

    PMAP-CutDBP01213.

    Expressioni

    Gene expression databases

    ArrayExpressiP01213.
    BgeeiP01213.
    CleanExiHS_PDYN.
    GenevestigatoriP01213.

    Organism-specific databases

    HPAiHPA049841.
    HPA053342.

    Interactioni

    Protein-protein interaction databases

    BioGridi111199. 1 interaction.
    STRINGi9606.ENSP00000217305.

    Structurei

    3D structure databases

    ProteinModelPortaliP01213.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG46156.
    HOGENOMiHOG000013003.
    HOVERGENiHBG000063.
    InParanoidiP01213.
    KOiK15840.
    OMAiWERCQGL.
    OrthoDBiEOG7BW0K5.
    PhylomeDBiP01213.
    TreeFamiTF332620.

    Family and domain databases

    InterProiIPR006024. Opioid_neupept.
    IPR000750. Proenkphlin_B.
    [Graphical view]
    PANTHERiPTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF4. PTHR11438:SF4. 1 hit.
    PfamiPF01160. Opiods_neuropep. 1 hit.
    [Graphical view]
    PRINTSiPR01028. OPIOIDPRCRSR.
    PR01030. PENKBPRCRSR.
    PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01213-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWQGLVLAA CLLMFPSTTA DCLSRCSLCA VKTQDGPKPI NPLICSLQCQ    50
    AALLPSEEWE RCQSFLSFFT PSTLGLNDKE DLGSKSVGEG PYSELAKLSG 100
    SFLKELEKSK FLPSISTKEN TLSKSLEEKL RGLSDGFREG AESELMRDAQ 150
    LNDGAMETGT LYLAEEDPKE QVKRYGGFLR KYPKRSSEVA GEGDGDSMGH 200
    EDLYKRYGGF LRRIRPKLKW DNQKRYGGFL RRQFKVVTRS QEDPNAYSGE 250
    LFDA 254
    Length:254
    Mass (Da):28,385
    Last modified:July 21, 1986 - v1
    Checksum:i783E7D6AC068CE68
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381R → S in SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue. 1 Publication
    VAR_064913
    Natural varianti211 – 2111L → S in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons. 1 Publication
    VAR_064914
    Natural varianti212 – 2121R → W in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect. 1 Publication
    Corresponds to variant rs201486601 [ dbSNP | Ensembl ].
    VAR_064915
    Natural varianti215 – 2151R → C in SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect. 1 Publication
    VAR_064916

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02536 Genomic DNA. No translation available.
    K02267 Genomic DNA. No translation available.
    AH002816 Genomic DNA. Translation: AAA58456.2.
    X00176 Genomic DNA. Translation: CAA24999.1.
    AK289618 mRNA. Translation: BAF82307.1.
    AL034562 Genomic DNA. Translation: CAB38875.1.
    CH471133 Genomic DNA. Translation: EAX10604.1.
    BC026334 mRNA. Translation: AAH26334.1.
    CCDSiCCDS13023.1.
    PIRiA01478. DFHU.
    RefSeqiNP_001177821.1. NM_001190892.1.
    NP_001177827.1. NM_001190898.2.
    NP_001177828.1. NM_001190899.2.
    NP_001177829.1. NM_001190900.1.
    NP_077722.1. NM_024411.4.
    UniGeneiHs.22584.

    Genome annotation databases

    EnsembliENST00000217305; ENSP00000217305; ENSG00000101327.
    ENST00000539905; ENSP00000440185; ENSG00000101327.
    ENST00000540134; ENSP00000442259; ENSG00000101327.
    GeneIDi5173.
    KEGGihsa:5173.
    UCSCiuc002wfv.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02536 Genomic DNA. No translation available.
    K02267 Genomic DNA. No translation available.
    AH002816 Genomic DNA. Translation: AAA58456.2 .
    X00176 Genomic DNA. Translation: CAA24999.1 .
    AK289618 mRNA. Translation: BAF82307.1 .
    AL034562 Genomic DNA. Translation: CAB38875.1 .
    CH471133 Genomic DNA. Translation: EAX10604.1 .
    BC026334 mRNA. Translation: AAH26334.1 .
    CCDSi CCDS13023.1.
    PIRi A01478. DFHU.
    RefSeqi NP_001177821.1. NM_001190892.1.
    NP_001177827.1. NM_001190898.2.
    NP_001177828.1. NM_001190899.2.
    NP_001177829.1. NM_001190900.1.
    NP_077722.1. NM_024411.4.
    UniGenei Hs.22584.

    3D structure databases

    ProteinModelPortali P01213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111199. 1 interaction.
    STRINGi 9606.ENSP00000217305.

    Chemistry

    BindingDBi P01213.
    ChEMBLi CHEMBL2227.

    Protein family/group databases

    TCDBi 1.C.89.1.1. the dynorphin channel-forming neuropeptide (dynorphin) family.

    PTM databases

    PhosphoSitei P01213.

    Proteomic databases

    PaxDbi P01213.
    PeptideAtlasi P01213.
    PRIDEi P01213.

    Protocols and materials databases

    DNASUi 5173.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217305 ; ENSP00000217305 ; ENSG00000101327 .
    ENST00000539905 ; ENSP00000440185 ; ENSG00000101327 .
    ENST00000540134 ; ENSP00000442259 ; ENSG00000101327 .
    GeneIDi 5173.
    KEGGi hsa:5173.
    UCSCi uc002wfv.3. human.

    Organism-specific databases

    CTDi 5173.
    GeneCardsi GC20M001907.
    HGNCi HGNC:8820. PDYN.
    HPAi HPA049841.
    HPA053342.
    MIMi 131340. gene.
    610245. phenotype.
    neXtProti NX_P01213.
    Orphaneti 101108. Spinocerebellar ataxia type 23.
    PharmGKBi PA33163.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46156.
    HOGENOMi HOG000013003.
    HOVERGENi HBG000063.
    InParanoidi P01213.
    KOi K15840.
    OMAi WERCQGL.
    OrthoDBi EOG7BW0K5.
    PhylomeDBi P01213.
    TreeFami TF332620.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_15295. Opioid Signalling.
    REACT_15457. G-protein activation.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GenomeRNAii 5173.
    NextBioi 20018.
    PMAP-CutDB P01213.
    PROi P01213.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01213.
    Bgeei P01213.
    CleanExi HS_PDYN.
    Genevestigatori P01213.

    Family and domain databases

    InterProi IPR006024. Opioid_neupept.
    IPR000750. Proenkphlin_B.
    [Graphical view ]
    PANTHERi PTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF4. PTHR11438:SF4. 1 hit.
    Pfami PF01160. Opiods_neuropep. 1 hit.
    [Graphical view ]
    PRINTSi PR01028. OPIOIDPRCRSR.
    PR01030. PENKBPRCRSR.
    PROSITEi PS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and structural organization of the human preproenkephalin B gene."
      Horikawa S., Takai T., Toyosato M., Takahashi H., Noda M., Kakidani H., Kubo T., Hirose T., Inayama S., Hayashida H., Miyata T., Numa S.
      Nature 306:611-614(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Tissue: Amygdala.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain.
    6. "NMR and structural model of dynorphin A (1-17) bound to dodecylphosphocholine micelles."
      Tessmer M.R., Kallick D.A.
      Biochemistry 36:1971-1981(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF DYNORPHIN A(1-17).
    7. "Dynorphin peptides differentially regulate the human kappa opioid receptor."
      Chen Y., Chen C., Liu-Chen L.-Y.
      Life Sci. 80:1439-1448(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Big dynorphin as a putative endogenous ligand for the kappa-opioid receptor."
      Merg F., Filliol D., Usynin I., Bazov I., Bark N., Hurd Y.L., Yakovleva T., Kieffer B.L., Bakalkin G.
      J. Neurochem. 97:292-301(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: VARIANTS SCA23 SER-138; SER-211; TRP-212 AND CYS-215, CHARACTERIZATION OF VARIANTS SCA23 SER-138; SER-211; TRP-212 AND CYS-215.

    Entry informationi

    Entry nameiPDYN_HUMAN
    AccessioniPrimary (citable) accession number: P01213
    Secondary accession number(s): A8K0Q3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 132 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 20
      Human chromosome 20: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3