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O94760

- DDAH1_HUMAN

UniProt

O94760 - DDAH1_HUMAN

Protein

N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

Gene

DDAH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.

    Catalytic activityi

    N(omega),N(omega)-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline.2 Publications

    Enzyme regulationi

    Inhibited by zinc ions By similarity. Enzyme purified in the absence of 1,10-phenanthroline contains on average 0.4 zinc atoms per subunit. Inhibited by 4-hydroxy-nonenal through the formation of a covalent adduct with His-173. Competitively inhibited by N(5)-iminopropyl-ornithine.By similarity2 Publications

    Kineticsi

    1. KM=69 µM for asymmetric dimethylarginine (ADMA)2 Publications
    2. KM=54 µM for monomethyl-L-arginine (MMA)2 Publications
    3. KM=3.1 µM for S-methyl-L-thiocitrulline2 Publications

    Vmax=356 nmol/min/mg enzyme with ADMA2 Publications

    Vmax=154 nmol/min/mg enzyme with NMA2 Publications

    pH dependencei

    Optimum pH is 8.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei30 – 301Substrate; via carbonyl oxygen
    Binding sitei73 – 731Substrate
    Binding sitei98 – 981Substrate
    Binding sitei145 – 1451Substrate
    Active sitei173 – 1731Proton donor1 Publication
    Binding sitei268 – 2681Substrate; via carbonyl oxygen
    Active sitei274 – 2741Nucleophile1 Publication
    Metal bindingi274 – 2741ZincBy similarity

    GO - Molecular functioni

    1. amino acid binding Source: Ensembl
    2. catalytic activity Source: ProtInc
    3. dimethylargininase activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine catabolic process Source: ProtInc
    2. citrulline metabolic process Source: UniProtKB
    3. nitric oxide mediated signal transduction Source: ProtInc
    4. positive regulation of angiogenesis Source: Ensembl
    5. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
    6. regulation of systemic arterial blood pressure Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (EC:3.5.3.18)
    Short name:
    DDAH-1
    Short name:
    Dimethylarginine dimethylaminohydrolase 1
    Alternative name(s):
    DDAHI
    Dimethylargininase-1
    Gene namesi
    Name:DDAH1
    Synonyms:DDAH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2715. DDAH1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301L → A: Reduces enzyme activity and affinity for asymmetric dimethylarginine about 12-fold. 1 Publication
    Mutagenesisi78 – 781E → A: Reduces enzyme activity about 1000-fold, and affinity for asymmetric dimethylarginine about 100-fold. 1 Publication
    Mutagenesisi271 – 2711L → G: Reduces enzyme activity about 10-fold, and affinity for asymmetric dimethylarginine about 7-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA27185.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 285284N(G),N(G)-dimethylarginine dimethylaminohydrolase 1PRO_0000171118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei222 – 2221S-nitrosocysteineBy similarity
    Modified residuei274 – 2741S-nitrosocysteineBy similarity

    Keywords - PTMi

    Acetylation, S-nitrosylation

    Proteomic databases

    MaxQBiO94760.
    PaxDbiO94760.
    PeptideAtlasiO94760.
    PRIDEiO94760.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00220342.

    PTM databases

    PhosphoSiteiO94760.

    Expressioni

    Tissue specificityi

    Detected in brain, liver, kidney and pancreas, and at low levels in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO94760.
    BgeeiO94760.
    CleanExiHS_DDAH1.
    GenevestigatoriO94760.

    Organism-specific databases

    HPAiHPA006308.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi117114. 4 interactions.
    IntActiO94760. 2 interactions.
    STRINGi9606.ENSP00000284031.

    Structurei

    Secondary structure

    1
    285
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196
    Helixi25 – 284
    Helixi40 – 5516
    Turni56 – 583
    Beta strandi61 – 655
    Turni72 – 754
    Helixi77 – 804
    Beta strandi81 – 844
    Beta strandi87 – 904
    Helixi96 – 1016
    Helixi102 – 1109
    Turni111 – 1133
    Beta strandi115 – 1184
    Helixi128 – 1303
    Beta strandi131 – 1333
    Beta strandi138 – 1458
    Helixi148 – 15710
    Turni158 – 1603
    Beta strandi163 – 1675
    Helixi174 – 1763
    Beta strandi177 – 1826
    Beta strandi185 – 1895
    Helixi192 – 20312
    Beta strandi205 – 2073
    Beta strandi210 – 2167
    Helixi217 – 2204
    Beta strandi223 – 2275
    Turni228 – 2303
    Beta strandi231 – 2377
    Turni239 – 2413
    Helixi243 – 2519
    Beta strandi255 – 2606
    Helixi263 – 2664
    Turni267 – 2693
    Helixi273 – 2753
    Beta strandi277 – 2793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JAIX-ray2.30A/B2-285[»]
    2JAJX-ray2.00A/B2-285[»]
    3I2EX-ray2.03A/B1-285[»]
    3I4AX-ray1.90A/B1-285[»]
    3P8EX-ray2.49A/B1-285[»]
    3P8PX-ray2.50A/B1-285[»]
    ProteinModelPortaliO94760.
    SMRiO94760. Positions 8-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94760.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni78 – 792Substrate binding

    Sequence similaritiesi

    Belongs to the DDAH family.Curated

    Phylogenomic databases

    eggNOGiCOG1834.
    HOGENOMiHOG000161035.
    HOVERGENiHBG055937.
    InParanoidiO94760.
    KOiK01482.
    OMAiKTMQQMS.
    OrthoDBiEOG73V6KV.
    PhylomeDBiO94760.
    TreeFamiTF314737.

    Family and domain databases

    InterProiIPR003198. Amidino_trans.
    [Graphical view]
    PfamiPF02274. Amidinotransf. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94760-1) [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

    MAGLGHPAAF GRATHAVVRA LPESLGQHAL RSAKGEEVDV ARAERQHQLY    50
    VGVLGSKLGL QVVELPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK 100
    EVDMMKEALE KLQLNIVEMK DENATLDGGD VLFTGREFFV GLSKRTNQRG 150
    AEILADTFKD YAVSTVPVAD GLHLKSFCSM AGPNLIAIGS SESAQKALKI 200
    MQQMSDHRYD KLTVPDDIAA NCIYLNIPNK GHVLLHRTPE EYPESAKVYE 250
    KLKDHMLIPV SMSELEKVDG LLTCCSVLIN KKVDS 285
    Length:285
    Mass (Da):31,122
    Last modified:January 23, 2007 - v3
    Checksum:iCD8875DF267EF39B
    GO
    Isoform 2 (identifier: O94760-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-103: Missing.

    Show »
    Length:182
    Mass (Da):20,189
    Checksum:i0612A4D0E824A1EE
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 103103Missing in isoform 2. 1 PublicationVSP_043813Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001915 mRNA. Translation: BAA37117.1.
    BX648145 mRNA. Translation: CAI45988.1.
    AC092807 Genomic DNA. No translation available.
    AL078459 Genomic DNA. No translation available.
    AL360219 Genomic DNA. No translation available.
    CH471097 Genomic DNA. Translation: EAW73199.1.
    BC033680 mRNA. Translation: AAH33680.1.
    BC043235 mRNA. Translation: AAH43235.2.
    CCDSiCCDS44170.1. [O94760-2]
    CCDS705.1. [O94760-1]
    RefSeqiNP_001127917.1. NM_001134445.1. [O94760-2]
    NP_036269.1. NM_012137.3. [O94760-1]
    XP_005270766.1. XM_005270709.2. [O94760-2]
    XP_005270767.1. XM_005270710.2. [O94760-2]
    XP_006710607.1. XM_006710544.1. [O94760-2]
    UniGeneiHs.713411.

    Genome annotation databases

    EnsembliENST00000284031; ENSP00000284031; ENSG00000153904. [O94760-1]
    ENST00000535924; ENSP00000439045; ENSG00000153904. [O94760-2]
    ENST00000539042; ENSP00000438604; ENSG00000153904. [O94760-1]
    GeneIDi23576.
    KEGGihsa:23576.
    UCSCiuc001dlb.3. human. [O94760-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001915 mRNA. Translation: BAA37117.1 .
    BX648145 mRNA. Translation: CAI45988.1 .
    AC092807 Genomic DNA. No translation available.
    AL078459 Genomic DNA. No translation available.
    AL360219 Genomic DNA. No translation available.
    CH471097 Genomic DNA. Translation: EAW73199.1 .
    BC033680 mRNA. Translation: AAH33680.1 .
    BC043235 mRNA. Translation: AAH43235.2 .
    CCDSi CCDS44170.1. [O94760-2 ]
    CCDS705.1. [O94760-1 ]
    RefSeqi NP_001127917.1. NM_001134445.1. [O94760-2 ]
    NP_036269.1. NM_012137.3. [O94760-1 ]
    XP_005270766.1. XM_005270709.2. [O94760-2 ]
    XP_005270767.1. XM_005270710.2. [O94760-2 ]
    XP_006710607.1. XM_006710544.1. [O94760-2 ]
    UniGenei Hs.713411.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JAI X-ray 2.30 A/B 2-285 [» ]
    2JAJ X-ray 2.00 A/B 2-285 [» ]
    3I2E X-ray 2.03 A/B 1-285 [» ]
    3I4A X-ray 1.90 A/B 1-285 [» ]
    3P8E X-ray 2.49 A/B 1-285 [» ]
    3P8P X-ray 2.50 A/B 1-285 [» ]
    ProteinModelPortali O94760.
    SMRi O94760. Positions 8-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117114. 4 interactions.
    IntActi O94760. 2 interactions.
    STRINGi 9606.ENSP00000284031.

    Chemistry

    BindingDBi O94760.
    ChEMBLi CHEMBL6036.
    DrugBanki DB00155. L-Citrulline.

    PTM databases

    PhosphoSitei O94760.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00220342.

    Proteomic databases

    MaxQBi O94760.
    PaxDbi O94760.
    PeptideAtlasi O94760.
    PRIDEi O94760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284031 ; ENSP00000284031 ; ENSG00000153904 . [O94760-1 ]
    ENST00000535924 ; ENSP00000439045 ; ENSG00000153904 . [O94760-2 ]
    ENST00000539042 ; ENSP00000438604 ; ENSG00000153904 . [O94760-1 ]
    GeneIDi 23576.
    KEGGi hsa:23576.
    UCSCi uc001dlb.3. human. [O94760-1 ]

    Organism-specific databases

    CTDi 23576.
    GeneCardsi GC01M085785.
    HGNCi HGNC:2715. DDAH1.
    HPAi HPA006308.
    MIMi 604743. gene.
    neXtProti NX_O94760.
    PharmGKBi PA27185.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1834.
    HOGENOMi HOG000161035.
    HOVERGENi HBG055937.
    InParanoidi O94760.
    KOi K01482.
    OMAi KTMQQMS.
    OrthoDBi EOG73V6KV.
    PhylomeDBi O94760.
    TreeFami TF314737.

    Miscellaneous databases

    ChiTaRSi DDAH1. human.
    EvolutionaryTracei O94760.
    GenomeRNAii 23576.
    NextBioi 46178.
    PROi O94760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94760.
    Bgeei O94760.
    CleanExi HS_DDAH1.
    Genevestigatori O94760.

    Family and domain databases

    InterProi IPR003198. Amidino_trans.
    [Graphical view ]
    Pfami PF02274. Amidinotransf. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, cDNA cloning and expression of human NG,NG-dimethylarginine dimethylaminohydrolase."
      Kimoto M., Miyatake S., Sasagawa T., Yamashita H., Okita M., Oka T., Ogawa T., Tsuji H.
      Eur. J. Biochem. 258:863-868(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-12 AND 35-50, ABSENCE OF BOUND ZINC, ACETYLATION AT ALA-2.
      Tissue: Kidney and Liver.
    2. "Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases."
      Leiper J.M., Santa Maria J., Chubb A., MacAllister R.J., Charles I.G., Whitley G.S., Vallance P.
      Biochem. J. 343:209-214(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Endometrial cancer.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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: Colon, Kidney, Stomach and Testis.
    7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 20-31; 46-57; 112-136; 150-196; 212-230 AND 268-281, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Mechanism of 4-HNE mediated inhibition of hDDAH-1: implications in NO regulation."
      Forbes S.P., Druhan L.J., Guzman J.E., Parinandi N., Zhang L., Green-Church K.B., Cardounel A.J.
      Biochemistry 47:1819-1826(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-284 IN COMPLEXES WITH CITRULLINE AND INHIBITOR L-257.
    12. "Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide."
      Wang Y., Monzingo A.F., Hu S., Schaller T.H., Robertus J.D., Fast W.
      Biochemistry 48:8624-8635(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH N-1-IMINOPROPYL-L-ORNITHINE, CATALYTIC ACTIVITY, ZINC-BINDING, ENZYME REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF LEU-30; GLU-78 AND LEU-271, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiDDAH1_HUMAN
    AccessioniPrimary (citable) accession number: O94760
    Secondary accession number(s): Q5HYC8, Q86XK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3