Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dopamine beta-hydroxylase

Gene

DBH

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

Functioni

Conversion of dopamine to noradrenaline.4 Publications

Catalytic activityi

3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O.3 Publications

Cofactori

Cu2+1 Publication1 PublicationNote: Binds 2 copper ions per subunit.1 Publication

Kineticsi

  1. KM=1.8 mM for tyramine1 Publication

    pH dependencei

    Optimum pH is 5.2.1 Publication

    Pathwayi: (R)-noradrenaline biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-noradrenaline from dopamine.3 Publications
    Proteins known to be involved in this subpathway in this organism are:
    1. Dopamine beta-hydroxylase (DBH)
    This subpathway is part of the pathway (R)-noradrenaline biosynthesis, which is itself part of Catecholamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-noradrenaline from dopamine, the pathway (R)-noradrenaline biosynthesis and in Catecholamine biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei230Sequence analysis1
    Metal bindingi262Copper ABy similarity1
    Metal bindingi263Copper ABy similarity1
    Metal bindingi333Copper ABy similarity1
    Active sitei412Sequence analysis1
    Metal bindingi412Copper BCombined sources1 Publication1
    Metal bindingi414Copper BCombined sources1 Publication1
    Metal bindingi487Copper BCombined sources1 Publication1

    GO - Molecular functioni

    • catalytic activity Source: ProtInc
    • copper ion binding Source: UniProtKB
    • dopamine beta-monooxygenase activity Source: UniProtKB
    • L-ascorbic acid binding Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Catecholamine biosynthesis

    Keywords - Ligandi

    Copper, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER66-381.
    BRENDAi1.14.17.1. 2681.
    ReactomeiR-HSA-209905. Catecholamine biosynthesis.
    SignaLinkiP09172.
    SIGNORiP09172.
    UniPathwayiUPA00748; UER00735.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dopamine beta-hydroxylase (EC:1.14.17.13 Publications)
    Alternative name(s):
    Dopamine beta-monooxygenase
    Cleaved into the following chain:
    Gene namesi
    Name:DBH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2689. DBH.

    Subcellular locationi

    Soluble dopamine beta-hydroxylase :

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 16CytoplasmicSequence analysisAdd BLAST16
    Transmembranei17 – 37Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini38 – 617IntragranularSequence analysisAdd BLAST580

    GO - Cellular componenti

    • chromaffin granule lumen Source: UniProtKB-SubCell
    • chromaffin granule membrane Source: UniProtKB-SubCell
    • cytoplasm Source: ProtInc
    • extracellular region Source: UniProtKB
    • extracellular space Source: UniProtKB
    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: ProtInc
    • secretory granule lumen Source: UniProtKB
    • secretory granule membrane Source: UniProtKB
    • transport vesicle membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Dopamine beta-hydroxylase deficiency (DBH deficiency)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionCharacterized by profound deficits in autonomic and cardiovascular function, but apparently only subtle signs, if any, of central nervous system dysfunction.
    See also OMIM:223360
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_022758101V → M in DBH deficiency. 1 PublicationCorresponds to variant rs267606760dbSNPEnsembl.1
    Natural variantiVAR_022759114D → E in DBH deficiency. 1 PublicationCorresponds to variant rs77576840dbSNPEnsembl.1
    Natural variantiVAR_022760345D → N in DBH deficiency. 1 PublicationCorresponds to variant rs267606761dbSNPEnsembl.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi1621.
    MalaCardsiDBH.
    MIMi223360. phenotype.
    OpenTargetsiENSG00000123454.
    Orphaneti230. Dopamine beta-hydroxylase deficiency.
    PharmGKBiPA136.

    Chemistry databases

    ChEMBLiCHEMBL3102.
    DrugBankiDB06774. Capsaicin.
    DB00822. Disulfiram.
    DB00988. Dopamine.
    DB00550. Propylthiouracil.
    DB00126. Vitamin C.
    GuidetoPHARMACOLOGYi2486.

    Polymorphism and mutation databases

    BioMutaiDBH.
    DMDMi158517849.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000063561 – 617Dopamine beta-hydroxylaseAdd BLAST617
    ChainiPRO_000030820940 – 617Soluble dopamine beta-hydroxylaseAdd BLAST578

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi64N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication1
    Disulfide bondi154 ↔ 596Combined sources1 Publication
    Glycosylationi184N-linked (GlcNAc...) (complex)Combined sources3 Publications1
    Disulfide bondi232 ↔ 283Combined sources1 Publication
    Disulfide bondi269 ↔ 295Combined sources1 Publication
    Disulfide bondi390 ↔ 503Combined sources1 Publication
    Disulfide bondi394 ↔ 565Combined sources1 Publication
    Disulfide bondi466 ↔ 488Combined sources1 Publication
    Disulfide bondi528Interchain (with C-530)Combined sources1 Publication
    Disulfide bondi530Interchain (with C-528)Combined sources1 Publication
    Glycosylationi566N-linked (GlcNAc...)Combined sources1 Publication1

    Post-translational modificationi

    N-glycosylated.2 Publications
    Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei39 – 40CleavageBy similarity2

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP09172.
    PeptideAtlasiP09172.
    PRIDEiP09172.

    PTM databases

    iPTMnetiP09172.
    PhosphoSitePlusiP09172.

    Expressioni

    Inductioni

    Activity is enhanced by nerve growth factor (in superior cervical ganglia and adrenal medulla). Trans-synaptic stimulation with reserpine, acetylcholine and glucocorticoids.

    Gene expression databases

    BgeeiENSG00000123454.
    CleanExiHS_DBH.
    ExpressionAtlasiP09172. baseline and differential.
    GenevisibleiP09172. HS.

    Organism-specific databases

    HPAiHPA005960.

    Interactioni

    Subunit structurei

    Homotetramer; composed of two disulfide-linked dimers.1 Publication

    Protein-protein interaction databases

    BioGridi107989. 4 interactors.
    IntActiP09172. 2 interactors.
    MINTiMINT-2843963.
    STRINGi9606.ENSP00000376776.

    Chemistry databases

    BindingDBiP09172.

    Structurei

    Secondary structure

    1617
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi48 – 52Combined sources5
    Beta strandi58 – 66Combined sources9
    Turni67 – 70Combined sources4
    Beta strandi71 – 80Combined sources10
    Beta strandi83 – 93Combined sources11
    Beta strandi98 – 104Combined sources7
    Beta strandi111 – 117Combined sources7
    Beta strandi123 – 125Combined sources3
    Beta strandi130 – 138Combined sources9
    Beta strandi143 – 151Combined sources9
    Beta strandi166 – 173Combined sources8
    Beta strandi191 – 195Combined sources5
    Beta strandi212 – 217Combined sources6
    Beta strandi220 – 222Combined sources3
    Beta strandi225 – 236Combined sources12
    Beta strandi244 – 252Combined sources9
    Turni255 – 260Combined sources6
    Beta strandi261 – 268Combined sources8
    Beta strandi279 – 284Combined sources6
    Beta strandi286 – 288Combined sources3
    Beta strandi290 – 294Combined sources5
    Beta strandi297 – 303Combined sources7
    Beta strandi313 – 319Combined sources7
    Beta strandi327 – 335Combined sources9
    Beta strandi348 – 356Combined sources9
    Beta strandi359 – 361Combined sources3
    Beta strandi363 – 369Combined sources7
    Beta strandi375 – 377Combined sources3
    Beta strandi382 – 390Combined sources9
    Helixi392 – 398Combined sources7
    Beta strandi404 – 412Combined sources9
    Beta strandi417 – 426Combined sources10
    Beta strandi429 – 439Combined sources11
    Beta strandi448 – 456Combined sources9
    Beta strandi461 – 468Combined sources8
    Beta strandi477 – 482Combined sources6
    Beta strandi489 – 496Combined sources8
    Beta strandi499 – 507Combined sources9
    Helixi509 – 522Combined sources14
    Helixi535 – 539Combined sources5
    Helixi546 – 558Combined sources13
    Beta strandi561 – 567Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4ZELX-ray2.90A/B40-617[»]
    ProteinModelPortaliP09172.
    SMRiP09172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini57 – 173DOMONPROSITE-ProRule annotationAdd BLAST117

    Sequence similaritiesi

    Contains 1 DOMON domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3568. Eukaryota.
    ENOG410XR89. LUCA.
    GeneTreeiENSGT00530000063085.
    HOGENOMiHOG000063669.
    HOVERGENiHBG005519.
    InParanoidiP09172.
    KOiK00503.
    OMAiSYFGDAW.
    OrthoDBiEOG091G03XS.
    PhylomeDBiP09172.
    TreeFamiTF320698.

    Family and domain databases

    Gene3Di2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProiIPR014784. Cu2_ascorb_mOase-like_C.
    IPR020611. Cu2_ascorb_mOase_CS-1.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR024548. Cu2_monoox_C.
    IPR000945. DBH-rel.
    IPR005018. DOMON_domain.
    IPR008977. PHM/PNGase_F_dom.
    IPR028460. Tbh/DBH.
    [Graphical view]
    PANTHERiPTHR10157. PTHR10157. 1 hit.
    PTHR10157:SF29. PTHR10157:SF29. 1 hit.
    PfamiPF03712. Cu2_monoox_C. 1 hit.
    PF01082. Cu2_monooxygen. 1 hit.
    PF03351. DOMON. 1 hit.
    [Graphical view]
    PRINTSiPR00767. DBMONOXGNASE.
    SMARTiSM00664. DoH. 1 hit.
    [Graphical view]
    SUPFAMiSSF49742. SSF49742. 2 hits.
    PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
    PS00085. CU2_MONOOXYGENASE_2. 1 hit.
    PS50836. DOMON. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P09172-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPALSRWASL PGPSMREAAF MYSTAVAIFL VILVAALQGS APRESPLPYH
    60 70 80 90 100
    IPLDPEGSLE LSWNVSYTQE AIHFQLLVRR LKAGVLFGMS DRGELENADL
    110 120 130 140 150
    VVLWTDGDTA YFADAWSDQK GQIHLDPQQD YQLLQVQRTP EGLTLLFKRP
    160 170 180 190 200
    FGTCDPKDYL IEDGTVHLVY GILEEPFRSL EAINGSGLQM GLQRVQLLKP
    210 220 230 240 250
    NIPEPELPSD ACTMEVQAPN IQIPSQETTY WCYIKELPKG FSRHHIIKYE
    260 270 280 290 300
    PIVTKGNEAL VHHMEVFQCA PEMDSVPHFS GPCDSKMKPD RLNYCRHVLA
    310 320 330 340 350
    AWALGAKAFY YPEEAGLAFG GPGSSRYLRL EVHYHNPLVI EGRNDSSGIR
    360 370 380 390 400
    LYYTAKLRRF NAGIMELGLV YTPVMAIPPR ETAFILTGYC TDKCTQLALP
    410 420 430 440 450
    PSGIHIFASQ LHTHLTGRKV VTVLVRDGRE WEIVNQDNHY SPHFQEIRML
    460 470 480 490 500
    KKVVSVHPGD VLITSCTYNT EDRELATVGG FGILEEMCVN YVHYYPQTQL
    510 520 530 540 550
    ELCKSAVDAG FLQKYFHLIN RFNNEDVCTC PQASVSQQFT SVPWNSFNRD
    560 570 580 590 600
    VLKALYSFAP ISMHCNKSSA VRFQGEWNLQ PLPKVISTLE EPTPQCPTSQ
    610
    GRSPAGPTVV SIGGGKG
    Length:617
    Mass (Da):69,065
    Last modified:July 24, 2007 - v3
    Checksum:i4D5586F0E358885D
    GO

    Sequence cautioni

    The sequence AAH17174 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA31631 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA31632 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA68285 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti505S → T in CAA68285 (PubMed:3443096).Curated1
    Sequence conflicti505S → T in CAA31631 (PubMed:2922261).Curated1
    Sequence conflicti505S → T in CAA31632 (PubMed:2922261).Curated1

    Polymorphismi

    There are two main alleles of DBH: DBH-A with Ala-318 and DBH-B with Ser-318 (PubMed:10490716, PubMed:10391209, PubMed:10391210).3 Publications

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04883812G → S.Corresponds to variant rs5318dbSNPEnsembl.1
    Natural variantiVAR_022758101V → M in DBH deficiency. 1 PublicationCorresponds to variant rs267606760dbSNPEnsembl.1
    Natural variantiVAR_022759114D → E in DBH deficiency. 1 PublicationCorresponds to variant rs77576840dbSNPEnsembl.1
    Natural variantiVAR_014706181E → Q.Corresponds to variant rs5319dbSNPEnsembl.1
    Natural variantiVAR_013947211A → T.2 PublicationsCorresponds to variant rs5320dbSNPEnsembl.1
    Natural variantiVAR_014707239K → N.Corresponds to variant rs5321dbSNPEnsembl.1
    Natural variantiVAR_014708250E → Q.Corresponds to variant rs5323dbSNPEnsembl.1
    Natural variantiVAR_014709290D → N.Corresponds to variant rs5324dbSNPEnsembl.1
    Natural variantiVAR_014710317L → P.Corresponds to variant rs5325dbSNPEnsembl.1
    Natural variantiVAR_002196318A → S in allele DBH-B. 3 PublicationsCorresponds to variant rs4531dbSNPEnsembl.1
    Natural variantiVAR_022760345D → N in DBH deficiency. 1 PublicationCorresponds to variant rs267606761dbSNPEnsembl.1
    Natural variantiVAR_013948549R → C.2 PublicationsCorresponds to variant rs6271dbSNPEnsembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL365494 Genomic DNA. Translation: CAI13354.2.
    Y00096 mRNA. Translation: CAA68285.1. Different initiation.
    BC017174 mRNA. Translation: AAH17174.1. Different initiation.
    X13255 mRNA. Translation: CAA31631.1. Different initiation.
    X13256 mRNA. Translation: CAA31632.1. Different initiation.
    CCDSiCCDS6977.2.
    PIRiS03020.
    RefSeqiNP_000778.3. NM_000787.3.
    UniGeneiHs.591890.

    Genome annotation databases

    EnsembliENST00000393056; ENSP00000376776; ENSG00000123454.
    GeneIDi1621.
    KEGGihsa:1621.
    UCSCiuc004cel.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Dopamine beta hydroxylase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL365494 Genomic DNA. Translation: CAI13354.2.
    Y00096 mRNA. Translation: CAA68285.1. Different initiation.
    BC017174 mRNA. Translation: AAH17174.1. Different initiation.
    X13255 mRNA. Translation: CAA31631.1. Different initiation.
    X13256 mRNA. Translation: CAA31632.1. Different initiation.
    CCDSiCCDS6977.2.
    PIRiS03020.
    RefSeqiNP_000778.3. NM_000787.3.
    UniGeneiHs.591890.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4ZELX-ray2.90A/B40-617[»]
    ProteinModelPortaliP09172.
    SMRiP09172.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107989. 4 interactors.
    IntActiP09172. 2 interactors.
    MINTiMINT-2843963.
    STRINGi9606.ENSP00000376776.

    Chemistry databases

    BindingDBiP09172.
    ChEMBLiCHEMBL3102.
    DrugBankiDB06774. Capsaicin.
    DB00822. Disulfiram.
    DB00988. Dopamine.
    DB00550. Propylthiouracil.
    DB00126. Vitamin C.
    GuidetoPHARMACOLOGYi2486.

    PTM databases

    iPTMnetiP09172.
    PhosphoSitePlusiP09172.

    Polymorphism and mutation databases

    BioMutaiDBH.
    DMDMi158517849.

    Proteomic databases

    PaxDbiP09172.
    PeptideAtlasiP09172.
    PRIDEiP09172.

    Protocols and materials databases

    DNASUi1621.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000393056; ENSP00000376776; ENSG00000123454.
    GeneIDi1621.
    KEGGihsa:1621.
    UCSCiuc004cel.4. human.

    Organism-specific databases

    CTDi1621.
    DisGeNETi1621.
    GeneCardsiDBH.
    GeneReviewsiDBH.
    H-InvDBHIX0008510.
    HGNCiHGNC:2689. DBH.
    HPAiHPA005960.
    MalaCardsiDBH.
    MIMi223360. phenotype.
    609312. gene.
    neXtProtiNX_P09172.
    OpenTargetsiENSG00000123454.
    Orphaneti230. Dopamine beta-hydroxylase deficiency.
    PharmGKBiPA136.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3568. Eukaryota.
    ENOG410XR89. LUCA.
    GeneTreeiENSGT00530000063085.
    HOGENOMiHOG000063669.
    HOVERGENiHBG005519.
    InParanoidiP09172.
    KOiK00503.
    OMAiSYFGDAW.
    OrthoDBiEOG091G03XS.
    PhylomeDBiP09172.
    TreeFamiTF320698.

    Enzyme and pathway databases

    UniPathwayiUPA00748; UER00735.
    BioCyciMetaCyc:MONOMER66-381.
    BRENDAi1.14.17.1. 2681.
    ReactomeiR-HSA-209905. Catecholamine biosynthesis.
    SignaLinkiP09172.
    SIGNORiP09172.

    Miscellaneous databases

    GeneWikiiDopamine_beta_hydroxylase.
    GenomeRNAii1621.
    PROiP09172.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000123454.
    CleanExiHS_DBH.
    ExpressionAtlasiP09172. baseline and differential.
    GenevisibleiP09172. HS.

    Family and domain databases

    Gene3Di2.60.120.230. 1 hit.
    2.60.120.310. 1 hit.
    InterProiIPR014784. Cu2_ascorb_mOase-like_C.
    IPR020611. Cu2_ascorb_mOase_CS-1.
    IPR014783. Cu2_ascorb_mOase_CS-2.
    IPR000323. Cu2_ascorb_mOase_N.
    IPR024548. Cu2_monoox_C.
    IPR000945. DBH-rel.
    IPR005018. DOMON_domain.
    IPR008977. PHM/PNGase_F_dom.
    IPR028460. Tbh/DBH.
    [Graphical view]
    PANTHERiPTHR10157. PTHR10157. 1 hit.
    PTHR10157:SF29. PTHR10157:SF29. 1 hit.
    PfamiPF03712. Cu2_monoox_C. 1 hit.
    PF01082. Cu2_monooxygen. 1 hit.
    PF03351. DOMON. 1 hit.
    [Graphical view]
    PRINTSiPR00767. DBMONOXGNASE.
    SMARTiSM00664. DoH. 1 hit.
    [Graphical view]
    SUPFAMiSSF49742. SSF49742. 2 hits.
    PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
    PS00085. CU2_MONOOXYGENASE_2. 1 hit.
    PS50836. DOMON. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDOPO_HUMAN
    AccessioniPrimary (citable) accession number: P09172
    Secondary accession number(s): Q5T381, Q96AG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 24, 2007
    Last modified: November 30, 2016
    This is version 184 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 9
      Human chromosome 9: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.