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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei230 – 2301Sequence analysis
    Metal bindingi262 – 2621Copper ABy similarity
    Metal bindingi263 – 2631Copper ABy similarity
    Metal bindingi333 – 3331Copper ABy similarity
    Active sitei412 – 4121Sequence analysis
    Metal bindingi412 – 4121Copper BCombined sources1 Publication
    Metal bindingi414 – 4141Copper BCombined sources1 Publication
    Metal bindingi487 – 4871Copper BCombined sources1 Publication

    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.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei17 – 3721Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
    BLAST
    Topological domaini38 – 617580IntragranularSequence analysisAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011V → M in DBH deficiency. 1 Publication
    Corresponds to variant rs267606760 [ dbSNP | Ensembl ].
    VAR_022758
    Natural varianti114 – 1141D → E in DBH deficiency. 1 Publication
    Corresponds to variant rs77576840 [ dbSNP | Ensembl ].
    VAR_022759
    Natural varianti345 – 3451D → N in DBH deficiency. 1 Publication
    Corresponds to variant rs267606761 [ dbSNP | Ensembl ].
    VAR_022760

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    Chemistry

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 617617Dopamine beta-hydroxylasePRO_0000006356Add
    BLAST
    Chaini40 – 617578Soluble dopamine beta-hydroxylasePRO_0000308209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysisCombined sources1 Publication
    Disulfide bondi154 ↔ 596Combined sources1 Publication
    Glycosylationi184 – 1841N-linked (GlcNAc...) (complex)Combined sources3 Publications
    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 bondi528 – 528Interchain (with C-530)Combined sources1 Publication
    Disulfide bondi530 – 530Interchain (with C-528)Combined sources1 Publication
    Glycosylationi566 – 5661N-linked (GlcNAc...)Combined sources1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei39 – 402CleavageBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP09172.
    PeptideAtlasiP09172.
    PRIDEiP09172.

    PTM databases

    iPTMnetiP09172.
    PhosphoSiteiP09172.

    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 interactions.
    IntActiP09172. 1 interaction.
    MINTiMINT-2843963.
    STRINGi9606.ENSP00000376776.

    Chemistry

    BindingDBiP09172.

    Structurei

    Secondary structure

    1
    617
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 525Combined sources
    Beta strandi58 – 669Combined sources
    Turni67 – 704Combined sources
    Beta strandi71 – 8010Combined sources
    Beta strandi83 – 9311Combined sources
    Beta strandi98 – 1047Combined sources
    Beta strandi111 – 1177Combined sources
    Beta strandi123 – 1253Combined sources
    Beta strandi130 – 1389Combined sources
    Beta strandi143 – 1519Combined sources
    Beta strandi166 – 1738Combined sources
    Beta strandi191 – 1955Combined sources
    Beta strandi212 – 2176Combined sources
    Beta strandi220 – 2223Combined sources
    Beta strandi225 – 23612Combined sources
    Beta strandi244 – 2529Combined sources
    Turni255 – 2606Combined sources
    Beta strandi261 – 2688Combined sources
    Beta strandi279 – 2846Combined sources
    Beta strandi286 – 2883Combined sources
    Beta strandi290 – 2945Combined sources
    Beta strandi297 – 3037Combined sources
    Beta strandi313 – 3197Combined sources
    Beta strandi327 – 3359Combined sources
    Beta strandi348 – 3569Combined sources
    Beta strandi359 – 3613Combined sources
    Beta strandi363 – 3697Combined sources
    Beta strandi375 – 3773Combined sources
    Beta strandi382 – 3909Combined sources
    Helixi392 – 3987Combined sources
    Beta strandi404 – 4129Combined sources
    Beta strandi417 – 42610Combined sources
    Beta strandi429 – 43911Combined sources
    Beta strandi448 – 4569Combined sources
    Beta strandi461 – 4688Combined sources
    Beta strandi477 – 4826Combined sources
    Beta strandi489 – 4968Combined sources
    Beta strandi499 – 5079Combined sources
    Helixi509 – 52214Combined sources
    Helixi535 – 5395Combined sources
    Helixi546 – 55813Combined sources
    Beta strandi561 – 5677Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4ZELX-ray2.90A/B40-617[»]
    ProteinModelPortaliP09172.
    SMRiP09172. Positions 205-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 173117DOMONPROSITE-ProRule annotationAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti505 – 5051S → T in CAA68285 (PubMed:3443096).Curated
    Sequence conflicti505 – 5051S → T in CAA31631 (PubMed:2922261).Curated
    Sequence conflicti505 – 5051S → T in CAA31632 (PubMed:2922261).Curated

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121G → S.
    Corresponds to variant rs5318 [ dbSNP | Ensembl ].
    VAR_048838
    Natural varianti101 – 1011V → M in DBH deficiency. 1 Publication
    Corresponds to variant rs267606760 [ dbSNP | Ensembl ].
    VAR_022758
    Natural varianti114 – 1141D → E in DBH deficiency. 1 Publication
    Corresponds to variant rs77576840 [ dbSNP | Ensembl ].
    VAR_022759
    Natural varianti181 – 1811E → Q.
    Corresponds to variant rs5319 [ dbSNP | Ensembl ].
    VAR_014706
    Natural varianti211 – 2111A → T.2 Publications
    Corresponds to variant rs5320 [ dbSNP | Ensembl ].
    VAR_013947
    Natural varianti239 – 2391K → N.
    Corresponds to variant rs5321 [ dbSNP | Ensembl ].
    VAR_014707
    Natural varianti250 – 2501E → Q.
    Corresponds to variant rs5323 [ dbSNP | Ensembl ].
    VAR_014708
    Natural varianti290 – 2901D → N.
    Corresponds to variant rs5324 [ dbSNP | Ensembl ].
    VAR_014709
    Natural varianti317 – 3171L → P.
    Corresponds to variant rs5325 [ dbSNP | Ensembl ].
    VAR_014710
    Natural varianti318 – 3181A → S in allele DBH-B. 3 Publications
    Corresponds to variant rs4531 [ dbSNP | Ensembl ].
    VAR_002196
    Natural varianti345 – 3451D → N in DBH deficiency. 1 Publication
    Corresponds to variant rs267606761 [ dbSNP | Ensembl ].
    VAR_022760
    Natural varianti549 – 5491R → C.2 Publications
    Corresponds to variant rs6271 [ dbSNP | Ensembl ].
    VAR_013948

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4ZELX-ray2.90A/B40-617[»]
    ProteinModelPortaliP09172.
    SMRiP09172. Positions 205-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107989. 4 interactions.
    IntActiP09172. 1 interaction.
    MINTiMINT-2843963.
    STRINGi9606.ENSP00000376776.

    Chemistry

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

    PTM databases

    iPTMnetiP09172.
    PhosphoSiteiP09172.

    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.
    GeneCardsiDBH.
    GeneReviewsiDBH.
    H-InvDBHIX0008510.
    HGNCiHGNC:2689. DBH.
    HPAiHPA005960.
    MalaCardsiDBH.
    MIMi223360. phenotype.
    609312. gene.
    neXtProtiNX_P09172.
    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.

    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: September 7, 2016
    This is version 181 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.