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O00204

- ST2B1_HUMAN

UniProt

O00204 - ST2B1_HUMAN

Protein

Sulfotransferase family cytosolic 2B member 1

Gene

SULT2B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol.2 Publications

    Catalytic activityi

    3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate.

    Kineticsi

    1. KM=10.9 µM for DHEA (at 37 degrees Celsius, in the presence of 1mM MgCl2)2 Publications
    2. KM=3.8 µM for DHEA (at 37 degrees Celsius, in the presence of 10mM MgCl2)2 Publications
    3. KM=11.8 µM for pregnenolone (at 37 degrees Celsius, in the presence of 1mM MgCl2)2 Publications
    4. KM=0.6 µM for PAPS (at 37 degrees Celsius, in the presence of 1mM MgCl2)2 Publications

    Vmax=1752 pmol/min/mg enzyme toward DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2)2 Publications

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. Retains 70% and 20% of activity when incubated at 42 degrees Celsius for 45 and 120 minutes, respectively. Activity is lost after 200 minutes incubation at 42 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981Substrate
    Binding sitei103 – 1031Substrate
    Active sitei125 – 1251Proton acceptor
    Binding sitei125 – 1251Substrate
    Binding sitei147 – 1471PAPS
    Binding sitei155 – 1551PAPS
    Binding sitei210 – 2101PAPS

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi70 – 756PAPS
    Nucleotide bindingi244 – 2496PAPS
    Nucleotide bindingi274 – 2763PAPS

    GO - Molecular functioni

    1. alcohol sulfotransferase activity Source: Reactome
    2. protein binding Source: IntAct
    3. steroid sulfotransferase activity Source: UniProtKB

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. small molecule metabolic process Source: Reactome
    3. steroid metabolic process Source: UniProtKB
    4. sulfate assimilation Source: Ensembl
    5. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid metabolism, Steroid metabolism

    Enzyme and pathway databases

    BRENDAi2.8.2.2. 2681.
    ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfotransferase family cytosolic 2B member 1 (EC:2.8.2.2)
    Short name:
    ST2B1
    Short name:
    Sulfotransferase 2B1
    Alternative name(s):
    Alcohol sulfotransferase
    Hydroxysteroid sulfotransferase 2
    Gene namesi
    Name:SULT2B1
    Synonyms:HSST2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:11459. SULT2B1.

    Subcellular locationi

    Cytoplasm. Microsome. Nucleus
    Note: Phosphorylation of Ser-348 is required for translocation to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. endoplasmic reticulum Source: UniProtKB-KW
    4. intracellular membrane-bounded organelle Source: HPA
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 2323Missing: Loss of the cholesterol sulfotransferase activity. Add
    BLAST
    Mutagenesisi1 – 1818Missing: Increases the cholesterol sulfotransferase activity. Add
    BLAST
    Mutagenesisi19 – 191D → A: Increases the cholesterol sulfotransferase activity. 1 Publication
    Mutagenesisi20 – 201I → A: Loss of the cholesterol sulfotransferase activity. 1 Publication
    Mutagenesisi21 – 211S → A: Increases the cholesterol sulfotransferase activity. 1 Publication
    Mutagenesisi22 – 221E → A: Increases the cholesterol sulfotransferase activity. 1 Publication
    Mutagenesisi23 – 231I → A: Loss of the cholesterol sulfotransferase activity. 1 Publication
    Mutagenesisi347 – 3471S → A: No change in subcellular localization. 1 Publication
    Mutagenesisi348 – 3481S → D: 10-fold increase in specific activity for DHEA sulfation. 10-fold increase in substrate affinity for DHEA and pregnenolone. No effect on substrate affinity for PAPS. Increases enzyme stability. 1 Publication
    Mutagenesisi348 – 3481S → G: Abolishes nuclear localization. 1 Publication
    Mutagenesisi352 – 3521S → G: No change in subcellular localization. 1 Publication
    Mutagenesisi357 – 3571S → G: No change in subcellular localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA36249.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 365365Sulfotransferase family cytosolic 2B member 1PRO_0000085149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei348 – 3481Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00204.
    PaxDbiO00204.
    PRIDEiO00204.

    PTM databases

    PhosphoSiteiO00204.

    Expressioni

    Tissue specificityi

    Expressed highly in placenta, prostate and trachea and lower expression in the small intestine and lung.1 Publication

    Gene expression databases

    BgeeiO00204.
    CleanExiHS_SULT2B1.
    GenevestigatoriO00204.

    Organism-specific databases

    HPAiCAB033013.
    HPA041724.
    HPA043539.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALS2CR12Q96Q353EBI-749441,EBI-750451

    Protein-protein interaction databases

    BioGridi112689. 2 interactions.
    IntActiO00204. 2 interactions.
    MINTiMINT-1440870.
    STRINGi9606.ENSP00000201586.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 257
    Beta strandi31 – 344
    Beta strandi37 – 415
    Helixi46 – 549
    Beta strandi63 – 686
    Helixi73 – 8412
    Turni85 – 873
    Helixi90 – 945
    Helixi97 – 1004
    Beta strandi103 – 1064
    Helixi110 – 1123
    Beta strandi121 – 1244
    Turni128 – 1303
    Helixi133 – 1353
    Beta strandi141 – 1466
    Helixi149 – 16214
    Beta strandi163 – 1664
    Helixi172 – 1809
    Helixi189 – 1968
    Helixi197 – 1993
    Beta strandi205 – 2095
    Helixi210 – 2156
    Helixi217 – 22812
    Helixi234 – 24411
    Helixi246 – 2505
    Turni253 – 2553
    Turni256 – 2594
    Turni262 – 2643
    Turni267 – 2693
    Helixi280 – 2834
    Helixi287 – 30014
    Turni301 – 3033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q1QX-ray2.91A24-365[»]
    1Q1ZX-ray2.40A19-312[»]
    1Q20X-ray2.30A19-312[»]
    1Q22X-ray2.50A19-312[»]
    DisProtiDP00404.
    ProteinModelPortaliO00204.
    SMRiO00204. Positions 19-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00204.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi305 – 36561Pro/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Phylogenomic databases

    eggNOGiNOG296990.
    HOGENOMiHOG000037209.
    HOVERGENiHBG001195.
    InParanoidiO00204.
    KOiK01015.
    OMAiPVGIYSP.
    OrthoDBiEOG7V49ZK.
    PhylomeDBiO00204.
    TreeFamiTF321745.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00204-1) [UniParc]FASTAAdd to Basket

    Also known as: SULT2B1b, B

    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

    MDGPAEPQIP GLWDTYEDDI SEISQKLPGE YFRYKGVPFP VGLYSLESIS    50
    LAENTQDVRD DDIFIITYPK SGTTWMIEII CLILKEGDPS WIRSVPIWER 100
    APWCETIVGA FSLPDQYSPR LMSSHLPIQI FTKAFFSSKA KVIYMGRNPR 150
    DVVVSLYHYS KIAGQLKDPG TPDQFLRDFL KGEVQFGSWF DHIKGWLRMK 200
    GKDNFLFITY EELQQDLQGS VERICGFLGR PLGKEALGSV VAHSTFSAMK 250
    ANTMSNYTLL PPSLLDHRRG AFLRKGVCGD WKNHFTVAQS EAFDRAYRKQ 300
    MRGMPTFPWD EDPEEDGSPD PEPSPEPEPK PSLEPNTSLE REPRPNSSPS 350
    PSPGQASETP HPRPS 365
    Length:365
    Mass (Da):41,308
    Last modified:January 4, 2005 - v2
    Checksum:i13E95248DD40DF91
    GO
    Isoform 2 (identifier: O00204-2) [UniParc]FASTAAdd to Basket

    Also known as: SULT2B1a, A

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MDGPAEPQIPGLWDTYEDDISEI → MASPPPFH

    Show »
    Length:350
    Mass (Da):39,599
    Checksum:iCE5BAA8F8874E3A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti350 – 3501S → N in AAC78498. (PubMed:9799594)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511L → S.
    Corresponds to variant rs16982149 [ dbSNP | Ensembl ].
    VAR_020887
    Natural varianti240 – 2401V → I.
    Corresponds to variant rs2302947 [ dbSNP | Ensembl ].
    VAR_021988
    Natural varianti345 – 3451P → L.
    Corresponds to variant rs17842463 [ dbSNP | Ensembl ].
    VAR_020888

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323MDGPA…DISEI → MASPPPFH in isoform 2. 1 PublicationVSP_012510Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92314 mRNA. Translation: AAC78498.1.
    U92315 mRNA. Translation: AAC78499.1.
    U92322
    , U92316, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78553.1.
    U92322
    , U92316, U92317, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78554.1.
    AC008403 Genomic DNA. No translation available.
    BC034694 mRNA. Translation: AAH34694.1.
    CCDSiCCDS12723.1. [O00204-1]
    CCDS12724.1. [O00204-2]
    RefSeqiNP_004596.2. NM_004605.2. [O00204-2]
    NP_814444.1. NM_177973.1. [O00204-1]
    UniGeneiHs.369331.

    Genome annotation databases

    EnsembliENST00000201586; ENSP00000201586; ENSG00000088002. [O00204-1]
    ENST00000323090; ENSP00000312880; ENSG00000088002. [O00204-2]
    GeneIDi6820.
    KEGGihsa:6820.
    UCSCiuc002pjl.3. human. [O00204-1]
    uc002pjm.3. human. [O00204-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92314 mRNA. Translation: AAC78498.1 .
    U92315 mRNA. Translation: AAC78499.1 .
    U92322
    , U92316 , U92318 , U92319 , U92320 , U92321 Genomic DNA. Translation: AAC78553.1 .
    U92322
    , U92316 , U92317 , U92318 , U92319 , U92320 , U92321 Genomic DNA. Translation: AAC78554.1 .
    AC008403 Genomic DNA. No translation available.
    BC034694 mRNA. Translation: AAH34694.1 .
    CCDSi CCDS12723.1. [O00204-1 ]
    CCDS12724.1. [O00204-2 ]
    RefSeqi NP_004596.2. NM_004605.2. [O00204-2 ]
    NP_814444.1. NM_177973.1. [O00204-1 ]
    UniGenei Hs.369331.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q1Q X-ray 2.91 A 24-365 [» ]
    1Q1Z X-ray 2.40 A 19-312 [» ]
    1Q20 X-ray 2.30 A 19-312 [» ]
    1Q22 X-ray 2.50 A 19-312 [» ]
    DisProti DP00404.
    ProteinModelPortali O00204.
    SMRi O00204. Positions 19-311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112689. 2 interactions.
    IntActi O00204. 2 interactions.
    MINTi MINT-1440870.
    STRINGi 9606.ENSP00000201586.

    Chemistry

    ChEMBLi CHEMBL1743297.

    PTM databases

    PhosphoSitei O00204.

    Proteomic databases

    MaxQBi O00204.
    PaxDbi O00204.
    PRIDEi O00204.

    Protocols and materials databases

    DNASUi 6820.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000201586 ; ENSP00000201586 ; ENSG00000088002 . [O00204-1 ]
    ENST00000323090 ; ENSP00000312880 ; ENSG00000088002 . [O00204-2 ]
    GeneIDi 6820.
    KEGGi hsa:6820.
    UCSCi uc002pjl.3. human. [O00204-1 ]
    uc002pjm.3. human. [O00204-2 ]

    Organism-specific databases

    CTDi 6820.
    GeneCardsi GC19P049055.
    HGNCi HGNC:11459. SULT2B1.
    HPAi CAB033013.
    HPA041724.
    HPA043539.
    MIMi 604125. gene.
    neXtProti NX_O00204.
    PharmGKBi PA36249.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296990.
    HOGENOMi HOG000037209.
    HOVERGENi HBG001195.
    InParanoidi O00204.
    KOi K01015.
    OMAi PVGIYSP.
    OrthoDBi EOG7V49ZK.
    PhylomeDBi O00204.
    TreeFami TF321745.

    Enzyme and pathway databases

    BRENDAi 2.8.2.2. 2681.
    Reactomei REACT_6913. Cytosolic sulfonation of small molecules.

    Miscellaneous databases

    EvolutionaryTracei O00204.
    GeneWikii SULT2B1.
    GenomeRNAii 6820.
    NextBioi 26633.
    PROi O00204.
    SOURCEi Search...

    Gene expression databases

    Bgeei O00204.
    CleanExi HS_SULT2B1.
    Genevestigatori O00204.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene."
      Her C., Wood T.C., Eichler E.E., Mohrenweiser H.W., Ramagli L.S., Siciliano M.J., Weinshilboum R.M.
      Genomics 53:284-295(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Skin.
    4. "Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase."
      Fuda H., Lee Y.C., Shimizu C., Javitt N.B., Strott C.A.
      J. Biol. Chem. 277:36161-36166(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 1-MET--ASP-18; 1-MET--ILE-23; ASP-19; ILE-20; SER-21; GLU-22 AND ILE-23.
    5. "Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation."
      He D., Falany C.N.
      Drug Metab. Dispos. 34:1749-1755(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    6. "Site-directed mutagenesis of human cytosolic sulfotransferase (SULT) 2B1b to phospho-mimetic Ser348Asp results in an isoform with increased catalytic activity."
      Salman E.D., He D., Runge-Morris M., Kocarek T.A., Falany C.N.
      J. Steroid Biochem. Mol. Biol. 127:315-323(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-348, MUTAGENESIS OF SER-347; SER-348; SER-352 AND SER-357.
    7. "Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms."
      Lee K.A., Fuda H., Lee Y.C., Negishi M., Strott C.A., Pedersen L.C.
      J. Biol. Chem. 278:44593-44599(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-312 IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND PREGNENOLONE.

    Entry informationi

    Entry nameiST2B1_HUMAN
    AccessioniPrimary (citable) accession number: O00204
    Secondary accession number(s): O00205, O75814
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 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. 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3