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O60704

- TPST2_HUMAN

UniProt

O60704 - TPST2_HUMAN

Protein

Protein-tyrosine sulfotransferase 2

Gene

TPST2

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 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.

    Catalytic activityi

    3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei78 – 7811 Publication
    Active sitei99 – 9911 Publication
    Sitei158 – 1581Transition state stabilizer
    Sitei285 – 2851Transition state stabilizer

    GO - Molecular functioni

    1. protein-tyrosine sulfotransferase activity Source: ProtInc

    GO - Biological processi

    1. fusion of sperm to egg plasma membrane Source: Ensembl
    2. peptidyl-tyrosine sulfation Source: ProtInc
    3. prevention of polyspermy Source: Ensembl

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BRENDAi2.8.2.20. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-tyrosine sulfotransferase 2 (EC:2.8.2.20)
    Alternative name(s):
    Tyrosylprotein sulfotransferase 2
    Short name:
    TPST-2
    Gene namesi
    Name:TPST2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:12021. TPST2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: LIFEdb
    2. extracellular vesicular exosome Source: UniProt
    3. Golgi membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: ProtInc

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781R → A: Significantly reduced enzymatic activity. 1 Publication
    Mutagenesisi99 – 991E → A: Abolishes sulfotransferase activity. 1 Publication
    Mutagenesisi101 – 1011R → A: Prevents dimerization. 1 Publication
    Mutagenesisi113 – 1131W → A: Prevents dimerization. 1 Publication
    Mutagenesisi158 – 1581K → A: Significantly reduced enzymatic activity. 1 Publication
    Mutagenesisi198 – 1981T → A: Decreases activity sulfotransferase activity. 1 Publication
    Mutagenesisi285 – 2851S → A: Abolishes sulfotransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA36700.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Protein-tyrosine sulfotransferase 2PRO_0000189829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi96 ↔ 1561 Publication
    Disulfide bondi225 ↔ 2331 Publication
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO60704.
    PaxDbiO60704.
    PRIDEiO60704.

    PTM databases

    PhosphoSiteiO60704.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiO60704.
    BgeeiO60704.
    CleanExiHS_TPST2.
    GenevestigatoriO60704.

    Organism-specific databases

    HPAiHPA021054.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    MINTiMINT-4721342.
    STRINGi9606.ENSP00000339813.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi52 – 543
    Beta strandi62 – 643
    Beta strandi71 – 744
    Beta strandi76 – 805
    Helixi81 – 899
    Helixi102 – 11514
    Helixi117 – 1259
    Helixi130 – 14718
    Beta strandi153 – 1586
    Helixi160 – 1656
    Helixi166 – 1727
    Beta strandi177 – 1826
    Helixi185 – 19511
    Helixi207 – 22822
    Turni230 – 2323
    Beta strandi233 – 2375
    Helixi238 – 2436
    Helixi245 – 25612
    Helixi262 – 2654
    Helixi267 – 2693
    Beta strandi283 – 2853
    Helixi286 – 2894
    Turni300 – 3034
    Helixi307 – 31610
    Helixi319 – 3224
    Beta strandi329 – 3313
    Helixi339 – 34911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AP1X-ray1.90A/B43-359[»]
    3AP2X-ray2.40A/B43-359[»]
    3AP3X-ray3.50A/B/C/D43-377[»]
    ProteinModelPortaliO60704.
    SMRiO60704. Positions 62-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60704.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88CytoplasmicSequence Analysis
    Topological domaini26 – 377352LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2517Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the protein sulfotransferase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG285918.
    HOGENOMiHOG000253020.
    HOVERGENiHBG001270.
    InParanoidiO60704.
    KOiK01021.
    OMAiGKDKCLP.
    OrthoDBiEOG7DFXD2.
    PhylomeDBiO60704.
    TreeFamiTF312910.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR026634. TPST.
    [Graphical view]
    PANTHERiPTHR12788. PTHR12788. 1 hit.
    SUPFAMiSSF52540. SSF52540. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    O60704-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLSVRRVLL AAGCALVLVL AVQLGQQVLE CRAVLAGLRS PRGAMRPEQE    50
    ELVMVGTNHV EYRYGKAMPL IFVGGVPRSG TTLMRAMLDA HPEVRCGEET 100
    RIIPRVLAMR QAWSKSGREK LRLDEAGVTD EVLDAAMQAF ILEVIAKHGE 150
    PARVLCNKDP FTLKSSVYLS RLFPNSKFLL MVRDGRASVH SMITRKVTIA 200
    GFDLSSYRDC LTKWNKAIEV MYAQCMEVGK EKCLPVYYEQ LVLHPRRSLK 250
    LILDFLGIAW SDAVLHHEDL IGKPGGVSLS KIERSTDQVI KPVNLEALSK 300
    WTGHIPGDVV RDMAQIAPML AQLGYDPYAN PPNYGNPDPF VINNTQRVLK 350
    GDYKTPANLK GYFQVNQNST SSHLGSS 377
    Length:377
    Mass (Da):41,912
    Last modified:August 1, 1998 - v1
    Checksum:iA658E50151FDBC12
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261Q → L in CAB66558. (PubMed:11230166)Curated
    Sequence conflicti26 – 261Q → L in CAG38559. 1 PublicationCurated
    Sequence conflicti73 – 731V → E in CAB66558. (PubMed:11230166)Curated
    Sequence conflicti73 – 731V → E in CAG38559. 1 PublicationCurated
    Sequence conflicti115 – 1151K → M in CAG38559. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061254 mRNA. Translation: AAC34296.1.
    AF049891 mRNA. Translation: AAC36061.1.
    AJ006198 mRNA. Translation: CAA06906.1.
    AL136623 mRNA. Translation: CAB66558.1.
    CR456597 mRNA. Translation: CAG30483.1.
    CR533528 mRNA. Translation: CAG38559.1.
    AK074538 mRNA. Translation: BAG51969.1.
    AK075139 mRNA. Translation: BAG52071.1.
    Z95115 Genomic DNA. Translation: CAB62950.1.
    CH471095 Genomic DNA. Translation: EAW59726.1.
    BC001057 mRNA. Translation: AAH01057.1.
    BC017509 mRNA. Translation: AAH17509.1.
    CCDSiCCDS13839.1.
    RefSeqiNP_001008566.1. NM_001008566.1.
    NP_003586.3. NM_003595.3.
    UniGeneiHs.632768.

    Genome annotation databases

    EnsembliENST00000338754; ENSP00000339813; ENSG00000128294.
    ENST00000398110; ENSP00000381180; ENSG00000128294.
    ENST00000403880; ENSP00000385192; ENSG00000128294.
    GeneIDi8459.
    KEGGihsa:8459.
    UCSCiuc003acw.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF061254 mRNA. Translation: AAC34296.1 .
    AF049891 mRNA. Translation: AAC36061.1 .
    AJ006198 mRNA. Translation: CAA06906.1 .
    AL136623 mRNA. Translation: CAB66558.1 .
    CR456597 mRNA. Translation: CAG30483.1 .
    CR533528 mRNA. Translation: CAG38559.1 .
    AK074538 mRNA. Translation: BAG51969.1 .
    AK075139 mRNA. Translation: BAG52071.1 .
    Z95115 Genomic DNA. Translation: CAB62950.1 .
    CH471095 Genomic DNA. Translation: EAW59726.1 .
    BC001057 mRNA. Translation: AAH01057.1 .
    BC017509 mRNA. Translation: AAH17509.1 .
    CCDSi CCDS13839.1.
    RefSeqi NP_001008566.1. NM_001008566.1.
    NP_003586.3. NM_003595.3.
    UniGenei Hs.632768.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AP1 X-ray 1.90 A/B 43-359 [» ]
    3AP2 X-ray 2.40 A/B 43-359 [» ]
    3AP3 X-ray 3.50 A/B/C/D 43-377 [» ]
    ProteinModelPortali O60704.
    SMRi O60704. Positions 62-352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4721342.
    STRINGi 9606.ENSP00000339813.

    Chemistry

    BindingDBi O60704.
    ChEMBLi CHEMBL3178.

    PTM databases

    PhosphoSitei O60704.

    Proteomic databases

    MaxQBi O60704.
    PaxDbi O60704.
    PRIDEi O60704.

    Protocols and materials databases

    DNASUi 8459.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338754 ; ENSP00000339813 ; ENSG00000128294 .
    ENST00000398110 ; ENSP00000381180 ; ENSG00000128294 .
    ENST00000403880 ; ENSP00000385192 ; ENSG00000128294 .
    GeneIDi 8459.
    KEGGi hsa:8459.
    UCSCi uc003acw.3. human.

    Organism-specific databases

    CTDi 8459.
    GeneCardsi GC22M026921.
    HGNCi HGNC:12021. TPST2.
    HPAi HPA021054.
    MIMi 603126. gene.
    neXtProti NX_O60704.
    PharmGKBi PA36700.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285918.
    HOGENOMi HOG000253020.
    HOVERGENi HBG001270.
    InParanoidi O60704.
    KOi K01021.
    OMAi GKDKCLP.
    OrthoDBi EOG7DFXD2.
    PhylomeDBi O60704.
    TreeFami TF312910.

    Enzyme and pathway databases

    BRENDAi 2.8.2.20. 2681.

    Miscellaneous databases

    EvolutionaryTracei O60704.
    GenomeRNAii 8459.
    NextBioi 31658.
    PROi O60704.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60704.
    Bgeei O60704.
    CleanExi HS_TPST2.
    Genevestigatori O60704.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR026634. TPST.
    [Graphical view ]
    PANTHERi PTHR12788. PTHR12788. 1 hit.
    SUPFAMi SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2."
      Beisswanger R., Corbeil D., Vannier C., Thiele C., Dohrmann U., Kellner R., Ashman K., Niehrs C., Huttner W.B.
      Proc. Natl. Acad. Sci. U.S.A. 95:11134-11139(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans."
      Ouyang Y.-B., Moore K.L.
      J. Biol. Chem. 273:24770-24774(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Bennett E.P.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo and Placenta.
    8. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 and Colon.
    11. "Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction."
      Teramoto T., Fujikawa Y., Kawaguchi Y., Kurogi K., Soejima M., Adachi R., Nakanishi Y., Mishiro-Sato E., Liu M.C., Sakakibara Y., Suiko M., Kimura M., Kakuta Y.
      Nat. Commun. 4:1572-1572(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 43-359 IN COMPLEX WITH SUBSTRATE PEPTIDE, DISULFIDE BONDS, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ARG-78; GLU-99; ARG-101; TRP-113; LYS-158; THR-198 AND SER-285.

    Entry informationi

    Entry nameiTPST2_HUMAN
    AccessioniPrimary (citable) accession number: O60704
    Secondary accession number(s): B3KQA7, Q6FI98, Q9H0V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 128 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

    Miscellaneous

    Substrate peptides must be flexible in order to adopt an L-shaped conformation in the deep binding cleft.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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