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O60704

- TPST2_HUMAN

UniProt

O60704 - TPST2_HUMAN

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Protein
Protein-tyrosine sulfotransferase 2
Gene
TPST2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Cytoplasmic Reviewed prediction
Transmembranei9 – 2517Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini26 – 377352Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 2
PRO_0000189829Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiO60704.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 127 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

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