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

Protein-tyrosine sulfotransferase 2

Gene

TPST2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2517Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini26 – 377352LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: LIFEdb
  2. extracellular vesicular exosome Source: UniProtKB
  3. Golgi membrane Source: UniProtKB-SubCell
  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 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

BgeeiO60704.
CleanExiHS_TPST2.
ExpressionAtlasiO60704. baseline and differential.
GenevestigatoriO60704.

Organism-specific databases

HPAiHPA021054.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi114037. 3 interactions.
MINTiMINT-4721342.
STRINGi9606.ENSP00000339813.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the protein sulfotransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG285918.
GeneTreeiENSGT00390000006030.
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

        10         20         30         40         50
MRLSVRRVLL AAGCALVLVL AVQLGQQVLE CRAVLAGLRS PRGAMRPEQE
60 70 80 90 100
ELVMVGTNHV EYRYGKAMPL IFVGGVPRSG TTLMRAMLDA HPEVRCGEET
110 120 130 140 150
RIIPRVLAMR QAWSKSGREK LRLDEAGVTD EVLDAAMQAF ILEVIAKHGE
160 170 180 190 200
PARVLCNKDP FTLKSSVYLS RLFPNSKFLL MVRDGRASVH SMITRKVTIA
210 220 230 240 250
GFDLSSYRDC LTKWNKAIEV MYAQCMEVGK EKCLPVYYEQ LVLHPRRSLK
260 270 280 290 300
LILDFLGIAW SDAVLHHEDL IGKPGGVSLS KIERSTDQVI KPVNLEALSK
310 320 330 340 350
WTGHIPGDVV RDMAQIAPML AQLGYDPYAN PPNYGNPDPF VINNTQRVLK
360 370
GDYKTPANLK GYFQVNQNST SSHLGSS
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 (Ref. 6) Curated
Sequence conflicti73 – 731V → E in CAB66558 (PubMed:11230166).Curated
Sequence conflicti73 – 731V → E in CAG38559 (Ref. 6) Curated
Sequence conflicti115 – 1151K → M in CAG38559 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi114037. 3 interactions.
MINTiMINT-4721342.
STRINGi9606.ENSP00000339813.

Chemistry

BindingDBiO60704.
ChEMBLiCHEMBL3178.

PTM databases

PhosphoSiteiO60704.

Proteomic databases

MaxQBiO60704.
PaxDbiO60704.
PRIDEiO60704.

Protocols and materials databases

DNASUi8459.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8459.
GeneCardsiGC22M026921.
HGNCiHGNC:12021. TPST2.
HPAiHPA021054.
MIMi603126. gene.
neXtProtiNX_O60704.
PharmGKBiPA36700.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285918.
GeneTreeiENSGT00390000006030.
HOGENOMiHOG000253020.
HOVERGENiHBG001270.
InParanoidiO60704.
KOiK01021.
OMAiGKDKCLP.
OrthoDBiEOG7DFXD2.
PhylomeDBiO60704.
TreeFamiTF312910.

Enzyme and pathway databases

BRENDAi2.8.2.20. 2681.

Miscellaneous databases

ChiTaRSiTPST2. human.
EvolutionaryTraceiO60704.
GenomeRNAii8459.
NextBioi31658.
PROiO60704.
SOURCEiSearch...

Gene expression databases

BgeeiO60704.
CleanExiHS_TPST2.
ExpressionAtlasiO60704. baseline and differential.
GenevestigatoriO60704.

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.
ProtoNetiSearch...

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: January 7, 2015
This is version 131 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

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 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.