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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)DescriptionActionsGraphical viewLength
Active sitei781 Publication1
Active sitei991 Publication1
Sitei158Transition state stabilizer1
Sitei285Transition state stabilizer1

GO - Molecular functioni

  • protein-tyrosine sulfotransferase activity Source: ProtInc

GO - Biological processi

  • peptidyl-tyrosine sulfation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciZFISH:HS05176-MONOMER.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:12021. TPST2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicSequence analysis8
Transmembranei9 – 25Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini26 – 377LumenalSequence analysisAdd BLAST352

GO - Cellular componenti

  • endoplasmic reticulum Source: LIFEdb
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: GO_Central
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78R → A: Significantly reduced enzymatic activity. 1 Publication1
Mutagenesisi99E → A: Abolishes sulfotransferase activity. 1 Publication1
Mutagenesisi101R → A: Prevents dimerization. 1 Publication1
Mutagenesisi113W → A: Prevents dimerization. 1 Publication1
Mutagenesisi158K → A: Significantly reduced enzymatic activity. 1 Publication1
Mutagenesisi198T → A: Decreases activity sulfotransferase activity. 1 Publication1
Mutagenesisi285S → A: Abolishes sulfotransferase activity. 1 Publication1

Organism-specific databases

DisGeNETi8459.
OpenTargetsiENSG00000128294.
PharmGKBiPA36700.

Chemistry databases

ChEMBLiCHEMBL3178.

Polymorphism and mutation databases

BioMutaiTPST2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001898291 – 377Protein-tyrosine sulfotransferase 2Add BLAST377

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi96 ↔ 1561 Publication
Disulfide bondi225 ↔ 2331 Publication
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi368N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO60704.
MaxQBiO60704.
PaxDbiO60704.
PeptideAtlasiO60704.
PRIDEiO60704.

PTM databases

iPTMnetiO60704.
PhosphoSitePlusiO60704.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000128294.
CleanExiHS_TPST2.
ExpressionAtlasiO60704. baseline and differential.
GenevisibleiO60704. HS.

Organism-specific databases

HPAiHPA021054.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi114037. 10 interactors.
MINTiMINT-4721342.
STRINGi9606.ENSP00000339813.

Chemistry databases

BindingDBiO60704.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 54Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi71 – 74Combined sources4
Beta strandi76 – 80Combined sources5
Helixi81 – 89Combined sources9
Helixi102 – 115Combined sources14
Helixi117 – 125Combined sources9
Helixi130 – 147Combined sources18
Beta strandi153 – 158Combined sources6
Helixi160 – 165Combined sources6
Helixi166 – 172Combined sources7
Beta strandi177 – 182Combined sources6
Helixi185 – 195Combined sources11
Helixi207 – 228Combined sources22
Turni230 – 232Combined sources3
Beta strandi233 – 237Combined sources5
Helixi238 – 243Combined sources6
Helixi245 – 256Combined sources12
Helixi262 – 265Combined sources4
Helixi267 – 269Combined sources3
Beta strandi283 – 285Combined sources3
Helixi286 – 289Combined sources4
Turni300 – 303Combined sources4
Helixi307 – 316Combined sources10
Helixi319 – 322Combined sources4
Beta strandi329 – 331Combined sources3
Helixi339 – 349Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AP1X-ray1.90A/B43-359[»]
3AP2X-ray2.40A/B43-359[»]
3AP3X-ray3.50A/B/C/D43-377[»]
ProteinModelPortaliO60704.
SMRiO60704.
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

eggNOGiKOG3988. Eukaryota.
ENOG410XQ2X. LUCA.
GeneTreeiENSGT00390000006030.
HOGENOMiHOG000253020.
HOVERGENiHBG001270.
InParanoidiO60704.
KOiK01021.
OMAiGKDKCLP.
OrthoDBiEOG091G09YJ.
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)DescriptionActionsGraphical viewLength
Sequence conflicti26Q → L in CAB66558 (PubMed:11230166).Curated1
Sequence conflicti26Q → L in CAG38559 (Ref. 6) Curated1
Sequence conflicti73V → E in CAB66558 (PubMed:11230166).Curated1
Sequence conflicti73V → E in CAG38559 (Ref. 6) Curated1
Sequence conflicti115K → M in CAG38559 (Ref. 6) Curated1

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.4. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AP1X-ray1.90A/B43-359[»]
3AP2X-ray2.40A/B43-359[»]
3AP3X-ray3.50A/B/C/D43-377[»]
ProteinModelPortaliO60704.
SMRiO60704.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114037. 10 interactors.
MINTiMINT-4721342.
STRINGi9606.ENSP00000339813.

Chemistry databases

BindingDBiO60704.
ChEMBLiCHEMBL3178.

PTM databases

iPTMnetiO60704.
PhosphoSitePlusiO60704.

Polymorphism and mutation databases

BioMutaiTPST2.

Proteomic databases

EPDiO60704.
MaxQBiO60704.
PaxDbiO60704.
PeptideAtlasiO60704.
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.4. human.

Organism-specific databases

CTDi8459.
DisGeNETi8459.
GeneCardsiTPST2.
HGNCiHGNC:12021. TPST2.
HPAiHPA021054.
MIMi603126. gene.
neXtProtiNX_O60704.
OpenTargetsiENSG00000128294.
PharmGKBiPA36700.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3988. Eukaryota.
ENOG410XQ2X. LUCA.
GeneTreeiENSGT00390000006030.
HOGENOMiHOG000253020.
HOVERGENiHBG001270.
InParanoidiO60704.
KOiK01021.
OMAiGKDKCLP.
OrthoDBiEOG091G09YJ.
PhylomeDBiO60704.
TreeFamiTF312910.

Enzyme and pathway databases

BioCyciZFISH:HS05176-MONOMER.
BRENDAi2.8.2.20. 2681.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000128294.
CleanExiHS_TPST2.
ExpressionAtlasiO60704. baseline and differential.
GenevisibleiO60704. HS.

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...

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: November 2, 2016
This is version 145 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

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.