O60704 (TPST2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein-tyrosine sulfotransferase 2
EC=2.8.2.20

Alternative name(s):
Tyrosylprotein sulfotransferase 2
Short name=TPST-2

Gene names

Name:

TPST2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides.
Catalytic activity	3'-phosphoadenylyl sulfate + protein tyrosine = adenosine 3',5'-bisphosphate + protein tyrosine-O-sulfate.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Widely expressed. Ref.1
Sequence similarities	Belongs to the protein sulfotransferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-tyrosine sulfation Traceable author statement. Source: ProtInc
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from direct assay. Source: LIFEdb integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Traceable author statement. Source: ProtInc
Molecular function	protein-tyrosine sulfotransferase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Protein-tyrosine sulfotransferase 2		PRO_0000189829
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 25	17	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	26 – 377	352	Lumenal Potential
Amino acid modifications
	Glycosylation	343	1	N-linked (GlcNAc...) Potential
	Glycosylation	368	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	26	1	Q → L in CAB66558. Ref.4
	Sequence conflict	26	1	Q → L in CAG38559. Ref.6
	Sequence conflict	73	1	V → E in CAB66558. Ref.4
	Sequence conflict	73	1	V → E in CAG38559. Ref.6
	Sequence conflict	115	1	K → M in CAG38559. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O60704 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: A658E50151FDBC12	FASTA	377	41,912
	10 20 30 40 50 60 MRLSVRRVLL AAGCALVLVL AVQLGQQVLE CRAVLAGLRS PRGAMRPEQE ELVMVGTNHV 70 80 90 100 110 120 EYRYGKAMPL IFVGGVPRSG TTLMRAMLDA HPEVRCGEET RIIPRVLAMR QAWSKSGREK 130 140 150 160 170 180 LRLDEAGVTD EVLDAAMQAF ILEVIAKHGE PARVLCNKDP FTLKSSVYLS RLFPNSKFLL 190 200 210 220 230 240 MVRDGRASVH SMITRKVTIA GFDLSSYRDC LTKWNKAIEV MYAQCMEVGK EKCLPVYYEQ 250 260 270 280 290 300 LVLHPRRSLK LILDFLGIAW SDAVLHHEDL IGKPGGVSLS KIERSTDQVI KPVNLEALSK 310 320 330 340 350 360 WTGHIPGDVV RDMAQIAPML AQLGYDPYAN PPNYGNPDPF VINNTQRVLK GDYKTPANLK 370 GYFQVNQNST SSHLGSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9736702] [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: 9733778] [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]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] 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: 16303743] [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: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Colon.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00031421.

RefSeq

NP_001008566.1. NM_001008566.1.
NP_003586.3. NM_003595.3.

UniGene

Hs.726122.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O60704.

ModBase

Search...

Protein-protein interaction databases

STRING

O60704.

Proteomic databases

PRIDE

O60704.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338754; ENSP00000339813; ENSG00000128294.
ENST00000398110; ENSP00000381180; ENSG00000128294.
ENST00000403880; ENSP00000385192; ENSG00000128294.
ENST00000446035; ENSP00000394835; ENSG00000128294.

GeneID

8459.

KEGG

hsa:8459.

UCSC

uc003acv.1. human.

Organism-specific databases

CTD

8459.

GeneCards

GC22M026921.

H-InvDB

HIX0016329.

HGNC

HGNC:12021. TPST2.

HPA

HPA021054.

MIM

603126. gene.

neXtProt

NX_O60704.

PharmGKB

PA36700.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06830.

GeneTree

ENSGT00390000006030.

HOGENOM

HBG382344.

HOVERGEN

HBG001270.

InParanoid

O60704.

OMA

VLECRAV.

OrthoDB

EOG4Z36DX.

PhylomeDB

O60704.

Enzyme and pathway databases

BRENDA

2.8.2.20. 2681.

Gene expression databases

ArrayExpress

O60704.

Bgee

O60704.

CleanEx

HS_TPST2.

Genevestigator

O60704.

GermOnline

ENSG00000128294. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

KO

K01021.

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

31658.

SOURCE

Search...

Entry information

Entry name

TPST2_HUMAN

Accession

Primary (citable) accession number: O60704
Secondary accession number(s): B3KQA7, Q6FI98, Q9H0V4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.