Reviewed, UniProtKB/Swiss-Prot O60704 (TPST2_HUMAN)

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) [Complete proteome]

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 transcript 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
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	peptidyl-tyrosine sulfation Ref.2 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum Inferred from direct assay. Source: LIFEdb integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein-tyrosine sulfotransferase activity Ref.1 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	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)
	O60704-1 [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. NP_003586.3.
UniGene	Hs.632768
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O60704.
Proteomic databases
PRIDE	O60704.
Genome annotation databases
Ensembl	ENST00000338754; ENSP00000339813; ENSG00000128294; Homo sapiens. [Genome view] ENST00000398110; ENSP00000381180; ENSG00000128294; Homo sapiens. [Genome view] ENST00000403880; ENSP00000385192; ENSG00000128294; Homo sapiens. [Genome view] ENST00000446035; ENSP00000394835; ENSG00000128294; Homo sapiens. [Genome view]
GeneID	8459.
KEGG	hsa:8459.
UCSC	uc003acv.1. human.
Organism-specific databases
CTD	8459.
GeneCards	GC22M025238.
H-InvDB	HIX0016329.
HGNC	HGNC:12021. TPST2.
HPA	HPA021054.
MIM	603126. gene.
PharmGKB	PA36700.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06830.
HOGENOM	HBG382344.
HOVERGEN	O60704.
InParanoid	O60704.
OMA	VLECRAV.
OrthoDB	EOG980MGP.
PhylomeDB	O60704.
Enzyme and pathway databases
BRENDA	2.8.2.20. 247.
Gene expression databases
ArrayExpress	O60704.
Bgee	O60704.
CleanEx	HS_TPST2.
Genevestigator	O60704.
GermOnline	ENSG00000128294. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
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:	February 9, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.