Reviewed, UniProtKB/Swiss-Prot O88856 (TPST2_MOUSE)

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
Synonyms:	D5ucla3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the protein sulfotransferase family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-tyrosine sulfotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	Protein-tyrosine sulfotransferase 2		PRO_0000189830
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 25	17	Signal-anchor for type II membrane protein Potential
	Topological domain	26 – 376	351	Lumenal Potential
Amino acid modifications
	Glycosylation	342	1	N-linked (GlcNAc...) Ref.4
	Glycosylation	367	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	89	1	A → S in BAC29428. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O88856-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: E714C7DE3D8718D0	FASTA	376	42,067
	10 20 30 40 50 60 MRLSVRKVLL AAGCALALVL AVQLGQQVLE CRAVLGGTRN PRRMRPEQEE LVMLGADHVE 70 80 90 100 110 120 YRYGKAMPLI FVGGVPRSGT TLMRAMLDAH PEVRCGEETR IIPRVLAMRQ AWTKSGREKL 130 140 150 160 170 180 RLDEAGVTDE VLDAAMQAFI LEVIAKHGEP ARVLCNKDPF TLKSSVYLAR LFPNSKFLLM 190 200 210 220 230 240 VRDGRASVHS MITRKVTIAG FDLSSYRDCL TKWNKAIEVM YAQCMEVGRD KCLPVYYEQL 250 260 270 280 290 300 VLHPRRSLKR ILDFLGIAWS DTVLHHEDLI GKPGGVSLSK IERSTDQVIK PVNLEALSKW 310 320 330 340 350 360 TGHIPRDVVR DMAQIAPMLA RLGYDPYANP PNYGNPDPIV INNTHRVLKG DYKTPANLKG 370 YFQVNQNSTS PHLGSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone and Embryo.
[3]	"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]. Strain: Czech II. Tissue: Mammary gland.
[4]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF049890 mRNA. Translation: AAC36060.1. AK036436 mRNA. Translation: BAC29428.1. AK075672 mRNA. Translation: BAC35887.1. BC003721 mRNA. Translation: AAH03721.1.
IPI	IPI00762677.
UniGene	Mm.250631
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O88856.
Proteomic databases
PRIDE	O88856.
Genome annotation databases
Ensembl	ENSMUST00000031287; ENSMUSP00000031287; ENSMUSG00000029344; Mus musculus. [Genome view] ENSMUST00000071455; ENSMUSP00000071399; ENSMUSG00000029344; Mus musculus. [Genome view] ENSMUST00000112373; ENSMUSP00000107992; ENSMUSG00000029344; Mus musculus. [Genome view]
UCSC	uc008ysx.1. mouse.
Organism-specific databases
MGI	MGI:1309516. Tpst2.
Phylogenomic databases
HOVERGEN	O88856.
Enzyme and pathway databases
BRENDA	2.8.2.20. 244.
Gene expression databases
ArrayExpress	O88856.
Bgee	O88856.
CleanEx	MM_TPST2.
Genevestigator	O88856.
GermOnline	ENSMUSG00000029344. Mus musculus.
Family and domain databases
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

TPST2_MOUSE

Accession

Primary (citable) accession number: O88856
Secondary accession number(s): Q8CBA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	October 13, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)