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B1AH48

- B1AH48_HUMAN

UniProt

B1AH48 - B1AH48_HUMAN

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Protein
Submitted name:

Thiosulfate sulfurtransferase

Gene
TST
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. thiosulfate sulfurtransferase activity Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Thiosulfate sulfurtransferaseImported
Gene namesi
Name:TSTImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:12388. TST.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiB1AH48.

Expressioni

Gene expression databases

ArrayExpressiB1AH48.

Structurei

3D structure databases

ProteinModelPortaliB1AH48.
SMRiB1AH48. Positions 2-124.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000157237.
HOVERGENiHBG002345.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

B1AH48-1 [UniParc]FASTAAdd to Basket

« Hide

MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE    50
RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD 100
GEHLGSFYAP RVWWMFRVFG HRTV 124
Length:124
Mass (Da):14,236
Last modified:April 8, 2008 - v1
Checksum:iADFFD39FD2A7615C
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei124 – 1241Imported

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z73420 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000438203; ENSP00000400764; ENSG00000128311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z73420 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortali B1AH48.
SMRi B1AH48. Positions 2-124.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi B1AH48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000438203 ; ENSP00000400764 ; ENSG00000128311 .

Organism-specific databases

HGNCi HGNC:12388. TST.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000157237.
HOVERGENi HBG002345.

Miscellaneous databases

NextBioi 35466348.

Gene expression databases

ArrayExpressi B1AH48.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view ]
Pfami PF00581. Rhodanese. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS00380. RHODANESE_1. 1 hit.
PS50206. RHODANESE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB1AH48_HUMAN
AccessioniPrimary (citable) accession number: B1AH48
Entry historyi
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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