Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-mercaptopyruvate sulfurtransferase

Gene

MPST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions (By similarity).By similarity

Catalytic activityi

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate.

Enzyme regulationi

By oxidative stress, and thioredoxin. Under oxidative stress conditions, the catalytic cysteine site is converted to a sulfenate which inhibits the MPST enzyme activity. Reduced thioredoxin cleaves an intersubunit disulfide bond to turn on the redox switch and reactivate the enzyme.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881SubstrateBy similarity
Active sitei248 – 2481Cysteine persulfide intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • 3-mercaptopyruvate sulfurtransferase activity Source: UniProtKB-EC
  • thiosulfate sulfurtransferase activity Source: ProtInc

GO - Biological processi

  • cyanate catabolic process Source: ProtInc
  • hydrogen sulfide biosynthetic process Source: UniProtKB
  • kidney development Source: Ensembl
  • liver development Source: Ensembl
  • response to toxic substance Source: ProtInc
  • spinal cord development Source: Ensembl
  • transsulfuration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS05177-MONOMER.
BRENDAi2.8.1.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.2)
Short name:
MST
Gene namesi
Name:MPST
Synonyms:TST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:7223. MPST.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • neuron projection Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Mitochondrion, Synapse, Synaptosome

Pathology & Biotechi

Involvement in diseasei

Aberrant MPST activity is found in a few cases of mercaptolactate-cysteine disulfiduria (MCDU) characterized by the appearance of large quantaties of the sulfur-containing amino acid, beta-mercaptolactate-cysteine disulfide, in the urine (PubMed:4973015, PubMed:4690911 and PubMed:6945862). Some cases have associated mental retardation (PubMed:4973015 and PubMed:6945862).

Organism-specific databases

MIMi249650. phenotype.
PharmGKBiPA30928.

Polymorphism and mutation databases

BioMutaiMPST.
DMDMi6226903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 2972963-mercaptopyruvate sulfurtransferasePRO_0000139398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei3 – 31PhosphoserineCombined sources
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei40 – 401N6-acetyllysine; alternateBy similarity
Modified residuei40 – 401N6-succinyllysine; alternateBy similarity
Modified residuei146 – 1461N6-succinyllysineBy similarity
Modified residuei164 – 1641N6-succinyllysineBy similarity
Disulfide bondi264 – 264Interchain (with C-264); redox-activeBy similarity
Isoform 2 (identifier: P25325-2)
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP25325.
MaxQBiP25325.
PaxDbiP25325.
PeptideAtlasiP25325.
PRIDEiP25325.

2D gel databases

OGPiP25325.
REPRODUCTION-2DPAGEIPI00165360.

PTM databases

iPTMnetiP25325.
PhosphoSiteiP25325.
SwissPalmiP25325.

Expressioni

Gene expression databases

BgeeiP25325.
CleanExiHS_MPST.
ExpressionAtlasiP25325. baseline and differential.
GenevisibleiP25325. HS.

Organism-specific databases

HPAiHPA001240.

Interactioni

Subunit structurei

Monomer; active form. Homodimer; disulfide-linked, inactive form.By similarity

Protein-protein interaction databases

BioGridi110497. 15 interactions.
DIPiDIP-613N.
IntActiP25325. 2 interactions.
STRINGi9606.ENSP00000380318.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 219Combined sources
Beta strandi29 – 335Combined sources
Helixi39 – 413Combined sources
Helixi45 – 517Combined sources
Turni62 – 643Combined sources
Beta strandi71 – 744Combined sources
Helixi79 – 8810Combined sources
Beta strandi96 – 1005Combined sources
Helixi110 – 11910Combined sources
Beta strandi125 – 1284Combined sources
Helixi131 – 1377Combined sources
Helixi160 – 1623Combined sources
Helixi166 – 17510Combined sources
Beta strandi178 – 1825Combined sources
Helixi186 – 1894Combined sources
Helixi213 – 2164Combined sources
Beta strandi219 – 2213Combined sources
Helixi226 – 23510Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi249 – 2524Combined sources
Helixi255 – 2639Combined sources
Beta strandi271 – 2744Combined sources
Helixi275 – 2839Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OLHX-ray2.50A11-289[»]
4JGTX-ray2.16A/B/C11-289[»]
ProteinModelPortaliP25325.
SMRiP25325. Positions 11-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 144120Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini174 – 288115Rhodanese 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 16016HingeAdd
BLAST

Domaini

Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).By similarity

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP25325.
KOiK01011.
OMAiSWGEWGS.
OrthoDBiEOG72ZCGB.
PhylomeDBiP25325.
TreeFamiTF315133.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25325-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE
60 70 80 90 100
ERHIPGAAFF DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY
110 120 130 140 150
DASDQGLYSA PRVWWMFRAF GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA
160 170 180 190 200
PAEFRAQLDP AFIKTYEDIK ENLESRRFQV VDSRATGRFR GTEPEPRDGI
210 220 230 240 250
EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL SKPLVATCGS
260 270 280 290
GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTH
Length:297
Mass (Da):33,178
Last modified:January 23, 2007 - v3
Checksum:i2313CC15A47A42EA
GO
Isoform 2 (identifier: P25325-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAEPGSRESETRARSPSVAAM

Show »
Length:317
Mass (Da):35,250
Checksum:iCDDCDD4B3AAC2869
GO

Sequence cautioni

The sequence AAH16737.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAG30409.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 483RRE → TQ in CAA42060 (PubMed:1953758).Curated
Sequence conflicti205 – 2051I → T in BAG51564 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAEPGSRESETRARSPSVAA M in isoform 2. 1 PublicationVSP_055027

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59434 mRNA. Translation: CAA42060.1.
BT019636 mRNA. Translation: AAV38442.1.
AK055733 mRNA. Translation: BAG51564.1.
CR541712 mRNA. Translation: CAG46513.1.
Z73420 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW60133.1.
CH471095 Genomic DNA. Translation: EAW60134.1.
CH471095 Genomic DNA. Translation: EAW60135.1.
BC003508 mRNA. Translation: AAH03508.1.
BC016737 mRNA. Translation: AAH16737.1. Different initiation.
BC018717 mRNA. Translation: AAH18717.1.
CR456523 mRNA. Translation: CAG30409.1. Different initiation.
CCDSiCCDS13939.1. [P25325-1]
CCDS46703.1. [P25325-2]
PIRiJH0461. ROHU.
RefSeqiNP_001013454.1. NM_001013436.2. [P25325-1]
NP_001123989.1. NM_001130517.2. [P25325-1]
NP_066949.2. NM_021126.5. [P25325-2]
XP_005261667.1. XM_005261610.2. [P25325-1]
UniGeneiHs.248267.

Genome annotation databases

EnsembliENST00000341116; ENSP00000342333; ENSG00000128309. [P25325-1]
ENST00000397225; ENSP00000380402; ENSG00000128309. [P25325-1]
ENST00000401419; ENSP00000384812; ENSG00000128309. [P25325-1]
ENST00000404802; ENSP00000383950; ENSG00000128309. [P25325-1]
ENST00000429360; ENSP00000411719; ENSG00000128309. [P25325-2]
GeneIDi4357.
KEGGihsa:4357.
UCSCiuc003aql.5. human. [P25325-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59434 mRNA. Translation: CAA42060.1.
BT019636 mRNA. Translation: AAV38442.1.
AK055733 mRNA. Translation: BAG51564.1.
CR541712 mRNA. Translation: CAG46513.1.
Z73420 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW60133.1.
CH471095 Genomic DNA. Translation: EAW60134.1.
CH471095 Genomic DNA. Translation: EAW60135.1.
BC003508 mRNA. Translation: AAH03508.1.
BC016737 mRNA. Translation: AAH16737.1. Different initiation.
BC018717 mRNA. Translation: AAH18717.1.
CR456523 mRNA. Translation: CAG30409.1. Different initiation.
CCDSiCCDS13939.1. [P25325-1]
CCDS46703.1. [P25325-2]
PIRiJH0461. ROHU.
RefSeqiNP_001013454.1. NM_001013436.2. [P25325-1]
NP_001123989.1. NM_001130517.2. [P25325-1]
NP_066949.2. NM_021126.5. [P25325-2]
XP_005261667.1. XM_005261610.2. [P25325-1]
UniGeneiHs.248267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OLHX-ray2.50A11-289[»]
4JGTX-ray2.16A/B/C11-289[»]
ProteinModelPortaliP25325.
SMRiP25325. Positions 11-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110497. 15 interactions.
DIPiDIP-613N.
IntActiP25325. 2 interactions.
STRINGi9606.ENSP00000380318.

PTM databases

iPTMnetiP25325.
PhosphoSiteiP25325.
SwissPalmiP25325.

Polymorphism and mutation databases

BioMutaiMPST.
DMDMi6226903.

2D gel databases

OGPiP25325.
REPRODUCTION-2DPAGEIPI00165360.

Proteomic databases

EPDiP25325.
MaxQBiP25325.
PaxDbiP25325.
PeptideAtlasiP25325.
PRIDEiP25325.

Protocols and materials databases

DNASUi4357.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341116; ENSP00000342333; ENSG00000128309. [P25325-1]
ENST00000397225; ENSP00000380402; ENSG00000128309. [P25325-1]
ENST00000401419; ENSP00000384812; ENSG00000128309. [P25325-1]
ENST00000404802; ENSP00000383950; ENSG00000128309. [P25325-1]
ENST00000429360; ENSP00000411719; ENSG00000128309. [P25325-2]
GeneIDi4357.
KEGGihsa:4357.
UCSCiuc003aql.5. human. [P25325-1]

Organism-specific databases

CTDi4357.
GeneCardsiMPST.
HGNCiHGNC:7223. MPST.
HPAiHPA001240.
MIMi249650. phenotype.
602496. gene.
neXtProtiNX_P25325.
PharmGKBiPA30928.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP25325.
KOiK01011.
OMAiSWGEWGS.
OrthoDBiEOG72ZCGB.
PhylomeDBiP25325.
TreeFamiTF315133.

Enzyme and pathway databases

BioCyciMetaCyc:HS05177-MONOMER.
BRENDAi2.8.1.2. 2681.

Miscellaneous databases

ChiTaRSiMPST. human.
GeneWikiiMPST.
GenomeRNAii4357.
PROiP25325.
SOURCEiSearch...

Gene expression databases

BgeeiP25325.
CleanExiHS_MPST.
ExpressionAtlasiP25325. baseline and differential.
GenevisibleiP25325. HS.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes."
    Pallini R., Guazzi G.C., Cannella C., Cacace M.G.
    Biochem. Biophys. Res. Commun. 180:887-893(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "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] (ISOFORM 1).
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Bone marrow, Muscle and Pancreas.
  8. Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  9. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 89-112 AND 119-133, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  10. "Mental deficiency and a new aminoaciduria."
    Ampola M.G., Efron M.L., Bixby E.M., Meshorer E.
    Am. J. Dis. Child. 117:66-70(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
  11. "beta-Mercaptolactate cysteine disulfiduria in two normal sisters. Isolation and characterization of beta-mercaptolactate cysteine disulfide."
    Niederwiesler A., Giliberti P., Baerlocher K.
    Clin. Chim. Acta 43:405-416(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
  12. "3-mercaptolactate cysteine disulfiduria: biochemical studies on affected and unaffected members of a family."
    Hannestad U., Martensson J., Sjodahl R., Sorbo B.
    Biochem. Med. 26:106-114(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-35, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-23 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Human 3-mercaptopyruvate sulfurtransferase."
    Structural genomics consortium (SGC)
    Submitted (SEP-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 11-289.

Entry informationi

Entry nameiTHTM_HUMAN
AccessioniPrimary (citable) accession number: P25325
Secondary accession number(s): A8MZ34
, B3KP52, J3KPV7, O75750, Q6FHN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 154 of the entry and version 3 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

Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are required to release hydrogen sulfide from the persulfide intermediate.By similarity

Caution

Was originally thought to be rhodanese.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.