Q9H3N1 (TMX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-related transmembrane protein 1

Alternative name(s):
Thioredoxin domain-containing protein 1
Transmembrane Trx-related protein

Gene names

Name:	TMX1
Synonyms:	TMX, TXNDC, TXNDC1
ORF Names:	PSEC0085, UNQ235/PRO268

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions.
Subcellular location	Membrane; Single-pass type I membrane protein Potential. Endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Note: Predominantly found in the endoplasmic reticulum. Ref.1
Tissue specificity	Ubiquitous. Highly expressed in kidney, liver, placenta and lung.
Sequence similarities	Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Redox-active center Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Non-traceable author statement Ref.1. Source: UniProtKB ER to Golgi vesicle-mediated transport Traceable author statement Ref.1. Source: UniProtKB cell proliferation Non-traceable author statement Ref.1. Source: UniProtKB cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW leukocyte activation Non-traceable author statement Ref.1. Source: UniProtKB negative regulation of apoptotic process Inferred from direct assay Ref.1. Source: UniProtKB positive regulation of growth Non-traceable author statement Ref.1. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement Ref.1. Source: UniProtKB response to stress Non-traceable author statement Ref.1. Source: UniProtKB signal transduction Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.1. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	arsenate reductase (thioredoxin) activity Non-traceable author statement Ref.1. Source: UniProtKB disulfide oxidoreductase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 280

254

Thioredoxin-related transmembrane protein 1

PRO_0000034153

Regions

Topological domain

27 – 180

154

Extracellular Potential

Transmembrane

181 – 203

23

Helical; Potential

Topological domain

204 – 280

77

Cytoplasmic Potential

Domain

27 – 132

106

Thioredoxin

Amino acid modifications

Modified residue

247

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Modified residue

270

1

Phosphoserine Ref.11 Ref.14 Ref.15 Ref.17

Modified residue

280

1

Phosphoserine Ref.11 Ref.15

Disulfide bond

56 ↔ 59

Redox-active Ref.1

Experimental info

Mutagenesis

56

1

C → S: Loss of reductase activity; when associated with S-59. Ref.1

Mutagenesis

59

1

C → S: Loss of reductase activity; when associated with S-56. Ref.1

Sequence conflict

14 – 16

3

LVL → MVP in AAH36460. Ref.8

Sequence conflict

98

1

T → N in AAH36460. Ref.8

Sequence conflict

177

1

V → A in BAC11593. Ref.4

Secondary structure

1

.

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.

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280

Helix Strand Turn

Details...

Beta strand

30 – 33

4

Turn

36 – 38

3

Helix

39 – 42

4

Beta strand

44 – 52

9

Helix

57 – 73

17

Helix

74 – 76

3

Beta strand

79 – 84

6

Turn

85 – 87

3

Helix

89 – 94

6

Beta strand

99 – 107

9

Beta strand

110 – 113

4

Helix

120 – 128

9

Helix

131 – 134

4

Sequences

	Sequence		Length	Mass (Da)
	Q9H3N1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: A57E222481A997DE	FASTA	280	31,791
	10 20 30 40 50 60 MAPSGSLAVP LAVLVLLLWG APWTHGRRSN VRVITDENWR ELLEGDWMIE FYAPWCPACQ 70 80 90 100 110 120 NLQPEWESFA EWGEDLEVNI AKVDVTEQPG LSGRFIITAL PTIYHCKDGE FRRYQGPRTK 130 140 150 160 170 180 KDFINFISDK EWKSIEPVSS WFGPGSVLMS SMSALFQLSM WIRTCHNYFI EDLGLPVWGS 190 200 210 220 230 240 YTVFALATLF SGLLLGLCMI FVADCLCPSK RRRPQPYPYP SKKLLSESAQ PLKKVEEEQE 250 260 270 280 ADEEDVSEEE AESKEGTNKD FPQNAIRQRS LGPSLATDKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel thioredoxin-related transmembrane protein." Matsuo Y., Akiyama N., Nakamura H., Yodoi J., Noda M., Kizaka-Kondoh S. J. Biol. Chem. 276:10032-10038(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF CYS-56 AND CYS-59.
[2]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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]. Tissue: Subthalamic nucleus.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Teratocarcinoma.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Duodenum and Hippocampus.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY. Tissue: Platelet.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-270 AND SER-280, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-270, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-270 AND SER-280, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-270, MASS SPECTROMETRY.
[18]	"The solution structure of the thioredoxin-like domain of human thioredoxin-related transmembrane protein." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 30-142.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB048246 mRNA. Translation: BAB20629.1.
AY358640 mRNA. Translation: AAQ89003.1.
AK075395 mRNA. Translation: BAC11593.1.
AK312905 mRNA. Translation: BAG35751.1.
AL080080 mRNA. Translation: CAB45700.2.
AL591807 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65678.1.
BC036460 mRNA. Translation: AAH36460.1.
BC056874 mRNA. Translation: AAH56874.2.

IPI

IPI00395887.

PIR

T12471.

RefSeq

NP_110382.3. NM_030755.4.

UniGene

Hs.125221.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X5E	NMR	-	A	30-142	[»]

ProteinModelPortal

Q9H3N1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H3N1. 8 interactions.

MINT

MINT-3067322.

STRING

9606.ENSP00000393316.

PTM databases

PhosphoSite

Q9H3N1.

Polymorphism databases

DMDM

47117631.

Proteomic databases

PaxDb

Q9H3N1.

PeptideAtlas

Q9H3N1.

PRIDE

Q9H3N1.

Protocols and materials databases

DNASU

81542.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000457354; ENSP00000393316; ENSG00000139921.

GeneID

81542.

KEGG

hsa:81542.

UCSC

uc001wza.4. human.

Organism-specific databases

CTD

81542.

GeneCards

GC14P051706.

HGNC

HGNC:15487. TMX1.

HPA

HPA003085.

MIM

610527. gene.

neXtProt

NX_Q9H3N1.

PharmGKB

PA37968.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000045750.

InParanoid

Q9H3N1.

OMA

LLWGAPW.

OrthoDB

EOG4KSPKM.

PhylomeDB

Q9H3N1.

Gene expression databases

ArrayExpress

Q9H3N1.

Bgee

Q9H3N1.

CleanEx

HS_TXNDC1.

Genevestigator

Q9H3N1.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF00085. Thioredoxin. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9H3N1.

GenomeRNAi

81542.

NextBio

71773.

SOURCE

Search...

Entry information

Entry name

TMX1_HUMAN

Accession

Primary (citable) accession number: Q9H3N1
Secondary accession number(s): B2R7A4 , Q8N487, Q8NBN5, Q9Y4T6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	March 1, 2001
Last modified:	May 29, 2013
This is version 119 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.