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Protein

Thioredoxin-related transmembrane protein 1

Gene

TMX1

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

Functioni

May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions.

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: UniProtKB
  2. protein disulfide isomerase activity Source: GO_Central

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. protein folding Source: GO_Central
  3. response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-related transmembrane protein 1
Alternative name(s):
Thioredoxin domain-containing protein 1
Transmembrane Trx-related protein
Gene namesi
Name:TMX1
Synonyms:TMX, TXNDC, TXNDC1
ORF Names:PSEC0085, UNQ235/PRO268
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:15487. TMX1.

Subcellular locationi

Membrane Curated; Single-pass type I membrane protein Curated. Endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated
Note: Predominantly found in the endoplasmic reticulum.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 180154ExtracellularSequence AnalysisAdd
BLAST
Transmembranei181 – 20323HelicalSequence AnalysisAdd
BLAST
Topological domaini204 – 28077CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561C → S: Loss of reductase activity; when associated with S-59. 1 Publication
Mutagenesisi59 – 591C → S: Loss of reductase activity; when associated with S-56. 1 Publication

Organism-specific databases

PharmGKBiPA37968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 280254Thioredoxin-related transmembrane protein 1PRO_0000034153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 59Redox-activePROSITE-ProRule annotation1 Publication
Modified residuei247 – 2471Phosphoserine8 Publications
Modified residuei270 – 2701Phosphoserine4 Publications
Modified residuei280 – 2801Phosphoserine2 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9H3N1.
PaxDbiQ9H3N1.
PeptideAtlasiQ9H3N1.
PRIDEiQ9H3N1.

PTM databases

PhosphoSiteiQ9H3N1.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in kidney, liver, placenta and lung.

Gene expression databases

BgeeiQ9H3N1.
CleanExiHS_TXNDC1.
ExpressionAtlasiQ9H3N1. baseline and differential.
GenevestigatoriQ9H3N1.

Organism-specific databases

HPAiHPA003085.

Interactioni

Protein-protein interaction databases

BioGridi123510. 15 interactions.
IntActiQ9H3N1. 12 interactions.
MINTiMINT-3067322.
STRINGi9606.ENSP00000393316.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 334Combined sources
Turni36 – 383Combined sources
Helixi39 – 424Combined sources
Beta strandi44 – 529Combined sources
Helixi57 – 7317Combined sources
Helixi74 – 763Combined sources
Beta strandi79 – 846Combined sources
Turni85 – 873Combined sources
Helixi89 – 946Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi110 – 1134Combined sources
Helixi120 – 1289Combined sources
Helixi131 – 1344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5ENMR-A30-142[»]
ProteinModelPortaliQ9H3N1.
SMRiQ9H3N1. Positions 24-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H3N1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 132106ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00390000011580.
HOGENOMiHOG000045750.
InParanoidiQ9H3N1.
OMAiAPWTHGR.
OrthoDBiEOG7KM5VC.
PhylomeDBiQ9H3N1.
TreeFamiTF106376.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H3N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSGSLAVP LAVLVLLLWG APWTHGRRSN VRVITDENWR ELLEGDWMIE
60 70 80 90 100
FYAPWCPACQ NLQPEWESFA EWGEDLEVNI AKVDVTEQPG LSGRFIITAL
110 120 130 140 150
PTIYHCKDGE FRRYQGPRTK KDFINFISDK EWKSIEPVSS WFGPGSVLMS
160 170 180 190 200
SMSALFQLSM WIRTCHNYFI EDLGLPVWGS YTVFALATLF SGLLLGLCMI
210 220 230 240 250
FVADCLCPSK RRRPQPYPYP SKKLLSESAQ PLKKVEEEQE ADEEDVSEEE
260 270 280
AESKEGTNKD FPQNAIRQRS LGPSLATDKS
Length:280
Mass (Da):31,791
Last modified:February 28, 2001 - v1
Checksum:iA57E222481A997DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 163LVL → MVP in AAH36460 (PubMed:15489334).Curated
Sequence conflicti98 – 981T → N in AAH36460 (PubMed:15489334).Curated
Sequence conflicti177 – 1771V → A in BAC11593 (PubMed:16303743).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41953.1.
PIRiT12471.
RefSeqiNP_110382.3. NM_030755.4.
UniGeneiHs.125221.

Genome annotation databases

EnsembliENST00000457354; ENSP00000393316; ENSG00000139921.
GeneIDi81542.
KEGGihsa:81542.
UCSCiuc001wza.4. human.

Polymorphism databases

DMDMi47117631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41953.1.
PIRiT12471.
RefSeqiNP_110382.3. NM_030755.4.
UniGeneiHs.125221.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5ENMR-A30-142[»]
ProteinModelPortaliQ9H3N1.
SMRiQ9H3N1. Positions 24-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123510. 15 interactions.
IntActiQ9H3N1. 12 interactions.
MINTiMINT-3067322.
STRINGi9606.ENSP00000393316.

PTM databases

PhosphoSiteiQ9H3N1.

Polymorphism databases

DMDMi47117631.

Proteomic databases

MaxQBiQ9H3N1.
PaxDbiQ9H3N1.
PeptideAtlasiQ9H3N1.
PRIDEiQ9H3N1.

Protocols and materials databases

DNASUi81542.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000457354; ENSP00000393316; ENSG00000139921.
GeneIDi81542.
KEGGihsa:81542.
UCSCiuc001wza.4. human.

Organism-specific databases

CTDi81542.
GeneCardsiGC14P051706.
HGNCiHGNC:15487. TMX1.
HPAiHPA003085.
MIMi610527. gene.
neXtProtiNX_Q9H3N1.
PharmGKBiPA37968.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00390000011580.
HOGENOMiHOG000045750.
InParanoidiQ9H3N1.
OMAiAPWTHGR.
OrthoDBiEOG7KM5VC.
PhylomeDBiQ9H3N1.
TreeFamiTF106376.

Miscellaneous databases

EvolutionaryTraceiQ9H3N1.
GeneWikiiTMX1.
GenomeRNAii81542.
NextBioi71773.
PROiQ9H3N1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3N1.
CleanExiHS_TXNDC1.
ExpressionAtlasiQ9H3N1. baseline and differential.
GenevestigatoriQ9H3N1.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF CYS-56 AND CYS-59.
  2. 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(2003) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Teratocarcinoma.
  5. 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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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(2003) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-270 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-270 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "The solution structure of the thioredoxin-like domain of human thioredoxin-related transmembrane protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 30-142.

Entry informationi

Entry nameiTMX1_HUMAN
AccessioniPrimary (citable) accession number: Q9H3N1
Secondary accession number(s): B2R7A4
, Q8N487, Q8NBN5, Q9Y4T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2004
Last sequence update: February 28, 2001
Last modified: March 3, 2015
This is version 135 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

External Data

Dasty 3

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 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.