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Protein

Thiamine-triphosphatase

Gene

THTPA

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

Functioni

Hydrolase highly specific for thiamine triphosphate (ThTP).2 Publications

Catalytic activityi

Thiamine triphosphate + H2O = thiamine diphosphate + phosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=8 µM for thiamine triphosphate1 Publication
  1. Vmax=59 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71MagnesiumBy similarity
Metal bindingi9 – 91MagnesiumBy similarity
Binding sitei11 – 111Substrate
Binding sitei55 – 551Substrate
Binding sitei57 – 571Substrate
Binding sitei65 – 651Substrate
Binding sitei125 – 1251Substrate
Metal bindingi145 – 1451MagnesiumBy similarity
Metal bindingi157 – 1571MagnesiumBy similarity
Binding sitei157 – 1571Substrate
Metal bindingi159 – 1591MagnesiumBy similarity
Binding sitei193 – 1931SubstrateCurated

GO - Molecular functioni

  • hydrolase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • thiamin-triphosphatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.6.1.28. 2681.
ReactomeiREACT_11117. Vitamin B1 (thiamin) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine-triphosphatase (EC:3.6.1.28)
Short name:
ThTPase
Gene namesi
Name:THTPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:18987. THTPA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111K → A: Mildly decreases enzyme activity. 1 Publication
Mutagenesisi37 – 371D → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
Mutagenesisi39 – 391Y → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
Mutagenesisi53 – 531W → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
Mutagenesisi65 – 651K → A: Strongly decreases enzyme activity. No effect on affinity for thiamine triphosphate. 1 Publication
Mutagenesisi79 – 791Y → A: Decreases enzyme activity. 1 Publication
Mutagenesisi81 – 811E → A: Mildly decreases enzyme activity. 1 Publication
Mutagenesisi147 – 1471D → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
Mutagenesisi193 – 1931K → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA38774.

Polymorphism and mutation databases

BioMutaiTHTPA.
DMDMi37538018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 230229Thiamine-triphosphatasePRO_0000221490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9BU02.
PaxDbiQ9BU02.
PeptideAtlasiQ9BU02.
PRIDEiQ9BU02.

PTM databases

PhosphoSiteiQ9BU02.

Expressioni

Tissue specificityi

Widely expressed but at a low level.1 Publication

Gene expression databases

BgeeiQ9BU02.
CleanExiHS_THTPA.
ExpressionAtlasiQ9BU02. baseline.
GenevisibleiQ9BU02. HS.

Organism-specific databases

HPAiHPA028876.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi122595. 11 interactions.
IntActiQ9BU02. 1 interaction.
STRINGi9606.ENSP00000288014.

Structurei

Secondary structure

1
230
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi18 – 247Combined sources
Beta strandi28 – 4114Combined sources
Helixi46 – 494Combined sources
Beta strandi53 – 575Combined sources
Turni58 – 603Combined sources
Beta strandi61 – 7010Combined sources
Beta strandi77 – 826Combined sources
Helixi85 – 9612Combined sources
Helixi106 – 1138Combined sources
Beta strandi116 – 13116Combined sources
Helixi132 – 1354Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi141 – 1499Combined sources
Beta strandi154 – 16411Combined sources
Helixi165 – 1673Combined sources
Helixi168 – 18114Combined sources
Helixi193 – 2019Combined sources
Helixi203 – 21311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BHDX-ray1.50A/B1-215[»]
3TVLX-ray2.30A/B1-230[»]
ProteinModelPortaliQ9BU02.
SMRiQ9BU02. Positions 3-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BU02.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 201197CYTHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ThTPase family.Curated
Contains 1 CYTH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG42323.
GeneTreeiENSGT00390000005996.
HOGENOMiHOG000154571.
HOVERGENiHBG057173.
InParanoidiQ9BU02.
KOiK05307.
OMAiRDTYYDT.
OrthoDBiEOG7288SN.
PhylomeDBiQ9BU02.
TreeFamiTF333398.

Family and domain databases

Gene3Di2.40.320.10. 1 hit.
InterProiIPR023577. CYTH-like_domain.
IPR012177. ThTPase.
[Graphical view]
PfamiPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFiPIRSF036561. ThTPase. 1 hit.
SUPFAMiSSF55154. SSF55154. 1 hit.
PROSITEiPS51707. CYTH. 1 hit.
[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: Q9BU02-1) [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
MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA
60 70 80 90 100
DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG
110 120 130 140 150
LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD
160 170 180 190 200
FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR
210 220 230
FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG
Length:230
Mass (Da):25,566
Last modified:January 23, 2007 - v3
Checksum:i49B79C6C1D19D91D
GO
Isoform 2 (identifier: Q9BU02-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-105: LRADGLGAGD → CLHRRQHQPS
     106-230: Missing.

Note: No experimental confirmation available.
Show »
Length:105
Mass (Da):12,038
Checksum:iD326E9A8991B8A1F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761H → R.
Corresponds to variant rs34015250 [ dbSNP | Ensembl ].
VAR_062152

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 10510LRADGLGAGD → CLHRRQHQPS in isoform 2. 1 PublicationVSP_047213
Alternative sequencei106 – 230125Missing in isoform 2. 1 PublicationVSP_047214Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF432862 mRNA. Translation: AAM22403.1.
AK057691 mRNA. Translation: BAB71546.1.
BX161435 mRNA. Translation: CAD61907.1.
BX378775 mRNA. No translation available.
AL135999 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66140.1.
CH471078 Genomic DNA. Translation: EAW66141.1.
BC002984 mRNA. Translation: AAH02984.1.
CCDSiCCDS32053.1. [Q9BU02-1]
CCDS58307.1. [Q9BU02-2]
RefSeqiNP_001119811.1. NM_001126339.3. [Q9BU02-1]
NP_001242991.1. NM_001256062.2. [Q9BU02-2]
NP_001243250.1. NM_001256321.2. [Q9BU02-2]
NP_001243251.1. NM_001256322.2.
NP_001243252.1. NM_001256323.2.
NP_077304.1. NM_024328.5. [Q9BU02-1]
UniGeneiHs.655179.
Hs.732304.
Hs.736905.

Genome annotation databases

EnsembliENST00000288014; ENSP00000288014; ENSG00000259431. [Q9BU02-1]
ENST00000404535; ENSP00000384580; ENSG00000259431. [Q9BU02-1]
ENST00000554789; ENSP00000450459; ENSG00000259431. [Q9BU02-2]
ENST00000556015; ENSP00000451835; ENSG00000259431. [Q9BU02-2]
GeneIDi79178.
KEGGihsa:79178.
UCSCiuc001wkg.5. human. [Q9BU02-1]
uc031qnv.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF432862 mRNA. Translation: AAM22403.1.
AK057691 mRNA. Translation: BAB71546.1.
BX161435 mRNA. Translation: CAD61907.1.
BX378775 mRNA. No translation available.
AL135999 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66140.1.
CH471078 Genomic DNA. Translation: EAW66141.1.
BC002984 mRNA. Translation: AAH02984.1.
CCDSiCCDS32053.1. [Q9BU02-1]
CCDS58307.1. [Q9BU02-2]
RefSeqiNP_001119811.1. NM_001126339.3. [Q9BU02-1]
NP_001242991.1. NM_001256062.2. [Q9BU02-2]
NP_001243250.1. NM_001256321.2. [Q9BU02-2]
NP_001243251.1. NM_001256322.2.
NP_001243252.1. NM_001256323.2.
NP_077304.1. NM_024328.5. [Q9BU02-1]
UniGeneiHs.655179.
Hs.732304.
Hs.736905.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BHDX-ray1.50A/B1-215[»]
3TVLX-ray2.30A/B1-230[»]
ProteinModelPortaliQ9BU02.
SMRiQ9BU02. Positions 3-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122595. 11 interactions.
IntActiQ9BU02. 1 interaction.
STRINGi9606.ENSP00000288014.

PTM databases

PhosphoSiteiQ9BU02.

Polymorphism and mutation databases

BioMutaiTHTPA.
DMDMi37538018.

Proteomic databases

MaxQBiQ9BU02.
PaxDbiQ9BU02.
PeptideAtlasiQ9BU02.
PRIDEiQ9BU02.

Protocols and materials databases

DNASUi79178.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288014; ENSP00000288014; ENSG00000259431. [Q9BU02-1]
ENST00000404535; ENSP00000384580; ENSG00000259431. [Q9BU02-1]
ENST00000554789; ENSP00000450459; ENSG00000259431. [Q9BU02-2]
ENST00000556015; ENSP00000451835; ENSG00000259431. [Q9BU02-2]
GeneIDi79178.
KEGGihsa:79178.
UCSCiuc001wkg.5. human. [Q9BU02-1]
uc031qnv.1. human.

Organism-specific databases

CTDi79178.
GeneCardsiGC14P024025.
HGNCiHGNC:18987. THTPA.
HPAiHPA028876.
MIMi611612. gene.
neXtProtiNX_Q9BU02.
PharmGKBiPA38774.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42323.
GeneTreeiENSGT00390000005996.
HOGENOMiHOG000154571.
HOVERGENiHBG057173.
InParanoidiQ9BU02.
KOiK05307.
OMAiRDTYYDT.
OrthoDBiEOG7288SN.
PhylomeDBiQ9BU02.
TreeFamiTF333398.

Enzyme and pathway databases

BRENDAi3.6.1.28. 2681.
ReactomeiREACT_11117. Vitamin B1 (thiamin) metabolism.

Miscellaneous databases

ChiTaRSiTHTPA. human.
EvolutionaryTraceiQ9BU02.
GenomeRNAii79178.
NextBioi68161.
PROiQ9BU02.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BU02.
CleanExiHS_THTPA.
ExpressionAtlasiQ9BU02. baseline.
GenevisibleiQ9BU02. HS.

Family and domain databases

Gene3Di2.40.320.10. 1 hit.
InterProiIPR023577. CYTH-like_domain.
IPR012177. ThTPase.
[Graphical view]
PfamiPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFiPIRSF036561. ThTPase. 1 hit.
SUPFAMiSSF55154. SSF55154. 1 hit.
PROSITEiPS51707. CYTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues."
    Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B., De Pauw E., Wins P., Grisar T., Bettendorff L.
    J. Biol. Chem. 277:13771-13777(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "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: Trachea.
  3. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Lung.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase."
    Delvaux D., Kerff F., Murty M.R., Lakaye B., Czerniecki J., Kohn G., Wins P., Herman R., Gabelica V., Heuze F., Tordoir X., Maree R., Matagne A., Charlier P., De Pauw E., Bettendorff L.
    Biochim. Biophys. Acta 1830:4513-4523(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH TRIPHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF LYS-11; ASP-37; TYR-39; TRP-53; LYS-65; TYR-79; GLU-81; ASP-147 AND LYS-193.

Entry informationi

Entry nameiTHTPA_HUMAN
AccessioniPrimary (citable) accession number: Q9BU02
Secondary accession number(s): D3DS50, G3V4J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 128 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

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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.