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Protein

Transient receptor potential cation channel subfamily A member 1

Gene

TRPA1

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

Functioni

Receptor-activated non-selective cation channel involved in detection of pain and possibly also in cold perception and inner ear function (PubMed:25389312, PubMed:25855297). Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of volatile irritants, such as mustard oil, cinnamaldehyde, garlic and acrolein, an irritant from tears gas and vehicule exhaust fumes (PubMed:25389312, PubMed:20547126). Is also activated by menthol (in vitro)(PubMed:25389312). Acts also as a ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:25389312). May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system (By similarity).By similarity3 Publications

Enzyme regulationi

Inhibited by ruthenium red, a potent blocker of TRPV channels.1 Publication

GO - Molecular functioni

  • channel activity Source: ProtInc
  • intracellular ligand-gated calcium channel activity Source: UniProtKB
  • temperature-gated cation channel activity Source: UniProtKB

GO - Biological processi

  • calcium ion transmembrane transport Source: UniProtKB
  • cell surface receptor signaling pathway Source: Ensembl
  • detection of chemical stimulus involved in sensory perception of pain Source: Ensembl
  • detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
  • ion transmembrane transport Source: Reactome
  • ion transport Source: ProtInc
  • protein homotetramerization Source: UniProtKB
  • response to cold Source: Ensembl
  • response to drug Source: Ensembl
  • response to hydrogen peroxide Source: Ensembl
  • response to organic cyclic compound Source: Ensembl
  • response to organic substance Source: UniProtKB
  • response to pain Source: Ensembl
  • sensory perception of pain Source: UniProtKB
  • thermoception Source: Ensembl
  • transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Protein family/group databases

TCDBi1.A.4.6.3. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily A member 1
Alternative name(s):
Ankyrin-like with transmembrane domains protein 1
Transformation-sensitive protein p120
Gene namesi
Name:TRPA1
Synonyms:ANKTM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:497. TRPA1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 719719Cytoplasmic1 PublicationAdd
BLAST
Transmembranei720 – 74021Helical; Name=11 PublicationAdd
BLAST
Topological domaini741 – 76424Extracellular1 PublicationAdd
BLAST
Transmembranei765 – 78521Helical; Name=21 PublicationAdd
BLAST
Topological domaini786 – 80318Cytoplasmic1 PublicationAdd
BLAST
Transmembranei804 – 82421Helical; Name=31 PublicationAdd
BLAST
Topological domaini825 – 8295Extracellular1 Publication
Transmembranei830 – 85021Helical; Name=41 PublicationAdd
BLAST
Topological domaini851 – 87323Cytoplasmic1 PublicationAdd
BLAST
Transmembranei874 – 89421Helical; Name=51 PublicationAdd
BLAST
Topological domaini895 – 9017Extracellular1 Publication
Intramembranei902 – 92221Pore-forming1 PublicationAdd
BLAST
Topological domaini923 – 93412Extracellular1 PublicationAdd
BLAST
Transmembranei935 – 95622Helical; Name=61 PublicationAdd
BLAST
Topological domaini957 – 1119163Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • stereocilium bundle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Episodic pain syndrome, familial, 1 (FEPS1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant neurologic disorder characterized by onset in infancy of episodic debilitating upper body pain triggered by fasting, cold, and physical stress. The period of intense pain is accompanied by breathing difficulties, tachycardia, sweating, generalized pallor, peribuccal cyanosis, and stiffness of the abdominal wall. Affected individuals do not manifest altered pain sensitivity outside the episodes.

See also OMIM:615040
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti855 – 8551N → S in FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation. 1 Publication
VAR_069737

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615040. phenotype.
Orphaneti391389. Familial episodic pain syndrome with predominantly upper body involvement.

Chemistry

DrugBankiDB00825. Menthol.

Polymorphism and mutation databases

BioMutaiTRPA1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11191119Transient receptor potential cation channel subfamily A member 1PRO_0000215369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi192 ↔ 665AlternateBy similarity
Disulfide bondi462 ↔ 665AlternateBy similarity
Disulfide bondi608 ↔ 621AlternateBy similarity
Disulfide bondi621 ↔ 665AlternateBy similarity
Glycosylationi747 – 7471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi753 – 7531N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO75762.
PRIDEiO75762.

PTM databases

PhosphoSiteiO75762.

Expressioni

Tissue specificityi

Expressed at very low level. Expressed at very low level in human fibroblasts and at a moderate level in liposarcoma cells.1 Publication

Gene expression databases

BgeeiO75762.
CleanExiHS_TRPA1.
ExpressionAtlasiO75762. baseline and differential.
GenevisibleiO75762. HS.

Organism-specific databases

HPAiHPA026630.

Interactioni

Subunit structurei

Homotetramer (PubMed:25389312, PubMed:25855297). Interacts with TMEM100 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi114471. 1 interaction.
STRINGi9606.ENSP00000262209.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Pelectron microscopy4.24A/B/C/D2-1119[»]
ProteinModelPortaliO75762.
SMRiO75762. Positions 34-640, 693-970.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati62 – 9231ANK 1Sequence Analysis1 PublicationAdd
BLAST
Repeati97 – 12630ANK 2Sequence Analysis1 PublicationAdd
BLAST
Repeati130 – 16031ANK 3Sequence Analysis1 PublicationAdd
BLAST
Repeati164 – 19330ANK 4Sequence Analysis1 PublicationAdd
BLAST
Repeati197 – 22630ANK 5Sequence Analysis1 PublicationAdd
BLAST
Repeati238 – 26730ANK 6Sequence Analysis1 PublicationAdd
BLAST
Repeati271 – 30131ANK 7Sequence Analysis1 PublicationAdd
BLAST
Repeati308 – 33730ANK 8Sequence Analysis1 PublicationAdd
BLAST
Repeati341 – 37030ANK 9Sequence Analysis1 PublicationAdd
BLAST
Repeati374 – 40330ANK 101 PublicationAdd
BLAST
Repeati412 – 44130ANK 11Sequence Analysis1 PublicationAdd
BLAST
Repeati445 – 47430ANK 12Sequence Analysis1 PublicationAdd
BLAST
Repeati481 – 51030ANK 13Sequence Analysis1 PublicationAdd
BLAST
Repeati513 – 54230ANK 14Sequence Analysis1 PublicationAdd
BLAST
Repeati547 – 57630ANK 15Sequence Analysis1 PublicationAdd
BLAST
Repeati579 – 60931ANK 16Sequence Analysis1 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1046 – 10527Inositolphosphate binding1 Publication

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1042 – 1071301 PublicationAdd
BLAST

Domaini

C-terminal helices from the four subunits associate to form atypical coiled coil structure; this region is probably involved in binding the inositol polyphosphates that are required for optimal channel activity (in vitro).1 Publication
The ANK repeat domain consists of a convex stem structure formed by five ANK repeats and 11 additional ANK repeats that form a crescent-shaped structure that surrounds the protein core.1 Publication

Sequence similaritiesi

Contains 16 ANK repeats.PROSITE-ProRule annotation1 Publication

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00800000124084.
HOGENOMiHOG000044486.
HOVERGENiHBG059027.
InParanoidiO75762.
KOiK04984.
OMAiWLAYGFR.
PhylomeDBiO75762.
TreeFamiTF317264.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR030288. TRPA1/painless.
[Graphical view]
PANTHERiPTHR24190:SF5. PTHR24190:SF5. 1 hit.
PfamiPF00023. Ank. 10 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 14 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSLRKMWR PGEKKEPQGV VYEDVPDDTE DFKESLKVVF EGSAYGLQNF
60 70 80 90 100
NKQKKLKRCD DMDTFFLHYA AAEGQIELME KITRDSSLEV LHEMDDYGNT
110 120 130 140 150
PLHCAVEKNQ IESVKFLLSR GANPNLRNFN MMAPLHIAVQ GMNNEVMKVL
160 170 180 190 200
LEHRTIDVNL EGENGNTAVI IACTTNNSEA LQILLKKGAK PCKSNKWGCF
210 220 230 240 250
PIHQAAFSGS KECMEIILRF GEEHGYSRQL HINFMNNGKA TPLHLAVQNG
260 270 280 290 300
DLEMIKMCLD NGAQIDPVEK GRCTAIHFAA TQGATEIVKL MISSYSGSVD
310 320 330 340 350
IVNTTDGCHE TMLHRASLFD HHELADYLIS VGADINKIDS EGRSPLILAT
360 370 380 390 400
ASASWNIVNL LLSKGAQVDI KDNFGRNFLH LTVQQPYGLK NLRPEFMQMQ
410 420 430 440 450
QIKELVMDED NDGCTPLHYA CRQGGPGSVN NLLGFNVSIH SKSKDKKSPL
460 470 480 490 500
HFAASYGRIN TCQRLLQDIS DTRLLNEGDL HGMTPLHLAA KNGHDKVVQL
510 520 530 540 550
LLKKGALFLS DHNGWTALHH ASMGGYTQTM KVILDTNLKC TDRLDEDGNT
560 570 580 590 600
ALHFAAREGH AKAVALLLSH NADIVLNKQQ ASFLHLALHN KRKEVVLTII
610 620 630 640 650
RSKRWDECLK IFSHNSPGNK CPITEMIEYL PECMKVLLDF CMLHSTEDKS
660 670 680 690 700
CRDYYIEYNF KYLQCPLEFT KKTPTQDVIY EPLTALNAMV QNNRIELLNH
710 720 730 740 750
PVCKEYLLMK WLAYGFRAHM MNLGSYCLGL IPMTILVVNI KPGMAFNSTG
760 770 780 790 800
IINETSDHSE ILDTTNSYLI KTCMILVFLS SIFGYCKEAG QIFQQKRNYF
810 820 830 840 850
MDISNVLEWI IYTTGIIFVL PLFVEIPAHL QWQCGAIAVY FYWMNFLLYL
860 870 880 890 900
QRFENCGIFI VMLEVILKTL LRSTVVFIFL LLAFGLSFYI LLNLQDPFSS
910 920 930 940 950
PLLSIIQTFS MMLGDINYRE SFLEPYLRNE LAHPVLSFAQ LVSFTIFVPI
960 970 980 990 1000
VLMNLLIGLA VGDIAEVQKH ASLKRIAMQV ELHTSLEKKL PLWFLRKVDQ
1010 1020 1030 1040 1050
KSTIVYPNKP RSGGMLFHIF CFLFCTGEIR QEIPNADKSL EMEILKQKYR
1060 1070 1080 1090 1100
LKDLTFLLEK QHELIKLIIQ KMEIISETED DDSHCSFQDR FKKEQMEQRN
1110
SRWNTVLRAV KAKTHHLEP
Length:1,119
Mass (Da):127,501
Last modified:November 30, 2010 - v3
Checksum:i283BF31BC77CF71B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31R → C.1 Publication
Corresponds to variant rs13268757 [ dbSNP | Ensembl ].
VAR_020660
Natural varianti58 – 581R → T.1 Publication
Corresponds to variant rs16937976 [ dbSNP | Ensembl ].
VAR_047471
Natural varianti179 – 1791E → K.
Corresponds to variant rs920829 [ dbSNP | Ensembl ].
VAR_020661
Natural varianti186 – 1861K → N.1 Publication
Corresponds to variant rs7819749 [ dbSNP | Ensembl ].
VAR_020662
Natural varianti855 – 8551N → S in FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation. 1 Publication
VAR_069737
Natural varianti1018 – 10181H → R.
Corresponds to variant rs959976 [ dbSNP | Ensembl ].
VAR_020663

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10601 mRNA. Translation: CAA71610.1.
AC022867 Genomic DNA. No translation available.
CCDSiCCDS34908.1.
RefSeqiNP_015628.2. NM_007332.2.
XP_011515927.1. XM_011517625.1.
UniGeneiHs.716816.

Genome annotation databases

EnsembliENST00000262209; ENSP00000262209; ENSG00000104321.
GeneIDi8989.
KEGGihsa:8989.
UCSCiuc003xza.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

The power behind pain - Issue 82 of May 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10601 mRNA. Translation: CAA71610.1.
AC022867 Genomic DNA. No translation available.
CCDSiCCDS34908.1.
RefSeqiNP_015628.2. NM_007332.2.
XP_011515927.1. XM_011517625.1.
UniGeneiHs.716816.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J9Pelectron microscopy4.24A/B/C/D2-1119[»]
ProteinModelPortaliO75762.
SMRiO75762. Positions 34-640, 693-970.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114471. 1 interaction.
STRINGi9606.ENSP00000262209.

Chemistry

BindingDBiO75762.
ChEMBLiCHEMBL6007.
DrugBankiDB00825. Menthol.
GuidetoPHARMACOLOGYi485.

Protein family/group databases

TCDBi1.A.4.6.3. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteiO75762.

Polymorphism and mutation databases

BioMutaiTRPA1.

Proteomic databases

PaxDbiO75762.
PRIDEiO75762.

Protocols and materials databases

DNASUi8989.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262209; ENSP00000262209; ENSG00000104321.
GeneIDi8989.
KEGGihsa:8989.
UCSCiuc003xza.3. human.

Organism-specific databases

CTDi8989.
GeneCardsiGC08M072932.
H-InvDBHIX0034373.
HIX0124652.
HGNCiHGNC:497. TRPA1.
HPAiHPA026630.
MIMi604775. gene.
615040. phenotype.
neXtProtiNX_O75762.
Orphaneti391389. Familial episodic pain syndrome with predominantly upper body involvement.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00800000124084.
HOGENOMiHOG000044486.
HOVERGENiHBG059027.
InParanoidiO75762.
KOiK04984.
OMAiWLAYGFR.
PhylomeDBiO75762.
TreeFamiTF317264.

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Miscellaneous databases

GenomeRNAii8989.
NextBioi33711.
PROiO75762.
SOURCEiSearch...

Gene expression databases

BgeeiO75762.
CleanExiHS_TRPA1.
ExpressionAtlasiO75762. baseline and differential.
GenevisibleiO75762. HS.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR030288. TRPA1/painless.
[Graphical view]
PANTHERiPTHR24190:SF5. PTHR24190:SF5. 1 hit.
PfamiPF00023. Ank. 10 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 14 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An ankyrin-like protein with transmembrane domains is specifically lost after oncogenic transformation of human fibroblasts."
    Jaquemar D., Schenker T., Trueb B.
    J. Biol. Chem. 274:7325-7333(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS CYS-3; THR-58 AND ASN-186.
    Tissue: Lung.
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Human TRPA1 is intrinsically cold- and chemosensitive with and without its N-terminal ankyrin repeat domain."
    Moparthi L., Survery S., Kreir M., Simonsen C., Kjellbom P., Hoegestaett E.D., Johanson U., Zygmunt P.M.
    Proc. Natl. Acad. Sci. U.S.A. 111:16901-16906(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ACTIVATION BY ELECTROPHILES.
  4. "Structure of the TRPA1 ion channel suggests regulatory mechanisms."
    Paulsen C.E., Armache J.P., Gao Y., Cheng Y., Julius D.
    Nature 520:511-517(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.24 ANGSTROMS) IN COMPLEXES WITH SYNTHETIC AGONISTS, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN.
  5. Cited for: VARIANT FEPS1 SER-855, CHARACTERIZATION OF VARIANT FEPS1 SER-855, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.

Entry informationi

Entry nameiTRPA1_HUMAN
AccessioniPrimary (citable) accession number: O75762
Secondary accession number(s): A6NIN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 30, 2010
Last modified: July 22, 2015
This is version 123 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 8
    Human chromosome 8: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. 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.