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Protein

Alpha-taxilin

Gene

TXLNA

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

Functioni

May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.

GO - Molecular functioni

  • cytokine activity Source: UniProtKB
  • high molecular weight B cell growth factor receptor binding Source: UniProtKB

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • B cell activation Source: Ensembl
  • cell proliferation Source: UniProtKB
  • exocytosis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-taxilin
Gene namesi
Name:TXLNA
Synonyms:TXLN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30685. TXLNA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: LIFEdb
  • extracellular region Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670668.

Polymorphism and mutation databases

BioMutaiTXLNA.
DMDMi55584162.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 546546Alpha-taxilinPRO_0000189421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei515 – 5151Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40222.
PaxDbiP40222.
PeptideAtlasiP40222.
PRIDEiP40222.

PTM databases

PhosphoSiteiP40222.

Expressioni

Tissue specificityi

Ubiquitous, with much higher expression in heart, kidney, liver and pancreas.1 Publication

Gene expression databases

BgeeiP40222.
GenevestigatoriP40222.

Organism-specific databases

HPAiHPA045383.

Interactioni

Subunit structurei

Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A, but not when these proteins are complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts with syntaxins that do not form the SNARE complex.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Azi2Q9QYP62EBI-359793,EBI-6115874From a different organism.
BTF3P202903EBI-359793,EBI-1054687
BTF3L4Q96K173EBI-359793,EBI-6137496
CCDC136Q96JN2-25EBI-359793,EBI-10171416
CCDC53Q9Y3C03EBI-359793,EBI-712969
CCDC67E9PJR55EBI-359793,EBI-10177066
CCDC67Q05D603EBI-359793,EBI-748597
CCHCR1Q8TD31-33EBI-359793,EBI-10175300
CDR2Q018503EBI-359793,EBI-1181367
CEP44Q9C0F13EBI-359793,EBI-744115
CEP57L1Q8IYX8-23EBI-359793,EBI-10181988
CEP63Q96MT83EBI-359793,EBI-741977
DKFZp451B226Q5HYH75EBI-359793,EBI-10173842
DTNBO609414EBI-359793,EBI-740402
EIF4ENIF1Q9NRA83EBI-359793,EBI-301024
GOLGA2Q083793EBI-359793,EBI-618309
GORASP2Q9H8Y83EBI-359793,EBI-739467
HAUS3Q68CZ63EBI-359793,EBI-2558217
HYPKQ9NX553EBI-359793,EBI-1048743
KANK2Q63ZY33EBI-359793,EBI-2556193
KRT13A1A4E93EBI-359793,EBI-10171552
KRT15P190123EBI-359793,EBI-739566
KRT20P359003EBI-359793,EBI-742094
KRT31Q153233EBI-359793,EBI-948001
KRT38O760153EBI-359793,EBI-1047263
KRT40Q6A1623EBI-359793,EBI-10171697
LCA5Q86VQ03EBI-359793,EBI-6658186
MBIPQ9NS73-53EBI-359793,EBI-10182361
MED4Q9NPJ63EBI-359793,EBI-394607
MEOX1P502213EBI-359793,EBI-2864512
MEOX2A4D1273EBI-359793,EBI-10172134
NACAQ137652EBI-359793,EBI-712216
NDC80O147773EBI-359793,EBI-715849
NMIQ132873EBI-359793,EBI-372942
NMIQ8WTW23EBI-359793,EBI-10174268
NSMCE2Q96MF73EBI-359793,EBI-2557388
NUP62P371983EBI-359793,EBI-347978
PPFIA1Q131363EBI-359793,EBI-745426
RCOR3Q9P2K33EBI-359793,EBI-743428
RINT1Q6NUQ13EBI-359793,EBI-726876
SMARCE1Q969G33EBI-359793,EBI-455078
SPERTQ8NA613EBI-359793,EBI-741724
STMN2Q930453EBI-359793,EBI-714194
TBK1Q9UHD24EBI-359793,EBI-356402
TCL1AP562793EBI-359793,EBI-749995
TFIP11Q9UBB93EBI-359793,EBI-1105213
TNIP1Q150253EBI-359793,EBI-357849
TP53BP2Q13625-33EBI-359793,EBI-10175039
TXLNBQ8N3L32EBI-359793,EBI-6116822
USHBP1Q8N6Y03EBI-359793,EBI-739895
VPS52Q8N1B43EBI-359793,EBI-2799833

Protein-protein interaction databases

BioGridi128297. 80 interactions.
DIPiDIP-27612N.
IntActiP40222. 55 interactions.
MINTiMINT-1150979.

Structurei

3D structure databases

ProteinModelPortaliP40222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili186 – 491306Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the taxilin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG252790.
GeneTreeiENSGT00390000001482.
HOVERGENiHBG104385.
InParanoidiP40222.
OMAiNPKNTPG.
OrthoDBiEOG70KGP6.
PhylomeDBiP40222.
TreeFamiTF318595.

Family and domain databases

InterProiIPR026183. Taxilin_fam.
[Graphical view]
PANTHERiPTHR16127. PTHR16127. 1 hit.
PfamiPF09728. Taxilin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNQDKKNGA AKQSNPKSSP GQPEAGPEGA QERPSQAAPA VEAEGPGSSQ
60 70 80 90 100
APRKPEGAQA RTAQSGALRD VSEELSRQLE DILSTYCVDN NQGGPGEDGA
110 120 130 140 150
QGEPAEPEDA EKSRTYVARN GEPEPTPVVN GEKEPSKGDP NTEEIRQSDE
160 170 180 190 200
VGDRDHRRPQ EKKKAKGLGK EITLLMQTLN TLSTPEEKLA ALCKKYAELL
210 220 230 240 250
EEHRNSQKQM KLLQKKQSQL VQEKDHLRGE HSKAVLARSK LESLCRELQR
260 270 280 290 300
HNRSLKEEGV QRAREEEEKR KEVTSHFQVT LNDIQLQMEQ HNERNSKLRQ
310 320 330 340 350
ENMELAERLK KLIEQYELRE EHIDKVFKHK DLQQQLVDAK LQQAQEMLKE
360 370 380 390 400
AEERHQREKD FLLKEAVESQ RMCELMKQQE THLKQQLALY TEKFEEFQNT
410 420 430 440 450
LSKSSEVFTT FKQEMEKMTK KIKKLEKETT MYRSRWESSN KALLEMAEEK
460 470 480 490 500
TVRDKELEGL QVKIQRLEKL CRALQTERND LNKRVQDLSA GGQGSLTDSG
510 520 530 540
PERRPEGPGA QAPSSPRVTE APCYPGAPST EASGQTGPQE PTSARA
Length:546
Mass (Da):61,891
Last modified:November 9, 2004 - v3
Checksum:i698CD74F78897DF6
GO

Sequence cautioni

The sequence AAH46565.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121K → Q in CAD89951 (PubMed:17974005).Curated
Sequence conflicti194 – 1941K → R in CAD89952 (PubMed:17974005).Curated
Sequence conflicti228 – 2281R → C in AAH80578 (PubMed:15489334).Curated
Sequence conflicti249 – 2502QR → HG (PubMed:8327514).Curated
Sequence conflicti278 – 2781Q → L in CAD89952 (PubMed:17974005).Curated
Sequence conflicti368 – 3681E → A in CAD89952 (PubMed:17974005).Curated
Sequence conflicti412 – 4121K → E in CAD89951 (PubMed:17974005).Curated
Sequence conflicti530 – 5301T → A in CAD91138 (PubMed:17974005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF516206 mRNA. Translation: AAO42465.1.
AL832636 mRNA. Translation: CAD89951.1.
AL832637 mRNA. Translation: CAD89952.1.
AL832338 mRNA. Translation: CAD91138.1.
AL049795 Genomic DNA. Translation: CAI22055.1.
CH471059 Genomic DNA. Translation: EAX07565.1.
CH471059 Genomic DNA. Translation: EAX07566.1.
BC029686 mRNA. Translation: AAH29686.1.
BC046565 mRNA. Translation: AAH46565.1. Different initiation.
BC080578 mRNA. Translation: AAH80578.1.
BC103823 mRNA. Translation: AAI03824.1.
BC103824 mRNA. Translation: AAI03825.1.
L15344 mRNA. No translation available.
CCDSiCCDS353.1.
PIRiA48203.
RefSeqiNP_787048.1. NM_175852.3.
UniGeneiHs.17987.

Genome annotation databases

EnsembliENST00000373609; ENSP00000362711; ENSG00000084652.
ENST00000373610; ENSP00000362712; ENSG00000084652.
GeneIDi200081.
KEGGihsa:200081.
UCSCiuc001bui.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF516206 mRNA. Translation: AAO42465.1.
AL832636 mRNA. Translation: CAD89951.1.
AL832637 mRNA. Translation: CAD89952.1.
AL832338 mRNA. Translation: CAD91138.1.
AL049795 Genomic DNA. Translation: CAI22055.1.
CH471059 Genomic DNA. Translation: EAX07565.1.
CH471059 Genomic DNA. Translation: EAX07566.1.
BC029686 mRNA. Translation: AAH29686.1.
BC046565 mRNA. Translation: AAH46565.1. Different initiation.
BC080578 mRNA. Translation: AAH80578.1.
BC103823 mRNA. Translation: AAI03824.1.
BC103824 mRNA. Translation: AAI03825.1.
L15344 mRNA. No translation available.
CCDSiCCDS353.1.
PIRiA48203.
RefSeqiNP_787048.1. NM_175852.3.
UniGeneiHs.17987.

3D structure databases

ProteinModelPortaliP40222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128297. 80 interactions.
DIPiDIP-27612N.
IntActiP40222. 55 interactions.
MINTiMINT-1150979.

PTM databases

PhosphoSiteiP40222.

Polymorphism and mutation databases

BioMutaiTXLNA.
DMDMi55584162.

Proteomic databases

MaxQBiP40222.
PaxDbiP40222.
PeptideAtlasiP40222.
PRIDEiP40222.

Protocols and materials databases

DNASUi200081.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373609; ENSP00000362711; ENSG00000084652.
ENST00000373610; ENSP00000362712; ENSG00000084652.
GeneIDi200081.
KEGGihsa:200081.
UCSCiuc001bui.3. human.

Organism-specific databases

CTDi200081.
GeneCardsiGC01P032645.
HGNCiHGNC:30685. TXLNA.
HPAiHPA045383.
MIMi608676. gene.
neXtProtiNX_P40222.
PharmGKBiPA142670668.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252790.
GeneTreeiENSGT00390000001482.
HOVERGENiHBG104385.
InParanoidiP40222.
OMAiNPKNTPG.
OrthoDBiEOG70KGP6.
PhylomeDBiP40222.
TreeFamiTF318595.

Miscellaneous databases

ChiTaRSiTXLNA. human.
GeneWikiiTXLNA.
GenomeRNAii200081.
NextBioi89822.
PROiP40222.
SOURCEiSearch...

Gene expression databases

BgeeiP40222.
GenevestigatoriP40222.

Family and domain databases

InterProiIPR026183. Taxilin_fam.
[Graphical view]
PANTHERiPTHR16127. PTHR16127. 1 hit.
PfamiPF09728. Taxilin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Taxilin; a novel syntaxin-binding protein that is involved in Ca2+-dependent exocytosis in neuroendocrine cells."
    Nogami S., Satoh S., Nakano M., Shimizu H., Fukushima H., Maruyama A., Terano A., Shirataki H.
    Genes Cells 8:17-28(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SYNTAXIN, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle and Spinal cord.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Ovary, Placenta and Uterus.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 234-546.
  7. "Interaction of taxilin with syntaxin which does not form the SNARE complex."
    Nogami S., Satoh S., Nakano M., Terano A., Shirataki H.
    Biochem. Biophys. Res. Commun. 311:797-802(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX1A; STX3A AND STX4A.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. 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-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTXLNA_HUMAN
AccessioniPrimary (citable) accession number: P40222
Secondary accession number(s): D3DPP6
, Q5TFJ6, Q66K62, Q86T54, Q86T85, Q86T86, Q86Y86, Q86YW3, Q8N2Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 9, 2004
Last modified: May 27, 2015
This is version 131 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

Caution

Was originally thought to be a high molecular weight interleukin (IL-14 or IL14).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.