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P40222

- TXLNA_HUMAN

UniProt

P40222 - TXLNA_HUMAN

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Protein

Alpha-taxilin

Gene

TXLNA

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. cytokine activity Source: UniProtKB
  2. high molecular weight B cell growth factor receptor binding Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: Ensembl
  2. cell proliferation Source: UniProtKB
  3. 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: Chromosome 1

Organism-specific databases

HGNCiHGNC:30685. TXLNA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. extracellular region Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670668.

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 – 5151Phosphoserine4 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.
NACAQ137652EBI-359793,EBI-712216
TBK1Q9UHD24EBI-359793,EBI-356402
TXLNBQ8N3L32EBI-359793,EBI-6116822

Protein-protein interaction databases

BioGridi128297. 29 interactions.
DIPiDIP-27612N.
IntActiP40222. 8 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.
OMAiRKPEGAQ.
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.

Polymorphism databases

DMDMi55584162.

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.
CCDSi CCDS353.1.
PIRi A48203.
RefSeqi NP_787048.1. NM_175852.3.
UniGenei Hs.17987.

3D structure databases

ProteinModelPortali P40222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128297. 29 interactions.
DIPi DIP-27612N.
IntActi P40222. 8 interactions.
MINTi MINT-1150979.

PTM databases

PhosphoSitei P40222.

Polymorphism databases

DMDMi 55584162.

Proteomic databases

MaxQBi P40222.
PaxDbi P40222.
PeptideAtlasi P40222.
PRIDEi P40222.

Protocols and materials databases

DNASUi 200081.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373609 ; ENSP00000362711 ; ENSG00000084652 .
ENST00000373610 ; ENSP00000362712 ; ENSG00000084652 .
GeneIDi 200081.
KEGGi hsa:200081.
UCSCi uc001bui.3. human.

Organism-specific databases

CTDi 200081.
GeneCardsi GC01P032645.
HGNCi HGNC:30685. TXLNA.
HPAi HPA045383.
MIMi 608676. gene.
neXtProti NX_P40222.
PharmGKBi PA142670668.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG252790.
GeneTreei ENSGT00390000001482.
HOVERGENi HBG104385.
InParanoidi P40222.
OMAi RKPEGAQ.
OrthoDBi EOG70KGP6.
PhylomeDBi P40222.
TreeFami TF318595.

Miscellaneous databases

ChiTaRSi TXLNA. human.
GeneWikii TXLNA.
GenomeRNAii 200081.
NextBioi 89822.
PROi P40222.
SOURCEi Search...

Gene expression databases

Bgeei P40222.
Genevestigatori P40222.

Family and domain databases

InterProi IPR026183. Taxilin_fam.
[Graphical view ]
PANTHERi PTHR16127. PTHR16127. 1 hit.
Pfami PF09728. Taxilin. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: November 26, 2014
This is version 126 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