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Protein

Gamma-taxilin

Gene

Txlng

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in intracellular vesicle traffic (By similarity). Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression.By similarity3 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • regulation of bone mineralization Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • regulation of cell cycle process Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-taxilin
Alternative name(s):
Factor inhibiting ATF4-mediated transcription
Short name:
FIAT
Lipopolysaccharide-responsive gene protein
Gene namesi
Name:Txlng
Synonyms:Lrg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:3590652. Txlng.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nuclear membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Gamma-taxilinPRO_0000189427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei283 – 2831PhosphotyrosineBy similarity
Modified residuei512 – 5121PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BHN1.
MaxQBiQ8BHN1.
PaxDbiQ8BHN1.
PeptideAtlasiQ8BHN1.
PRIDEiQ8BHN1.

PTM databases

iPTMnetiQ8BHN1.
PhosphoSiteiQ8BHN1.

Expressioni

Developmental stagei

At E16.5, expressed in osteoblasts surrounding newly formed trabecular bone. At postnatal day 2, detected in most osteoblasts and lining cells, and also strongly expressed in osteocytes. By postnatal week 4, strongly expressed in osteocytes (at protein level).1 Publication

Inductioni

By LPS.1 Publication

Gene expression databases

BgeeiQ8BHN1.
CleanExiMM_4932441K18RIK.
ExpressionAtlasiQ8BHN1. baseline and differential.
GenevisibleiQ8BHN1. MM.

Interactioni

Subunit structurei

Binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A and STX4A (By similarity). Forms a heterodimer with ATF4 in osteoblasts.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TBK1Q9UHD22EBI-6116854,EBI-356402From a different organism.

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

IntActiQ8BHN1. 3 interactions.
STRINGi10090.ENSMUSP00000038615.

Structurei

3D structure databases

ProteinModelPortaliQ8BHN1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili153 – 465313Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the taxilin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1850. Eukaryota.
ENOG410XQH1. LUCA.
GeneTreeiENSGT00390000001482.
HOGENOMiHOG000231384.
HOVERGENiHBG104385.
InParanoidiQ8BHN1.
OMAiEPKSQRS.
OrthoDBiEOG70KGP6.
PhylomeDBiQ8BHN1.
TreeFamiTF318595.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BHN1-1) [UniParc]FASTAAdd to basket

Also known as: LrgW

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
MATRLEEVTR GRGGGTEEAS EGGRGGRRRS PPQKFEIGTM EEARICGLGV
60 70 80 90 100
KADMVCNSQA NDILQHQDPS CGGTTKKHSL EGDEGSDFIT KNRNLVSSVF
110 120 130 140 150
CTQEKREEIP GREARTGPPD GQQDSECSRN KEKTLGKEVL LLMQALNTLS
160 170 180 190 200
TPEEKLAALC KKYADLLEES RNVQKQMKIL QKKQAQIVKE KVHLQSEHSK
210 220 230 240 250
AILARSKLES LCRELQRHNK TLKEENMQQA REEEERRKEA TAHFQITLNE
260 270 280 290 300
IQAQLEQHDI HNAKLRQENI ELGEKLKKLI EQYALREEHI DKVFKHKELQ
310 320 330 340 350
QQLVDAKLQQ TTQLIKEADE KHQREREFLL KEATESRHKY EQMKQQEVQL
360 370 380 390 400
KQQLSLYMDK FEEFQTTMAK SNELFTTFRQ EMEKMTKKIK KLEKETIIWR
410 420 430 440 450
TKWENNNKAL LQMAEEKTVR DKEYKAFQIK LERLEKLCRA LQTERNELNE
460 470 480 490 500
KVEVLKEQVS IKAADGDLVS PATQPCAVLD SFKETSRRTL GMHLEARAKS
510 520
VCEKSAAQKP SSSGSPAQGI ESVD
Length:524
Mass (Da):60,309
Last modified:March 1, 2003 - v1
Checksum:i0228777633E4ED7C
GO
Isoform 2 (identifier: Q8BHN1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-103: Missing.
     289-290: HI → VI
     291-524: Missing.

Note: No experimental confirmation available.
Show »
Length:241
Mass (Da):27,598
Checksum:i1E0C7A38E169F31A
GO
Isoform 3 (identifier: Q8BHN1-3) [UniParc]FASTAAdd to basket

Also known as: LrgS

The sequence of this isoform differs from the canonical sequence as follows:
     55-103: Missing.

Show »
Length:475
Mass (Da):55,016
Checksum:iF504425EAC95774A
GO

Sequence cautioni

The sequence ABC47035.1 differs from that shown. Reason: Frameshift at position 520. Curated
The sequence ABC47035.1 differs from that shown. Reason: Erroneous termination at position 518. Translated as Gln.Curated
The sequence ABC60327.1 differs from that shown. Reason: Frameshift at position 520. Curated
The sequence ABC60327.1 differs from that shown. Reason: Erroneous termination at position 518. Translated as Gln.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721G → D in ABC47035 (PubMed:19913514).Curated
Sequence conflicti84 – 841E → D in ABC47035 (PubMed:19913514).Curated
Sequence conflicti306 – 3061A → G in ABC47035 (PubMed:19913514).Curated
Sequence conflicti306 – 3061A → G in ABC60327 (PubMed:19913514).Curated
Sequence conflicti446 – 4461N → T in ABC60327 (PubMed:19913514).Curated
Sequence conflicti494 – 4941L → W in ABC47035 (PubMed:19913514).Curated
Sequence conflicti514 – 5141G → S in ABC60327 (PubMed:19913514).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 10349Missing in isoform 2 and isoform 3. 3 PublicationsVSP_011835Add
BLAST
Alternative sequencei289 – 2902HI → VI in isoform 2. 1 PublicationVSP_011836
Alternative sequencei291 – 524234Missing in isoform 2. 1 PublicationVSP_011837Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ316984 mRNA. Translation: ABC47035.1. Sequence problems.
DQ320011 mRNA. Translation: ABC60327.1. Sequence problems.
AK030100 mRNA. Translation: BAC26785.1.
AK031783 mRNA. Translation: BAC27547.1.
AK044130 mRNA. Translation: BAC31791.1.
AK078477 mRNA. Translation: BAC37296.1.
AL672123 Genomic DNA. Translation: CAM24319.1.
AL672123 Genomic DNA. Translation: CAM24320.1.
BC117898 mRNA. Translation: AAI17899.1.
BC117899 mRNA. Translation: AAI17900.1.
CCDSiCCDS30510.1. [Q8BHN1-1]
CCDS72463.1. [Q8BHN1-3]
CCDS81194.1. [Q8BHN1-2]
RefSeqiNP_001277705.1. NM_001290776.1. [Q8BHN1-3]
NP_001277706.1. NM_001290777.1. [Q8BHN1-2]
NP_849266.1. NM_178935.5. [Q8BHN1-1]
UniGeneiMm.270186.
Mm.371732.

Genome annotation databases

EnsembliENSMUST00000041370; ENSMUSP00000038615; ENSMUSG00000038344. [Q8BHN1-1]
ENSMUST00000112315; ENSMUSP00000107934; ENSMUSG00000038344. [Q8BHN1-2]
ENSMUST00000112316; ENSMUSP00000107935; ENSMUSG00000038344. [Q8BHN1-3]
GeneIDi353170.
KEGGimmu:353170.
UCSCiuc009uuh.2. mouse. [Q8BHN1-1]
uc009uui.2. mouse. [Q8BHN1-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ316984 mRNA. Translation: ABC47035.1. Sequence problems.
DQ320011 mRNA. Translation: ABC60327.1. Sequence problems.
AK030100 mRNA. Translation: BAC26785.1.
AK031783 mRNA. Translation: BAC27547.1.
AK044130 mRNA. Translation: BAC31791.1.
AK078477 mRNA. Translation: BAC37296.1.
AL672123 Genomic DNA. Translation: CAM24319.1.
AL672123 Genomic DNA. Translation: CAM24320.1.
BC117898 mRNA. Translation: AAI17899.1.
BC117899 mRNA. Translation: AAI17900.1.
CCDSiCCDS30510.1. [Q8BHN1-1]
CCDS72463.1. [Q8BHN1-3]
CCDS81194.1. [Q8BHN1-2]
RefSeqiNP_001277705.1. NM_001290776.1. [Q8BHN1-3]
NP_001277706.1. NM_001290777.1. [Q8BHN1-2]
NP_849266.1. NM_178935.5. [Q8BHN1-1]
UniGeneiMm.270186.
Mm.371732.

3D structure databases

ProteinModelPortaliQ8BHN1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BHN1. 3 interactions.
STRINGi10090.ENSMUSP00000038615.

PTM databases

iPTMnetiQ8BHN1.
PhosphoSiteiQ8BHN1.

Proteomic databases

EPDiQ8BHN1.
MaxQBiQ8BHN1.
PaxDbiQ8BHN1.
PeptideAtlasiQ8BHN1.
PRIDEiQ8BHN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041370; ENSMUSP00000038615; ENSMUSG00000038344. [Q8BHN1-1]
ENSMUST00000112315; ENSMUSP00000107934; ENSMUSG00000038344. [Q8BHN1-2]
ENSMUST00000112316; ENSMUSP00000107935; ENSMUSG00000038344. [Q8BHN1-3]
GeneIDi353170.
KEGGimmu:353170.
UCSCiuc009uuh.2. mouse. [Q8BHN1-1]
uc009uui.2. mouse. [Q8BHN1-3]

Organism-specific databases

CTDi55787.
MGIiMGI:3590652. Txlng.

Phylogenomic databases

eggNOGiKOG1850. Eukaryota.
ENOG410XQH1. LUCA.
GeneTreeiENSGT00390000001482.
HOGENOMiHOG000231384.
HOVERGENiHBG104385.
InParanoidiQ8BHN1.
OMAiEPKSQRS.
OrthoDBiEOG70KGP6.
PhylomeDBiQ8BHN1.
TreeFamiTF318595.

Miscellaneous databases

PROiQ8BHN1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BHN1.
CleanExiMM_4932441K18RIK.
ExpressionAtlasiQ8BHN1. baseline and differential.
GenevisibleiQ8BHN1. MM.

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. "Molecular cloning and functional characterization of a mouse gene upregulated by lipopolysaccharide treatment reveals alternative splicing."
    Du K., Chen Y., Dai Z., Bi Y., Cai T., Hou L., Chai Y., Song Q., Chen S., Luo W., Chen J.
    Biochem. Biophys. Res. Commun. 391:267-271(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-523 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, INDUCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain cortex, Head and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 3).
  5. "FIAT represses ATF4-mediated transcription to regulate bone mass in transgenic mice."
    Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J., Gauthier C., Roughley P.J., St-Arnaud R.
    J. Cell Biol. 169:591-601(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "FIAT is co-expressed with its dimerization target ATF4 in early osteoblasts, but not in osteocytes."
    Yu V.W., Akhouayri O., St-Arnaud R.
    Gene Expr. Patterns 9:335-340(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
  8. "FIAT inhibition increases osteoblast activity by modulating Atf4-dependent functions."
    Yu V.W., El-Hoss J., St-Arnaud R.
    J. Cell. Biochem. 106:186-192(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung and Spleen.

Entry informationi

Entry nameiTXLNG_MOUSE
AccessioniPrimary (citable) accession number: Q8BHN1
Secondary accession number(s): A2AFJ5
, Q148Z8, Q2LGB1, Q2PMX1, Q8BP11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.