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Protein

Alpha-tubulin N-acetyltransferase 1

Gene

Atat1

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

Functioni

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly. Required for normal sperm flagellar function. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity (PubMed:23275437).5 Publications

Catalytic activityi

Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Crucial for catalytic activityUniRule annotation

GO - Molecular functioni

  • coenzyme binding Source: MGI
  • tubulin N-acetyltransferase activity Source: UniProtKB

GO - Biological processi

  • alpha-tubulin acetylation Source: MGI
  • dentate gyrus development Source: MGI
  • neuron development Source: UniProtKB-HAMAP
  • positive regulation of NLRP3 inflammasome complex assembly Source: MGI
  • regulation of fat cell differentiation Source: MGI
  • regulation of microtubule cytoskeleton organization Source: UniProtKB-HAMAP
  • spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-MMU-5617833. Assembly of the primary cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-tubulin N-acetyltransferase 1UniRule annotation (EC:2.3.1.108UniRule annotation)
Short name:
Alpha-TATUniRule annotation
Short name:
Alpha-TAT1UniRule annotation
Short name:
TATUniRule annotation
Alternative name(s):
Acetyltransferase mec-17 homologUniRule annotation
Gene namesi
Name:Atat1
Synonyms:Mec17
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1913869. Atat1.

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Cytoplasmcytoskeleton UniRule annotation1 Publication
  • Cell projectionaxon UniRule annotation1 Publication
  • Cytoplasmcytoskeletonspindle UniRule annotation1 Publication
  • Membraneclathrin-coated pit UniRule annotation
  • Cell junctionfocal adhesion UniRule annotation

  • Note: In primary root dorsal ganglion neurons, localizes with acetylated tubulin in axons. Recruited to the mitotic spindle during cell division.

GO - Cellular componenti

  • axon Source: UniProtKB-SubCell
  • coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • focal adhesion Source: UniProtKB-SubCell
  • Golgi apparatus Source: MGI
  • microtubule Source: InterPro
  • microtubule bundle Source: MGI
  • mitotic spindle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Coated pit, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice are viable and show no overt phenotype. Drastic loss of tubulin acetylation in all tissues anlyzed, including in early embryos. In dorsal hippocampus, but not in ventral hippocampus, the dentate gyrus is slightly deformed, showing a prominent bulge in the lateral blade of the granular cell layers. In addition, the lateral ventricle appears to be dilated (PubMed:23720746). Homozygous mutant males exhibit decreased fertility (PubMed:23748901). Mature spermatozoa from cauda epididymis often show the presence of a cytoplasmic droplet attached to the annulus of the tail, indicative of impaired maturation. The flagella length is also significantly decreased in spermatozoa, especially in those cells with a cytoplasmic droplet. Spermatozoa display significantly lower motility than control sperm. However, sperm flagella display the characteristic 9 + 2 organization of axoneme microtubules (PubMed:23748901).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561K → R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-146; R-233 and R-244. 1 Publication
Mutagenesisi134 – 1341G → W: Loss of catalytic activity, but function in microtubule stability not affected; when associated with W-136 and P-139. 1 Publication
Mutagenesisi136 – 1361G → W: Loss of activity, but function in microtubule stability not affected; when associated with W-134 and P-139. 1 Publication
Mutagenesisi139 – 1391L → P: Loss of activity, but function in microtubule stability not affected; when associated with W-134 and W-136. 1 Publication
Mutagenesisi146 – 1461K → R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-233 and R-244. 1 Publication
Mutagenesisi233 – 2331K → R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-146 and R-244. 1 Publication
Mutagenesisi244 – 2441K → R: Strong reduction in tubulin acetylation, no effect on tubulin-binding; when associated with R-56; R-146 and R-233. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Alpha-tubulin N-acetyltransferase 1PRO_0000348067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-acetyllysine; by autocatalysisUniRule annotation1 Publication
Modified residuei146 – 1461N6-acetyllysine; by autocatalysisUniRule annotation1 Publication
Modified residuei233 – 2331N6-acetyllysine; by autocatalysisUniRule annotationCombined sources1 Publication
Modified residuei244 – 2441N6-acetyllysine; by autocatalysisUniRule annotation1 Publication
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei276 – 2761PhosphoserineBy similarity
Modified residuei315 – 3151PhosphoserineCombined sources

Post-translational modificationi

Autoacetylation strongly increases tubulin acetylation.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8K341.
PaxDbiQ8K341.
PRIDEiQ8K341.

PTM databases

iPTMnetiQ8K341.
PhosphoSiteiQ8K341.

Expressioni

Tissue specificityi

Widely expressed with highest levels in neuronal tissues. In the brain, expressed in the cortex, cerebellum and hippocampus, including the pyramidal layers in CA1 and CA3, as well as the granular cell layers in the lateral blade (suprapyramidal portion) and the medial blade (infrapyramidal portion) of the dentate gyrus. In testis, mainly expressed in the internal cell layers of seminiferous tubules, where spermatocytes and spermatids are located.2 Publications

Developmental stagei

Widely expressed in embryos during development with particularly high expression in the spinal cord at 13.5 dpc.1 Publication

Gene expression databases

BgeeiQ8K341.
ExpressionAtlasiQ8K341. baseline and differential.
GenevisibleiQ8K341. MM.

Interactioni

Subunit structurei

Component of the BBSome complex (By similarity). Interacts with AP2 alpha-adaptins, including AP2A2, but not with AP1 gamma-adaptin (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin acetylation, hence clathrin-coated pits are sites of microtubule acetylation.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi215858. 1 interaction.
DIPiDIP-60604N.
STRINGi10090.ENSMUSP00000056383.

Structurei

3D structure databases

ProteinModelPortaliQ8K341.
SMRiQ8K341. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 190190N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 13714Acetyl-CoA bindingUniRule annotationAdd
BLAST
Regioni160 – 16910Acetyl-CoA bindingUniRule annotation
Regioni308 – 38780Required for AP2A2-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the acetyltransferase ATAT1 family.UniRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4601. Eukaryota.
ENOG4111Q8H. LUCA.
GeneTreeiENSGT00390000008276.
HOVERGENiHBG055797.
InParanoidiQ8K341.
KOiK19573.
OMAiPMHTAPP.
OrthoDBiEOG76739W.
TreeFamiTF315643.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
HAMAPiMF_03130. mec17.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR007965. GNAT_ATAT.
[Graphical view]
PfamiPF05301. Acetyltransf_16. 1 hit.
[Graphical view]
PROSITEiPS51730. GNAT_ATAT. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q8K341-1) [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
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL
60 70 80 90 100
GKASAKAQHL PAPITSALRM QSNRHVIYIL KDTSARPAGK GAIIGFLKVG
110 120 130 140 150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QHMLQKERVE
160 170 180 190 200
PHQLAIDRPS PKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPTSS
210 220 230 240 250
LRATRHSRAA VADPIPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP
260 270 280 290 300
WPLNRAPRRA TPPAHPPPRS SSLGNSPDRG PLRPFVPEQE LLRSLRLCPP
310 320 330 340 350
HPTARLLLAT DPGGSPAQRR RTRGTPWGLV AQSCHYSRHG GFNTSFLGTG
360 370 380 390 400
NQERKQGEQE AEDRSASEDR VLLLDGSGEE PTQTGAPRAQ APPPQSWTVG
410 420
GDIMNARVIR NLQERRSTRP W
Length:421
Mass (Da):47,164
Last modified:October 1, 2002 - v1
Checksum:iE47F1060F183D19C
GO
Isoform 21 Publication (identifier: Q8K341-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-218: RPPTSSLRATRHSRAAVADPIPAA → P

Show »
Length:398
Mass (Da):44,780
Checksum:i274CC3D32CA11CB1
GO
Isoform 31 Publication (identifier: Q8K341-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-353: GTPWGLVAQSCHYSRHGGFNTSFLGTGNQE → SHTHTTTVSLDAWYFHRQPRTEAGGTGSGG
     354-421: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:353
Mass (Da):39,603
Checksum:iC42201C82267F320
GO
Isoform 41 Publication (identifier: Q8K341-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     323-333: RGTPWGLVAQS → SSLPRSDESRY
     334-421: Missing.

Show »
Length:333
Mass (Da):37,528
Checksum:i7D54796E19DD98F3
GO
Isoform 51 Publication (identifier: Q8K341-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-218: RPPTSSLRATRHSRAAVADPIPAA → P
     323-333: RGTPWGLVAQS → SSLPRSDESRY
     334-421: Missing.

Show »
Length:310
Mass (Da):35,144
Checksum:iF70634A8F614833E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921A → V in AAH30669 (PubMed:15489334).Curated
Sequence conflicti102 – 1021K → E in BAC28808 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 21824RPPTS…PIPAA → P in isoform 2 and isoform 5. 2 PublicationsVSP_052905Add
BLAST
Alternative sequencei323 – 33311RGTPWGLVAQS → SSLPRSDESRY in isoform 4 and isoform 5. 1 PublicationVSP_052906Add
BLAST
Alternative sequencei324 – 35330GTPWG…TGNQE → SHTHTTTVSLDAWYFHRQPR TEAGGTGSGG in isoform 3. 1 PublicationVSP_052908Add
BLAST
Alternative sequencei334 – 42188Missing in isoform 4 and isoform 5. 1 PublicationVSP_052907Add
BLAST
Alternative sequencei354 – 42168Missing in isoform 3. 1 PublicationVSP_052909Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028297 mRNA. Translation: BAC25866.1.
AK034725 mRNA. Translation: BAC28808.1.
AK133694 mRNA. Translation: BAE21786.1.
CR974451 Genomic DNA. Translation: CAX15764.1.
CR974451 Genomic DNA. Translation: CAX15766.1.
BC028847 mRNA. Translation: AAH28847.1.
BC030669 mRNA. Translation: AAH30669.1.
CCDSiCCDS28711.1. [Q8K341-5]
CCDS50096.1. [Q8K341-1]
CCDS50097.1. [Q8K341-4]
RefSeqiNP_001136216.1. NM_001142744.1. [Q8K341-1]
NP_001136217.1. NM_001142745.1. [Q8K341-4]
NP_082752.3. NM_028476.4. [Q8K341-5]
XP_011241195.1. XM_011242893.1. [Q8K341-3]
XP_011244957.1. XM_011246655.1. [Q8K341-3]
XP_011249629.1. XM_011251327.1. [Q8K341-3]
UniGeneiMm.273155.

Genome annotation databases

EnsembliENSMUST00000056034; ENSMUSP00000053853; ENSMUSG00000024426. [Q8K341-5]
ENSMUST00000061052; ENSMUSP00000056383; ENSMUSG00000024426. [Q8K341-1]
ENSMUST00000077494; ENSMUSP00000076703; ENSMUSG00000024426. [Q8K341-2]
ENSMUST00000141662; ENSMUSP00000115004; ENSMUSG00000024426. [Q8K341-4]
ENSMUST00000149277; ENSMUSP00000122715; ENSMUSG00000024426. [Q8K341-3]
GeneIDi73242.
KEGGimmu:73242.
UCSCiuc008cja.3. mouse. [Q8K341-1]
uc008cjb.3. mouse. [Q8K341-3]
uc008cjc.3. mouse. [Q8K341-2]
uc008cjd.3. mouse. [Q8K341-5]
uc008cje.3. mouse. [Q8K341-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028297 mRNA. Translation: BAC25866.1.
AK034725 mRNA. Translation: BAC28808.1.
AK133694 mRNA. Translation: BAE21786.1.
CR974451 Genomic DNA. Translation: CAX15764.1.
CR974451 Genomic DNA. Translation: CAX15766.1.
BC028847 mRNA. Translation: AAH28847.1.
BC030669 mRNA. Translation: AAH30669.1.
CCDSiCCDS28711.1. [Q8K341-5]
CCDS50096.1. [Q8K341-1]
CCDS50097.1. [Q8K341-4]
RefSeqiNP_001136216.1. NM_001142744.1. [Q8K341-1]
NP_001136217.1. NM_001142745.1. [Q8K341-4]
NP_082752.3. NM_028476.4. [Q8K341-5]
XP_011241195.1. XM_011242893.1. [Q8K341-3]
XP_011244957.1. XM_011246655.1. [Q8K341-3]
XP_011249629.1. XM_011251327.1. [Q8K341-3]
UniGeneiMm.273155.

3D structure databases

ProteinModelPortaliQ8K341.
SMRiQ8K341. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215858. 1 interaction.
DIPiDIP-60604N.
STRINGi10090.ENSMUSP00000056383.

PTM databases

iPTMnetiQ8K341.
PhosphoSiteiQ8K341.

Proteomic databases

MaxQBiQ8K341.
PaxDbiQ8K341.
PRIDEiQ8K341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056034; ENSMUSP00000053853; ENSMUSG00000024426. [Q8K341-5]
ENSMUST00000061052; ENSMUSP00000056383; ENSMUSG00000024426. [Q8K341-1]
ENSMUST00000077494; ENSMUSP00000076703; ENSMUSG00000024426. [Q8K341-2]
ENSMUST00000141662; ENSMUSP00000115004; ENSMUSG00000024426. [Q8K341-4]
ENSMUST00000149277; ENSMUSP00000122715; ENSMUSG00000024426. [Q8K341-3]
GeneIDi73242.
KEGGimmu:73242.
UCSCiuc008cja.3. mouse. [Q8K341-1]
uc008cjb.3. mouse. [Q8K341-3]
uc008cjc.3. mouse. [Q8K341-2]
uc008cjd.3. mouse. [Q8K341-5]
uc008cje.3. mouse. [Q8K341-4]

Organism-specific databases

CTDi79969.
MGIiMGI:1913869. Atat1.

Phylogenomic databases

eggNOGiKOG4601. Eukaryota.
ENOG4111Q8H. LUCA.
GeneTreeiENSGT00390000008276.
HOVERGENiHBG055797.
InParanoidiQ8K341.
KOiK19573.
OMAiPMHTAPP.
OrthoDBiEOG76739W.
TreeFamiTF315643.

Enzyme and pathway databases

ReactomeiR-MMU-5617833. Assembly of the primary cilium.

Miscellaneous databases

NextBioi337742.
PROiQ8K341.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K341.
ExpressionAtlasiQ8K341. baseline and differential.
GenevisibleiQ8K341. MM.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
HAMAPiMF_03130. mec17.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR007965. GNAT_ATAT.
[Graphical view]
PfamiPF05301. Acetyltransf_16. 1 hit.
[Graphical view]
PROSITEiPS51730. GNAT_ATAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 3; 4 AND 5).
    Strain: C57BL/6JImported.
    Tissue: EmbryoImported, Embryonic headImported and PituitaryImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6JImported and Czech IIImported.
    Tissue: Mammary glandImported and Mammary tumorImported.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Heart.
  5. Cited for: FUNCTION.
  6. "Mice lacking alpha-tubulin acetyltransferase 1 are viable but display alpha-tubulin acetylation deficiency and dentate gyrus distortion."
    Kim G.W., Li L., Gorbani M., You L., Yang X.J.
    J. Biol. Chem. 288:20334-20350(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. "Tubulin acetyltransferase alphaTAT1 destabilizes microtubules independently of its acetylation activity."
    Kalebic N., Martinez C., Perlas E., Hublitz P., Bilbao-Cortes D., Fiedorczuk K., Andolfo A., Heppenstall P.A.
    Mol. Cell. Biol. 33:1114-1123(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACETYLATION AT LYS-56; LYS-146; LYS-233 AND LYS-244, MUTAGENESIS OF LYS-56; GLY-134; GLY-136; LEU-139; LYS-146; LYS-233 AND LYS-244.
  9. "alphaTAT1 is the major alpha-tubulin acetyltransferase in mice."
    Kalebic N., Sorrentino S., Perlas E., Bolasco G., Martinez C., Heppenstall P.A.
    Nat. Commun. 4:1962-1962(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. Cited for: FUNCTION, INTERACTION WITH AP2A2.

Entry informationi

Entry nameiATAT_MOUSE
AccessioniPrimary (citable) accession number: Q8K341
Secondary accession number(s): B8JJ75
, B8JJ77, Q3UZR9, Q8BM67, Q8C1D1, Q8K2M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 84 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.