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Q5SQI0 (ATAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-tubulin N-acetyltransferase 1

Short name=Alpha-TAT
Short name=Alpha-TAT1
Short name=TAT
EC=2.3.1.108
Alternative name(s):
Acetyltransferase mec-17 homolog
Gene names
Name:ATAT1
Synonyms:C6orf134, MEC17
ORF Names:Nbla00487
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Required for normal sperm flagellar function. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. 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.

Catalytic activity

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

Subunit structure

Component of the BBSome complex. 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.

Subcellular location

Cytoplasm. Membraneclathrin-coated pit. Cell junctionfocal adhesion. Cell projectionaxon By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonspindle By similarity.

Post-translational modification

Autoacetylation strongly increases tubulin acetylation By similarity.

Sequence similarities

Belongs to the acetyltransferase ATAT1 family.

Biophysicochemical properties

Kinetic parameters:

kcat is 2.2 h(-1) for the acetylation of polymerized tubulin (microtubules), 0.35 h(-1) for the acetylation of free tubulin, and 1.47 h(-1)with acetyl-CoA as substrate.

KM=2.0 µM for free alpha-tubulin

KM=1.6 µM for polymerized tubulin (microtubules)

KM=2.2 µM for acetyl-CoA

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q5SQI0-1)

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.
Isoform 2 Ref.3 Ref.5 (identifier: Q5SQI0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.
     13-36: ERITVLDQHLRPPARRPGTTTPAR → MWLTWPFCFLTITLREEGVCHLES
Isoform 3 Ref.3 (identifier: Q5SQI0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     195-218: RPPAPSLRATRHSRAAAVDPTPAA → P
Isoform 4 Ref.1 Ref.3 Ref.6 (identifier: Q5SQI0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     323-333: RGTPPGLVAQS → SSLPRSEESRY
     334-421: Missing.
Isoform 5 Ref.2 Ref.3 Ref.4 (identifier: Q5SQI0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     324-421: Missing.
Isoform 6 Ref.3 (identifier: Q5SQI0-6)

The sequence of this isoform differs from the canonical sequence as follows:
     195-218: RPPAPSLRATRHSRAAAVDPTPAA → P
     323-333: RGTPPGLVAQS → SSLPRSEESRY
     334-421: Missing.
Isoform 7 Ref.3 Ref.4 Ref.5 (identifier: Q5SQI0-7)

The sequence of this isoform differs from the canonical sequence as follows:
     195-218: RPPAPSLRATRHSRAAAVDPTPAA → P
     324-421: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Alpha-tubulin N-acetyltransferase 1
PRO_0000348066

Regions

Region124 – 13714Acetyl-CoA binding
Region160 – 16910Acetyl-CoA binding

Sites

Site581Crucial for catalytic activity

Amino acid modifications

Modified residue561N6-acetyllysine; by autocatalysis By similarity
Modified residue1461N6-acetyllysine; by autocatalysis By similarity
Modified residue2331N6-acetyllysine; by autocatalysis By similarity
Modified residue2441N6-acetyllysine; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 1212Missing in isoform 2. Ref.3 Ref.5
VSP_052899
Alternative sequence13 – 3624ERITV…TTPAR → MWLTWPFCFLTITLREEGVC HLES in isoform 2. Ref.3 Ref.5
VSP_052900
Alternative sequence195 – 21824RPPAP…PTPAA → P in isoform 3, isoform 6 and isoform 7. Ref.3 Ref.4 Ref.5
VSP_052901
Alternative sequence323 – 33311RGTPPGLVAQS → SSLPRSEESRY in isoform 4 and isoform 6. Ref.1 Ref.3 Ref.6
VSP_052902
Alternative sequence324 – 42198Missing in isoform 5 and isoform 7. Ref.2 Ref.3 Ref.4 Ref.5
VSP_052903
Alternative sequence334 – 42188Missing in isoform 4 and isoform 6. Ref.1 Ref.3 Ref.6
VSP_052904

Experimental info

Mutagenesis581Q → A: Loss of acetyltransferase activity.
Mutagenesis611S → A: No effect on catalytic activity.
Mutagenesis641I → A: Strong reduction in acetyltransferase activity.
Mutagenesis691R → A: Strong reduction in acetyltransferase activity.
Mutagenesis1051F → A: Reduced activity.
Mutagenesis1061V → A: Reduced activity.
Mutagenesis1071L → A: Reduced activity.
Mutagenesis1081D → A: Reduced activity.
Mutagenesis1091D → A: Slight increase in activity.
Mutagenesis1091D → R: Marginal increase in activity.
Mutagenesis1111E → A: 2-fold increase in activity.
Mutagenesis1111E → R: No effect on catalytic activity.
Mutagenesis1151E → A: Reduced activity.
Mutagenesis1171E → A: Reduced activity.
Mutagenesis1201C → A or S: Strong reduction in microtubule acetylation.
Mutagenesis1571D → E or N: Strong reduction in microtubule acetylation.
Mutagenesis1581R → A: 20% of wild-type acetyltransferase activity.
Mutagenesis1821N → A: Strong reduction in activity.
Mutagenesis1831F → A: Strong reduction in activity.

Secondary structure

.................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 6CC9B4B844930842

FASTA42146,810
        10         20         30         40         50         60 
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL GKASAKAQNL 

        70         80         90        100        110        120 
SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG YKKLFVLDDR EAHNEVEPLC 

       130        140        150        160        170        180 
ILDFYIHESV QRHGHGRELF QYMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV 

       190        200        210        220        230        240 
NNFVIFEGFF AHQHRPPAPS LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR 

       250        260        270        280        290        300 
EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP 

       310        320        330        340        350        360 
HPTARLLLAA DPGGSPAQRR RTRGTPPGLV AQSCCYSRHG GVNSSSPNTG NQDSKQGEQE 

       370        380        390        400        410        420 
TKNRSASEEQ ALSQDGSGEK PMHTAPPQAP APPAQSWTVG GDILNARFIR NLQERRSTRP 


W 

« Hide

Isoform 2 [UniParc].

Checksum: D2D140F7FADEDEEA
Show »

FASTA40945,574
Isoform 3 [UniParc].

Checksum: 4E53964B391B8C4F
Show »

FASTA39844,458
Isoform 4 [UniParc].

Checksum: 9AF89C8C2FF122FC
Show »

FASTA33337,478
Isoform 5 [UniParc].

Checksum: E3D8C0B120A640FB
Show »

FASTA32336,342
Isoform 6 [UniParc].

Checksum: 1F8BD442CF9A9797
Show »

FASTA31035,126
Isoform 7 [UniParc].

Checksum: 359BE466FD5562B1
Show »

FASTA30033,990

References

« Hide 'large scale' references
[1]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Neuroblastoma.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 2 AND 7).
Tissue: Brain and Lung.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-421 (ISOFORM 4).
Tissue: Brain.
[7]"MEC-17 is an alpha-tubulin acetyltransferase."
Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S., Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.
Nature 467:218-222(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[8]"The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation."
Shida T., Cueva J.G., Xu Z., Goodman M.B., Nachury M.V.
Proc. Natl. Acad. Sci. U.S.A. 107:21517-21522(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE BBSOME COMPLEX, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-157.
[9]"alphaTAT1 catalyses microtubule acetylation at clathrin-coated pits."
Montagnac G., Meas-Yedid V., Irondelle M., Castro-Castro A., Franco M., Shida T., Nachury M.V., Benmerah A., Olivo-Marin J.C., Chavrier P.
Nature 502:567-570(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AP2A2, SUBCELLULAR LOCATION.
[10]"Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA."
Taschner M., Vetter M., Lorentzen E.
Proc. Natl. Acad. Sci. U.S.A. 109:19649-19654(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 1-196 IN COMPLEX WITH ACETYL-COA, MUTAGENESIS OF GLN-58; SER-61; ILE-64 AND ARG-158.
[11]"Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and implications for tubulin-specific acetylation."
Friedmann D.R., Aguilar A., Fan J., Nachury M.V., Marmorstein R.
Proc. Natl. Acad. Sci. U.S.A. 109:19655-19660(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 2-236 IN COMPLEX WITH ACETYL-COA, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ILE-64; ARG-69; PHE-105; VAL-106; LEU-107; ASP-108; ASP-109; GLU-111; GLU-115; GLU-117; CYS-120; ASP-157; ASN-182 AND PHE-183.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB075512 mRNA. Translation: BAE45758.1.
AK023220 mRNA. Translation: BAB14472.1.
AL845353 Genomic DNA. Translation: CAI41872.2.
AL845353 Genomic DNA. Translation: CAI41875.2.
AL662800 Genomic DNA. Translation: CAI18164.1.
AL662800 Genomic DNA. Translation: CAI18165.1.
AL662800 Genomic DNA. Translation: CAI18166.2.
AL662800 Genomic DNA. Translation: CAI18167.2.
AL662800 Genomic DNA. Translation: CAI18168.2.
AL662800 Genomic DNA. Translation: CAM25498.1.
AL732442 Genomic DNA. Translation: CAI17752.1.
AL732442 Genomic DNA. Translation: CAI17753.1.
AL732442 Genomic DNA. Translation: CAI17754.2.
AL732442 Genomic DNA. Translation: CAI17755.1.
AL732442 Genomic DNA. Translation: CAM25005.1.
AL732442 Genomic DNA. Translation: CAM25006.1.
AL845353 Genomic DNA. Translation: CAI41870.1.
AL845353 Genomic DNA. Translation: CAI41871.1.
AL845353 Genomic DNA. Translation: CAI41873.2.
AL845353 Genomic DNA. Translation: CAI41874.2.
BX119957 Genomic DNA. Translation: CAM25912.1.
BX119957 Genomic DNA. Translation: CAM25913.1.
BX119957 Genomic DNA. Translation: CAM25914.1.
BX119957 Genomic DNA. Translation: CAM25915.1.
BX119957 Genomic DNA. Translation: CAM25916.1.
BX119957 Genomic DNA. Translation: CAM25917.1.
BX908728 Genomic DNA. Translation: CAQ07413.1.
BX908728 Genomic DNA. Translation: CAQ07414.1.
BX908728 Genomic DNA. Translation: CAQ07415.1.
BX908728 Genomic DNA. Translation: CAQ07416.1.
BX908728 Genomic DNA. Translation: CAQ07417.1.
BX908728 Genomic DNA. Translation: CAQ07418.1.
CR753328 Genomic DNA. Translation: CAP58454.1.
CR753328 Genomic DNA. Translation: CAP58455.1.
CR753328 Genomic DNA. Translation: CAP58456.1.
CR753328 Genomic DNA. Translation: CAP58457.1.
CR753328 Genomic DNA. Translation: CAP58458.1.
CR753328 Genomic DNA. Translation: CAP58459.1.
CR759778 Genomic DNA. Translation: CAQ09406.1.
CR759778 Genomic DNA. Translation: CAQ09407.1.
CR759778 Genomic DNA. Translation: CAQ09408.1.
CR759778 Genomic DNA. Translation: CAQ09409.1.
CR759778 Genomic DNA. Translation: CAQ09410.1.
CR759778 Genomic DNA. Translation: CAQ09411.1.
CH471081 Genomic DNA. Translation: EAX03306.1.
CH471081 Genomic DNA. Translation: EAX03307.1.
BC006105 mRNA. Translation: AAH06105.1.
BC047303 mRNA. Translation: AAH47303.1.
AL833858 mRNA. Translation: CAD38717.1.
RefSeqNP_001026892.1. NM_001031722.2.
NP_001241881.1. NM_001254952.1.
NP_079185.2. NM_024909.2.
XP_005249474.1. XM_005249417.1.
XP_005272955.1. XM_005272898.1.
XP_005275110.1. XM_005275053.1.
XP_005275245.1. XM_005275188.1.
XP_005275367.1. XM_005275310.1.
XP_005275540.1. XM_005275483.1.
XP_005275671.1. XM_005275614.1.
UniGeneHs.654798.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VWDX-ray1.25A1-194[»]
3VWEX-ray1.96A1-194[»]
4B5OX-ray1.05A1-196[»]
4B5PX-ray1.60A/B1-196[»]
4GS4X-ray2.11A2-236[»]
ProteinModelPortalQ5SQI0.
SMRQ5SQI0. Positions 1-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123036. 3 interactions.
IntActQ5SQI0. 1 interaction.

PTM databases

PhosphoSiteQ5SQI0.

Polymorphism databases

DMDM74743537.

Proteomic databases

PaxDbQ5SQI0.
PRIDEQ5SQI0.

Protocols and materials databases

DNASU79969.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318999; ENSP00000324222; ENSG00000137343. [Q5SQI0-7]
ENST00000319027; ENSP00000324459; ENSG00000137343. [Q5SQI0-6]
ENST00000329992; ENSP00000332374; ENSG00000137343. [Q5SQI0-4]
ENST00000330083; ENSP00000327832; ENSG00000137343. [Q5SQI0-2]
ENST00000376478; ENSP00000365661; ENSG00000137343. [Q5SQI0-3]
ENST00000376483; ENSP00000365666; ENSG00000137343. [Q5SQI0-5]
ENST00000376485; ENSP00000365668; ENSG00000137343. [Q5SQI0-1]
ENST00000383582; ENSP00000373076; ENSG00000206488. [Q5SQI0-2]
ENST00000383583; ENSP00000373077; ENSG00000206488. [Q5SQI0-4]
ENST00000383584; ENSP00000373078; ENSG00000206488. [Q5SQI0-7]
ENST00000383585; ENSP00000373079; ENSG00000206488. [Q5SQI0-1]
ENST00000400575; ENSP00000383419; ENSG00000206488. [Q5SQI0-5]
ENST00000400576; ENSP00000383420; ENSG00000206488. [Q5SQI0-6]
ENST00000411724; ENSP00000388617; ENSG00000234549. [Q5SQI0-5]
ENST00000416435; ENSP00000412993; ENSG00000235658. [Q5SQI0-2]
ENST00000416917; ENSP00000402998; ENSG00000234549. [Q5SQI0-7]
ENST00000417183; ENSP00000393868; ENSG00000231257. [Q5SQI0-7]
ENST00000418248; ENSP00000411362; ENSG00000231257. [Q5SQI0-5]
ENST00000420586; ENSP00000411050; ENSG00000231257. [Q5SQI0-1]
ENST00000423338; ENSP00000415000; ENSG00000223752. [Q5SQI0-7]
ENST00000423654; ENSP00000403142; ENSG00000235658. [Q5SQI0-5]
ENST00000424121; ENSP00000412198; ENSG00000223752. [Q5SQI0-6]
ENST00000425448; ENSP00000391244; ENSG00000223752. [Q5SQI0-2]
ENST00000428764; ENSP00000399509; ENSG00000235658. [Q5SQI0-4]
ENST00000430611; ENSP00000409296; ENSG00000235658. [Q5SQI0-6]
ENST00000432356; ENSP00000416994; ENSG00000234549. [Q5SQI0-1]
ENST00000432643; ENSP00000416925; ENSG00000231257. [Q5SQI0-2]
ENST00000442844; ENSP00000394914; ENSG00000235658. [Q5SQI0-1]
ENST00000443114; ENSP00000405656; ENSG00000229061. [Q5SQI0-7]
ENST00000443391; ENSP00000406071; ENSG00000229061. [Q5SQI0-6]
ENST00000445486; ENSP00000398422; ENSG00000223752. [Q5SQI0-1]
ENST00000445973; ENSP00000415408; ENSG00000231257. [Q5SQI0-6]
ENST00000446100; ENSP00000393269; ENSG00000229061. [Q5SQI0-5]
ENST00000448670; ENSP00000389129; ENSG00000229061. [Q5SQI0-2]
ENST00000449905; ENSP00000399529; ENSG00000235658. [Q5SQI0-7]
ENST00000450003; ENSP00000406421; ENSG00000223752. [Q5SQI0-4]
ENST00000450220; ENSP00000405036; ENSG00000231257. [Q5SQI0-4]
ENST00000454794; ENSP00000409067; ENSG00000229061. [Q5SQI0-1]
ENST00000454987; ENSP00000410415; ENSG00000234549. [Q5SQI0-6]
ENST00000456215; ENSP00000399452; ENSG00000234549. [Q5SQI0-4]
ENST00000456704; ENSP00000394357; ENSG00000229061. [Q5SQI0-4]
ENST00000457161; ENSP00000388171; ENSG00000223752. [Q5SQI0-5]
ENST00000457334; ENSP00000398374; ENSG00000234549. [Q5SQI0-2]
ENST00000546440; ENSP00000449304; ENSG00000231257. [Q5SQI0-3]
ENST00000547124; ENSP00000449503; ENSG00000235658. [Q5SQI0-3]
ENST00000550031; ENSP00000449729; ENSG00000234549. [Q5SQI0-3]
ENST00000551737; ENSP00000448247; ENSG00000206488. [Q5SQI0-3]
ENST00000553018; ENSP00000448905; ENSG00000229061. [Q5SQI0-3]
ENST00000553093; ENSP00000449160; ENSG00000223752. [Q5SQI0-3]
GeneID79969.
KEGGhsa:79969.
UCSCuc003nqr.4. human. [Q5SQI0-4]
uc003nqs.4. human. [Q5SQI0-6]
uc003nqv.3. human. [Q5SQI0-2]
uc003rdc.3. human. [Q5SQI0-1]
uc003rdd.3. human. [Q5SQI0-7]

Organism-specific databases

CTD79969.
GeneCardsGC06P030605.
GC06Pj30584.
GC06Pk30584.
GC06Pl30639.
GC06Pm30673.
GC06Pn30584.
GC06Po30586.
H-InvDBHIX0166068.
HIX0166337.
HIX0166615.
HIX0166865.
HIX0167123.
HIX0167356.
HIX0184148.
HGNCHGNC:21186. ATAT1.
HPAHPA046816.
HPA050999.
MIM615556. gene.
neXtProtNX_Q5SQI0.
PharmGKBPA134948212.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249793.
HOVERGENHBG055797.
InParanoidQ5SQI0.
OMAMFNARFI.
OrthoDBEOG76739W.
TreeFamTF315643.

Gene expression databases

BgeeQ5SQI0.
CleanExHS_C6orf134.
GenevestigatorQ5SQI0.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
HAMAPMF_03130. mec17.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR007965. Alpha-TAT.
[Graphical view]
PANTHERPTHR12327. PTHR12327. 1 hit.
PfamPF05301. Mec-17. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi79969.
NextBio69981.
PROQ5SQI0.
SOURCESearch...

Entry information

Entry nameATAT_HUMAN
AccessionPrimary (citable) accession number: Q5SQI0
Secondary accession number(s): A2AB28 expand/collapse secondary AC list , Q3LIB0, Q5JP39, Q5JP40, Q5JP42, Q5SQI1, Q5SU03, Q86X42, Q8NDK9, Q9BRS1, Q9H8X5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM