ATAT1

Functionⁱ

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. 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.

UniRule annotation4 Publications

Catalytic activityⁱ

acetyl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-lysyl-[α-tubulin]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁶-acetyl-L-lysyl-[α-tubulin]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03130
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.9
  "Luminal localization of alpha-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules."
  Soppina V., Herbstman J.F., Skiniotis G., Verhey K.J.
  PLoS ONE 7:E48204-E48204(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION.
- Ref.14
  "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, CATALYTIC ACTIVITY, 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.
- Ref.15
  "Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase."
  Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L., Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.
  Cell 157:1405-1415(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-194 IN COMPLEX WITH ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-64; LYS-102 AND ARG-158.
EC:
2.3.1.108
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03130
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.9
  "Luminal localization of alpha-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules."
  Soppina V., Herbstman J.F., Skiniotis G., Verhey K.J.
  PLoS ONE 7:E48204-E48204(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION.
- Ref.14
  "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, CATALYTIC ACTIVITY, 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.
- Ref.15
  "Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase."
  Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L., Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.
  Cell 157:1405-1415(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-194 IN COMPLEX WITH ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-64; LYS-102 AND ARG-158.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
acetyl-CoA
zoom
+
L-lysyl-[α-tubulin]
L-lysine residue
zoom
=
CoA
+
H⁺
+
N⁶-acetyl-L-lysyl-[α-tubulin]
N⁶-acetyl-L-lysine residue
zoom

Kineticsⁱ

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.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	58	Crucial for catalytic activityUniRule annotation1 Publication		1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase

Molecular function

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAⁱ	2.3.1.108, 2681
PathwayCommonsⁱ	Q5SQI0
Reactomeⁱ	R-HSA-5617833, Cilium Assembly

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Alpha-tubulin N-acetyltransferase 1UniRule annotation (EC:2.3.1.108UniRule annotation3 Publications) 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:ATAT1UniRule annotation Synonyms:C6orf134, MEC17UniRule annotation ORF Names:Nbla00487
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:21186, ATAT1
MIMⁱ	615556, gene
neXtProtⁱ	NX_Q5SQI0
VEuPathDBⁱ	HostDB:ENSG00000137343.17

Keywords - Cellular componentⁱ

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

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	58	Q → A: Loss of acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	61	S → A: No effect on catalytic activity. 1 Publication	1
Mutagenesisⁱ	64	I → A: Strong reduction in acetyltransferase activity. 3 Publications	1
Mutagenesisⁱ	69	R → A: Strong reduction in acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	102	K → A: Strong reduction in acetyltransferase activity. 1 Publication	1
Mutagenesisⁱ	105	F → A: Reduced activity. 1 Publication	1
Mutagenesisⁱ	106	V → A: Reduced activity. 1 Publication	1
Mutagenesisⁱ	107	L → A: Reduced activity. 1 Publication	1
Mutagenesisⁱ	108	D → A: Reduced activity. 1 Publication	1
Mutagenesisⁱ	109	D → A: Slight increase in activity. 1 Publication	1
Mutagenesisⁱ	109	D → R: Marginal increase in activity. 1 Publication	1
Mutagenesisⁱ	111	E → A: 2-fold increase in activity. 1 Publication	1
Mutagenesisⁱ	111	E → R: No effect on catalytic activity. 1 Publication	1
Mutagenesisⁱ	115	E → A: Reduced activity. 1 Publication	1
Mutagenesisⁱ	117	E → A: Reduced activity. 1 Publication	1
Mutagenesisⁱ	120	C → A or S: Strong reduction in microtubule acetylation. 1 Publication	1
Mutagenesisⁱ	157	D → E or N: Strong reduction in microtubule acetylation. 2 Publications	1
Mutagenesisⁱ	158	R → A: 20% of wild-type acetyltransferase activity. 2 Publications	1
Mutagenesisⁱ	182	N → A: Strong reduction in activity. 1 Publication	1
Mutagenesisⁱ	183	F → A: Strong reduction in activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	79969
Open Targets More...OpenTargetsⁱ	ENSG00000137343
PharmGKBⁱ	PA134948212

Miscellaneous databases

Pharosⁱ	Q5SQI0, Tbio

Pharosⁱ

Q5SQI0, Tbio

Genetic variation databases

BioMutaⁱ	ATAT1
DMDMⁱ	74743537

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000348066	1 – 421	Alpha-tubulin N-acetyltransferase 1Add BLAST		421

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	56	N6-acetyllysine; by autocatalysisUniRule annotationBy similarity	1
Modified residueⁱ	146	N6-acetyllysine; by autocatalysisUniRule annotationBy similarity	1
Modified residueⁱ	233	N6-acetyllysine; by autocatalysisUniRule annotationBy similarity	1
Modified residueⁱ	244	N6-acetyllysine; by autocatalysisUniRule annotationBy similarity	1
Modified residueⁱ	272	PhosphoserineBy similarity	1
Modified residueⁱ	276	PhosphoserineCombined sources	1
Modified residueⁱ	305	Asymmetric dimethylarginineBy similarity	1
Modified residueⁱ	315	PhosphoserineCombined sources	1
Modified residueⁱ	323	Omega-N-methylarginineCombined sources	1

Post-translational modificationⁱ

Autoacetylation strongly increases tubulin acetylation.UniRule annotation

Keywords - PTMⁱ

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q5SQI0
jPOSTⁱ	Q5SQI0
MassIVEⁱ	Q5SQI0
PaxDbⁱ	Q5SQI0
PeptideAtlas More...PeptideAtlasⁱ	Q5SQI0
PRIDEⁱ	Q5SQI0
ProteomicsDBⁱ	63801 [Q5SQI0-1] 63802 [Q5SQI0-2] 63803 [Q5SQI0-3] 63804 [Q5SQI0-4] 63805 [Q5SQI0-5] 63806 [Q5SQI0-6] 63807 [Q5SQI0-7]

PTM databases

iPTMnetⁱ	Q5SQI0
PhosphoSitePlusⁱ	Q5SQI0

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000137343, Expressed in cortical plate and 180 other tissues
ExpressionAtlasⁱ	Q5SQI0, baseline and differential
Genevisibleⁱ	Q5SQI0, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000137343, Low tissue specificity

HPAⁱ

ENSG00000137343, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

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.

UniRule annotation4 Publications

Protein-protein interaction databases

BioGRIDⁱ	123036, 10 interactors
IntActⁱ	Q5SQI0, 8 interactors
STRINGⁱ	9606.ENSP00000327832

Miscellaneous databases

RNActⁱ	Q5SQI0, protein

RNActⁱ

Q5SQI0, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	7 – 10	Combined sources	4
Beta strandⁱ	13 – 18	Combined sources	6
Helixⁱ	36 – 57	Combined sources	22
Helixⁱ	67 – 72	Combined sources	6
Beta strandⁱ	76 – 81	Combined sources	6
Beta strandⁱ	93 – 101	Combined sources	9
Beta strandⁱ	104 – 107	Combined sources	4
Beta strandⁱ	109 – 111	Combined sources	3
Beta strandⁱ	113 – 116	Combined sources	4
Beta strandⁱ	119 – 126	Combined sources	8
Helixⁱ	128 – 130	Combined sources	3
Helixⁱ	135 – 147	Combined sources	13
Helixⁱ	151 – 153	Combined sources	3
Beta strandⁱ	155 – 158	Combined sources	4
Helixⁱ	161 – 171	Combined sources	11
Beta strandⁱ	182 – 184	Combined sources	3
Turnⁱ	187 – 190	Combined sources	4
Helixⁱ	191 – 194	Combined sources	4

Show more details

3D structure databases

SMRⁱ	Q5SQI0
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 190	N-acetyltransferaseUniRule annotationAdd BLAST		190

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	124 – 137	Acetyl-CoA bindingUniRule annotation3 PublicationsAdd BLAST	14
Regionⁱ	160 – 169	Acetyl-CoA bindingUniRule annotation3 Publications	10
Regionⁱ	196 – 235	DisorderedSequence analysisAdd BLAST	40
Regionⁱ	252 – 284	DisorderedSequence analysisAdd BLAST	33
Regionⁱ	306 – 402	DisorderedSequence analysisAdd BLAST	97

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	255 – 270	Pro residuesSequence analysisAdd BLAST		16
Compositional biasⁱ	337 – 356	Polar residuesSequence analysisAdd BLAST		20

Sequence similaritiesⁱ

Belongs to the acetyltransferase ATAT1 family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	KOG4601, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008276
HOGENOMⁱ	CLU_025013_0_0_1
InParanoidⁱ	Q5SQI0
OMAⁱ	HESRQRC
PhylomeDBⁱ	Q5SQI0
TreeFamⁱ	TF315643

Family and domain databases

HAMAPⁱ	MF_03130, mec17, 1 hit
InterProⁱ	View protein in InterPro IPR038746, Atat IPR007965, GNAT_ATAT
PANTHERⁱ	PTHR12327, PTHR12327, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05301, Acetyltransf_16, 1 hit
PROSITEⁱ	View protein in PROSITE PS51730, GNAT_ATAT, 1 hit

Sequences (7)ⁱ

Sequence statusⁱ: Complete.

This entry describes 7 isoformsⁱ produced by alternative splicing. Align Add to basket

Isoform 11 Publication (identifier: Q5SQI0-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ 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 QQIMTIIDEL 
        60         70         80         90        100
GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 
       110        120        130        140        150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 
       160        170        180        190        200
PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPAPS 
       210        220        230        240        250
LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP 
       260        270        280        290        300
WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP 
       310        320        330        340        350
HPTARLLLAA DPGGSPAQRR RTRGTPPGLV AQSCCYSRHG GVNSSSPNTG 
       360        370        380        390        400
NQDSKQGEQE TKNRSASEEQ ALSQDGSGEK PMHTAPPQAP APPAQSWTVG 
       410        420 
GDILNARFIR NLQERRSTRP W

Length:421

Mass (Da):46,810

Last modified:December 21, 2004 - v1

Checksum:ⁱ6CC9B4B844930842

GO

Isoform 22 Publications (identifier: Q5SQI0-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-12: Missing.
13-36: ERITVLDQHLRPPARRPGTTTPAR → MWLTWPFCFLTITLREEGVCHLES

« Hide

        10         20         30         40         50
MWLTWPFCFL TITLREEGVC HLESVDLQQQ IMTIIDELGK ASAKAQNLSA 
        60         70         80         90        100
PITSASRMQS NRHVVYILKD SSARPAGKGA IIGFIKVGYK KLFVLDDREA 
       110        120        130        140        150
HNEVEPLCIL DFYIHESVQR HGHGRELFQY MLQKERVEPH QLAIDRPSQK 
       160        170        180        190        200
LLKFLNKHYN LETTVPQVNN FVIFEGFFAH QHRPPAPSLR ATRHSRAAAV 
       210        220        230        240        250
DPTPAAPARK LPPKRAEGDI KPYSSSDREF LKVAVEPPWP LNRAPRRATP 
       260        270        280        290        300
PAHPPPRSSS LGNSPERGPL RPFVPEQELL RSLRLCPPHP TARLLLAADP 
       310        320        330        340        350
GGSPAQRRRT RGTPPGLVAQ SCCYSRHGGV NSSSPNTGNQ DSKQGEQETK 
       360        370        380        390        400
NRSASEEQAL SQDGSGEKPM HTAPPQAPAP PAQSWTVGGD ILNARFIRNL 

QERRSTRPW

Show »

Length:409

Mass (Da):45,574

Checksum:ⁱD2D140F7FADEDEEA

GO

Isoform 31 Publication (identifier: Q5SQI0-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL 
        60         70         80         90        100
GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 
       110        120        130        140        150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 
       160        170        180        190        200
PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHPPARKL 
       210        220        230        240        250
PPKRAEGDIK PYSSSDREFL KVAVEPPWPL NRAPRRATPP AHPPPRSSSL 
       260        270        280        290        300
GNSPERGPLR PFVPEQELLR SLRLCPPHPT ARLLLAADPG GSPAQRRRTR 
       310        320        330        340        350
GTPPGLVAQS CCYSRHGGVN SSSPNTGNQD SKQGEQETKN RSASEEQALS 
       360        370        380        390 
QDGSGEKPMH TAPPQAPAPP AQSWTVGGDI LNARFIRNLQ ERRSTRPW

Show »

Length:398

Mass (Da):44,458

Checksum:ⁱ4E53964B391B8C4F

GO

Isoform 42 Publications (identifier: Q5SQI0-4) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL 
        60         70         80         90        100
GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 
       110        120        130        140        150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 
       160        170        180        190        200
PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPAPS 
       210        220        230        240        250
LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP 
       260        270        280        290        300
WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP 
       310        320        330 
HPTARLLLAA DPGGSPAQRR RTSSLPRSEE SRY

Show »

Length:333

Mass (Da):37,478

Checksum:ⁱ9AF89C8C2FF122FC

GO

Isoform 52 Publications (identifier: Q5SQI0-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
324-421: Missing.

« Hide

        10         20         30         40         50
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL 
        60         70         80         90        100
GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 
       110        120        130        140        150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 
       160        170        180        190        200
PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHRPPAPS 
       210        220        230        240        250
LRATRHSRAA AVDPTPAAPA RKLPPKRAEG DIKPYSSSDR EFLKVAVEPP 
       260        270        280        290        300
WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP 
       310        320 
HPTARLLLAA DPGGSPAQRR RTR

Show »

Length:323

Mass (Da):36,342

Checksum:ⁱE3D8C0B120A640FB

GO

Isoform 61 Publication (identifier: Q5SQI0-6) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-218: RPPAPSLRATRHSRAAAVDPTPAA → P
     323-333: RGTPPGLVAQS → SSLPRSEESRY
     334-421: Missing.

« Hide

        10         20         30         40         50
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL 
        60         70         80         90        100
GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 
       110        120        130        140        150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 
       160        170        180        190        200
PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHPPARKL 
       210        220        230        240        250
PPKRAEGDIK PYSSSDREFL KVAVEPPWPL NRAPRRATPP AHPPPRSSSL 
       260        270        280        290        300
GNSPERGPLR PFVPEQELLR SLRLCPPHPT ARLLLAADPG GSPAQRRRTS 
       310
SLPRSEESRY

Show »

Length:310

Mass (Da):35,126

Checksum:ⁱ1F8BD442CF9A9797

GO

Isoform 72 Publications (identifier: Q5SQI0-7) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL 
        60         70         80         90        100
GKASAKAQNL SAPITSASRM QSNRHVVYIL KDSSARPAGK GAIIGFIKVG 
       110        120        130        140        150
YKKLFVLDDR EAHNEVEPLC ILDFYIHESV QRHGHGRELF QYMLQKERVE 
       160        170        180        190        200
PHQLAIDRPS QKLLKFLNKH YNLETTVPQV NNFVIFEGFF AHQHPPARKL 
       210        220        230        240        250
PPKRAEGDIK PYSSSDREFL KVAVEPPWPL NRAPRRATPP AHPPPRSSSL 
       260        270        280        290        300
GNSPERGPLR PFVPEQELLR SLRLCPPHPT ARLLLAADPG GSPAQRRRTR

Show »

Length:300

Mass (Da):33,990

Checksum:ⁱ359BE466FD5562B1

GO

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_052899	1 – 12	Missing in isoform 2. 2 PublicationsAdd BLAST	12
Alternative sequenceⁱVSP_052900	13 – 36	ERITV…TTPAR → MWLTWPFCFLTITLREEGVC HLES in isoform 2. 2 PublicationsAdd BLAST	24
Alternative sequenceⁱVSP_052901	195 – 218	RPPAP…PTPAA → P in isoform 3, isoform 6 and isoform 7. 2 PublicationsAdd BLAST	24
Alternative sequenceⁱVSP_052902	323 – 333	RGTPPGLVAQS → SSLPRSEESRY in isoform 4 and isoform 6. 3 PublicationsAdd BLAST	11
Alternative sequenceⁱVSP_052903	324 – 421	Missing in isoform 5 and isoform 7. 3 PublicationsAdd BLAST	98
Alternative sequenceⁱVSP_052904	334 – 421	Missing in isoform 4 and isoform 6. 3 PublicationsAdd BLAST	88

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB075512 mRNA Translation: BAE45758.1 AK023220 mRNA Translation: BAB14472.1 AL662800 Genomic DNA No translation available. AL732442 Genomic DNA No translation available. AL845353 Genomic DNA No translation available. BX119957 Genomic DNA No translation available. BX908728 Genomic DNA No translation available. CR753328 Genomic DNA No translation available. CR759778 Genomic DNA No translation available. 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4683.2 [Q5SQI0-4] CCDS54978.1 [Q5SQI0-2] CCDS59002.1 [Q5SQI0-6] CCDS83072.1 [Q5SQI0-5] CCDS83073.1 [Q5SQI0-7]
NCBI Reference Sequences More...RefSeqⁱ	NP_001026892.1, NM_001031722.3 [Q5SQI0-2] NP_001177653.1, NM_001190724.2 NP_001241881.1, NM_001254952.2 [Q5SQI0-6] NP_001305691.1, NM_001318762.1 [Q5SQI0-7] NP_001305692.1, NM_001318763.1 [Q5SQI0-5] NP_079185.2, NM_024909.3 [Q5SQI0-4]

Genome annotation databases

Ensemblⁱ	ENST00000318999; ENSP00000324222; ENSG00000137343 [Q5SQI0-7] ENST00000319027; ENSP00000324459; ENSG00000137343 [Q5SQI0-6] ENST00000329992; ENSP00000332374; ENSG00000137343 [Q5SQI0-4] ENST00000330083; ENSP00000327832; ENSG00000137343 [Q5SQI0-2] 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]
GeneIDⁱ	79969
KEGGⁱ	hsa:79969
UCSC genome browser More...UCSCⁱ	uc003nqr.5, human [Q5SQI0-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q5SQI0-2	Alpha-tubulin N-acetyltransferase 1		HUMAN		409	UniRef100_A0A1U9X797
Q5SQI0-4	Alpha-tubulin N-acetyltransferase 1		PANPA		333	UniRef100_A0A2R9ADW2
Alpha-tubulin N-acetyltransferase 1		NOMLE		333
+1
Q5SQI0-5	Alpha-tubulin N-acetyltransferase 1		PANPA		423	UniRef100_A0A2R9AD03
Alpha-tubulin N-acetyltransferase 1		NOMLE		423
+1
Q5SQI0-6	Alpha-tubulin N-acetyltransferase 1		PANPA		310	UniRef100_A0A2R9ACX9
Alpha-tubulin N-acetyltransferase 1		NOMLE		310
+1

Protein	Similar proteins		Species	Score	Length	Source
Q5SQI0	Alpha-tubulin N-acetyltransferase 1		MACMU		487	UniRef90_Q5SQI0
Alpha-tubulin N-acetyltransferase 1		MACFA		487
Alpha-tubulin N-acetyltransferase 1		MANLE		423
Alpha-tubulin N-acetyltransferase 1		CHLSB		487
Alpha-tubulin N-acetyltransferase 1		PONAB		425
+98
Q5SQI0-6	Alpha-tubulin N-acetyltransferase 1		PANPA		310	UniRef90_A0A2R9ACX9
Alpha-tubulin N-acetyltransferase 1		NOMLE		310
Alpha-tubulin N-acetyltransferase 1		PANTR		310
Alpha-tubulin N-acetyltransferase 1		PAPAN		310
Alpha-tubulin N-acetyltransferase 1		RHIRO		310
+9

Protein	Similar proteins		Species	Score	Length	Source
Q5SQI0	Alpha-tubulin N-acetyltransferase 1		MACMU		323	UniRef50_Q5SQI0
Alpha-tubulin N-acetyltransferase 1		MACFA		487
Alpha-tubulin N-acetyltransferase 1		MANLE		423
Alpha-tubulin N-acetyltransferase 1		CHLSB		487
Alpha-tubulin N-acetyltransferase 1		PONAB		425
+235
Q5SQI0-6	Alpha-tubulin N-acetyltransferase 1		MOUSE		421	UniRef50_Q8K341
Alpha-tubulin N-acetyltransferase 1		MUSCR		421
Alpha-tubulin N-acetyltransferase 1		DIPOR		444
Alpha-tubulin N-acetyltransferase 1		PIG		392
Alpha-tubulin N-acetyltransferase 1		PROCO		310
+305

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB075512 mRNA Translation: BAE45758.1 AK023220 mRNA Translation: BAB14472.1 AL662800 Genomic DNA No translation available. AL732442 Genomic DNA No translation available. AL845353 Genomic DNA No translation available. BX119957 Genomic DNA No translation available. BX908728 Genomic DNA No translation available. CR753328 Genomic DNA No translation available. CR759778 Genomic DNA No translation available. 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
CCDSⁱ	CCDS4683.2 [Q5SQI0-4] CCDS54978.1 [Q5SQI0-2] CCDS59002.1 [Q5SQI0-6] CCDS83072.1 [Q5SQI0-5] CCDS83073.1 [Q5SQI0-7]
RefSeqⁱ	NP_001026892.1, NM_001031722.3 [Q5SQI0-2] NP_001177653.1, NM_001190724.2 NP_001241881.1, NM_001254952.2 [Q5SQI0-6] NP_001305691.1, NM_001318762.1 [Q5SQI0-7] NP_001305692.1, NM_001318763.1 [Q5SQI0-5] NP_079185.2, NM_024909.3 [Q5SQI0-4]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3VWD	X-ray	1.25	A	1-194	[»]
	3VWE	X-ray	1.96	A	1-194	[»]
	4B5O	X-ray	1.05	A	1-196	[»]
	4B5P	X-ray	1.60	A/B	1-196	[»]
	4GS4	X-ray	2.11	A	2-236	[»]
	4IF5	X-ray	1.70	A	1-193	[»]
	4PK2	X-ray	1.35	A	1-194	[»]
	4PK3	X-ray	1.35	A	1-194	[»]
	4U9Y	X-ray	2.20	A	1-194	[»]
	4U9Z	X-ray	1.80	A	1-194	[»]
SMRⁱ	Q5SQI0
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	123036, 10 interactors
IntActⁱ	Q5SQI0, 8 interactors
STRINGⁱ	9606.ENSP00000327832

PTM databases

iPTMnetⁱ	Q5SQI0
PhosphoSitePlusⁱ	Q5SQI0

Genetic variation databases

BioMutaⁱ	ATAT1
DMDMⁱ	74743537

Proteomic databases

EPDⁱ	Q5SQI0
jPOSTⁱ	Q5SQI0
MassIVEⁱ	Q5SQI0
PaxDbⁱ	Q5SQI0
PeptideAtlasⁱ	Q5SQI0
PRIDEⁱ	Q5SQI0
ProteomicsDBⁱ	63801 [Q5SQI0-1] 63802 [Q5SQI0-2] 63803 [Q5SQI0-3] 63804 [Q5SQI0-4] 63805 [Q5SQI0-5] 63806 [Q5SQI0-6] 63807 [Q5SQI0-7]

Protocols and materials databases

ABCDⁱ	Q5SQI0, 1 sequenced antibody
Antibodypediaⁱ	26411, 128 antibodies
The DNASU plasmid repository More...DNASUⁱ	79969

Genome annotation databases

Ensemblⁱ	ENST00000318999; ENSP00000324222; ENSG00000137343 [Q5SQI0-7] ENST00000319027; ENSP00000324459; ENSG00000137343 [Q5SQI0-6] ENST00000329992; ENSP00000332374; ENSG00000137343 [Q5SQI0-4] ENST00000330083; ENSP00000327832; ENSG00000137343 [Q5SQI0-2] 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]
GeneIDⁱ	79969
KEGGⁱ	hsa:79969
UCSCⁱ	uc003nqr.5, human [Q5SQI0-1]

Organism-specific databases

CTDⁱ	79969
DisGeNETⁱ	79969
GeneCardsⁱ	ATAT1
HGNCⁱ	HGNC:21186, ATAT1
HPAⁱ	ENSG00000137343, Low tissue specificity
MIMⁱ	615556, gene
neXtProtⁱ	NX_Q5SQI0
OpenTargetsⁱ	ENSG00000137343
PharmGKBⁱ	PA134948212
VEuPathDBⁱ	HostDB:ENSG00000137343.17
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG4601, Eukaryota
GeneTreeⁱ	ENSGT00390000008276
HOGENOMⁱ	CLU_025013_0_0_1
InParanoidⁱ	Q5SQI0
OMAⁱ	HESRQRC
PhylomeDBⁱ	Q5SQI0
TreeFamⁱ	TF315643

Enzyme and pathway databases

BRENDAⁱ	2.3.1.108, 2681
PathwayCommonsⁱ	Q5SQI0
Reactomeⁱ	R-HSA-5617833, Cilium Assembly

Miscellaneous databases

BioGRID-ORCSⁱ	79969, 7 hits in 991 CRISPR screens
ChiTaRSⁱ	ATAT1, human
GenomeRNAiⁱ	79969
Pharosⁱ	Q5SQI0, Tbio
Protein Ontology More...PROⁱ	PR:Q5SQI0
RNActⁱ	Q5SQI0, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000137343, Expressed in cortical plate and 180 other tissues
ExpressionAtlasⁱ	Q5SQI0, baseline and differential
Genevisibleⁱ	Q5SQI0, HS

Family and domain databases

HAMAPⁱ	MF_03130, mec17, 1 hit
InterProⁱ	View protein in InterPro IPR038746, Atat IPR007965, GNAT_ATAT
PANTHERⁱ	PTHR12327, PTHR12327, 1 hit
Pfamⁱ	View protein in Pfam PF05301, Acetyltransf_16, 1 hit
PROSITEⁱ	View protein in PROSITE PS51730, GNAT_ATAT, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ATAT_HUMAN
Accessionⁱ	Q5SQI0Primary (citable) accession number: Q5SQI0 Secondary accession number(s): A2AB28 Q9H8X5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
	Last sequence update:	December 21, 2004
	Last modified:	June 2, 2021
	This is version 136 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Uncharacterized protein families (UPF)
List of uncharacterized protein family (UPF) entries
Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - Q5SQI0 (ATAT_HUMAN)

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Alpha-tubulin N-acetyltransferase 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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Keywords - Cellular componenti

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<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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Sequence databases

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Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

Catalytic activityⁱ

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GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

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Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

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Keywords - PTMⁱ

Expressionⁱ

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Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ