ATAT_HUMAN - dbPTM
ATAT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATAT_HUMAN
UniProt AC Q5SQI0
Protein Name Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130}
Gene Name ATAT1 {ECO:0000255|HAMAP-Rule:MF_03130}
Organism Homo sapiens (Human).
Sequence Length 421
Subcellular Localization Cytoplasm . Membrane, clathrin-coated pit . Cell junction, focal adhesion . Cell projection, axon . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle .
Protein Description 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..
Protein Sequence MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
44UbiquitinationVDLQQQIMTIIDELG
HHHHHHHHHHHHHHH		1.59-
44MethylationVDLQQQIMTIIDELG
HHHHHHHHHHHHHHH		1.59-
56AcetylationELGKASAKAQNLSAP
HHHHHHHHHHCCCCC		48.27-
56UbiquitinationELGKASAKAQNLSAP
HHHHHHHHHHCCCCC		48.27-
56MethylationELGKASAKAQNLSAP
HHHHHHHHHHCCCCC		48.27-
61PhosphorylationSAKAQNLSAPITSAS
HHHHHCCCCCCCCHH		39.2828060719
65PhosphorylationQNLSAPITSASRMQS
HCCCCCCCCHHHHHC		19.7229759185
66PhosphorylationNLSAPITSASRMQSN
CCCCCCCCHHHHHCC		25.6029759185
68PhosphorylationSAPITSASRMQSNRH
CCCCCCHHHHHCCCE		28.2229759185
72PhosphorylationTSASRMQSNRHVVYI
CCHHHHHCCCEEEEE		26.8728060719
78PhosphorylationQSNRHVVYILKDSSA
HCCCEEEEEEECCCC		10.2328060719
142PhosphorylationHGRELFQYMLQKERV
CHHHHHHHHHHHCCC		7.77-
146AcetylationLFQYMLQKERVEPHQ
HHHHHHHHCCCCHHH		43.45-
150UbiquitinationMLQKERVEPHQLAID
HHHHCCCCHHHCCCC		43.20-
153UbiquitinationKERVEPHQLAIDRPS
HCCCCHHHCCCCCHH		43.22-
162AcetylationAIDRPSQKLLKFLNK
CCCCHHHHHHHHHHH		61.1925953088
210AcetylationATRHSRAAAVDPTPA
HHCCCCCCCCCCCCC		13.6019608861
221AcetylationPTPAAPARKLPPKRA
CCCCCCCHHCCCCCC		39.7319608861
225PhosphorylationAPARKLPPKRAEGDI
CCCHHCCCCCCCCCC		49.56-
233AcetylationKRAEGDIKPYSSSDR
CCCCCCCCCCCCCCH		42.5123749302
237PhosphorylationGDIKPYSSSDREFLK
CCCCCCCCCCHHHHE		30.34-
244AcetylationSSDREFLKVAVEPPW
CCCHHHHEEEECCCC		33.21-
249PhosphorylationFLKVAVEPPWPLNRA
HHEEEECCCCCCCCC		29.6527251275
258PhosphorylationWPLNRAPRRATPPAH
CCCCCCCCCCCCCCC		39.62-
259PhosphorylationPLNRAPRRATPPAHP
CCCCCCCCCCCCCCC		41.5827251275
260PhosphorylationLNRAPRRATPPAHPP
CCCCCCCCCCCCCCC		26.24-
261PhosphorylationNRAPRRATPPAHPPP
CCCCCCCCCCCCCCC		28.1730576142
264PhosphorylationPRRATPPAHPPPRSS
CCCCCCCCCCCCCCC		29.0827251275
270PhosphorylationPAHPPPRSSSLGNSP
CCCCCCCCCCCCCCC		30.0126846344
271PhosphorylationAHPPPRSSSLGNSPE
CCCCCCCCCCCCCCC		30.7526846344
272PhosphorylationHPPPRSSSLGNSPER
CCCCCCCCCCCCCCC		41.3526846344
276PhosphorylationRSSSLGNSPERGPLR
CCCCCCCCCCCCCCC		26.7526846344
281MethylationGNSPERGPLRPFVPE
CCCCCCCCCCCCCCH		31.27-
292 (in isoform 7)Phosphorylation-3.2625849741
293MethylationVPEQELLRSLRLCPP
CCHHHHHHHCCCCCC		46.39-
303PhosphorylationRLCPPHPTARLLLAA
CCCCCCCCCHHHHHH		22.7527251275
305MethylationCPPHPTARLLLAADP
CCCCCCCHHHHHHCC		28.48-
305Asymmetric dimethylarginineCPPHPTARLLLAADP
CCCCCCCHHHHHHCC		28.48-
311MethylationARLLLAADPGGSPAQ
CHHHHHHCCCCCHHH		36.45-
313PhosphorylationLLLAADPGGSPAQRR
HHHHHCCCCCHHHHH		50.1627251275
315 (in isoform 5)Phosphorylation-23.9925849741
315PhosphorylationLAADPGGSPAQRRRT
HHHCCCCCHHHHHCC		23.9929255136
321PhosphorylationGSPAQRRRTRGTPPG
CCHHHHHCCCCCCCC		30.85-
322PhosphorylationSPAQRRRTRGTPPGL
CHHHHHCCCCCCCCH		31.4727251275
323PhosphorylationPAQRRRTRGTPPGLV
HHHHHCCCCCCCCHH		45.2224719451
323MethylationPAQRRRTRGTPPGLV
HHHHHCCCCCCCCHH		45.2224129315
325PhosphorylationQRRRTRGTPPGLVAQ
HHHCCCCCCCCHHHH		24.0328985074
333PhosphorylationPPGLVAQSCCYSRHG
CCCHHHHHHHCCCCC		9.0922115753
336PhosphorylationLVAQSCCYSRHGGVN
HHHHHHHCCCCCCCC		17.0522115753
337PhosphorylationVAQSCCYSRHGGVNS
HHHHHHCCCCCCCCC		12.1422115753
346PhosphorylationHGGVNSSSPNTGNQD
CCCCCCCCCCCCCCC		23.2230576142
349PhosphorylationVNSSSPNTGNQDSKQ
CCCCCCCCCCCCCHH		40.6828985074
355AcetylationNTGNQDSKQGEQETK
CCCCCCCHHCHHHHH		71.2925953088
368AcetylationTKNRSASEEQALSQD
HHHCCHHHHHHHHCC		54.57-
380AcetylationSQDGSGEKPMHTAPP
HCCCCCCCCCCCCCC		51.6823749302
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
237SPhosphorylationKinaseMAP3K7O43318
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATAT_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ATAT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATAT_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND MASS SPECTROMETRY.

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