AT7L3_HUMAN - dbPTM
AT7L3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT7L3_HUMAN
UniProt AC Q14CW9
Protein Name Ataxin-7-like protein 3 {ECO:0000255|HAMAP-Rule:MF_03047}
Gene Name ATXN7L3 {ECO:0000255|HAMAP-Rule:MF_03047}
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Nucleus .
Protein Description Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. [PubMed: 18206972]
Protein Sequence MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYNNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDSFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN
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
123PhosphorylationANRRIANSNNMNKSE
HHHHHHCCCCCCCCC
22.1328450419
129PhosphorylationNSNNMNKSESDQEDN
CCCCCCCCCCCCCCC
37.0130175587
131PhosphorylationNNMNKSESDQEDNDD
CCCCCCCCCCCCCCC
52.2422115753
145PhosphorylationDINDNDWSYGSEKKA
CCCCCCCCHHHHHHH
23.6027251275
146PhosphorylationINDNDWSYGSEKKAK
CCCCCCCHHHHHHHH
22.0327251275
148PhosphorylationDNDWSYGSEKKAKKR
CCCCCHHHHHHHHHC
37.7027251275
157PhosphorylationKKAKKRKSDKNPNSP
HHHHHCCCCCCCCCH
58.8320068231
162 (in isoform 2)Phosphorylation-74.23-
163PhosphorylationKSDKNPNSPRRSKSL
CCCCCCCCHHHHHHC
22.5024719451
170 (in isoform 2)Phosphorylation-8.5028450419
180PhosphorylationKNGELSNSDPFKYNN
CCCCCCCCCCCCCCC
43.2021815630
184AcetylationLSNSDPFKYNNSTGI
CCCCCCCCCCCCCCC
53.0824886847
213PhosphorylationTTQCGVISEHTKKMC
HHHHCCCCHHHHHHH
22.4028674419
277PhosphorylationSRLQWDGSSDLSPSD
HHHCCCCCCCCCCCC
20.4330266825
278PhosphorylationRLQWDGSSDLSPSDS
HHCCCCCCCCCCCCC
48.3730266825
281PhosphorylationWDGSSDLSPSDSGSS
CCCCCCCCCCCCCCC
27.6122167270
283PhosphorylationGSSDLSPSDSGSSKT
CCCCCCCCCCCCCCC
40.8230266825
285PhosphorylationSDLSPSDSGSSKTSE
CCCCCCCCCCCCCCC
44.9330266825
287PhosphorylationLSPSDSGSSKTSENQ
CCCCCCCCCCCCCCC
32.3923663014
288PhosphorylationSPSDSGSSKTSENQG
CCCCCCCCCCCCCCC
43.4030266825
290PhosphorylationSDSGSSKTSENQGWG
CCCCCCCCCCCCCCC
43.13-
302PhosphorylationGWGLGTNSSESRKTK
CCCCCCCCHHHHCCC
35.0121815630
312AcetylationSRKTKKKKSHLSLVG
HHCCCCCHHHHHHHH
52.577369519
313PhosphorylationRKTKKKKSHLSLVGT
HCCCCCHHHHHHHHH
38.24-
316PhosphorylationKKKKSHLSLVGTASG
CCCHHHHHHHHHHCC
18.6528450419
320PhosphorylationSHLSLVGTASGLGSN
HHHHHHHHHCCCCCC
15.3528450419
322PhosphorylationLSLVGTASGLGSNKK
HHHHHHHCCCCCCCC
34.1028450419
326PhosphorylationGTASGLGSNKKKKPK
HHHCCCCCCCCCCCC
50.9825159151
328AcetylationASGLGSNKKKKPKPP
HCCCCCCCCCCCCCC
68.617369527
339PhosphorylationPKPPAPPTPSIYDDI
CCCCCCCCCCCCCCC
28.7130576142
341PhosphorylationPPAPPTPSIYDDIN-
CCCCCCCCCCCCCC-
35.9428985074
343PhosphorylationAPPTPSIYDDIN---
CCCCCCCCCCCC---
16.3523312004

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

Oops, there are no upstream regulatory protein records of AT7L3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT7L3_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 AT7L3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRRAP_HUMANTRRAPphysical
18206972
ATX7_HUMANATXN7physical
18206972
KAT2A_HUMANKAT2Aphysical
18206972
UBP22_HUMANUSP22physical
18206972
SUPT3_HUMANSUPT3Hphysical
18206972
TAF10_HUMANTAF10physical
18206972
ENY2_HUMANENY2physical
18206972
TAF5L_HUMANTAF5Lphysical
18206972
ATX7_HUMANATXN7physical
19843541
H2A2C_HUMANHIST2H2ACphysical
21746879
H2B2E_HUMANHIST2H2BEphysical
21746879
SEBP2_HUMANSECISBP2physical
16713569
UCHL3_HUMANUCHL3physical
16713569
UBP6_HUMANUSP6physical
16713569
PICK1_HUMANPICK1physical
16713569
SRTD1_HUMANSERTAD1physical
16713569
TRRAP_HUMANTRRAPphysical
26186194
SGF29_HUMANCCDC101physical
26186194
UBP22_HUMANUSP22physical
26186194
UBP27_HUMANUSP27Xphysical
26186194
TAF9B_HUMANTAF9Bphysical
26186194
TAF9_HUMANTAF9physical
26186194
AT7L2_HUMANATXN7L2physical
26186194
ATX7_HUMANATXN7physical
26186194
TADA1_HUMANTADA1physical
26186194
AT7L1_HUMANATXN7L1physical
26186194
TADA3_HUMANTADA3physical
26186194
TAF12_HUMANTAF12physical
26186194
ENY2_HUMANENY2physical
26186194
KAT2B_HUMANKAT2Bphysical
26186194
KAT2A_HUMANKAT2Aphysical
26186194
TAF5L_HUMANTAF5Lphysical
26186194
SUPT3_HUMANSUPT3Hphysical
26186194
SP20H_HUMANSUPT20Hphysical
26186194
TAD2B_HUMANTADA2Bphysical
26186194
ST65G_HUMANSUPT7Lphysical
26186194
ATX7_HUMANATXN7physical
28514442
UBP27_HUMANUSP27Xphysical
28514442
AT7L2_HUMANATXN7L2physical
28514442
UBP22_HUMANUSP22physical
28514442
AT7L1_HUMANATXN7L1physical
28514442
TADA1_HUMANTADA1physical
28514442
TAD2B_HUMANTADA2Bphysical
28514442
TAF5L_HUMANTAF5Lphysical
28514442
TAF9B_HUMANTAF9Bphysical
28514442
ST65G_HUMANSUPT7Lphysical
28514442
KAT2B_HUMANKAT2Bphysical
28514442
KAT2A_HUMANKAT2Aphysical
28514442
SP20H_HUMANSUPT20Hphysical
28514442
TADA3_HUMANTADA3physical
28514442
TAF12_HUMANTAF12physical
28514442
SUPT3_HUMANSUPT3Hphysical
28514442
TAF9_HUMANTAF9physical
28514442
TRRAP_HUMANTRRAPphysical
28514442
SGF29_HUMANCCDC101physical
28514442
ENY2_HUMANENY2physical
28514442
TAF10_HUMANTAF10physical
28514442
ENY2_HUMANENY2physical
27601583
UBP22_HUMANUSP22physical
27601583
ATX7_HUMANATXN7physical
27601583
TAF5L_HUMANTAF5Lphysical
27601583
TAF6L_HUMANTAF6Lphysical
27601583
TAF9_HUMANTAF9physical
27601583
TAF10_HUMANTAF10physical
27601583
TAF9B_HUMANTAF9Bphysical
27601583
TAF12_HUMANTAF12physical
27601583
SGF29_HUMANCCDC101physical
27601583
TAD2B_HUMANTADA2Bphysical
27601583
TADA3_HUMANTADA3physical
27601583
TADA1_HUMANTADA1physical
27601583
KAT2A_HUMANKAT2Aphysical
27601583
SUPT3_HUMANSUPT3Hphysical
27601583
TRRAP_HUMANTRRAPphysical
27601583
SP20H_HUMANSUPT20Hphysical
27601583
ST65G_HUMANSUPT7Lphysical
27601583

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 AT7L3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND MASSSPECTROMETRY.

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