EST1A_HUMAN - dbPTM
EST1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EST1A_HUMAN
UniProt AC Q86US8
Protein Name Telomerase-binding protein EST1A
Gene Name SMG6
Organism Homo sapiens (Human).
Sequence Length 1419
Subcellular Localization Nucleus, nucleolus. Chromosome, telomere . Cytoplasm, cytosol. Particularly enriched in the nucleolus.
Protein Description Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER).; Plays a role in nonsense-mediated mRNA decay. Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA..
Protein Sequence MAEGLERVRISASELRGILATLAPQAGSRENMKELKEARPRKDNRRPDLEIYKPGLSRLRNKPKIKEPPGSEEFKDEIVNDRDCSAVENGTQPVKDVCKELNNQEQNGPIDPENNRGQESFPRTAGQEDRSLKIIKRTKKPDLQIYQPGRRLQTVSKESASRVEEEEVLNQVEQLRVEEDECRGNVAKEEVANKPDRAEIEKSPGGGRVGAAKGEKGKRMGKGEGVRETHDDPARGRPGSAKRYSRSDKRRNRYRTRSTSSAGSNNSAEGAGLTDNGCRRRRQDRTKERPRLKKQVSVSSTDSLDEDRIDEPDGLGPRRSSERKRHLERNWSGRGEGEQKNSAKEYRGTLRVTFDAEAMNKESPMVRSARDDMDRGKPDKGLSSGGKGSEKQESKNPKQELRGRGRGILILPAHTTLSVNSAGSPESAPLGPRLLFGSGSKGSRSWGRGGTTRRLWDPNNPDQKPALKTQTPQLHFLDTDDEVSPTSWGDSRQAQASYYKFQNSDNPYYYPRTPGPASQYPYTGYNPLQYPVGPTNGVYPGPYYPGYPTPSGQYVCSPLPTSTMSPEEVEQHMRNLQQQELHRLLRVADNQELQLSNLLSRDRISPEGLEKMAQLRAELLQLYERCILLDIEFSDNQNVDQILWKNAFYQVIEKFRQLVKDPNVENPEQIRNRLLELLDEGSDFFDSLLQKLQVTYKFKLEDYMDGLAIRSKPLRKTVKYALISAQRCMICQGDIARYREQASDTANYGKARSWYLKAQHIAPKNGRPYNQLALLAVYTRRKLDAVYYYMRSLAASNPILTAKESLMSLFEETKRKAEQMEKKQHEEFDLSPDQWRKGKKSTFRHVGDDTTRLEIWIHPSHPRSSQGTESGKDSEQENGLGSLSPSDLNKRFILSFLHAHGKLFTRIGMETFPAVAEKVLKEFQVLLQHSPSPIGSTRMLQLMTINMFAVHNSQLKDCFSEECRSVIQEQAAALGLAMFSLLVRRCTCLLKESAKAQLSSPEDQDDQDDIKVSSFVPDLKELLPSVKVWSDWMLGYPDTWNPPPTSLDLPSHVAVDVWSTLADFCNILTAVNQSEVPLYKDPDDDLTLLILEEDRLLSGFVPLLAAPQDPCYVEKTSDKVIAADCKRVTVLKYFLEALCGQEEPLLAFKGGKYVSVAPVPDTMGKEMGSQEGTRLEDEEEDVVIEDFEEDSEAEGSGGEDDIRELRAKKLALARKIAEQQRRQEKIQAVLEDHSQMRQMELEIRPLFLVPDTNGFIDHLASLARLLESRKYILVVPLIVINELDGLAKGQETDHRAGGYARVVQEKARKSIEFLEQRFESRDSCLRALTSRGNELESIAFRSEDITGQLGNNDDLILSCCLHYCKDKAKDFMPASKEEPIRLLREVVLLTDDRNLRVKALTRNVPVRDIPAFLTWAQVG
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
11PhosphorylationGLERVRISASELRGI
CHHHEEECHHHHHHH
18.3823403867
28PhosphorylationTLAPQAGSRENMKEL
HHCCCCCCHHHHHHH
39.1628348404
36UbiquitinationRENMKELKEARPRKD
HHHHHHHHHHCCCCC
50.8824816145
52PhosphorylationRRPDLEIYKPGLSRL
CCCCCCCCCCCHHHH
11.1821945579
53AcetylationRPDLEIYKPGLSRLR
CCCCCCCCCCHHHHC
37.9725953088
57PhosphorylationEIYKPGLSRLRNKPK
CCCCCCHHHHCCCCC
34.8721945579
60UbiquitinationKPGLSRLRNKPKIKE
CCCHHHHCCCCCCCC
48.2729967540
71PhosphorylationKIKEPPGSEEFKDEI
CCCCCCCCHHHHHHH
39.4628348404
83UbiquitinationDEIVNDRDCSAVENG
HHHCCCCCCHHHHCC
33.3222817900
85PhosphorylationIVNDRDCSAVENGTQ
HCCCCCCHHHHCCCC
39.3724719451
87UbiquitinationNDRDCSAVENGTQPV
CCCCCHHHHCCCCCH
3.1822817900
91PhosphorylationCSAVENGTQPVKDVC
CHHHHCCCCCHHHHH
41.0824719451
103UbiquitinationDVCKELNNQEQNGPI
HHHHHHCCCCCCCCC
60.4329967540
126UbiquitinationESFPRTAGQEDRSLK
CCCCCCCCCCHHHHH
30.6924816145
138PhosphorylationSLKIIKRTKKPDLQI
HHHHHHCCCCCCCEE
38.12-
146PhosphorylationKKPDLQIYQPGRRLQ
CCCCCEEECCCCCEE
8.8321945579
154PhosphorylationQPGRRLQTVSKESAS
CCCCCEEECCHHHHC
31.1923312004
156PhosphorylationGRRLQTVSKESASRV
CCCEEECCHHHHCHH
33.8123312004
157AcetylationRRLQTVSKESASRVE
CCEEECCHHHHCHHC
51.8825953088
157UbiquitinationRRLQTVSKESASRVE
CCEEECCHHHHCHHC
51.8824816145
182UbiquitinationLRVEEDECRGNVAKE
HHCCCCHHCCHHHHH
11.9024816145
203PhosphorylationDRAEIEKSPGGGRVG
CHHHHHCCCCCCCCC
18.9123401153
213UbiquitinationGGRVGAAKGEKGKRM
CCCCCCCCCCCCCCC
68.0524816145
220UbiquitinationKGEKGKRMGKGEGVR
CCCCCCCCCCCCCCC
8.0829967540
229PhosphorylationKGEGVRETHDDPARG
CCCCCCCCCCCCCCC
21.7526074081
240PhosphorylationPARGRPGSAKRYSRS
CCCCCCCCHHCCCCC
33.0426074081
241UbiquitinationARGRPGSAKRYSRSD
CCCCCCCHHCCCCCH
13.2729967540
245PhosphorylationPGSAKRYSRSDKRRN
CCCHHCCCCCHHHHH
29.37-
247PhosphorylationSAKRYSRSDKRRNRY
CHHCCCCCHHHHHCC
41.36-
256PhosphorylationKRRNRYRTRSTSSAG
HHHHCCCCCCCCCCC
21.7523090842
258PhosphorylationRNRYRTRSTSSAGSN
HHCCCCCCCCCCCCC
31.8423663014
259PhosphorylationNRYRTRSTSSAGSNN
HCCCCCCCCCCCCCC
24.3423663014
260PhosphorylationRYRTRSTSSAGSNNS
CCCCCCCCCCCCCCC
21.3123663014
261PhosphorylationYRTRSTSSAGSNNSA
CCCCCCCCCCCCCCC
36.4223663014
264PhosphorylationRSTSSAGSNNSAEGA
CCCCCCCCCCCCCCC
32.3323663014
267PhosphorylationSSAGSNNSAEGAGLT
CCCCCCCCCCCCCCC
31.7623663014
274PhosphorylationSAEGAGLTDNGCRRR
CCCCCCCCCCCHHHH
26.8823090842
287UbiquitinationRRRQDRTKERPRLKK
HHCCCCCCCCCCHHC
53.2529967540
297PhosphorylationPRLKKQVSVSSTDSL
CCHHCCEECCCCCCC
17.4928985074
299PhosphorylationLKKQVSVSSTDSLDE
HHCCEECCCCCCCCC
21.7330177828
300PhosphorylationKKQVSVSSTDSLDED
HCCEECCCCCCCCCC
33.7930177828
301PhosphorylationKQVSVSSTDSLDEDR
CCEECCCCCCCCCCC
23.3130177828
303PhosphorylationVSVSSTDSLDEDRID
EECCCCCCCCCCCCC
37.5030177828
332PhosphorylationRHLERNWSGRGEGEQ
HHHHHHCCCCCCCCC
23.3523401153
353PhosphorylationYRGTLRVTFDAEAMN
HEEEEEEEECHHHHC
14.9024905233
363PhosphorylationAEAMNKESPMVRSAR
HHHHCCCCCCHHHCH
21.6525159151
367UbiquitinationNKESPMVRSARDDMD
CCCCCCHHHCHHHCC
20.5324816145
368PhosphorylationKESPMVRSARDDMDR
CCCCCHHHCHHHCCC
19.0824905233
398UbiquitinationKQESKNPKQELRGRG
HCCCCCCCHHHCCCC
66.8424816145
401UbiquitinationSKNPKQELRGRGRGI
CCCCCHHHCCCCCEE
6.9729967540
404DimethylationPKQELRGRGRGILIL
CCHHHCCCCCEEEEE
25.79-
404MethylationPKQELRGRGRGILIL
CCHHHCCCCCEEEEE
25.79-
406DimethylationQELRGRGRGILILPA
HHHCCCCCEEEEECC
27.84-
406MethylationQELRGRGRGILILPA
HHHCCCCCEEEEECC
27.84-
424PhosphorylationLSVNSAGSPESAPLG
EEECCCCCCCCCCCC
25.80-
433MethylationESAPLGPRLLFGSGS
CCCCCCCEEEECCCC
42.07-
438PhosphorylationGPRLLFGSGSKGSRS
CCEEEECCCCCCCCC
32.3423911959
440PhosphorylationRLLFGSGSKGSRSWG
EEEECCCCCCCCCCC
35.2222199227
441UbiquitinationLLFGSGSKGSRSWGR
EEECCCCCCCCCCCC
65.51-
443PhosphorylationFGSGSKGSRSWGRGG
ECCCCCCCCCCCCCC
27.2023186163
468UbiquitinationPDQKPALKTQTPQLH
CCCCCCCCCCCCCEE
40.4729967540
469PhosphorylationDQKPALKTQTPQLHF
CCCCCCCCCCCCEEE
38.2323927012
471PhosphorylationKPALKTQTPQLHFLD
CCCCCCCCCCEEECC
20.4523927012
479PhosphorylationPQLHFLDTDDEVSPT
CCEEECCCCCCCCCC
47.7123927012
484PhosphorylationLDTDDEVSPTSWGDS
CCCCCCCCCCCCCCC
22.0330266825
486PhosphorylationTDDEVSPTSWGDSRQ
CCCCCCCCCCCCCCH
29.6130266825
487PhosphorylationDDEVSPTSWGDSRQA
CCCCCCCCCCCCCHH
32.2330266825
491PhosphorylationSPTSWGDSRQAQASY
CCCCCCCCCHHHHHE
23.5030266825
508PhosphorylationFQNSDNPYYYPRTPG
ECCCCCCCCCCCCCC
23.1428796482
509PhosphorylationQNSDNPYYYPRTPGP
CCCCCCCCCCCCCCC
14.3028796482
510PhosphorylationNSDNPYYYPRTPGPA
CCCCCCCCCCCCCCH
4.7628796482
512MethylationDNPYYYPRTPGPASQ
CCCCCCCCCCCCHHH
37.11-
629UbiquitinationLYERCILLDIEFSDN
HHHHHHHHCCCCCCC
2.9424816145
660UbiquitinationEKFRQLVKDPNVENP
HHHHHHHCCCCCCCH
75.8624816145
711PhosphorylationMDGLAIRSKPLRKTV
CCCEEECCCCHHHHH
32.2924719451
769PhosphorylationAPKNGRPYNQLALLA
CCCCCCCCHHHHHHH
17.7426657352
778PhosphorylationQLALLAVYTRRKLDA
HHHHHHHHHHHHHHH
6.7430206219
779PhosphorylationLALLAVYTRRKLDAV
HHHHHHHHHHHHHHH
19.8730206219
788PhosphorylationRKLDAVYYYMRSLAA
HHHHHHHHHHHHHHH
5.56-
789PhosphorylationKLDAVYYYMRSLAAS
HHHHHHHHHHHHHHC
2.88-
796PhosphorylationYMRSLAASNPILTAK
HHHHHHHCCCCCCHH
37.22-
803AcetylationSNPILTAKESLMSLF
CCCCCCHHHHHHHHH
42.477667043
814UbiquitinationMSLFEETKRKAEQME
HHHHHHHHHHHHHHH
56.00-
823UbiquitinationKAEQMEKKQHEEFDL
HHHHHHHHHHHCCCC
43.5129967540
831PhosphorylationQHEEFDLSPDQWRKG
HHHCCCCCHHHHHCC
28.4225159151
860PhosphorylationLEIWIHPSHPRSSQG
EEEEECCCCCCCCCC
31.7723898821
864PhosphorylationIHPSHPRSSQGTESG
ECCCCCCCCCCCCCC
31.3123927012
865PhosphorylationHPSHPRSSQGTESGK
CCCCCCCCCCCCCCC
33.6323927012
868PhosphorylationHPRSSQGTESGKDSE
CCCCCCCCCCCCCCC
21.2423927012
870PhosphorylationRSSQGTESGKDSEQE
CCCCCCCCCCCCCCC
51.4823401153
874PhosphorylationGTESGKDSEQENGLG
CCCCCCCCCCCCCCC
44.6723927012
882PhosphorylationEQENGLGSLSPSDLN
CCCCCCCCCCHHHHH
30.6223403867
884PhosphorylationENGLGSLSPSDLNKR
CCCCCCCCHHHHHHH
24.8525159151
886PhosphorylationGLGSLSPSDLNKRFI
CCCCCCHHHHHHHHH
51.8923403867
918AcetylationTFPAVAEKVLKEFQV
CCHHHHHHHHHHHHH
43.0315612443
960UbiquitinationSQLKDCFSEECRSVI
HHHHHHCCHHHHHHH
38.5222817900
964UbiquitinationDCFSEECRSVIQEQA
HHCCHHHHHHHHHHH
36.9222817900
987PhosphorylationSLLVRRCTCLLKESA
HHHHHHHHHHHHHHH
12.3623403867
991UbiquitinationRRCTCLLKESAKAQL
HHHHHHHHHHHHHHC
36.3522817900
995UbiquitinationCLLKESAKAQLSSPE
HHHHHHHHHHCCCCC
46.0422817900
995 (in isoform 1)Ubiquitination-46.0421906983
999PhosphorylationESAKAQLSSPEDQDD
HHHHHHCCCCCCCCC
31.5925159151
1000PhosphorylationSAKAQLSSPEDQDDQ
HHHHHCCCCCCCCCH
40.6821815630
1011UbiquitinationQDDQDDIKVSSFVPD
CCCHHCCCHHHCCCC
42.9629967540
1025PhosphorylationDLKELLPSVKVWSDW
CHHHHHHCCCEECCH
34.2427794612
1149UbiquitinationEEPLLAFKGGKYVSV
CCCEEEEECCCEEEE
62.2329967540
1152UbiquitinationLLAFKGGKYVSVAPV
EEEEECCCEEEEEEC
51.66-
1169PhosphorylationTMGKEMGSQEGTRLE
CCCHHCCCCCCCCCC
24.6128634120
1173PhosphorylationEMGSQEGTRLEDEEE
HCCCCCCCCCCCCCC
31.1828634120
1191PhosphorylationIEDFEEDSEAEGSGG
EECCCCCCCCCCCCC
41.8227422710
1196PhosphorylationEDSEAEGSGGEDDIR
CCCCCCCCCCHHHHH
34.8227422710
1225UbiquitinationEQQRRQEKIQAVLED
HHHHHHHHHHHHHHC
31.60-
1236SulfoxidationVLEDHSQMRQMELEI
HHHCHHHHHHCCEEE
3.4421406390
1309UbiquitinationVVQEKARKSIEFLEQ
HHHHHHHHHHHHHHH
61.7229967540
1346PhosphorylationAFRSEDITGQLGNND
EEECCCCCCCCCCCH
31.0629759185
1358PhosphorylationNNDDLILSCCLHYCK
CCHHHHHHHHHHHHH
8.8729759185
1376UbiquitinationKDFMPASKEEPIRLL
HHCCCCCCHHHHHHH
69.1029967540
1390PhosphorylationLREVVLLTDDRNLRV
HHEEEEECCCCCHHH
31.5220860994

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 EST1A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EST1A_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
256Phosphorylation263 (7)KQrs216195
  • Intraocular pressure
29617998
258Phosphorylation263 (5)KQrs216195
  • Intraocular pressure
29617998
259Phosphorylation263 (4)KQrs216195
  • Intraocular pressure
29617998
260Phosphorylation263 (3)KQrs216195
  • Intraocular pressure
29617998
261Phosphorylation263 (2)KQrs216195
  • Intraocular pressure
29617998
267Phosphorylation263 (4)KQrs216195
  • Intraocular pressure
29617998

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC8_HUMANHDAC8physical
16809764
HBB_HUMANHBBphysical
21145460
RBM8A_HUMANRBM8Aphysical
20930030
RENT1_HUMANUPF1physical
20930030
MGN_HUMANMAGOHphysical
20930030
PABP1_HUMANPABPC1physical
20930030
EST1A_HUMANSMG6physical
20930030
REN3B_HUMANUPF3Bphysical
20930030
SMG5_HUMANSMG5physical
20930030
SMG7_HUMANSMG7physical
20930030

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 EST1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
"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 THR-479, AND MASSSPECTROMETRY.

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