BTF3_HUMAN - dbPTM
BTF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTF3_HUMAN
UniProt AC P20290
Protein Name Transcription factor BTF3
Gene Name BTF3
Organism Homo sapiens (Human).
Sequence Length 206
Subcellular Localization Cytoplasm . Nucleus . The heterodimer with NACA is cytoplasmic.
Protein Description When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription..
Protein Sequence MRRTGAPAQADSRGRGRARGGCPGGEATLSQPPPRGGTRGQEPQMKETIMNQEKLAKLQAQVRIGGKGTARRKKKVVHRTATADDKKLQFSLKKLGVNNISGIEEVNMFTNQGTVIHFNNPKVQASLAANTFTITGHAETKQLTEMLPSILNQLGADSLTSLRRLAEALPKQSVDGKAPLATGEDDDDEVPDLVENFDEASKNEAN
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
2Ubiquitination------MRRTGAPAQ
------CCCCCCCCC
44.8829967540
4 (in isoform 2)Phosphorylation-27.5929507054
4Phosphorylation----MRRTGAPAQAD
----CCCCCCCCCCC
27.5921406692
10 (in isoform 2)Ubiquitination-20.8921890473
10UbiquitinationRTGAPAQADSRGRGR
CCCCCCCCCCCCCCC
20.8923000965
12PhosphorylationGAPAQADSRGRGRAR
CCCCCCCCCCCCCCC
39.3821406692
13MethylationAPAQADSRGRGRARG
CCCCCCCCCCCCCCC
39.10-
13 (in isoform 2)Ubiquitination-39.10-
13DimethylationAPAQADSRGRGRARG
CCCCCCCCCCCCCCC
39.10-
13UbiquitinationAPAQADSRGRGRARG
CCCCCCCCCCCCCCC
39.1023000965
15DimethylationAQADSRGRGRARGGC
CCCCCCCCCCCCCCC
30.25-
15MethylationAQADSRGRGRARGGC
CCCCCCCCCCCCCCC
30.25-
17MethylationADSRGRGRARGGCPG
CCCCCCCCCCCCCCC
21.54-
19MethylationSRGRGRARGGCPGGE
CCCCCCCCCCCCCCC
40.4524129315
23UbiquitinationGRARGGCPGGEATLS
CCCCCCCCCCCCCCC
58.0422053931
28PhosphorylationGCPGGEATLSQPPPR
CCCCCCCCCCCCCCC
23.7329255136
30PhosphorylationPGGEATLSQPPPRGG
CCCCCCCCCCCCCCC
35.9623401153
31UbiquitinationGGEATLSQPPPRGGT
CCCCCCCCCCCCCCC
58.6024816145
35MethylationTLSQPPPRGGTRGQE
CCCCCCCCCCCCCCC
63.04-
38PhosphorylationQPPPRGGTRGQEPQM
CCCCCCCCCCCCHHH
34.1628985074
39MethylationPPPRGGTRGQEPQMK
CCCCCCCCCCCHHHH
48.34-
42UbiquitinationRGGTRGQEPQMKETI
CCCCCCCCHHHHHHH
40.0829967540
43UbiquitinationGGTRGQEPQMKETIM
CCCCCCCHHHHHHHH
31.5133845483
46UbiquitinationRGQEPQMKETIMNQE
CCCCHHHHHHHHCHH
46.5932015554
46AcetylationRGQEPQMKETIMNQE
CCCCHHHHHHHHCHH
46.5925953088
46MethylationRGQEPQMKETIMNQE
CCCCHHHHHHHHCHH
46.5924129315
48PhosphorylationQEPQMKETIMNQEKL
CCHHHHHHHHCHHHH
21.7320068231
49UbiquitinationEPQMKETIMNQEKLA
CHHHHHHHHCHHHHH
2.2727667366
49 (in isoform 2)Ubiquitination-2.27-
50 (in isoform 2)Ubiquitination-5.7521890473
50UbiquitinationPQMKETIMNQEKLAK
HHHHHHHHCHHHHHH
5.7521890473
50SulfoxidationPQMKETIMNQEKLAK
HHHHHHHHCHHHHHH
5.7530846556
542-HydroxyisobutyrylationETIMNQEKLAKLQAQ
HHHHCHHHHHHHHHH
43.94-
54UbiquitinationETIMNQEKLAKLQAQ
HHHHCHHHHHHHHHH
43.9423000965
54 (in isoform 1)Ubiquitination-43.9421890473
54MethylationETIMNQEKLAKLQAQ
HHHHCHHHHHHHHHH
43.9424129315
54AcetylationETIMNQEKLAKLQAQ
HHHHCHHHHHHHHHH
43.9426051181
57 (in isoform 2)Phosphorylation-52.12-
57 (in isoform 1)Ubiquitination-52.1221890473
572-HydroxyisobutyrylationMNQEKLAKLQAQVRI
HCHHHHHHHHHHHCC
52.12-
57AcetylationMNQEKLAKLQAQVRI
HCHHHHHHHHHHHCC
52.1225953088
57UbiquitinationMNQEKLAKLQAQVRI
HCHHHHHHHHHHHCC
52.1223000965
67 (in isoform 1)Ubiquitination-48.1221890473
67UbiquitinationAQVRIGGKGTARRKK
HHHCCCCCCHHHHCC
48.1222053931
67AcetylationAQVRIGGKGTARRKK
HHHCCCCCCHHHHCC
48.1221669532
67MethylationAQVRIGGKGTARRKK
HHHCCCCCCHHHHCC
48.12-
69PhosphorylationVRIGGKGTARRKKKV
HCCCCCCHHHHCCEE
22.0722496350
75UbiquitinationGTARRKKKVVHRTAT
CHHHHCCEEEEEECC
53.1524816145
80PhosphorylationKKKVVHRTATADDKK
CCEEEEEECCCCHHH
17.3022496350
82PhosphorylationKVVHRTATADDKKLQ
EEEEEECCCCHHHHH
29.9723401153
86UbiquitinationRTATADDKKLQFSLK
EECCCCHHHHHHHHH
56.8029967540
87UbiquitinationTATADDKKLQFSLKK
ECCCCHHHHHHHHHH
55.2933845483
91PhosphorylationDDKKLQFSLKKLGVN
CHHHHHHHHHHHCCC
26.7323927012
93AcetylationKKLQFSLKKLGVNNI
HHHHHHHHHHCCCCC
44.7625953088
93UbiquitinationKKLQFSLKKLGVNNI
HHHHHHHHHHCCCCC
44.7627667366
94 (in isoform 1)Ubiquitination-56.6221890473
94UbiquitinationKLQFSLKKLGVNNIS
HHHHHHHHHCCCCCC
56.6222817900
101PhosphorylationKLGVNNISGIEEVNM
HHCCCCCCCCEEEEE
35.5220068231
110PhosphorylationIEEVNMFTNQGTVIH
CEEEEECCCCCEEEE
18.8324425749
114PhosphorylationNMFTNQGTVIHFNNP
EECCCCCEEEEECCH
13.4120068231
116 (in isoform 2)Phosphorylation-2.85-
127UbiquitinationNPKVQASLAANTFTI
CHHHEEEEECCEEEE
6.1423000965
127 (in isoform 2)Ubiquitination-6.1421890473
133UbiquitinationSLAANTFTITGHAET
EEECCEEEEECCHHH
18.6523000965
133 (in isoform 2)Ubiquitination-18.6521890473
144PhosphorylationHAETKQLTEMLPSIL
CHHHHHHHHHHHHHH
19.4928450419
146SulfoxidationETKQLTEMLPSILNQ
HHHHHHHHHHHHHHH
5.8528183972
149PhosphorylationQLTEMLPSILNQLGA
HHHHHHHHHHHHHCC
35.4328450419
157 (in isoform 2)Phosphorylation-42.24-
158UbiquitinationLNQLGADSLTSLRRL
HHHHCCHHHHHHHHH
32.7729967540
158 (in isoform 2)Ubiquitination-32.7721890473
158PhosphorylationLNQLGADSLTSLRRL
HHHHCCHHHHHHHHH
32.7725159151
160PhosphorylationQLGADSLTSLRRLAE
HHCCHHHHHHHHHHH
29.6630183078
161PhosphorylationLGADSLTSLRRLAEA
HCCHHHHHHHHHHHH
25.7722115753
171UbiquitinationRLAEALPKQSVDGKA
HHHHHCCCCCCCCCC
56.9323000965
171MethylationRLAEALPKQSVDGKA
HHHHHCCCCCCCCCC
56.93-
171AcetylationRLAEALPKQSVDGKA
HHHHHCCCCCCCCCC
56.9326051181
171 (in isoform 1)Ubiquitination-56.9321890473
173PhosphorylationAEALPKQSVDGKAPL
HHHCCCCCCCCCCCC
28.4423927012
177AcetylationPKQSVDGKAPLATGE
CCCCCCCCCCCCCCC
42.2226051181
177UbiquitinationPKQSVDGKAPLATGE
CCCCCCCCCCCCCCC
42.2223000965
177 (in isoform 1)Ubiquitination-42.2221890473
182PhosphorylationDGKAPLATGEDDDDE
CCCCCCCCCCCCCCC
49.11-
201PhosphorylationVENFDEASKNEAN--
HHHHHHHHHHCCC--
33.6925159151
202 (in isoform 1)Ubiquitination-66.8921890473
202UbiquitinationENFDEASKNEAN---
HHHHHHHHHCCC---
66.8929967540

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 BTF3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BTF3_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 BTF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK2B_HUMANCSNK2Bphysical
10094400
RPB2_HUMANPOLR2Bphysical
2320128
A4_HUMANAPPphysical
21832049
RL11_HUMANRPL11physical
22939629
NACA2_HUMANNACA2physical
22939629
PDRG1_HUMANPDRG1physical
22939629
RWDD4_HUMANRWDD4physical
22939629
RL29_HUMANRPL29physical
22939629
ESR1_HUMANESR1physical
18025262
POL_HV1H2gag-polphysical
20016921
2AAA_HUMANPPP2R1Aphysical
22863883
TXLNB_HUMANTXLNBphysical
25416956
TXLNA_HUMANTXLNAphysical
25416956
NACAM_HUMANNACAphysical
26344197
NACA_HUMANNACAphysical
26344197
NACA2_HUMANNACA2physical
26344197
SRSF2_HUMANSRSF2physical
26344197

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 BTF3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.

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