BTAF1_HUMAN - dbPTM
BTAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTAF1_HUMAN
UniProt AC O14981
Protein Name TATA-binding protein-associated factor 172
Gene Name BTAF1
Organism Homo sapiens (Human).
Sequence Length 1849
Subcellular Localization Nucleus.
Protein Description Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner..
Protein Sequence MAVSRLDRLFILLDTGTTPVTRKAAAQQLGEVVKLHPHELNNLLSKVLIYLRSANWDTRIAAGQAVEAIVKNVPEWNPVPRTRQEPTSESSMEDSPTTERLNFDRFDICRLLQHGASLLGSAGAEFEVQDEKSGEVDPKERIARQRKLLQKKLGLNMGEAIGMSTEELFNDEDLDYTPTSASFVNKQPTLQAAELIDSEFRAGMSNRQKNKAKRMAKLFAKQRSRDAVETNEKSNDSTDGEPEEKRRKIANVVINQSANDSKVLIDNIPDSSSLIEETNEWPLESFCEELCNDLFNPSWEVRHGAGTGLREILKAHGKSGGKMGDSTLEEMIQQHQEWLEDLVIRLLCVFALDRFGDFVSDEVVAPVRETCAQTLGVVLKHMNETGVHKTVDVLLKLLTQEQWEVRHGGLLGIKYALAVRQDVINTLLPKVLTRIIEGLQDLDDDVRAVAAASLVPVVESLVYLQTQKVPFIINTLWDALLELDDLTASTNSIMTLLSSLLTYPQVQQCSIQQSLTVLVPRVWPFLHHTISSVRRAALETLFTLLSTQDQNSSSWLIPILPDMLRHIFQFCVLESSQEILDLIHKVWMELLSKASVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLEVKARAKEKTGGKVRQGQSQNKEVLQEYIAGADTIMEDPATRDFVVMRARMMAAKLLGALCCCICDPGVNVVTQEIKPAESLGQLLLFHLNSKSALQRISVALVICEWAALQKECKAVTLAVQPRLLDILSEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNNNVLTIDQASDLVTTVFNEATSSFDLNPQVLQQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTRTPCPNSKIIKNLCSSLCVDPYLTPCVTCPVPTQSGQENSKGSTSEKDGMHHTVTKHRGIITLYRHQKAAFAITSRRGPTPKAVKAQIADLPAGSSGNILVELDEAQKPYLVQRRGAEFALTTIVKHFGGEMAVKLPHLWDAMVGPLRNTIDINNFDGKSLLDKGDSPAQELVNSLQVFETAAASMDSELHPLLVQHLPHLYMCLQYPSTAVRHMAARCVGVMSKIATMETMNIFLEKVLPWLGAIDDSVKQEGAIEALACVMEQLDVGIVPYIVLLVVPVLGRMSDQTDSVRFMATQCFATLIRLMPLEAGIPDPPNMSAELIQLKAKERHFLEQLLDGKKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYARSKLAECMPLPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRAKCDVDETVSSATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLTPQHPEFKTTAEKLAVQNSSLHDIQHAPKLSALKQLLLDCGLGNGSTSESGTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQENSSLQSMGTDQLLDLFTLDKDGKAEKADTSTSGKASMKSILENLSDLWDQEQYDSEYSLENFMHSLK
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
23UbiquitinationGTTPVTRKAAAQQLG
CCCHHCHHHHHHHHC		32.77-
34UbiquitinationQQLGEVVKLHPHELN
HHHCHHHHCCHHHHH		46.37-
58PhosphorylationLRSANWDTRIAAGQA
HHCCCCCHHHHHHHH		18.6522210691
71UbiquitinationQAVEAIVKNVPEWNP
HHHHHHHHCCCCCCC		46.22-
80UbiquitinationVPEWNPVPRTRQEPT
CCCCCCCCCCCCCCC		32.93-
82PhosphorylationEWNPVPRTRQEPTSE
CCCCCCCCCCCCCCC		30.5428450419
87PhosphorylationPRTRQEPTSESSMED
CCCCCCCCCCCCCCC		44.3628450419
88PhosphorylationRTRQEPTSESSMEDS
CCCCCCCCCCCCCCC		46.3128450419
90PhosphorylationRQEPTSESSMEDSPT
CCCCCCCCCCCCCCC		34.4521815630
91PhosphorylationQEPTSESSMEDSPTT
CCCCCCCCCCCCCCC		23.3421712546
92SulfoxidationEPTSESSMEDSPTTE
CCCCCCCCCCCCCCC		10.3821406390
95PhosphorylationSESSMEDSPTTERLN
CCCCCCCCCCCCCCC		15.7321712546
96UbiquitinationESSMEDSPTTERLNF
CCCCCCCCCCCCCCC		56.51-
97PhosphorylationSSMEDSPTTERLNFD
CCCCCCCCCCCCCCC		45.2828450419
98PhosphorylationSMEDSPTTERLNFDR
CCCCCCCCCCCCCCH		23.6128450419
110UbiquitinationFDRFDICRLLQHGAS
CCHHHHHHHHHHHHH		38.47-
217AcetylationNKAKRMAKLFAKQRS
HHHHHHHHHHHHHHH		34.4925953088
224PhosphorylationKLFAKQRSRDAVETN
HHHHHHHHHHHHHHC		31.8328985074
230PhosphorylationRSRDAVETNEKSNDS
HHHHHHHHCCCCCCC		41.9230108239
234PhosphorylationAVETNEKSNDSTDGE
HHHHCCCCCCCCCCC		39.4230108239
237PhosphorylationTNEKSNDSTDGEPEE
HCCCCCCCCCCCHHH		32.4225159151
238PhosphorylationNEKSNDSTDGEPEEK
CCCCCCCCCCCHHHH		51.3830108239
248UbiquitinationEPEEKRRKIANVVIN
CHHHHHHHHHHEEEE		50.64-
257PhosphorylationANVVINQSANDSKVL
HHEEEECCCCCCCEE		25.2625159151
261PhosphorylationINQSANDSKVLIDNI
EECCCCCCCEEEECC		25.1919691289
273PhosphorylationDNIPDSSSLIEETNE
ECCCCCHHHHHHCCC		37.0024275569
295UbiquitinationEELCNDLFNPSWEVR
HHHHHHHHCCCHHHH		16.42-
314UbiquitinationTGLREILKAHGKSGG
CCHHHHHHHHCCCCC		43.96-
415PhosphorylationGGLLGIKYALAVRQD
CCHHHHHHHHHHHHH		12.6219658100
426PhosphorylationVRQDVINTLLPKVLT
HHHHHHHHHHHHHHH		20.6723403867
430UbiquitinationVINTLLPKVLTRIIE
HHHHHHHHHHHHHHH		50.2521890473
430UbiquitinationVINTLLPKVLTRIIE
HHHHHHHHHHHHHHH		50.2521890473
531PhosphorylationPFLHHTISSVRRAAL
HHHHHHHHHHHHHHH		24.7624719451
597UbiquitinationLLSKASVQYVVAAAC
HHHHHCHHHHHHHHC		23.86-
641AcetylationAKEKTGGKVRQGQSQ
HHHHHCCCCCCCCCC		35.2730592801
744UbiquitinationAALQKECKAVTLAVQ
HHHHHHHCHHHHHCC		47.16-
884PhosphorylationIIKPLMETIKKEENT
HHHHHHHHHHHHHCH		24.91-
887UbiquitinationPLMETIKKEENTLVQ
HHHHHHHHHHCHHHH		67.42-
972PhosphorylationTKHRGIITLYRHQKA
CCCCCEEEEEECCHH		18.8024248375
974PhosphorylationHRGIITLYRHQKAAF
CCCEEEEEECCHHHH		9.4422817900
990PhosphorylationITSRRGPTPKAVKAQ
HCCCCCCCCHHHHHH		40.0023684312
1005PhosphorylationIADLPAGSSGNILVE
HCCCCCCCCCCEEEE		36.8623684312
1006PhosphorylationADLPAGSSGNILVEL
CCCCCCCCCCEEEEE		34.6323684312
1018UbiquitinationVELDEAQKPYLVQRR
EEECCCCCCEEHHCC		42.55-
1069UbiquitinationDINNFDGKSLLDKGD
ECCCCCCHHHCCCCC		39.51-
1251UbiquitinationLEQLLDGKKLENYKI
HHHHHCCCCCCCCCC		54.58-
1252UbiquitinationEQLLDGKKLENYKIP
HHHHCCCCCCCCCCC		67.5721890473
1252UbiquitinationEQLLDGKKLENYKIP
HHHHCCCCCCCCCCC		67.5721890473
1256PhosphorylationDGKKLENYKIPVPIN
CCCCCCCCCCCCCCC		10.8322817900
1268UbiquitinationPINAELRKYQQDGVN
CCCHHHHHHHHCCCC		61.10-
1282UbiquitinationNWLAFLNKYKLHGIL
CHHHHHHHHCCCCEE		46.00-
1284UbiquitinationLAFLNKYKLHGILCD
HHHHHHHCCCCEECC		35.30-
1350PhosphorylationDEVGKFCSREYLNPL
HHHHHHCCHHHCCCC		31.1424719451
1359PhosphorylationEYLNPLHYTGPPTER
HHCCCCCCCCCCHHH		22.5217053785
1360PhosphorylationYLNPLHYTGPPTERI
HCCCCCCCCCCHHHH		32.2524719451
1400PhosphorylationFRNIKFNYCILDEGH
HHHCCCCEEEECCCC		5.5222461510
1457PhosphorylationLMPGFLGTERQFAAR
HCCCCCCCHHHHHHH		30.0924719451
1465PhosphorylationERQFAARYGKPILAS
HHHHHHHHCCCEEEC		25.44-
1467UbiquitinationQFAARYGKPILASRD
HHHHHHCCCEEECCC		21.68-
1472PhosphorylationYGKPILASRDARSSS
HCCCEEECCCCCCCC		27.52-
1477PhosphorylationLASRDARSSSREQEA
EECCCCCCCCHHHHH		34.0923898821
1478PhosphorylationASRDARSSSREQEAG
ECCCCCCCCHHHHHH		28.0623312004
1479PhosphorylationSRDARSSSREQEAGV
CCCCCCCCHHHHHHH		40.8723312004
1538PhosphorylationLYEDFAKSRAKCDVD
HHHHHHHHHCCCCCC		33.76-
1541UbiquitinationDFAKSRAKCDVDETV
HHHHHHCCCCCCCCC		29.83-
1547PhosphorylationAKCDVDETVSSATLS
CCCCCCCCCCCCCCC		22.6423312004
1549PhosphorylationCDVDETVSSATLSEE
CCCCCCCCCCCCCCC		22.9823312004
1550PhosphorylationDVDETVSSATLSEET
CCCCCCCCCCCCCCC		22.4223312004
1552PhosphorylationDETVSSATLSEETEK
CCCCCCCCCCCCCCC		32.5323312004
1554PhosphorylationTVSSATLSEETEKPK
CCCCCCCCCCCCCCH		29.0923312004
1594UbiquitinationTPQHPEFKTTAEKLA
CCCCHHHCCHHHHHH		43.22-
1595PhosphorylationPQHPEFKTTAEKLAV
CCCHHHCCHHHHHHH		36.2424275569
1599UbiquitinationEFKTTAEKLAVQNSS
HHCCHHHHHHHCCCC		39.00-
1605PhosphorylationEKLAVQNSSLHDIQH
HHHHHCCCCHHHCCC		19.7227080861
1606PhosphorylationKLAVQNSSLHDIQHA
HHHHCCCCHHHCCCH		36.9527080861
1615UbiquitinationHDIQHAPKLSALKQL
HHCCCHHHHHHHHHH		56.72-
1680PhosphorylationTYLRLDGSIPPGQRH
EEEEECCCCCCCCCC		31.4320860994
1756PhosphorylationVNVYRLITRGTLEEK
HHHHHHHHHCCHHHH		27.86-
1769AcetylationEKIMGLQKFKMNIAN
HHHHCHHHHHHHHHH		52.5818530203
1769UbiquitinationEKIMGLQKFKMNIAN
HHHHCHHHHHHHHHH		52.58-
1784PhosphorylationTVISQENSSLQSMGT
HHHCCCCHHHHCCCH		31.50-
1799PhosphorylationDQLLDLFTLDKDGKA
HHHHHHEEECCCCCC		41.15-
1811PhosphorylationGKAEKADTSTSGKAS
CCCCCCCCCCCCHHH		38.47-
1812PhosphorylationKAEKADTSTSGKASM
CCCCCCCCCCCHHHH		22.56-
1813PhosphorylationAEKADTSTSGKASMK
CCCCCCCCCCHHHHH		43.52-
1818PhosphorylationTSTSGKASMKSILEN
CCCCCHHHHHHHHHH		30.17-
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 BTAF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BTAF1_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 BTAF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBP_HUMANTBPphysical
9159119
TF2H4_HUMANGTF2H4physical
9159119
TBP_HUMANTBPphysical
9488487
TBP_HUMANTBPphysical
22939629
PIAS4_HUMANPIAS4physical
21988832
PIHD3_HUMANPIH1D3physical
25416956
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 BTAF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-257, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1359, AND MASSSPECTROMETRY.

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