BTBD7_HUMAN - dbPTM
BTBD7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BTBD7_HUMAN
UniProt AC Q9P203
Protein Name BTB/POZ domain-containing protein 7
Gene Name BTBD7
Organism Homo sapiens (Human).
Sequence Length 1132
Subcellular Localization Nucleus.
Protein Description Acts as a mediator of epithelial dynamics and organ branching by promoting cleft progression. Induced following accumulation of fibronectin in forming clefts, leading to local expression of the cell-scattering SNAIL2 and suppression of E-cadherin levels, thereby altering cell morphology and reducing cell-cell adhesion. This stimulates cell separation at the base of forming clefts by local, dynamic intercellular gap formation and promotes cleft progression (By similarity)..
Protein Sequence MGANASNYPHSCSPRVGGNSQAQQTFIGTSSYSQQGYGCESKLYSLDHGHEKPQDKKKRTSGLATLKKKFIKRRKSNRSADHAKQMRELLSGWDVRDVNALVEEYEGTSALKELSLQASLARPEARTLQKDMADLYEYKYCTDVDLIFQETCFPVHRAILAARCPFFKTLLSSSPEYGAEIIMDINTAGIDMPMFSALLHYLYTGEFGMEDSRFQNVDILVQLSEEFGTPNSLDVDMRGLFDYMCYYDVVLSFSSDSELVEAFGGNQNCLDEELKAHKAVISARSPFFRNLLQRRIRTGEEITDRTLRTPTRIILDESIIPKKYATVILHCMYTDVVDLSVLHCSPSVGSLSEVQALVAGKPNMTRAEEAMELYHIALFLEFNMLAQGCEDIIAESISLDTLIAILKWSSHPYGSKWVHRQALHFLCEEFSQVMTSDVFYELSKDHLLTAIQSDYLQASEQDILKYLIKWGEHQLMKRIADREPNLLSGTAHSVNKRGVKRRDLDMEELREILSSLLPFVRIEHILPINSEVLSDAMKRGLISTPPSDMLPTTEGGKSNAWLRQKNAGIYVRPRLFSPYVEEAKSVLDEMMVEQTDLVRLRMVRMSNVPDTLYMVNNAVPQCCHMISHQQISSNQSSPPSVVANEIPVPRLLIMKDMVRRLQELRHTEQVQRAYALNCGEGATVSYEIQIRVLREFGLADAAAELLQNPHKFFPDERFGDESPLLTMRQPGRCRVNSTPPAETMFTDLDSFVAFHPPLPPPPPPYHPPATPIHNQLKAGWKQRPPSQHPSRSFSYPCNHSLFHSRTAPKAGPPPVYLPSVKAAPPDCTSTAGLGRQTVAAAAATTTSTATAAAAAASEKQVRTQPVLNDLMPDIAVGVSTLSLKDRRLPELAVDTELSQSVSEAGPGPPQHLSCIPQRHTHTSRKKHTLEQKTDTRENPQEYPDFYDFSNAACRPSTPALSRRTPSPSQGGYFGPDLYSHNKASPSGLKSAYLPGQTSPKKQEEARREYPLSPDGHLHRQKNEPIHLDVVEQPPQRSDFPLAAPENASTGPAHVRGRTAVETDLTFGLTPNRPSLSACSSEAPEERSGRRLADSESLGHGAQRNTDLEREDSISRGRRSPSKPDFLYKKSAL
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
2Myristoylation------MGANASNYP
------CCCCCCCCC		38.5520213681
2N-myristoyl glycine------MGANASNYP
------CCCCCCCCC		38.55-
6Phosphorylation--MGANASNYPHSCS
--CCCCCCCCCCCCC		36.3823663014
8PhosphorylationMGANASNYPHSCSPR
CCCCCCCCCCCCCCC		10.3823663014
11PhosphorylationNASNYPHSCSPRVGG
CCCCCCCCCCCCCCC		16.2823663014
13PhosphorylationSNYPHSCSPRVGGNS
CCCCCCCCCCCCCCC		20.8223663014
44PhosphorylationYGCESKLYSLDHGHE
CCCCCEEEECCCCCC		15.7827642862
60PhosphorylationPQDKKKRTSGLATLK
CCCHHCCCCCHHHHH		35.7123403867
61PhosphorylationQDKKKRTSGLATLKK
CCHHCCCCCHHHHHH		35.5223403867
63UbiquitinationKKKRTSGLATLKKKF
HHCCCCCHHHHHHHH		3.0922817900
65PhosphorylationKRTSGLATLKKKFIK
CCCCCHHHHHHHHHH		44.1223403867
79PhosphorylationKRRKSNRSADHAKQM
HHHHHCCCHHHHHHH		42.15-
145UbiquitinationYKYCTDVDLIFQETC
CCCCCCHHHHCCCCC		36.5429967540
187 (in isoform 5)Ubiquitination-26.9621906983
187UbiquitinationEIIMDINTAGIDMPM
EEEEECCCCCCCHHH		26.9622817900
206UbiquitinationLHYLYTGEFGMEDSR
HHHHHHCCCCCCCCC		31.0929967540
214UbiquitinationFGMEDSRFQNVDILV
CCCCCCCCCCCEEEE		7.7929967540
309PhosphorylationITDRTLRTPTRIILD
CCCCCCCCCCEEEEC		31.93-
311PhosphorylationDRTLRTPTRIILDES
CCCCCCCCEEEECCC		33.61-
410PhosphorylationIAILKWSSHPYGSKW
HHHHHHCCCCCCCHH		27.63-
488PhosphorylationDREPNLLSGTAHSVN
HCCCCCCCCCCCCCC		36.9524260401
493PhosphorylationLLSGTAHSVNKRGVK
CCCCCCCCCCCCCCC		25.56-
496UbiquitinationGTAHSVNKRGVKRRD
CCCCCCCCCCCCHHC		48.6629967540
538UbiquitinationEVLSDAMKRGLISTP
HHHHHHHHCCCCCCC		45.0622817900
538 (in isoform 1)Ubiquitination-45.0621906983
547PhosphorylationGLISTPPSDMLPTTE
CCCCCCHHHHCCCCC		36.53-
552PhosphorylationPPSDMLPTTEGGKSN
CHHHHCCCCCCCCCC		33.25-
557UbiquitinationLPTTEGGKSNAWLRQ
CCCCCCCCCCHHHHH		51.9329967540
565UbiquitinationSNAWLRQKNAGIYVR
CCHHHHHHCCCEEEC		42.1929967540
570PhosphorylationRQKNAGIYVRPRLFS
HHHCCCEEECCCCCH		6.8927642862
655UbiquitinationVPRLLIMKDMVRRLQ
CCHHHHHHHHHHHHH		35.36-
683PhosphorylationLNCGEGATVSYEIQI
HCCCCCCEEEEEEEH		22.35-
685PhosphorylationCGEGATVSYEIQIRV
CCCCCEEEEEEEHHH		16.82-
686PhosphorylationGEGATVSYEIQIRVL
CCCCEEEEEEEHHHH		16.83-
722PhosphorylationDERFGDESPLLTMRQ
CCCCCCCCCCCCCCC		26.1130266825
726PhosphorylationGDESPLLTMRQPGRC
CCCCCCCCCCCCCCC		20.2830266825
792PhosphorylationPSQHPSRSFSYPCNH
CCCCCCCCCCCCCCC		23.9224719451
794PhosphorylationQHPSRSFSYPCNHSL
CCCCCCCCCCCCCCC		29.4328152594
795PhosphorylationHPSRSFSYPCNHSLF
CCCCCCCCCCCCCCC		15.1428152594
816PhosphorylationKAGPPPVYLPSVKAA
CCCCCCCCCCCCCCC		20.76-
845PhosphorylationVAAAAATTTSTATAA
HHHHHHCCHHHHHHH		17.6428674151
846PhosphorylationAAAAATTTSTATAAA
HHHHHCCHHHHHHHH		21.5228674151
847PhosphorylationAAAATTTSTATAAAA
HHHHCCHHHHHHHHH		17.6028674151
942PhosphorylationTRENPQEYPDFYDFS
CCCCCCCCCCHHHCC		11.6727642862
946PhosphorylationPQEYPDFYDFSNAAC
CCCCCCHHHCCCCCC		24.3727642862
949PhosphorylationYPDFYDFSNAACRPS
CCCHHHCCCCCCCCC		23.7428348404
956PhosphorylationSNAACRPSTPALSRR
CCCCCCCCCCCCCCC		27.8928348404
957PhosphorylationNAACRPSTPALSRRT
CCCCCCCCCCCCCCC		18.4428348404
964PhosphorylationTPALSRRTPSPSQGG
CCCCCCCCCCCCCCC		27.3228450419
966PhosphorylationALSRRTPSPSQGGYF
CCCCCCCCCCCCCCC		36.2528450419
968PhosphorylationSRRTPSPSQGGYFGP
CCCCCCCCCCCCCCC		45.8828450419
972PhosphorylationPSPSQGGYFGPDLYS
CCCCCCCCCCCCCCC		16.5228450419
978PhosphorylationGYFGPDLYSHNKASP
CCCCCCCCCCCCCCC		18.4427642862
979PhosphorylationYFGPDLYSHNKASPS
CCCCCCCCCCCCCCC		28.0728270605
984PhosphorylationLYSHNKASPSGLKSA
CCCCCCCCCCCCCCC		22.6228270605
986PhosphorylationSHNKASPSGLKSAYL
CCCCCCCCCCCCCCC		55.0228270605
990PhosphorylationASPSGLKSAYLPGQT
CCCCCCCCCCCCCCC		27.4729083192
992PhosphorylationPSGLKSAYLPGQTSP
CCCCCCCCCCCCCCH		22.1123312004
997PhosphorylationSAYLPGQTSPKKQEE
CCCCCCCCCHHHHHH		53.5728450419
998PhosphorylationAYLPGQTSPKKQEEA
CCCCCCCCHHHHHHH		27.1725159151
1009PhosphorylationQEEARREYPLSPDGH
HHHHHHHCCCCCCCC		13.9923186163
1012PhosphorylationARREYPLSPDGHLHR
HHHHCCCCCCCCCCC		19.2128985074
1048PhosphorylationLAAPENASTGPAHVR
CCCCCCCCCCCCCCC		45.5424719451
1049PhosphorylationAAPENASTGPAHVRG
CCCCCCCCCCCCCCC		44.7824719451
1074PhosphorylationGLTPNRPSLSACSSE
CCCCCCCCCCCCCCC		31.55-
1076PhosphorylationTPNRPSLSACSSEAP
CCCCCCCCCCCCCCC		31.41-
1112PhosphorylationTDLEREDSISRGRRS
CHHCCHHHHCCCCCC		20.0823312004
1114PhosphorylationLEREDSISRGRRSPS
HCCHHHHCCCCCCCC		32.4127251275
1119PhosphorylationSISRGRRSPSKPDFL
HHCCCCCCCCCCCCH		31.9725159151
1121PhosphorylationSRGRRSPSKPDFLYK
CCCCCCCCCCCCHHC		59.0523312004
1127PhosphorylationPSKPDFLYKKSAL--
CCCCCCHHCCCCC--		19.1623312004
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 BTBD7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BTBD7_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 BTBD7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of BTBD7_HUMAN !!
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 BTBD7_HUMAN

loading...

Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
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-998, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory