AB1B_ARATH - dbPTM
AB1B_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB1B_ARATH
UniProt AC Q9ZR72
Protein Name ABC transporter B family member 1
Gene Name ABCB1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1286
Subcellular Localization Cell membrane
Multi-pass membrane protein . Non-polar distribution in apical cells. Predominant basal (top) localization in root tissues above the elongation zone, especially in mature cortical and endodermal cells. Basal and apical localization in
Protein Description Auxin efflux transporter that acts as a negative regulator of light signaling to promote hypocotyl elongation. Mediates the accumulation of chlorophyll and anthocyanin, as well as the expression of genes in response to light. Participates directly in auxin efflux and thus regulates the polar (presumably basipetal) auxin transport (from root tips to root elongating zone). Transports also some auxin metabolites such as oxindoleacetic acid and indoleacetaldehyde. Involved in diverse auxin-mediated responses including gravitropism, phototropism and lateral root formation. Confers resistance to herbicides such as dicamba, pendimethalin, oryzalin, and monosodium acid methanearsonate (MSMA), but not to herbicides such as glyphosate, atrazine, bentazon and fluazifop-p-butyl. Mediates also resistance to xenobiotics such as cycloheximide and the cytokinin N6-(2-isopentenyl)adenine (2IP)..
Protein Sequence MDNDGGAPPPPPTLVVEEPKKAEIRGVAFKELFRFADGLDYVLMGIGSVGAFVHGCSLPLFLRFFADLVNSFGSNSNNVEKMMEEVLKYALYFLVVGAAIWASSWAEISCWMWSGERQTTKMRIKYLEAALNQDIQFFDTEVRTSDVVFAINTDAVMVQDAISEKLGNFIHYMATFVSGFIVGFTAVWQLALVTLAVVPLIAVIGGIHTTTLSKLSNKSQESLSQAGNIVEQTVVQIRVVMAFVGESRASQAYSSALKIAQKLGYKTGLAKGMGLGATYFVVFCCYALLLWYGGYLVRHHLTNGGLAIATMFAVMIGGLALGQSAPSMAAFAKAKVAAAKIFRIIDHKPTIERNSESGVELDSVTGLVELKNVDFSYPSRPDVKILNNFCLSVPAGKTIALVGSSGSGKSTVVSLIERFYDPNSGQVLLDGQDLKTLKLRWLRQQIGLVSQEPALFATSIKENILLGRPDADQVEIEEAARVANAHSFIIKLPDGFDTQVGERGLQLSGGQKQRIAIARAMLKNPAILLLDEATSALDSESEKLVQEALDRFMIGRTTLIIAHRLSTIRKADLVAVLQQGSVSEIGTHDELFSKGENGVYAKLIKMQEAAHETAMSNARKSSARPSSARNSVSSPIMTRNSSYGRSPYSRRLSDFSTSDFSLSIDASSYPNYRNEKLAFKDQANSFWRLAKMNSPEWKYALLGSVGSVICGSLSAFFAYVLSAVLSVYYNPDHEYMIKQIDKYCYLLIGLSSAALVFNTLQHSFWDIVGENLTKRVREKMLSAVLKNEMAWFDQEENESARIAARLALDANNVRSAIGDRISVIVQNTALMLVACTAGFVLQWRLALVLVAVFPVVVAATVLQKMFMTGFSGDLEAAHAKGTQLAGEAIANVRTVAAFNSEAKIVRLYTANLEPPLKRCFWKGQIAGSGYGVAQFCLYASYALGLWYASWLVKHGISDFSKTIRVFMVLMVSANGAAETLTLAPDFIKGGQAMRSVFELLDRKTEIEPDDPDTTPVPDRLRGEVELKHIDFSYPSRPDIQIFRDLSLRARAGKTLALVGPSGCGKSSVISLIQRFYEPSSGRVMIDGKDIRKYNLKAIRKHIAIVPQEPCLFGTTIYENIAYGHECATEAEIIQAATLASAHKFISALPEGYKTYVGERGVQLSGGQKQRIAIARALVRKAEIMLLDEATSALDAESERSVQEALDQACSGRTSIVVAHRLSTIRNAHVIAVIDDGKVAEQGSHSHLLKNHPDGIYARMIQLQRFTHTQVIGMTSGSSSRVKEDDA
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
217N-linked_GlycosylationTTLSKLSNKSQESLS
HHHHHHCCCCHHHHH		59.44-
411PhosphorylationSSGSGKSTVVSLIER
CCCCCHHHHHHHHHH		28.5423328941
621PhosphorylationAMSNARKSSARPSSA
HHHHHHHHCCCCCHH		24.5525561503
622PhosphorylationMSNARKSSARPSSAR
HHHHHHHCCCCCHHC		31.1925561503
626PhosphorylationRKSSARPSSARNSVS
HHHCCCCCHHCCCCC		30.9525561503
627PhosphorylationKSSARPSSARNSVSS
HHCCCCCHHCCCCCC		33.6529654922
631PhosphorylationRPSSARNSVSSPIMT
CCCHHCCCCCCCCCC		20.1615308754
633PhosphorylationSSARNSVSSPIMTRN
CHHCCCCCCCCCCCC		30.1615308754
634PhosphorylationSARNSVSSPIMTRNS
HHCCCCCCCCCCCCC		19.1130291188
638PhosphorylationSVSSPIMTRNSSYGR
CCCCCCCCCCCCCCC		27.6719376835
640N-linked_GlycosylationSSPIMTRNSSYGRSP
CCCCCCCCCCCCCCC		26.58-
641PhosphorylationSPIMTRNSSYGRSPY
CCCCCCCCCCCCCCC		22.9629654922
642PhosphorylationPIMTRNSSYGRSPYS
CCCCCCCCCCCCCCC		34.8519880383
643PhosphorylationIMTRNSSYGRSPYSR
CCCCCCCCCCCCCCC		19.1725561503
646PhosphorylationRNSSYGRSPYSRRLS
CCCCCCCCCCCCCCC		24.6729654922
648PhosphorylationSSYGRSPYSRRLSDF
CCCCCCCCCCCCCCC		18.9619880383
649PhosphorylationSYGRSPYSRRLSDFS
CCCCCCCCCCCCCCC		17.8219880383
656PhosphorylationSRRLSDFSTSDFSLS
CCCCCCCCCCCCEEE		31.8015308754
657PhosphorylationRRLSDFSTSDFSLSI
CCCCCCCCCCCEEEE		32.1015308754
658PhosphorylationRLSDFSTSDFSLSID
CCCCCCCCCCEEEEC		35.1515308754
771N-linked_GlycosylationFWDIVGENLTKRVRE
HHHHHCHHHHHHHHH		47.27-
797N-linked_GlycosylationAWFDQEENESARIAA
CCCCCCCCHHHHHHH		48.01-
882PhosphorylationEAAHAKGTQLAGEAI
HHHHHHCCHHHHHHH		21.5024894044
962PhosphorylationGISDFSKTIRVFMVL
CCCCHHHHHHHHHHE		16.9025368622
972PhosphorylationVFMVLMVSANGAAET
HHHHEHHCCCCHHHH		11.3125368622
979PhosphorylationSANGAAETLTLAPDF
CCCCHHHHHHCCCCH		21.9525368622
1013PhosphorylationIEPDDPDTTPVPDRL
CCCCCCCCCCCCCCC		38.0915308754
1014PhosphorylationEPDDPDTTPVPDRLR
CCCCCCCCCCCCCCC		29.6615308754
1061PhosphorylationTLALVGPSGCGKSSV
EEEEECCCCCCHHHH		40.5628295753
1197PhosphorylationTSALDAESERSVQEA
HHCCCHHHHHHHHHH		39.7824243849
1274PhosphorylationHTQVIGMTSGSSSRV
CEEEEEECCCCCCCC		25.4017317660
1275PhosphorylationTQVIGMTSGSSSRVK
EEEEEECCCCCCCCC		27.9917317660
1277PhosphorylationVIGMTSGSSSRVKED
EEEECCCCCCCCCCC		25.5517317660
1278PhosphorylationIGMTSGSSSRVKEDD
EEECCCCCCCCCCCC		26.2017317660
1279PhosphorylationGMTSGSSSRVKEDDA
EECCCCCCCCCCCCC		42.6717317660
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 AB1B_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AB1B_ARATH !!
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 AB1B_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AB1B_ARATHABCB1genetic
15908594
AXR1_ARATHAXR1genetic
15908594
FKB42_ARATHTWD1physical
23321285
UBC34_ARATHUBC34physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
PINI_ARATHPIN1physical
17237354
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AB1B_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND MASSSPECTROMETRY.
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASSSPECTROMETRY.

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