AB2B_ARATH - dbPTM
AB2B_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AB2B_ARATH
UniProt AC Q8LPK2
Protein Name ABC transporter B family member 2
Gene Name ABCB2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1273
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MYISLIFFLSNHFPPLISIPIFIFLSFSSPTNYTHLKLKKMQPSGDPAPEKEKEMTQPKVSLLKLFSFADFYDCVLMTLGSVGACIHGASVPIFFIFFGKLINIIGLAYLFPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAAAYPIFKMIERNTVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDGAYSSLLRLQETASLQRNPSLNRTLSRPHSIKYSRELSRTRSSFCSERESVTRPDGADPSKKVKVTVGRLYSMIRPDWMYGVCGTICAFIAGSQMPLFALGVSQALVSYYSGWDETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEVDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKGLAGFKSVMKTFMVLIVTALAMGETLALAPDLLKGNQMVASVFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVLNKSGPYFKLISLQQQQQP
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
466N-linked_GlycosylationAVLLDGNNISELDIK
CEEECCCCCCHHHHH
44.70-
649PhosphorylationASLQRNPSLNRTLSR
HHCCCCCCHHHCCCC
41.6519376835
651N-linked_GlycosylationLQRNPSLNRTLSRPH
CCCCCCHHHCCCCCC
38.95-
655PhosphorylationPSLNRTLSRPHSIKY
CCHHHCCCCCCHHHH
43.0627531888
659PhosphorylationRTLSRPHSIKYSREL
HCCCCCCHHHHHHHH
24.3730300945
663PhosphorylationRPHSIKYSRELSRTR
CCCHHHHHHHHHCCC
17.8025561503
671PhosphorylationRELSRTRSSFCSERE
HHHHCCCCCHHCCCC
27.4425561503
672PhosphorylationELSRTRSSFCSERES
HHHCCCCCHHCCCCC
27.2925561503
675PhosphorylationRTRSSFCSERESVTR
CCCCCHHCCCCCCCC
37.3625561503
806N-linked_GlycosylationGWFDEVDNTSSMLAS
CCCCCCCCHHHHHHH
47.22-
918PhosphorylationEKILELYSRELLEPS
HHHHHHHHHHHHCCC
31.7224894044
1217N-linked_GlycosylationALDRLMANRTTVVVA
HHHHHHCCCCEEEEE
28.06-
1256N-linked_GlycosylationSHRKLVLNKSGPYFK
CCEEEEEECCCCCEE
29.03-

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 AB2B_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AB2B_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 AB2B_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AB2B_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AB2B_ARATH

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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-649, AND MASSSPECTROMETRY.

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