UniProt ID | AB4B_ARATH | |
---|---|---|
UniProt AC | O80725 | |
Protein Name | ABC transporter B family member 4 | |
Gene Name | ABCB4 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 1286 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . Non-polar distribution in apical cells. Apical (bottom) localization in mature root cells. Basal (top) localization in the root elongation zone. |
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Protein Description | Auxin influx transporter that mediates the transport of auxin in roots. Contributes to the basipetal transport in hypocotyls and root tips by establishing an auxin uptake sink in the root cap. Confers sensitivity to 1-N-naphthylphthalamic acid (NPA). Regulates the root elongation, the initiation of lateral roots and the development of root hairs. Can transport IAA, indole-3-propionic acid, NPA syringic acid, vanillic acid and some auxin metabolites, but not 2,4-D and 1-naphthaleneacetic acid.. | |
Protein Sequence | MASESGLNGDPNILEEVSETKRDKEEEEEVKKTEKKDEEHEKTKTVPFYKLFAFADSFDFLLMILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDIDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETIERRPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIRLQEEKKSDENAAEEQKMSSIESFKQSSLRKSSLGRSLSKGGSSRGNSSRHSFNMFGFPAGIDGNVVQDQEEDDTTQPKTEPKKVSIFRIAALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEPENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSVFRVFFALTMAAMAISQSSSLSPDSSKADVAAASIFAIMDRESKIDPSVESGRVLDNVKGDIELRHVSFKYPARPDVQIFQDLCLSIRAGKTVALVGESGSGKSTVIALLQRFYDPDSGEITLDGVEIKSLRLKWLRQQTGLVSQEPILFNETIRANIAYGKGGDASESEIVSSAELSNAHGFISGLQQGYDTMVGERGIQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTIVVAHRLSTIKNADVIAVVKNGVIVEKGKHDTLINIKDGVYASLVQLHLTAAS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MASESGLNGD -----CCCCCCCCCC | 44.12 | 30407730 | |
5 | Phosphorylation | ---MASESGLNGDPN ---CCCCCCCCCCCC | 46.19 | 19880383 | |
18 | Phosphorylation | PNILEEVSETKRDKE CCHHHHHHHHHCCHH | 42.71 | 30407730 | |
20 | Phosphorylation | ILEEVSETKRDKEEE HHHHHHHHHCCHHHH | 24.71 | 30407730 | |
94 | N-linked_Glycosylation | LIDAFGENQTNTTDK HHHHHCCCCCCCCHH | 55.12 | - | |
97 | N-linked_Glycosylation | AFGENQTNTTDKVSK HHCCCCCCCCHHHHH | 31.08 | - | |
427 | Phosphorylation | QSGSGKSTVVSLIER CCCCCHHHHHHHHHH | 28.54 | 23328941 | |
500 | N-linked_Glycosylation | KAAAELANASKFVDK HHHHHHHHHHHHHHH | 58.32 | - | |
502 | Phosphorylation | AAELANASKFVDKLP HHHHHHHHHHHHHCC | 26.83 | 23328941 | |
571 | N-linked_Glycosylation | ALDRIMVNRTTVVVA HHHHHCCCCCEEEEE | 20.43 | - | |
638 | Phosphorylation | AAEEQKMSSIESFKQ HHHHHHHHHHHHHHH | 34.89 | 23111157 | |
639 | Phosphorylation | AEEQKMSSIESFKQS HHHHHHHHHHHHHHH | 27.20 | 20374526 | |
642 | Phosphorylation | QKMSSIESFKQSSLR HHHHHHHHHHHHHCC | 35.75 | 19880383 | |
646 | Phosphorylation | SIESFKQSSLRKSSL HHHHHHHHHCCHHHH | 31.75 | 15308754 | |
647 | Phosphorylation | IESFKQSSLRKSSLG HHHHHHHHCCHHHHC | 29.69 | 15308754 | |
656 | Phosphorylation | RKSSLGRSLSKGGSS CHHHHCCHHCCCCCC | 34.89 | 25561503 | |
658 | Phosphorylation | SSLGRSLSKGGSSRG HHHCCHHCCCCCCCC | 30.42 | 25561503 | |
662 | Phosphorylation | RSLSKGGSSRGNSSR CHHCCCCCCCCCCCC | 26.07 | 25561503 | |
666 | N-linked_Glycosylation | KGGSSRGNSSRHSFN CCCCCCCCCCCCCCC | 35.38 | - | |
671 | Phosphorylation | RGNSSRHSFNMFGFP CCCCCCCCCCCCCCC | 19.73 | 15308754 | |
816 | N-linked_Glycosylation | GWFDEPENSSGTIGA ECCCCCCCCCCCCCC | 52.79 | - | |
846 | N-linked_Glycosylation | SLAQTVQNLSSILAG HHHHHHHHHHHHHHH | 37.24 | - | |
1094 | Phosphorylation | IALLQRFYDPDSGEI HHHHHHHCCCCCCEE | 28.84 | 19880383 | |
1131 | N-linked_Glycosylation | SQEPILFNETIRANI CCCCCCCCHHHHHHH | 41.90 | - | |
1230 | N-linked_Glycosylation | ALDRVMVNRTTIVVA HHHHHHCCCCEEEEE | 19.93 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of AB4B_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of AB4B_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of AB4B_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of AB4B_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of plasma membrane proteinsreveals regulatory mechanisms of plant innate immune responses."; Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C.; Plant J. 51:931-940(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642, 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-642 AND SER-671, ANDMASS SPECTROMETRY. | |
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-646 ANDSER-647, AND MASS SPECTROMETRY. |