UniProt ID | AT11B_HUMAN | |
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UniProt AC | Q9Y2G3 | |
Protein Name | Probable phospholipid-transporting ATPase IF | |
Gene Name | ATP11B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1177 | |
Subcellular Localization |
Recycling endosome membrane Multi-pass membrane protein. Early endosome . Endoplasmic reticulum . Golgi apparatus, trans-Golgi network . Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B (PubMed:21914794). In the |
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Protein Description | Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (Probable). Involved in regulation of sensitivity to cisplatin; may contribute to secretory vesicle transport of cisplatin from Golgi to plasma membrane.. | |
Protein Sequence | MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLFEQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVNGAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGETNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPESLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISEAVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVTVEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFRECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETELIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAARIGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESSILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEKLAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSCGHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLFMEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMGKEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYCLFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKTFLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALETHFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMVVTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERVIGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | GFDPPHQSDTRTIYV CCCCCCCCCCCEEEE | 37.60 | - | |
19 | Phosphorylation | DPPHQSDTRTIYVAN CCCCCCCCCEEEEEE | 34.65 | 26074081 | |
21 | Phosphorylation | PHQSDTRTIYVANRF CCCCCCCEEEEEECC | 20.82 | 26074081 | |
23 | Phosphorylation | QSDTRTIYVANRFPQ CCCCCEEEEEECCCC | 7.90 | 26074081 | |
34 | Phosphorylation | RFPQNGLYTPQKFID CCCCCCCCCCHHHCC | 20.13 | - | |
38 | Ubiquitination | NGLYTPQKFIDNRII CCCCCCHHHCCCCCC | 45.55 | - | |
125 | Phosphorylation | EVNGAPVYVVRSGGL CCCCCCEEEEECCCE | 7.68 | - | |
261 | Phosphorylation | EIFGVAVYTGMETKM HEEEEEEECCHHHHH | 6.45 | 29116813 | |
262 | Phosphorylation | IFGVAVYTGMETKMA EEEEEEECCHHHHHH | 24.37 | 29116813 | |
266 | Phosphorylation | AVYTGMETKMALNYK EEECCHHHHHHHCCC | 19.75 | 29116813 | |
272 | Phosphorylation | ETKMALNYKSKSQKR HHHHHHCCCCHHHHH | 19.93 | 29116813 | |
274 | Phosphorylation | KMALNYKSKSQKRSA HHHHCCCCHHHHHHH | 27.46 | 29116813 | |
276 | Phosphorylation | ALNYKSKSQKRSAVE HHCCCCHHHHHHHHH | 48.28 | 29116813 | |
326 | O-linked_Glycosylation | EPWYNQKTEHQRNSS CCCCCCCCHHHHCHH | 29.00 | 30620550 | |
403 | Phosphorylation | EELGQVEYVFTDKTG HHHCCEEEEEECCCC | 11.29 | 27642862 | |
428 | Ubiquitination | ECSINGMKYQEINGR ECCCCCEEEEEECCE | 45.22 | - | |
442 | Phosphorylation | RLVPEGPTPDSSEGN EECCCCCCCCCCCCC | 51.05 | 27135362 | |
445 | Phosphorylation | PEGPTPDSSEGNLSY CCCCCCCCCCCCHHH | 31.34 | 26657352 | |
446 | Phosphorylation | EGPTPDSSEGNLSYL CCCCCCCCCCCHHHH | 57.83 | 26657352 | |
451 | Phosphorylation | DSSEGNLSYLSSLSH CCCCCCHHHHHHCHH | 28.20 | 28796482 | |
452 | Phosphorylation | SSEGNLSYLSSLSHL CCCCCHHHHHHCHHH | 17.48 | 28796482 | |
454 | Phosphorylation | EGNLSYLSSLSHLNN CCCHHHHHHCHHHCC | 22.47 | 28796482 | |
455 | Phosphorylation | GNLSYLSSLSHLNNL CCHHHHHHCHHHCCC | 31.15 | 28796482 | |
457 | Phosphorylation | LSYLSSLSHLNNLSH HHHHHHCHHHCCCHH | 28.07 | 28348404 | |
463 | Phosphorylation | LSHLNNLSHLTTSSS CHHHCCCHHCCCCCC | 20.69 | 28348404 | |
466 | Phosphorylation | LNNLSHLTTSSSFRT HCCCHHCCCCCCCCC | 21.14 | 28348404 | |
467 | Phosphorylation | NNLSHLTTSSSFRTS CCCHHCCCCCCCCCC | 32.73 | 28348404 | |
468 | Phosphorylation | NLSHLTTSSSFRTSP CCHHCCCCCCCCCCC | 20.81 | 28348404 | |
469 | Phosphorylation | LSHLTTSSSFRTSPE CHHCCCCCCCCCCCC | 31.25 | 28348404 | |
470 | Phosphorylation | SHLTTSSSFRTSPEN HHCCCCCCCCCCCCC | 20.65 | 28348404 | |
473 | Phosphorylation | TTSSSFRTSPENETE CCCCCCCCCCCCHHH | 46.77 | 30108239 | |
474 | Phosphorylation | TSSSFRTSPENETEL CCCCCCCCCCCHHHH | 26.43 | 21815630 | |
479 | Phosphorylation | RTSPENETELIKEHD CCCCCCHHHHHHHCH | 47.90 | 30108239 | |
483 | Ubiquitination | ENETELIKEHDLFFK CCHHHHHHHCHHHHH | 62.71 | - | |
599 | Phosphorylation | LFAKGAESSILPKCI EEECCCCCCCCCHHH | 23.34 | 23403867 | |
600 | Phosphorylation | FAKGAESSILPKCIG EECCCCCCCCCHHHC | 21.46 | 23403867 | |
612 | Ubiquitination | CIGGEIEKTRIHVDE HHCCCEEECEEEHHH | 49.08 | - | |
623 | Ubiquitination | HVDEFALKGLRTLCI EHHHHHHHHHHHHHH | 53.09 | - | |
638 | Ubiquitination | AYRKFTSKEYEEIDK HHHHCCCHHHHHHHH | 62.35 | - | |
706 | Phosphorylation | GIKVWVLTGDKHETA CCEEEEEECCCCCEE | 33.44 | - | |
726 | Phosphorylation | SCGHFHRTMNILELI ECCCHHHHHHHHHHH | 13.14 | - | |
736 | Ubiquitination | ILELINQKSDSECAE HHHHHHCCCHHHHHH | 52.31 | - | |
788 | Phosphorylation | MEVCRNCSAVLCCRM HHHHHCCCCHHHCCC | 25.59 | 29449344 | |
802 | Ubiquitination | MAPLQKAKVIRLIKI CCHHCCCEEEEEEEE | 45.27 | - | |
957 | Phosphorylation | ISKNRLLSIKTFLYW CCCCCHHHHHHHHHH | 26.99 | 24719451 | |
1145 | Phosphorylation | ERVIGRCSPTHISRS HHHHCCCCCCCCCCC | 31.32 | 26657352 | |
1147 | Phosphorylation | VIGRCSPTHISRSWS HHCCCCCCCCCCCCC | 18.62 | 28122231 | |
1150 | Phosphorylation | RCSPTHISRSWSASD CCCCCCCCCCCCCCC | 16.80 | 25404012 | |
1152 | Phosphorylation | SPTHISRSWSASDPF CCCCCCCCCCCCCCC | 20.70 | 21945579 | |
1154 | Phosphorylation | THISRSWSASDPFYT CCCCCCCCCCCCCCC | 21.09 | 23927012 | |
1156 | Phosphorylation | ISRSWSASDPFYTND CCCCCCCCCCCCCCC | 40.06 | 21945579 | |
1160 | Phosphorylation | WSASDPFYTNDRSIL CCCCCCCCCCCCCEE | 15.26 | 21945579 | |
1161 | Phosphorylation | SASDPFYTNDRSILT CCCCCCCCCCCCEEE | 30.90 | 21945579 | |
1170 | Phosphorylation | DRSILTLSTMDSSTC CCCEEEEEECCCCCC | 19.22 | 27690223 | |
1171 | Phosphorylation | RSILTLSTMDSSTC- CCEEEEEECCCCCC- | 28.27 | 27690223 | |
1174 | Phosphorylation | LTLSTMDSSTC---- EEEEECCCCCC---- | 19.41 | 27690223 | |
1175 | Phosphorylation | TLSTMDSSTC----- EEEECCCCCC----- | 29.54 | 27690223 | |
1176 | Phosphorylation | LSTMDSSTC------ EEECCCCCC------ | 26.62 | 27690223 |
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 AT11B_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AT11B_HUMAN !! |
* 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 AT11B_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CC50A_HUMAN | TMEM30A | physical | 21914794 | |
IFN21_HUMAN | IFNA21 | physical | 28514442 |
Kegg Disease | ||||||
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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. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, AND MASSSPECTROMETRY. |