AT8B2_HUMAN - dbPTM
AT8B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT8B2_HUMAN
UniProt AC P98198
Protein Name Phospholipid-transporting ATPase ID
Gene Name ATP8B2
Organism Homo sapiens (Human).
Sequence Length 1209
Subcellular Localization Cell membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein . TMEM30A, but not TMEM30B, is required for its export from endoplasmic reticulum to the plasma membrane.
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)..
Protein Sequence MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNILTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDYFRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLCYIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENKFPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIFGFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNIMVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGDPHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVHEMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTTMDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMMLLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIVTGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHSLAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSMIKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFAFTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYEPGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSLVIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTLAQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGRTGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPSGGADKPLKG
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
194UbiquitinationLDGETNMKVRQAIPV
ECCCCCHHHHHCCCC		36.0129967540
207UbiquitinationPVTSELGDISKLAKF
CCCCCCCCHHHHHHC		55.3922817900
210 (in isoform 4)Ubiquitination-53.4421890473
210UbiquitinationSELGDISKLAKFDGE
CCCCCHHHHHHCCCE		53.4421890473
226UbiquitinationICEPPNNKLDKFSGT
EECCCCCCCCCCCCE		65.7822817900
227UbiquitinationCEPPNNKLDKFSGTL
ECCCCCCCCCCCCEE		10.6029967540
229UbiquitinationPPNNKLDKFSGTLYW
CCCCCCCCCCCEEEE		52.4422817900
229 (in isoform 2)Ubiquitination-52.4421890473
229 (in isoform 1)Ubiquitination-52.4421890473
240UbiquitinationTLYWKENKFPLSNQN
EEEECCCCCCCCCCC		49.8322817900
243UbiquitinationWKENKFPLSNQNMLL
ECCCCCCCCCCCEEH		9.3921890473
243 (in isoform 3)Ubiquitination-9.3921890473
254UbiquitinationNMLLRGCVLRNTEWC
CEEHHCEECCCCCCE		6.65-
346 (in isoform 4)Phosphorylation-5.6721712546
351 (in isoform 4)Phosphorylation-1.9121712546
358 (in isoform 4)Phosphorylation-13.2026546556
367 (in isoform 4)Phosphorylation-2.6419664995
369UbiquitinationYVSVEVIRLGHSYFI
EEEEEEEECCCCEEE		39.5332015554
393UbiquitinationKKRTPAEARTTTLNE
CCCCCCHHHHCCHHH		19.0722817900
412UbiquitinationVEYIFSDKTGTLTQN
EEEEEECCCCCEEEE		47.8922817900
426UbiquitinationNIMVFNKCSINGHSY
EEEEEEECEECCCCC		5.3222817900
477UbiquitinationPSLLEAVKIGDPHTH
HHHHHHHHCCCCCHH		48.2829967540
512PhosphorylationELYYKAQSPDEGALV
EEEEEEECCCCCCCH		38.9022673903
520PhosphorylationPDEGALVTAARNFGF
CCCCCCHHHHHHCCE		18.5622673903
526PhosphorylationVTAARNFGFVFRSRT
HHHHHHCCEEEECCC		22.74-
534PhosphorylationFVFRSRTPKTITVHE
EEEECCCCCEEEEEE		30.59-
579UbiquitinationGKIRLYCKGADTILL
CCEEEEECCCCEEEH		43.51-
592PhosphorylationLLDRLHHSTQELLNT
EHHHCCHHHHHHHHH		22.4928122231
593UbiquitinationLDRLHHSTQELLNTT
HHHCCHHHHHHHHHH		23.00-
593 (in isoform 3)Ubiquitination-23.00-
593PhosphorylationLDRLHHSTQELLNTT
HHHCCHHHHHHHHHH		23.0028122231
599PhosphorylationSTQELLNTTMDHLNE
HHHHHHHHHHHHHHH		24.3828122231
600PhosphorylationTQELLNTTMDHLNEY
HHHHHHHHHHHHHHH		21.3828122231
607PhosphorylationTMDHLNEYAGEGLRT
HHHHHHHHCCCCHHH		20.8728122231
620UbiquitinationRTLVLAYKDLDEEYY
HHHHHEECCCCHHHH		46.32-
693PhosphorylationNIKIWVLTGDKQETA
CCEEEEECCCCCHHE		33.44-
742PhosphorylationAREKMMDSSRSVGNG
HHHHHHHCCCCCCCC		15.11-
743PhosphorylationREKMMDSSRSVGNGF
HHHHHHCCCCCCCCC		25.0630576142
755UbiquitinationNGFTYQDKLSSSKLT
CCCCCHHHCCHHHHH		34.44-
757PhosphorylationFTYQDKLSSSKLTSV
CCCHHHCCHHHHHHH		38.0030576142
769 (in isoform 3)Ubiquitination-16.49-
769UbiquitinationTSVLEAVAGEYALVI
HHHHHHHCCCEEEEE		16.49-
823PhosphorylationVVELVKKYKKAVTLA
HHHHHHHHCCCEEEE		16.4128122231
828PhosphorylationKKYKKAVTLAIGDGA
HHHCCCEEEEECCCC		18.4822210691
839PhosphorylationGDGANDVSMIKTAHI
CCCCCCCEEEEEEEE		20.0428122231
952PhosphorylationQDVPEQRSMEYPKLY
CCCCCHHCCCCCCCC		18.7029978859
955PhosphorylationPEQRSMEYPKLYEPG
CCHHCCCCCCCCCCC		9.3129978859
959PhosphorylationSMEYPKLYEPGQLNL
CCCCCCCCCCCCEEE		26.6329978859
1110UbiquitinationFRFLRLNLKPDLSDT
HHHHHCCCCCCCHHH		11.4530230243
1111UbiquitinationRFLRLNLKPDLSDTV
HHHHCCCCCCCHHHH		35.1030230243
1117PhosphorylationLKPDLSDTVRYTQLV
CCCCCHHHHHHHHHH		11.9617192257
1125 (in isoform 3)Ubiquitination-49.39-
1125UbiquitinationVRYTQLVRKKQKAQH
HHHHHHHHHHHHHHH		49.39-
1129UbiquitinationQLVRKKQKAQHRCMR
HHHHHHHHHHHHHHH		59.9230230243
1131PhosphorylationVRKKQKAQHRCMRRV
HHHHHHHHHHHHHHH		31.4318691976
1169PhosphorylationSGKNMRLSSLALSSF
CCCCCCCHHHHHHCC		16.9730266825
1170PhosphorylationGKNMRLSSLALSSFT
CCCCCCHHHHHHCCC		23.4230266825
1174PhosphorylationRLSSLALSSFTTRSS
CCHHHHHHCCCCCCC		20.1430266825
1175PhosphorylationLSSLALSSFTTRSSS
CHHHHHHCCCCCCCH		27.7130266825
1177PhosphorylationSLALSSFTTRSSSSW
HHHHHCCCCCCCHHH		24.2129978859
1178PhosphorylationLALSSFTTRSSSSWI
HHHHCCCCCCCHHHH		26.9229978859
1180PhosphorylationLSSFTTRSSSSWIES
HHCCCCCCCHHHHHH		32.2623403867
1181PhosphorylationSSFTTRSSSSWIESL
HCCCCCCCHHHHHHH		25.7123403867
1182PhosphorylationSFTTRSSSSWIESLR
CCCCCCCHHHHHHHH		30.8223403867
1183PhosphorylationFTTRSSSSWIESLRR
CCCCCCHHHHHHHHH		33.7423403867
1187PhosphorylationSSSSWIESLRRKKSD
CCHHHHHHHHHHCCC		20.3123403867
1189PhosphorylationSSWIESLRRKKSDSA
HHHHHHHHHHCCCCC		58.62-
1193PhosphorylationESLRRKKSDSASSPS
HHHHHHCCCCCCCCC		39.5730108239
1195PhosphorylationLRRKKSDSASSPSGG
HHHHCCCCCCCCCCC		36.8230108239
1197PhosphorylationRKKSDSASSPSGGAD
HHCCCCCCCCCCCCC		46.8925002506
1200PhosphorylationSDSASSPSGGADKPL
CCCCCCCCCCCCCCC		52.38-
1201PhosphorylationDSASSPSGGADKPLK
CCCCCCCCCCCCCCC		38.40-
1207PhosphorylationSGGADKPLKG-----
CCCCCCCCCC-----		14.14-
1209PhosphorylationGADKPLKG-------
CCCCCCCC-------		50.90-
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 AT8B2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT8B2_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 AT8B2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AT8B2_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 AT8B2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1117, AND MASSSPECTROMETRY.

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