AT8A2_HUMAN - dbPTM
AT8A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT8A2_HUMAN
UniProt AC Q9NTI2
Protein Name Phospholipid-transporting ATPase IB
Gene Name ATP8A2
Organism Homo sapiens (Human).
Sequence Length 1148
Subcellular Localization Membrane
Multi-pass membrane protein . Golgi apparatus . Endosome. Cell projection, cilium, photoreceptor outer segment. Cell membrane . Localizes to the Golgi and endosomes in photoreceptor cells. Localizes to disk membranes of rod photoreceptor o
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. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Involved in regulation of neurite outgrowth; acting in synergy with TMEM30A. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival..
Protein Sequence MSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQWVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNRSHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREPSSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNIIYQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDVALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESMLRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRGQATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLRDSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDTTKKKSRKK
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
2Phosphorylation------MSRATSVGD
------CCCCCCHHH
41.7620363803
5Phosphorylation---MSRATSVGDQLE
---CCCCCCHHHHCC
23.8820363803
6Phosphorylation--MSRATSVGDQLEA
--CCCCCCHHHHCCC
24.1020363803
23PhosphorylationRTIYLNQPHLNKFRD
EEEEECCHHHHHCCC
32.6224719451
24PhosphorylationTIYLNQPHLNKFRDN
EEEECCHHHHHCCCC
32.0724719451
30PhosphorylationPHLNKFRDNQISTAK
HHHHHCCCCCCCHHH
55.2924719451
34PhosphorylationKFRDNQISTAKYSVL
HCCCCCCCHHHHHHH
16.73-
45PhosphorylationYSVLTFLPRFLYEQI
HHHHHHHHHHHHHHH
22.30-
46PhosphorylationSVLTFLPRFLYEQIR
HHHHHHHHHHHHHHH
36.0319664994
112AcetylationADNAVNKKKTIVLRN
CCCCCCCCCEEEEEC
50.3620167786
128AcetylationMWHTIMWKEVAVGDI
CEEEEEEEEEECCCE
25.5720167786
239PhosphorylationRGTQLRNTQWVFGIV
ECCCCCCCCEEEEEE
19.85-
248PhosphorylationWVFGIVVYTGHDTKL
EEEEEEEEECCCHHH
8.98-
249PhosphorylationVFGIVVYTGHDTKLM
EEEEEEEECCCHHHC
19.21-
253PhosphorylationVVYTGHDTKLMQNST
EEEECCCHHHCCCCC
22.02-
259PhosphorylationDTKLMQNSTKAPLKR
CHHHCCCCCCCCCCC
17.88-
260PhosphorylationTKLMQNSTKAPLKRS
HHHCCCCCCCCCCCC
38.48-
267PhosphorylationTKAPLKRSNVEKVTN
CCCCCCCCCCCCCHH
43.57-
372PhosphorylationDTPAMARTSNLNEEL
CCHHHHHCCCCCHHH
16.66-
373PhosphorylationTPAMARTSNLNEELG
CHHHHHCCCCCHHHC
33.4923898821
383UbiquitinationNEELGQVKYLFSDKT
CHHHCCCEEEEECCC
28.48-
384PhosphorylationEELGQVKYLFSDKTG
HHHCCCEEEEECCCC
17.7023898821
387PhosphorylationGQVKYLFSDKTGTLT
CCCEEEEECCCCEEE
35.2923898821
390PhosphorylationKYLFSDKTGTLTCNI
EEEEECCCCEEEEEE
40.1522210691
404PhosphorylationIMNFKKCSIAGVTYG
EECCCCCEEEEEEEC
25.09-
409PhosphorylationKCSIAGVTYGHFPEL
CCEEEEEEECCCHHH
23.91-
410PhosphorylationCSIAGVTYGHFPELA
CEEEEEEECCCHHHC
13.24-
421PhosphorylationPELAREPSSDDFCRM
HHHCCCCCCCCCCCC
41.4629691806
422PhosphorylationELAREPSSDDFCRMP
HHCCCCCCCCCCCCC
52.4929691806
453PhosphorylationNIEDRHPTAPCIQEF
CCHHHCCCCHHHHHH
36.79-
506PhosphorylationGFVFTARTPFSVIIE
CEEEEECCCCCHHHH
26.65-
509PhosphorylationFTARTPFSVIIEAMG
EEECCCCCHHHHHCC
17.38-
563PhosphorylationNVIFERLSKDSKYME
CEEEEECCCCCHHHH
40.4120068231
566PhosphorylationFERLSKDSKYMEETL
EEECCCCCHHHHHHH
29.4420068231
603PhosphorylationENEYEEWLKVYQEAS
CCHHHHHHHHHHHHH
2.8020068231
606PhosphorylationYEEWLKVYQEASTIL
HHHHHHHHHHHHHHH
10.0720068231
650PhosphorylationLQAGVPETIATLLKA
HHCCCCHHHHHHHHH
15.16-
695PhosphorylationLILLKEDSLDATRAA
EEEEECCCCHHHHHH
29.28-
762PhosphorylationRVSPLQKSEIVDVVK
CCCCCCCCHHHHHHH
21.4227794612
1005PhosphorylationWLVFFGIYSTIWPTI
HHHHHHHHHHHCCCC
10.5124248375
1006PhosphorylationLVFFGIYSTIWPTIP
HHHHHHHHHHCCCCC
16.1124248375
1101PhosphorylationIKRLGRKTPPTLFRG
HHHHCCCCCCCCCCC
32.8929691806
1104PhosphorylationLGRKTPPTLFRGSSL
HCCCCCCCCCCCCCC
39.4729691806
1109PhosphorylationPPTLFRGSSLQQGVP
CCCCCCCCCCCCCCC
24.5022210691
1110PhosphorylationPTLFRGSSLQQGVPH
CCCCCCCCCCCCCCC
32.7822210691
1119PhosphorylationQQGVPHGYAFSQEEH
CCCCCCCCCCCHHHC
11.0522210691
1130PhosphorylationQEEHGAVSQEEVIRA
HHHCCCCCHHHHHHH
31.1922210691
1138PhosphorylationQEEVIRAYDTTKKKS
HHHHHHHHHCCCCCC
12.1820860994
1141PhosphorylationVIRAYDTTKKKSRKK
HHHHHHCCCCCCCCC
37.6620860994

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 AT8A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT8A2_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 AT8A2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UIMC1_HUMANUIMC1physical
17621610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT8A2_HUMAN

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Related Literatures of Post-Translational Modification

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