NKAIN_DROME - dbPTM
NKAIN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NKAIN_DROME
UniProt AC A6MHQ4
Protein Name Sodium/potassium-transporting ATPase subunit beta-1-interacting protein
Gene Name NKAIN
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 658
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Induces a small but significant sodium conductance when expressed in Xenopus oocytes..
Protein Sequence MGSCSCTRRHFLLSICFLQVITIIERQVFDFLGYMWAPILVNFFHILFIIFGFYGAYHFRVKYIITYLIWNFLWIGWNTFLICFYLNVGQLNRDSDLLNLGTGSVSWFEANGYGCKPTYNMAADDTFRPQRPERVEGCLLDYPLVEITHSGVQCALALLGILGAILISCIFLDEDDRFDFMNGDAKSPQHTVVHPMYVSYTSIPTTSASATMQSNKHLQLQHQQPQQNSLKLYHHQQQQQPKLHHFNKNYQLSGSNNNTLNNNLHQRAPALLPPNTTNNRSASFQTQSHPSNNHVTQRTGGEGSNCSSLRRHRQHHSKALVSPSPMSPQTTPSLSYASLQNSSPYLAGNSLSNSNYSIFQSPDSLQGSSHFARIHHKPKPPKSDYPVSGEFNPGGNISSPVRPLDRLSRSLEDDEDNFSLQKFAPGEHGVTYVPFQSPTPNSLFLGENNNSQPHLVFHTNSRSSPNNNAYPYDQSGLPSSLRMGSNSNARRPTHIPLPTVPMHNCQEVENDEDADGESEQDHDQMLTPPPPPLVRPHIHQRLGQAPYLDLSPEVAERYAIPSKLGPSLPIQVPLPVPHGSPMVRRSNRRPRPSNPVNFCDQIRATPPGYVVRAQSDDRLMEQVEADAAPHVNRRSGRGGSGQKTRPRSFCNSIVGVQG
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
229PhosphorylationHQQPQQNSLKLYHHQ
CCCCCHHHHHHHHHH
23.6519429919
233PhosphorylationQQNSLKLYHHQQQQQ
CHHHHHHHHHHHHHC
8.8219429919
250PhosphorylationLHHFNKNYQLSGSNN
CCCCCCCCCCCCCCC
16.6718281928
257N-linked_GlycosylationYQLSGSNNNTLNNNL
CCCCCCCCCCCCCCH
44.56-
275N-linked_GlycosylationAPALLPPNTTNNRSA
CCCCCCCCCCCCCCC
58.56-
279N-linked_GlycosylationLPPNTTNNRSASFQT
CCCCCCCCCCCCCCC
36.87-
291PhosphorylationFQTQSHPSNNHVTQR
CCCCCCCCCCCCCCC
44.8518327897
305N-linked_GlycosylationRTGGEGSNCSSLRRH
CCCCCCCCHHHHHHH
40.31-
307PhosphorylationGGEGSNCSSLRRHRQ
CCCCCCHHHHHHHHH
36.3427626673
308PhosphorylationGEGSNCSSLRRHRQH
CCCCCHHHHHHHHHH
28.2625749252
355N-linked_GlycosylationGNSLSNSNYSIFQSP
CCCCCCCCCCCCCCC
38.53-
396N-linked_GlycosylationGEFNPGGNISSPVRP
CCCCCCCCCCCCCCC
36.56-
398PhosphorylationFNPGGNISSPVRPLD
CCCCCCCCCCCCCHH
32.3718327897
399PhosphorylationNPGGNISSPVRPLDR
CCCCCCCCCCCCHHH
24.5012537569
417N-linked_GlycosylationSLEDDEDNFSLQKFA
CCCCCCCCCCCCCCC
26.76-
419PhosphorylationEDDEDNFSLQKFAPG
CCCCCCCCCCCCCCC
35.8225749252
449N-linked_GlycosylationSLFLGENNNSQPHLV
CEEECCCCCCCCEEE
45.27-
472PhosphorylationPNNNAYPYDQSGLPS
CCCCCCCCCCCCCCC
17.5918281928
580PhosphorylationPLPVPHGSPMVRRSN
CCCCCCCCCCCCCCC
13.5423607784
615PhosphorylationGYVVRAQSDDRLMEQ
CEEEEECCCCHHHHH
40.2622668510
648PhosphorylationGQKTRPRSFCNSIVG
CCCCCCCCHHHHHCC
36.5129892262
652PhosphorylationRPRSFCNSIVGVQG-
CCCCHHHHHCCCCC-
21.6029892262

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 NKAIN_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NKAIN_DROME !!

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 NKAIN_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATPB2_DROMEnrv2physical
17606467

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; SER-308; SER-398AND SER-399, AND MASS SPECTROMETRY.

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