AT1A4_HUMAN - dbPTM
AT1A4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT1A4_HUMAN
UniProt AC Q13733
Protein Name Sodium/potassium-transporting ATPase subunit alpha-4
Gene Name ATP1A4
Organism Homo sapiens (Human).
Sequence Length 1029
Subcellular Localization Cell membrane
Multi-pass membrane protein . In mature sperm, located in the principle piece of the sperm flagellum.
Protein Description This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. Plays a role in sperm motility..
Protein Sequence MGLWGKKGTVAPHDQSPRRRPKKGLIKKKMVKREKQKRNMEELKKEVVMDDHKLTLEELSTKYSVDLTKGHSHQRAKEILTRGGPNTVTPPPTTPEWVKFCKQLFGGFSLLLWTGAILCFVAYSIQIYFNEEPTKDNLYLSIVLSVVVIVTGCFSYYQEAKSSKIMESFKNMVPQQALVIRGGEKMQINVQEVVLGDLVEIKGGDRVPADLRLISAQGCKVDNSSLTGESEPQSRSPDFTHENPLETRNICFFSTNCVEGTARGIVIATGDSTVMGRIASLTSGLAVGQTPIAAEIEHFIHLITVVAVFLGVTFFALSLLLGYGWLEAIIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDMTVYEADTTEEQTGKTFTKSSDTWFMLARIAGLCNRADFKANQEILPIAKRATTGDASESALLKFIEQSYSSVAEMREKNPKVAEIPFNSTNKYQMSIHLREDSSQTHVLMMKGAPERILEFCSTFLLNGQEYSMNDEMKEAFQNAYLELGGLGERVLGFCFLNLPSSFSKGFPFNTDEINFPMDNLCFVGLISMIDPPRAAVPDAVSKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGTETAEEVAARLKIPISKVDASAAKAIVVHGAELKDIQSKQLDQILQNHPEIVFARTSPQQKLIIVEGCQRLGAVVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIMYTLTSNIPEITPFLMFIILGIPLPLGTITILCIDLGTDMVPAISLAYESAESDIMKRLPRNPKTDNLVNHRLIGMAYGQIGMIQALAGFFTYFVILAENGFRPVDLLGIRLHWEDKYLNDLEDSYGQQWTYEQRKVVEFTCQTAFFVTIVVVQWADLIISKTRRNSLFQQGMRNKVLIFGILEETLLAAFLSYTPGMDVALRMYPLKITWWLCAIPYSILIFVYDEIRKLLIRQHPDGWVERETYY
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
16PhosphorylationTVAPHDQSPRRRPKK
CCCCCCCCCCCCCCC		26.8230622161
45AcetylationRNMEELKKEVVMDDH
CCHHHHHHHHHHCCC		69.2519608861
55PhosphorylationVMDDHKLTLEELSTK
HHCCCCCCHHHHHHH		36.6121082442
72PhosphorylationVDLTKGHSHQRAKEI
CCCCCCCCHHHHHHH		29.9526329039
102UbiquitinationPEWVKFCKQLFGGFS
HHHHHHHHHHHCHHH		53.8422817900
105UbiquitinationVKFCKQLFGGFSLLL
HHHHHHHHCHHHHHH		9.2423000965
111UbiquitinationLFGGFSLLLWTGAIL
HHCHHHHHHHHHHHH		3.4821890473
161UbiquitinationFSYYQEAKSSKIMES
CHHHHHHHHHHHHHH		55.2822817900
162PhosphorylationSYYQEAKSSKIMESF
HHHHHHHHHHHHHHH		43.8628152594
163PhosphorylationYYQEAKSSKIMESFK
HHHHHHHHHHHHHHH		26.0428152594
164 (in isoform 1)Ubiquitination-53.8421890473
164UbiquitinationYQEAKSSKIMESFKN
HHHHHHHHHHHHHHH		53.8423000965
168PhosphorylationKSSKIMESFKNMVPQ
HHHHHHHHHHHCCCC		24.9228152594
170 (in isoform 1)Ubiquitination-54.1121890473
170UbiquitinationSKIMESFKNMVPQQA
HHHHHHHHHCCCCEE		54.1121890473
170UbiquitinationSKIMESFKNMVPQQA
HHHHHHHHHCCCCEE		54.1123000965
172SulfoxidationIMESFKNMVPQQALV
HHHHHHHCCCCEEEE		4.8528183972
225PhosphorylationGCKVDNSSLTGESEP
CCEECCCCCCCCCCC		35.8828985074
235MethylationGESEPQSRSPDFTHE
CCCCCCCCCCCCCCC		47.14-
236PhosphorylationESEPQSRSPDFTHEN
CCCCCCCCCCCCCCC		33.78-
240PhosphorylationQSRSPDFTHENPLET
CCCCCCCCCCCCCCC		35.34-
303UbiquitinationIEHFIHLITVVAVFL
HHHHHHHHHHHHHHH		1.3722817900
308UbiquitinationHLITVVAVFLGVTFF
HHHHHHHHHHHHHHH		2.4821890473
326UbiquitinationLLLGYGWLEAIIFLI
HHHCCHHHHHHHHHH		2.5027667366
362UbiquitinationTAKRMARKNCLVKNL
HHHHHHHCCCEECCH		42.3422817900
367 (in isoform 1)Ubiquitination-42.7521890473
367UbiquitinationARKNCLVKNLEAVET
HHCCCEECCHHHHHH		42.7521890473
367UbiquitinationARKNCLVKNLEAVET
HHCCCEECCHHHHHH		42.7522817900
377PhosphorylationEAVETLGSTSTICSD
HHHHHHCCCCCCCCC		23.4628857561
378PhosphorylationAVETLGSTSTICSDK
HHHHHCCCCCCCCCC		28.2628857561
379PhosphorylationVETLGSTSTICSDKT
HHHHCCCCCCCCCCC		19.9228857561
380PhosphorylationETLGSTSTICSDKTG
HHHCCCCCCCCCCCC		26.5428857561
383PhosphorylationGSTSTICSDKTGTLT
CCCCCCCCCCCCCCC		37.9928857561
385 (in isoform 1)Ubiquitination-32.3421890473
385UbiquitinationTSTICSDKTGTLTQN
CCCCCCCCCCCCCCC		32.3427667366
386PhosphorylationSTICSDKTGTLTQNR
CCCCCCCCCCCCCCC		40.1528857561
388PhosphorylationICSDKTGTLTQNRMT
CCCCCCCCCCCCCEE		31.6828857561
390PhosphorylationSDKTGTLTQNRMTVA
CCCCCCCCCCCEEEE		24.5228857561
418PhosphorylationTEEQTGKTFTKSSDT
CHHHCCCEEECCHHH		37.57-
471PhosphorylationLLKFIEQSYSSVAEM
HHHHHHHHHHHHHHH		17.7523312004
472PhosphorylationLKFIEQSYSSVAEMR
HHHHHHHHHHHHHHH		12.5023312004
473PhosphorylationKFIEQSYSSVAEMRE
HHHHHHHHHHHHHHH		24.4723312004
474PhosphorylationFIEQSYSSVAEMREK
HHHHHHHHHHHHHHH		19.6723312004
559UbiquitinationLGGLGERVLGFCFLN
HCCCHHHHHEEEEEC		5.5122817900
570PhosphorylationCFLNLPSSFSKGFPF
EEECCCCCCCCCCCC		31.4424719451
572UbiquitinationLNLPSSFSKGFPFNT
ECCCCCCCCCCCCCC		33.5423000965
576UbiquitinationSSFSKGFPFNTDEIN
CCCCCCCCCCCCCCC		30.1923000965
614PhosphorylationDAVSKCRSAGIKVIM
HHHHHHHHCCCEEEE		40.0720068231
618 (in isoform 1)Ubiquitination-25.4521890473
618UbiquitinationKCRSAGIKVIMVTGD
HHHHCCCEEEEECCC		25.4522817900
623PhosphorylationGIKVIMVTGDHPITA
CCEEEEECCCCCCCH		21.3620068231
629PhosphorylationVTGDHPITAKAIAKG
ECCCCCCCHHHHHHC		26.9320068231
631UbiquitinationGDHPITAKAIAKGVG
CCCCCCHHHHHHCCE		31.5123000965
631UbiquitinationGDHPITAKAIAKGVG
CCCCCCHHHHHHCCE		31.5121890473
631 (in isoform 1)Ubiquitination-31.5121890473
635UbiquitinationITAKAIAKGVGIISE
CCHHHHHHCCEEEEC		48.2723000965
635UbiquitinationITAKAIAKGVGIISE
CCHHHHHHCCEEEEC		48.2721890473
635 (in isoform 1)Ubiquitination-48.2721890473
645UbiquitinationGIISEGTETAEEVAA
EEEECCCCCHHHHHH		57.8023000965
659PhosphorylationARLKIPISKVDASAA
HHCCCCHHHCCHHHC		22.6724702127
664PhosphorylationPISKVDASAAKAIVV
CHHHCCHHHCEEEEE		25.0524702127
704 (in isoform 1)Ubiquitination-36.0821890473
704UbiquitinationARTSPQQKLIIVEGC
EECCCCCEEEEEECC		36.0821890473
704UbiquitinationARTSPQQKLIIVEGC
EECCCCCEEEEEECC		36.0823000965
711S-palmitoylationKLIIVEGCQRLGAVV
EEEEEECCCCCCCEE		1.0329575903
720UbiquitinationRLGAVVAVTGDGVND
CCCCEEEEECCCCCC		4.0921890473
728PhosphorylationTGDGVNDSPALKKAD
ECCCCCCCHHHHHCC		13.5820068231
732UbiquitinationVNDSPALKKADIGIA
CCCCHHHHHCCEEEE		48.2832142685
779 (in isoform 1)Ubiquitination-51.2121890473
779UbiquitinationRLIFDNLKKSIMYTL
EEEEHHHHHHHHHHH		51.2121890473
945PhosphorylationADLIISKTRRNSLFQ
HHHHHHHHHHCHHHH		28.2420068231
949PhosphorylationISKTRRNSLFQQGMR
HHHHHHCHHHHHHCC		28.8420068231
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
949SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT1A4_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 AT1A4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AT1A4_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
D00112 G-Strophanthin (JAN); Ouabain; Ouabain octahydrate
D00297 Digitoxin (JP16/USP/INN); Crystodigin (TN)
D00298 Digoxin (JP16/USP); Lanoxicaps (TN); Lanoxin (TN)
D01240 Deslanoside (JP16/USP/INN); Cedilanid-d (TN)
D01379 Proscillaridin (JAN/USAN/INN); Talusin (TN)
D01972 Lanatoside C (JP16/INN); Digilanogen C (TN)
D02587 Metildigoxin (JP16); Lanirapid (TN)
D06881 Acetyldigitoxin (INN); Acylanid (TN)
D07147 Gitoformate (INN)
D07555 Acetyldigoxin; Cedigossima (TN)
D07556 beta-Acetyldigoxin; Acetyldigoxin beta isomer; Corotal (TN)
D09847 Metildigoxin (INN); Medigoxin (BAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AT1A4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-45, AND MASS SPECTROMETRY.

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