KAD9_HUMAN - dbPTM
KAD9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAD9_HUMAN
UniProt AC Q5TCS8
Protein Name Adenylate kinase 9
Gene Name AK9
Organism Homo sapiens (Human).
Sequence Length 1911
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has both nucleoside monophosphate and diphosphate kinase activities. Catalyzes the phosphorylation of AMP, dAMP, CMP and dCMP with ATP as phosphate donor and of CMP with GTP as phosphate donor. Also catalyzes the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor. Shows substrate preference of CDP > UDP > ADP > GDP > TDP..
Protein Sequence MTSQEKTEEYPFADIFDEDETERNFLLSKPVCFVVFGKPGVGKTTLARYITQAWKCIRVEALPILEEQIAAETESGVMLQSMLISGQSIPDELVIKLMLEKLNSPEVCHFGYIITEIPSLSQDAMTTLQQIELIKNLNLKPDVIINIKCPDYDLCQRISGQRQHNNTGYIYSRDQWDPEVIENHRKKKKEAQKDGKGEEEEEEEEQEEEEAFIAEMQMVAEILHHLVQRPEDYLENVENIVKLYKETILQTLEEVMAEHNPQYLIELNGNKPAEELFMIVMDRLKYLNLKRAAILTKLQGAEEEINDTMENDELFRTLASYKLIAPRYRWQRSKWGRTCPVNLKDGNIYSGLPDYSVSFLGKIYCLSSEEALKPFLLNPRPYLLPPMPGPPCKVFILGPQYSGKTTLCNMLAENYKGKVVDYAQLVQPRFDKARETLVENTIAEATAAAIKVVKEKLLRELQARKQAETALREFQRQYEKMEFGVFPMEATHSSIDEEGYIQGSQRDRGSSLVDTEEAKTKSENVLHDQAAKVDKDDGKETGETFTFKRHSQDASQDVKLYSDTAPTEDLIEEVTADHPEVVTMIEETIKMSQDINFEQPYEKHAEILQEVLGEVMEENKDRFPGAPKYGGWIVDNCPIVKELWMALIKKGIIPDLVIYLSDTENNGKCLFNRIYLQKKSEIDSKILERLLEELQKKKKEEEEARKATEEELRLEEENRRLLELMKVKAKEAEETDNEDEEEIEGDELEVHEEPEASHDTRGSWLPEEFEASEVPETEPEAVSEPIEETTVETEIPKGSKEGLEIEKLSETVVLPEFPEDSYPDVPEMEPFKEKIGSFIILWKQLEATISEAYIKILNLEIADRTPQELLQKVVETMEKPFQYTAWELTGEDYEEETEDYQTEAEVDEELEEEEEEEGEDKMKERKRHLGDTKHFCPVVLKENFILQPGNTEEAAKYREKIYYFSSAEAKEKFLEHPEDYVAHEEPLKAPPLRICLVGPQGSGKTMCGRQLAEKLNIFHIQFEEVLQEKLLLKTEKKVGPEFEEDSENEQAAKQELEELAIQANVKVEEENTKKQLPEVQLTEEEEVIKSSLMENEPLPPEILEVILSEWWLKEPIRSTGFILDGFPRYPEEAQFLGDRGFFPDAAVFIQVDDQDIFDRLLPAQIEKWKLKQKKKLERKKLIKDMKAKIRVDTIAKRRAELILERDKKRRENVVRDDEEISEEELEEDNDDIENILEDEFPKDEEEMSGEEDEEQETDAIERLRGELGEKFEADTHNLQIIQDELERYLIPIISINGARRNHIVQYTLNMKLKPLVENRASIFEKCHPIPAPLAQKMLTFTYKYISSFGYWDPVKLSEGETIKPVENAENPIYPVIHRQYIYFLSSKETKEKFMKNPIKYIRQPKPKPTVPIRIIIVGPPKSGKTTVAKKITSEYGLKHLSIGGALRYVLNNHPETELALMLNWHLHKGMTAPDELAIQALELSLMESVCNTAGVVIDGYPVTKHQMNLLEARSIIPMVIFELSVPSKEIFKRLLLEKENEQRLPYPLHNSAQIVAVNNVKYRKNIGEIRQYYQEQHQNWYVIDGFHSKWWVWNEVIKNVQMVNKYMQTYLERIKAGKAACIDKLCITPQELLSRLGEFEQFCPVSLAESQELFDCSATDSLEFAAEFRGHYYKMSSQEKLNKFLENPELYVPPLAPHPLPSADMIPKRLTLSELKSRFPKCAELQGYCPVTYKDGNQRYEALVPGSINYALEYHNRIYICENKEKLQKFLRSPLKYWEQKLPHKLPPLREPILLTSLPLPGYLEQGIATSLIKAMNAAGCLKPKFPFLSIRRSALLYIALHLKAFNPKGSEYTRKKYKKKMEQFMESCELITYLGAKMTRKYKEPQFRAIDFDHKLKTFLSLRNIDPING
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
55UbiquitinationRYITQAWKCIRVEAL
HHHHHHHHHHEEEHH
-
82UbiquitinationSGVMLQSMLISGQSI
CCCEEEHHHHCCCCC
21963094
148UbiquitinationPDVIINIKCPDYDLC
CCEEEEEECCCCCHH
-
169PhosphorylationRQHNNTGYIYSRDQW
CCCCCCCCEEECCCC
18083107
172PhosphorylationNNTGYIYSRDQWDPE
CCCCCEEECCCCCHH
24719451
297UbiquitinationKRAAILTKLQGAEEE
HHHHHHHHHHCCHHH
21963094
322UbiquitinationFRTLASYKLIAPRYR
HHHHHHHCCCCCCHH
-
344UbiquitinationRTCPVNLKDGNIYSG
CCCCCCCCCCCCCCC
-
369UbiquitinationKIYCLSSEEALKPFL
EEEECCCHHHHHHHH
21963094
401PhosphorylationVFILGPQYSGKTTLC
EEEECCCCCCHHHHH
46161605
415PhosphorylationCNMLAENYKGKVVDY
HHHHHHHCCCCCCCH
25884760
436PhosphorylationRFDKARETLVENTIA
CCHHHHHHHHHHHHH
68733983
510PhosphorylationGSQRDRGSSLVDTEE
CCCCCCCCCCCCHHH
30622161
511PhosphorylationSQRDRGSSLVDTEEA
CCCCCCCCCCCHHHH
30622161
541O-linked_GlycosylationDKDDGKETGETFTFK
CCCCCCCCCCEEEEE
30379171
551PhosphorylationTFTFKRHSQDASQDV
EEEEEECCCCCCCCC
30622161
724 (in isoform 1)Phosphorylation--
799PhosphorylationETEIPKGSKEGLEIE
EEECCCCCCCCCEEE
46161585
865PhosphorylationNLEIADRTPQELLQK
CHHHCCCCHHHHHHH
50564439
957PhosphorylationNTEEAAKYREKIYYF
CHHHHHHHHHHHEEE
18357099
1046PhosphorylationGPEFEEDSENEQAAK
CCCCCCCCCCHHHHH
30622161
1193PhosphorylationKAKIRVDTIAKRRAE
HHHHHHHHHHHHHHH
23403867
1306PhosphorylationRRNHIVQYTLNMKLK
CCCCHHEEECCCCCH
46161597
1307PhosphorylationRNHIVQYTLNMKLKP
CCCHHEEECCCCCHH
46161589
1425PhosphorylationGPPKSGKTTVAKKIT
CCCCCCCCCHHHHHH
27251275
1426PhosphorylationPPKSGKTTVAKKITS
CCCCCCCCHHHHHHC
27251275
1441PhosphorylationEYGLKHLSIGGALRY
HHCCCCCCHHHHHHH
30631047
1514PhosphorylationMNLLEARSIIPMVIF
HHHHHHHCCCCEEEE
29083192
1524PhosphorylationPMVIFELSVPSKEIF
CEEEEECCCCCHHHH
29083192
1527PhosphorylationIFELSVPSKEIFKRL
EEECCCCCHHHHHHH
29083192
1561AcetylationIVAVNNVKYRKNIGE
EEEEECEEECCCHHH
25038526
1606PhosphorylationNVQMVNKYMQTYLER
HHHHHHHHHHHHHHH
25003641
1609PhosphorylationMVNKYMQTYLERIKA
HHHHHHHHHHHHHHC
25003641
1610PhosphorylationVNKYMQTYLERIKAG
HHHHHHHHHHHHHCC
25003641
1634PhosphorylationITPQELLSRLGEFEQ
CCHHHHHHHHCCHHH
24719451
1711PhosphorylationDMIPKRLTLSELKSR
CCCCCCCCHHHHHHH
21964256
1711O-linked_GlycosylationDMIPKRLTLSELKSR
CCCCCCCCHHHHHHH
30379171
1740PhosphorylationYKDGNQRYEALVPGS
EECCCEEEEEECCCC
25907765
1747PhosphorylationYEALVPGSINYALEY
EEEECCCCHHHHHHH
25907765
1750PhosphorylationLVPGSINYALEYHNR
ECCCCHHHHHHHCCE
25907765
1754PhosphorylationSINYALEYHNRIYIC
CHHHHHHHCCEEEEE
25907765
1811PhosphorylationLEQGIATSLIKAMNA
HHHHHHHHHHHHHHH
24719451
1838PhosphorylationIRRSALLYIALHLKA
HHHHHHHHHHHHHHH
46161601
1858PhosphorylationSEYTRKKYKKKMEQF
CHHHHHHHHHHHHHH
26074081
1868PhosphorylationKMEQFMESCELITYL
HHHHHHHHHHHHHHH
26074081
1873PhosphorylationMESCELITYLGAKMT
HHHHHHHHHHHHHHH
26074081
1874PhosphorylationESCELITYLGAKMTR
HHHHHHHHHHHHHHH
26074081
1880PhosphorylationTYLGAKMTRKYKEPQ
HHHHHHHHHCCCCCC
26074081

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 KAD9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAD9_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 KAD9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ENPL_HUMANHSP90B1physical
26344197
RHOA_HUMANRHOAphysical
28514442
LRC23_HUMANLRRC23physical
28514442
EXOG_HUMANEXOGphysical
28514442
CE034_HUMANC5orf34physical
28514442
HDAC3_HUMANHDAC3physical
28514442
TAF2_HUMANTAF2physical
28514442
MYO9A_HUMANMYO9Aphysical
28514442
PRI1_HUMANPRIM1physical
28514442

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 KAD9_HUMAN

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Related Literatures of Post-Translational Modification

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