KAD1_HUMAN - dbPTM
KAD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAD1_HUMAN
UniProt AC P00568
Protein Name Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171}
Gene Name AK1 {ECO:0000255|HAMAP-Rule:MF_03171}
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism..
Protein Sequence MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDSVFSQVCTHLDALK
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
1Acetylation-------MEEKLKKT
-------CHHHHCCC		15.75183954
19PhosphorylationFVVGGPGSGKGTQCE
EEECCCCCCCHHHHH		40.2363724133
21AcetylationVGGPGSGKGTQCEKI
ECCCCCCCHHHHHHH		61.5626051181
21MalonylationVGGPGSGKGTQCEKI
ECCCCCCCHHHHHHH		61.5626320211
25S-nitrosylationGSGKGTQCEKIVQKY
CCCCHHHHHHHHHHH		6.0524105792
27AcetylationGKGTQCEKIVQKYGY
CCHHHHHHHHHHHCC		56.6626051181
27UbiquitinationGKGTQCEKIVQKYGY
CCHHHHHHHHHHHCC		56.66-
31AcetylationQCEKIVQKYGYTHLS
HHHHHHHHHCCCCCC		29.7425038526
31UbiquitinationQCEKIVQKYGYTHLS
HHHHHHHHHCCCCCC		29.742189047
32PhosphorylationCEKIVQKYGYTHLST
HHHHHHHHCCCCCCH		9.7726437602
34PhosphorylationKIVQKYGYTHLSTGD
HHHHHHCCCCCCHHH		6.4623186163
35PhosphorylationIVQKYGYTHLSTGDL
HHHHHCCCCCCHHHH		16.3926657352
38PhosphorylationKYGYTHLSTGDLLRS
HHCCCCCCHHHHHHH		23.8025693802
39PhosphorylationYGYTHLSTGDLLRSE
HCCCCCCHHHHHHHH		40.8625693802
58PhosphorylationSARGKKLSEIMEKGQ
CCCCHHHHHHHHCCC		33.6828555341
71PhosphorylationGQLVPLETVLDMLRD
CCCCCHHHHHHHHHH		33.7750564305
75SulfoxidationPLETVLDMLRDAMVA
CHHHHHHHHHHHHHH		2.6430846556
83UbiquitinationLRDAMVAKVNTSKGF
HHHHHHHHCCCCCCE		25.30-
88UbiquitinationVAKVNTSKGFLIDGY
HHHCCCCCCEEECCC		52.20-
107MethylationQQGEEFERRIGQPTL
HCHHHHHHHHCCCEE		40.62-
145PhosphorylationRVDDNEETIKKRLET
CCCCCHHHHHHHHHH		31.7337817135
152PhosphorylationTIKKRLETYYKATEP
HHHHHHHHHHHHCCC		36.4222210691
153PhosphorylationIKKRLETYYKATEPV
HHHHHHHHHHHCCCE		8.1320068231
154PhosphorylationKKRLETYYKATEPVI
HHHHHHHHHHCCCEE		11.1020068231
157PhosphorylationLETYYKATEPVIAFY
HHHHHHHCCCEEEHH		36.3522210691
164PhosphorylationTEPVIAFYEKRGIVR
CCCEEEHHHHCCCEE		16.1222210691
166UbiquitinationPVIAFYEKRGIVRKV
CEEEHHHHCCCEEEE		44.54-
166SuccinylationPVIAFYEKRGIVRKV
CEEEHHHHCCCEEEE		44.5423954790
178PhosphorylationRKVNAEGSVDSVFSQ
EEECCCCCHHHHHHH		17.7925849741
181PhosphorylationNAEGSVDSVFSQVCT
CCCCCHHHHHHHHHH		23.9419764811
184PhosphorylationGSVDSVFSQVCTHLD
CCHHHHHHHHHHHHH		21.3926657352
187S-nitrosylationDSVFSQVCTHLDALK
HHHHHHHHHHHHHCC		1.2124105792
188PhosphorylationSVFSQVCTHLDALK-
HHHHHHHHHHHHCC-		26.9827732954
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 KAD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAD1_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 KAD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KMT2C_HUMANKMT2Cphysical
17353931
A4_HUMANAPPphysical
21832049
DECR_HUMANDECR1physical
26496610
MRE11_HUMANMRE11Aphysical
26496610
S12A2_HUMANSLC12A2physical
26496610
TIA1_HUMANTIA1physical
26496610
OGT1_HUMANOGTphysical
26496610
SUCB2_HUMANSUCLG2physical
26496610
CD2B2_HUMANCD2BP2physical
26496610
COBL1_HUMANCOBLL1physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
GEMI5_HUMANGEMIN5physical
26496610
PCF11_HUMANPCF11physical
26496610
NBAS_HUMANNBASphysical
26496610
KDM3B_HUMANKDM3Bphysical
26496610
BUD13_HUMANBUD13physical
26496610
UTP4_HUMANCIRH1Aphysical
26496610
B3GLT_HUMANB3GALTLphysical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612631Hemolytic anemia due to adenylate kinase deficiency (HAAKD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAD1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Primary and tertiary structure of the principal human adenylatekinase.";
von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R.H.,Pai E.F.;
Eur. J. Biochem. 68:281-290(1976).
Cited for: PROTEIN SEQUENCE.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory