KAD2_HUMAN - dbPTM
KAD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAD2_HUMAN
UniProt AC P54819
Protein Name Adenylate kinase 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03168}
Gene Name AK2 {ECO:0000255|HAMAP-Rule:MF_03168}
Organism Homo sapiens (Human).
Sequence Length 239
Subcellular Localization Mitochondrion intermembrane space .
Protein Description Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis..
Protein Sequence MAPSVPAAEPEYPKGIRAVLLGPPGAGKGTQAPRLAENFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPLCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIPDSLLIRRITGRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNEKALKIRLQAYHTQTTPLIEYYRKRGIHSAIDASQTPDVVFASILAAFSKATCKDLVMFI
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-------MAPSVPAA
-------CCCCCCCC		12.8119413330
4Phosphorylation----MAPSVPAAEPE
----CCCCCCCCCCC		31.0626657352
4O-linked_Glycosylation----MAPSVPAAEPE
----CCCCCCCCCCC		31.0630379171
12PhosphorylationVPAAEPEYPKGIRAV
CCCCCCCCCCCEEEE		22.4428152594
14AcetylationAAEPEYPKGIRAVLL
CCCCCCCCCEEEEEE		67.1019608861
14UbiquitinationAAEPEYPKGIRAVLL
CCCCCCCCCEEEEEE		67.1019608861
14MalonylationAAEPEYPKGIRAVLL
CCCCCCCCCEEEEEE		67.1026320211
28 (in isoform 1)Ubiquitination-59.2421890473
282-HydroxyisobutyrylationLGPPGAGKGTQAPRL
ECCCCCCCCCCCCHH		59.24-
28MalonylationLGPPGAGKGTQAPRL
ECCCCCCCCCCCCHH		59.2426320211
28 (in isoform 2)Ubiquitination-59.2421890473
28 (in isoform 3)Ubiquitination-59.2421890473
28AcetylationLGPPGAGKGTQAPRL
ECCCCCCCCCCCCHH		59.2425953088
28UbiquitinationLGPPGAGKGTQAPRL
ECCCCCCCCCCCCHH		59.24-
28 (in isoform 5)Ubiquitination-59.2421890473
30PhosphorylationPPGAGKGTQAPRLAE
CCCCCCCCCCCHHHH		25.6626437602
40S-nitrosylationPRLAENFCVCHLATG
CHHHHCCEEEEECCH		4.8724105792
42S-nitrosylationLAENFCVCHLATGDM
HHHCCEEEEECCHHH		1.9824105792
42GlutathionylationLAENFCVCHLATGDM
HHHCCEEEEECCHHH		1.9822555962
46 (in isoform 4)Ubiquitination-39.8221890473
46 (in isoform 6)Ubiquitination-39.8221890473
46PhosphorylationFCVCHLATGDMLRAM
CEEEEECCHHHHHHH		39.8268709411
53SulfoxidationTGDMLRAMVASGSEL
CHHHHHHHHHCCCHH		1.7721406390
56PhosphorylationMLRAMVASGSELGKK
HHHHHHHCCCHHHHH		31.2920068231
58PhosphorylationRAMVASGSELGKKLK
HHHHHCCCHHHHHHH		27.4420068231
62MalonylationASGSELGKKLKATMD
HCCCHHHHHHHHHHH		68.5026320211
62UbiquitinationASGSELGKKLKATMD
HCCCHHHHHHHHHHH		68.50-
622-HydroxyisobutyrylationASGSELGKKLKATMD
HCCCHHHHHHHHHHH		68.50-
62SuccinylationASGSELGKKLKATMD
HCCCHHHHHHHHHHH		68.50-
62AcetylationASGSELGKKLKATMD
HCCCHHHHHHHHHHH		68.5025953088
62SuccinylationASGSELGKKLKATMD
HCCCHHHHHHHHHHH		68.50-
652-HydroxyisobutyrylationSELGKKLKATMDAGK
CHHHHHHHHHHHHCC		51.17-
67PhosphorylationLGKKLKATMDAGKLV
HHHHHHHHHHHCCCC		17.6226437602
70 (in isoform 6)Ubiquitination-13.2421890473
70 (in isoform 4)Ubiquitination-13.2421890473
72AcetylationKATMDAGKLVSDEMV
HHHHHHCCCCCHHHH		47.657977205
75PhosphorylationMDAGKLVSDEMVVEL
HHHCCCCCHHHHHHH		37.9973244727
78SulfoxidationGKLVSDEMVVELIEK
CCCCCHHHHHHHHHH		4.9921406390
85UbiquitinationMVVELIEKNLETPLC
HHHHHHHHCCCCCCC		60.89-
89PhosphorylationLIEKNLETPLCKNGF
HHHHCCCCCCCCCCE		25.40110746747
92S-nitrosylationKNLETPLCKNGFLLD
HCCCCCCCCCCEECC		3.2019483679
92GlutathionylationKNLETPLCKNGFLLD
HCCCCCCCCCCEECC		3.2022555962
92S-nitrosocysteineKNLETPLCKNGFLLD
HCCCCCCCCCCEECC		3.20-
93 (in isoform 2)Ubiquitination-68.7221890473
93 (in isoform 1)Ubiquitination-68.7221890473
93SuccinylationNLETPLCKNGFLLDG
CCCCCCCCCCEECCC		68.7221890473
93UbiquitinationNLETPLCKNGFLLDG
CCCCCCCCCCEECCC		68.7221890473
93SuccinylationNLETPLCKNGFLLDG
CCCCCCCCCCEECCC		68.72-
93 (in isoform 3)Ubiquitination-68.7221890473
93AcetylationNLETPLCKNGFLLDG
CCCCCCCCCCEECCC		68.7223954790
93 (in isoform 5)Ubiquitination-68.7221890473
1172-HydroxyisobutyrylationMLDDLMEKRKEKLDS
HHHHHHHHHHHHHHH		55.60-
117 (in isoform 2)Ubiquitination-55.6021890473
117 (in isoform 3)Ubiquitination-55.6021890473
117UbiquitinationMLDDLMEKRKEKLDS
HHHHHHHHHHHHHHH		55.602190698
117 (in isoform 1)Ubiquitination-55.6021890473
117AcetylationMLDDLMEKRKEKLDS
HHHHHHHHHHHHHHH		55.6027452117
117 (in isoform 5)Ubiquitination-55.6021890473
133PhosphorylationIEFSIPDSLLIRRIT
EEECCCHHHHHHHHH		21.5222673903
147UbiquitinationTGRLIHPKSGRSYHE
HCCEECCCCCCCCCH		51.91-
148PhosphorylationGRLIHPKSGRSYHEE
CCEECCCCCCCCCHH		43.8425159151
151PhosphorylationIHPKSGRSYHEEFNP
ECCCCCCCCCHHCCC		34.0725159151
152PhosphorylationHPKSGRSYHEEFNPP
CCCCCCCCCHHCCCC		16.3428270605
163SulfoxidationFNPPKEPMKDDITGE
CCCCCCCCCCCCCCC		8.5730846556
176PhosphorylationGEPLIRRSDDNEKAL
CCCCEECCCCCCHHH		39.1972243551
181UbiquitinationRRSDDNEKALKIRLQ
ECCCCCCHHHHHHHH		66.33-
181AcetylationRRSDDNEKALKIRLQ
ECCCCCCHHHHHHHH		66.3323954790
190PhosphorylationLKIRLQAYHTQTTPL
HHHHHHHHHCCCCHH		7.7620090780
192PhosphorylationIRLQAYHTQTTPLIE
HHHHHHHCCCCHHHH		18.2228152594
194PhosphorylationLQAYHTQTTPLIEYY
HHHHHCCCCHHHHHH		31.3828152594
195PhosphorylationQAYHTQTTPLIEYYR
HHHHCCCCHHHHHHH		13.2825159151
200PhosphorylationQTTPLIEYYRKRGIH
CCCHHHHHHHHCCCC		11.1120090780
201PhosphorylationTTPLIEYYRKRGIHS
CCHHHHHHHHCCCCC		9.2528152594
208PhosphorylationYRKRGIHSAIDASQT
HHHCCCCCCCCCHHC		25.6228450419
213PhosphorylationIHSAIDASQTPDVVF
CCCCCCCHHCCHHHH		30.7328450419
215PhosphorylationSAIDASQTPDVVFAS
CCCCCHHCCHHHHHH		20.9728450419
222PhosphorylationTPDVVFASILAAFSK
CCHHHHHHHHHHHCC		13.4828450419
228PhosphorylationASILAAFSKATCKDL
HHHHHHHCCCCCHHH		19.3620068231
232S-nitrosylationAAFSKATCKDLVMFI
HHHCCCCCHHHHHCC		3.7424105792
233UbiquitinationAFSKATCKDLVMFI-
HHCCCCCHHHHHCC-		50.14-
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 KAD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAD2_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 KAD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAFB1_HUMANSAFBphysical
22939629
RM12_HUMANMRPL12physical
22939629
RAVR1_HUMANRAVER1physical
22939629
TELO2_HUMANTELO2physical
22939629
THIM_HUMANACAA2physical
26344197
AFG32_HUMANAFG3L2physical
26344197
DUT_HUMANDUTphysical
26344197
FSCN1_HUMANFSCN1physical
26344197
RACK1_HUMANGNB2L1physical
26344197
RT07_HUMANMRPS7physical
26344197
NDKB_HUMANNME2physical
26344197
SGMR1_HUMANSIGMAR1physical
26344197
TKT_HUMANTKTphysical
26344197
TRAP1_HUMANTRAP1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
267500Reticular dysgenesis (RDYS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAD2_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-14, AND MASS SPECTROMETRY.

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