KCRU_HUMAN - dbPTM
KCRU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCRU_HUMAN
UniProt AC P12532
Protein Name Creatine kinase U-type, mitochondrial
Gene Name CKMT1A
Organism Homo sapiens (Human).
Sequence Length 417
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Intermembrane side.
Protein Description Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa..
Protein Sequence MAGPFSRLLSARPGLRLLALAGAGSLAAGFLLRPEPVRAASERRRLYPPSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFADLFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDTAATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDIRIPTPVIHTKH
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
10PhosphorylationGPFSRLLSARPGLRL
CHHHHHHHCCCHHHH		27.1624719451
40UbiquitinationRPEPVRAASERRRLY
CCHHCCCHHHHHCCC		11.0230230243
47PhosphorylationASERRRLYPPSAEYP
HHHHHCCCCCCCCCC		15.9930266825
50PhosphorylationRRRLYPPSAEYPDLR
HHCCCCCCCCCCCHH		29.2730266825
53PhosphorylationLYPPSAEYPDLRKHN
CCCCCCCCCCHHHCC		11.1930266825
62S-nitrosylationDLRKHNNCMASHLTP
CHHHCCCCCHHHCCH		2.6724105792
70UbiquitinationMASHLTPAVYARLCD
CHHHCCHHHHHHHCC		11.1723503661
72 (in isoform 2)Phosphorylation-6.5226552605
75 (in isoform 2)Phosphorylation-3.1826552605
77 (in isoform 2)Phosphorylation-56.8026552605
78AcetylationVYARLCDKTTPTGWT
HHHHHCCCCCCCCCC		53.9926051181
81 (in isoform 2)Phosphorylation-33.8626552605
82PhosphorylationLCDKTTPTGWTLDQC
HCCCCCCCCCCHHHH		43.1723909892
84 (in isoform 2)Phosphorylation-9.0326552605
85PhosphorylationKTTPTGWTLDQCIQT
CCCCCCCCHHHHHHH		23.0823909892
89GlutathionylationTGWTLDQCIQTGVDN
CCCCHHHHHHHCCCC		2.1922555962
92PhosphorylationTLDQCIQTGVDNPGH
CHHHHHHHCCCCCCC		21.1823909892
107UbiquitinationPFIKTVGMVAGDEET
CCEEEEEEECCCHHH		1.3024816145
116UbiquitinationAGDEETYEVFADLFD
CCCHHHHHHHHHHHH		38.2824816145
141PhosphorylationDPRTMKHTTDLDASK
CCCCCCCCCCCCHHH		19.2520833797
147PhosphorylationHTTDLDASKIRSGYF
CCCCCCHHHCCCCCC		28.4326437602
148UbiquitinationTTDLDASKIRSGYFD
CCCCCHHHCCCCCCC		43.8124816145
151PhosphorylationLDASKIRSGYFDERY
CCHHHCCCCCCCCEE		41.1228152594
153PhosphorylationASKIRSGYFDERYVL
HHHCCCCCCCCEEEE		14.7621082442
157MethylationRSGYFDERYVLSSRV
CCCCCCCEEEEECCC		28.80-
158PhosphorylationSGYFDERYVLSSRVR
CCCCCCEEEEECCCC		12.0520068231
161PhosphorylationFDERYVLSSRVRTGR
CCCEEEEECCCCCCC		13.1720068231
162PhosphorylationDERYVLSSRVRTGRS
CCEEEEECCCCCCCC		30.5420068231
166PhosphorylationVLSSRVRTGRSIRGL
EEECCCCCCCCCCCC		33.8121406692
169PhosphorylationSRVRTGRSIRGLSLP
CCCCCCCCCCCCCCC		20.2720068231
174PhosphorylationGRSIRGLSLPPACTR
CCCCCCCCCCCCCCH		41.4720068231
179UbiquitinationGLSLPPACTRAERRE
CCCCCCCCCHHHHHH		3.0524816145
180PhosphorylationLSLPPACTRAERREV
CCCCCCCCHHHHHHH		34.7120068231
188UbiquitinationRAERREVERVVVDAL
HHHHHHHHHHHHHHH		34.7023503661
196PhosphorylationRVVVDALSGLKGDLA
HHHHHHHHCCCHHHH		43.7424076635
199UbiquitinationVDALSGLKGDLAGRY
HHHHHCCCHHHHHHE		54.6330230243
199AcetylationVDALSGLKGDLAGRY
HHHHHCCCHHHHHHE		54.6326051181
213PhosphorylationYYRLSEMTEAEQQQL
EEEHHHCCHHHHHHH		28.17-
229UbiquitinationDDHFLFDKPVSPLLT
CCCCCCCCCCHHHHH		39.7323503661
230UbiquitinationDHFLFDKPVSPLLTA
CCCCCCCCCHHHHHH		33.3930230243
232PhosphorylationFLFDKPVSPLLTAAG
CCCCCCCHHHHHHHH		20.5428348404
234UbiquitinationFDKPVSPLLTAAGMA
CCCCCHHHHHHHHHC		5.3124816145
236PhosphorylationKPVSPLLTAAGMARD
CCCHHHHHHHHHCCC		23.3428102081
251PhosphorylationWPDARGIWHNNEKSF
CCCCCCCEECCCCCE		7.3232142685
260UbiquitinationNNEKSFLIWVNEEDH
CCCCCEEEEECCCCC		3.4823503661
275AcetylationTRVISMEKGGNMKRV
EEEEEEECCCHHHHH		64.5726051181
275UbiquitinationTRVISMEKGGNMKRV
EEEEEEECCCHHHHH		64.5724816145
291SuccinylationERFCRGLKEVERLIQ
HHHHHHHHHHHHHHH		63.6423954790
306UbiquitinationERGWEFMWNERLGYI
HHCCHHHHCCCCEEE		14.6224816145
312PhosphorylationMWNERLGYILTCPSN
HHCCCCEEEEECCCC		9.4328152594
315PhosphorylationERLGYILTCPSNLGT
CCCEEEEECCCCCCC		16.8927251275
316GlutathionylationRLGYILTCPSNLGTG
CCEEEEECCCCCCCC		2.8922555962
318PhosphorylationGYILTCPSNLGTGLR
EEEEECCCCCCCCCC		47.0027499020
322PhosphorylationTCPSNLGTGLRAGVH
ECCCCCCCCCCCCEE		35.8927251275
331AcetylationLRAGVHIKLPLLSKD
CCCCEEEECCCCCCC		29.2226051181
336PhosphorylationHIKLPLLSKDSRFPK
EEECCCCCCCCCCHH		41.9421712546
337SuccinylationIKLPLLSKDSRFPKI
EECCCCCCCCCCHHH		60.7423954790
337AcetylationIKLPLLSKDSRFPKI
EECCCCCCCCCCHHH		60.7426051181
339PhosphorylationLPLLSKDSRFPKILE
CCCCCCCCCCHHHHH		39.2921712546
343AcetylationSKDSRFPKILENLRL
CCCCCCHHHHHHHCC		58.1526051181
349MethylationPKILENLRLQKRGTG
HHHHHHHCCHHCCCC		46.80-
355PhosphorylationLRLQKRGTGGVDTAA
HCCHHCCCCCCCCCC		34.4923312004
360PhosphorylationRGTGGVDTAATGGVF
CCCCCCCCCCCCCEE		18.7824076635
363PhosphorylationGGVDTAATGGVFDIS
CCCCCCCCCCEEECC		31.8224076635
396GlutathionylationGVNYLIDCERRLERG
CCHHHHCHHHHHHCC		3.3022555962
407MethylationLERGQDIRIPTPVIH
HHCCCCCCCCCCCCC		36.80-
410PhosphorylationGQDIRIPTPVIHTKH
CCCCCCCCCCCCCCC		28.0230266825
415PhosphorylationIPTPVIHTKH-----
CCCCCCCCCC-----		21.4923312004
441Phosphorylation-------------------------------
-------------------------------		32142685
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
153YPhosphorylationKinaseABLP00519
PSP
-KUbiquitinationE3 ubiquitin ligaseASB9Q96DX5
PMID:20302626
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCRU_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 KCRU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASB9_HUMANASB9physical
20302626
HYEP_HUMANEPHX1physical
26344197
GPD1L_HUMANGPD1Lphysical
26344197
CH10_HUMANHSPE1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
DB00148Creatine
Regulatory Network of KCRU_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-153, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-153, AND MASSSPECTROMETRY.

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