KCRM_HUMAN - dbPTM
KCRM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCRM_HUMAN
UniProt AC P06732
Protein Name Creatine kinase M-type
Gene Name CKM
Organism Homo sapiens (Human).
Sequence Length 381
Subcellular Localization Cytoplasm.
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 MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDDLDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMTEKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISMEKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLAHLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLMVEMEKKLEKGQSIDDMIPAQK
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
14PhosphorylationHNKFKLNYKPEEEYP
CCCCCCCCCCHHHCC
38.05-
14NitrationHNKFKLNYKPEEEYP
CCCCCCCCCCHHHCC
38.05-
20PhosphorylationNYKPEEEYPDLSKHN
CCCCHHHCCCHHHCC
12.8219764811
20NitrationNYKPEEEYPDLSKHN
CCCCHHHCCCHHHCC
12.82-
24PhosphorylationEEEYPDLSKHNNHMA
HHHCCCHHHCCCHHH
38.9726437602
35PhosphorylationNHMAKVLTLELYKKL
CHHHHHHHHHHHHHH
22.6019764811
39PhosphorylationKVLTLELYKKLRDKE
HHHHHHHHHHHCCCC
9.19-
40AcetylationVLTLELYKKLRDKET
HHHHHHHHHHCCCCC
58.9430585839
41AcetylationLTLELYKKLRDKETP
HHHHHHHHHCCCCCC
34.8930585845
47PhosphorylationKKLRDKETPSGFTVD
HHHCCCCCCCCCCHH
28.6122673903
52PhosphorylationKETPSGFTVDDVIQT
CCCCCCCCHHHHHHH
26.9322673903
59PhosphorylationTVDDVIQTGVDNPGH
CHHHHHHHCCCCCCC
28.2222673903
71PhosphorylationPGHPFIMTVGCVAGD
CCCCEEEEEEEECCC
14.6622673903
81PhosphorylationCVAGDEESYEVFKEL
EECCCHHHHHHHHHH
25.2522673903
82PhosphorylationVAGDEESYEVFKELF
ECCCHHHHHHHHHHH
21.2822673903
82NitrationVAGDEESYEVFKELF
ECCCHHHHHHHHHHH
21.28-
94PhosphorylationELFDPIISDRHGGYK
HHHHHHHCCCCCCCC
29.3426437602
100PhosphorylationISDRHGGYKPTDKHK
HCCCCCCCCCCCCCC
20.5622673903
103PhosphorylationRHGGYKPTDKHKTDL
CCCCCCCCCCCCCCC
54.2326437602
108PhosphorylationKPTDKHKTDLNHENL
CCCCCCCCCCCCCCC
45.5026437602
125PhosphorylationGDDLDPNYVLSSRVR
CCCCCHHHEEECCCC
14.2520068231
128PhosphorylationLDPNYVLSSRVRTGR
CCHHHEEECCCCCCC
13.1720068231
129PhosphorylationDPNYVLSSRVRTGRS
CHHHEEECCCCCCCC
30.5420068231
133PhosphorylationVLSSRVRTGRSIKGY
EEECCCCCCCCCCCC
33.81-
136PhosphorylationSRVRTGRSIKGYTLP
CCCCCCCCCCCCCCC
29.96-
140PhosphorylationTGRSIKGYTLPPHCS
CCCCCCCCCCCCCCC
10.4919764811
141PhosphorylationGRSIKGYTLPPHCSR
CCCCCCCCCCCCCCH
41.2719764811
164PhosphorylationLSVEALNSLTGEFKG
HCHHHHHHCCCCCCC
28.3219764811
166PhosphorylationVEALNSLTGEFKGKY
HHHHHHCCCCCCCEE
34.1922777824
170AcetylationNSLTGEFKGKYYPLK
HHCCCCCCCEEECCC
50.6319862999
173PhosphorylationTGEFKGKYYPLKSMT
CCCCCCEEECCCCCC
20.9822817900
174PhosphorylationGEFKGKYYPLKSMTE
CCCCCEEECCCCCCH
12.9419764811
178PhosphorylationGKYYPLKSMTEKEQQ
CEEECCCCCCHHHHH
38.3219764811
180PhosphorylationYYPLKSMTEKEQQQL
EECCCCCCHHHHHHH
51.5022673903
199PhosphorylationFLFDKPVSPLLLASG
CCCCCCCHHHHHHHC
20.5422496350
215MethylationARDWPDARGIWHNDN
CCCCCCCCCCEECCC
44.50-
224PhosphorylationIWHNDNKSFLVWVNE
CEECCCCCEEEEECH
30.0226437602
247AcetylationMEKGGNMKEVFRRFC
EECCCCHHHHHHHHH
55.51156255
265AcetylationQKIEEIFKKAGHPFM
HHHHHHHHHCCCCCC
47.587923447
279PhosphorylationMWNQHLGYVLTCPSN
CCCCCCEEEEECCCC
9.92-
285PhosphorylationGYVLTCPSNLGTGLR
EEEEECCCCCCCCCC
47.0026437602
303PhosphorylationHVKLAHLSKHPKFEE
EEEEHHHHCCCCHHH
21.0326437602
313PhosphorylationPKFEEILTRLRLQKR
CCHHHHHHHHHHHHC
33.0619764811
322PhosphorylationLRLQKRGTGGVDTAA
HHHHHCCCCCCCCCC
34.4919764811
327PhosphorylationRGTGGVDTAAVGSVF
CCCCCCCCCCEECEE
17.7019764811
332PhosphorylationVDTAAVGSVFDVSNA
CCCCCEECEEECCCC
17.0119764811
337PhosphorylationVGSVFDVSNADRLGS
EECEEECCCCCCCCC
28.3022210691
365AcetylationKLMVEMEKKLEKGQS
HHHHHHHHHHHCCCC
62.4419863011
372PhosphorylationKKLEKGQSIDDMIPA
HHHHCCCCHHHCCCC
36.3322777824

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
-KUbiquitinationE3 ubiquitin ligaseTRIM63Q969Q1
PMID:18222470

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCRM_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 KCRM_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI63_HUMANTRIM63physical
18222470
ASB9_HUMANASB9physical
25416956
VATC2_HUMANATP6V1C2physical
26186194
PALM2_HUMANPALM2physical
26186194
ABCB7_HUMANABCB7physical
26344197
ASB9_HUMANASB9physical
21516116
VATC2_HUMANATP6V1C2physical
28514442
PALM2_HUMANPALM2physical
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
DB00148Creatine
Regulatory Network of KCRM_HUMAN

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Related Literatures of Post-Translational Modification

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