KCRM_RAT - dbPTM
KCRM_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCRM_RAT
UniProt AC P00564
Protein Name Creatine kinase M-type
Gene Name Ckm
Organism Rattus norvegicus (Rat).
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 MPFGNTHNKFKLNYKPQEEYPDLSKHNNHMAKVLTPDLYNKLRDKETPSGFTLDDVIQTGVDNPGHPFIMTVGCVAGDEESYTVFKDLFDPIIQDRHGGYKPTDKHKTDLNHENLKGGDDLDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMTEQEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISMEKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNEHLGYVLTCPSNLGTGLRGGVHVKLANLSKHPKFEEILTRLRLQKRGTGGVDTAAVGAVFDISNADRLGSSEVEQVQLVVDGVKLMVEMEKKLEKGQSIDDMIPAQK
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
11AcetylationGNTHNKFKLNYKPQE
CCCCCCCCCCCCCHH
37.1222902405
32AcetylationKHNNHMAKVLTPDLY
HCCCHHHHHCCHHHH
30.1522902405
35PhosphorylationNHMAKVLTPDLYNKL
CHHHHHCCHHHHHHH
20.1122673903
39PhosphorylationKVLTPDLYNKLRDKE
HHCCHHHHHHHCCCC
20.0322673903
41AcetylationLTPDLYNKLRDKETP
CCHHHHHHHCCCCCC
31.2022902405
107AcetylationYKPTDKHKTDLNHEN
CCCCCCCCCCCCCCC
49.8522902405
116AcetylationDLNHENLKGGDDLDP
CCCCCCCCCCCCCCH
72.8722902405
125PhosphorylationGDDLDPNYVLSSRVR
CCCCCHHHEEECCCC
14.2523991683
128PhosphorylationLDPNYVLSSRVRTGR
CCHHHEEECCCCCCC
13.1723991683
129PhosphorylationDPNYVLSSRVRTGRS
CHHHEEECCCCCCCC
30.5423991683
138AcetylationVRTGRSIKGYTLPPH
CCCCCCCCCCCCCCC
47.3022902405
140PhosphorylationTGRSIKGYTLPPHCS
CCCCCCCCCCCCCCC
10.4922609512
141PhosphorylationGRSIKGYTLPPHCSR
CCCCCCCCCCCCCCH
41.27-
156AcetylationGERRAVEKLSVEALN
HHHHHHHHHCHHHHH
39.1922902405
164PhosphorylationLSVEALNSLTGEFKG
HCHHHHHHCCCCCCC
28.3222673903
166PhosphorylationVEALNSLTGEFKGKY
HHHHHHCCCCCCCEE
34.1922673903
170AcetylationNSLTGEFKGKYYPLK
HHCCCCCCCEEECCC
50.6326302492
172AcetylationLTGEFKGKYYPLKSM
CCCCCCCEEECCCCC
42.0522902405
174PhosphorylationGEFKGKYYPLKSMTE
CCCCCEEECCCCCCH
12.9422609512
177AcetylationKGKYYPLKSMTEQEQ
CCEEECCCCCCHHHH
33.4122902405
178PhosphorylationGKYYPLKSMTEQEQQ
CEEECCCCCCHHHHH
38.3222673903
180PhosphorylationYYPLKSMTEQEQQQL
EECCCCCCHHHHHHH
41.4222673903
196AcetylationDDHFLFDKPVSPLLL
CCCCCCCCCCHHHHH
39.7322902405
199PhosphorylationFLFDKPVSPLLLASG
CCCCCCCHHHHHHHC
20.5422673903
205PhosphorylationVSPLLLASGMARDWP
CHHHHHHHCCCCCCC
29.1322673903
223AcetylationGIWHNDNKSFLVWVN
CCEECCCCCEEEEEC
45.5122902405
242AcetylationLRVISMEKGGNMKEV
EEEEEEECCCCHHHH
64.5722902405
247AcetylationMEKGGNMKEVFRRFC
EECCCCHHHHHHHHH
55.5122902405
259AcetylationRFCVGLQKIEEIFKK
HHHHHHHHHHHHHHH
58.0726302492
265AcetylationQKIEEIFKKAGHPFM
HHHHHHHHHCCCCCC
47.5822902405
266AcetylationKIEEIFKKAGHPFMW
HHHHHHHHCCCCCCC
49.1826302492
279PhosphorylationMWNEHLGYVLTCPSN
CCCCCCCEEEECCCC
9.92-
298AcetylationLRGGVHVKLANLSKH
CCCCEEEEECCCCCC
27.3122902405
303PhosphorylationHVKLANLSKHPKFEE
EEEECCCCCCCCHHH
28.8222673903
304AcetylationVKLANLSKHPKFEEI
EEECCCCCCCCHHHH
68.0722902405
307AcetylationANLSKHPKFEEILTR
CCCCCCCCHHHHHHH
66.1922902405
313PhosphorylationPKFEEILTRLRLQKR
CCHHHHHHHHHHHHC
33.0622673903
322PhosphorylationLRLQKRGTGGVDTAA
HHHHHCCCCCCCHHH
34.4922673903
327PhosphorylationRGTGGVDTAAVGAVF
CCCCCCCHHHHHHEE
17.7022673903
344PhosphorylationSNADRLGSSEVEQVQ
CCCCCCCCCCCEEEE
28.1122673903
345PhosphorylationNADRLGSSEVEQVQL
CCCCCCCCCCEEEEE
43.8122673903
365AcetylationKLMVEMEKKLEKGQS
HHHHHHHHHHHCCCC
62.4422902405
366AcetylationLMVEMEKKLEKGQSI
HHHHHHHHHHCCCCH
48.8826302492
369AcetylationEMEKKLEKGQSIDDM
HHHHHHHCCCCHHHC
73.0922902405
372PhosphorylationKKLEKGQSIDDMIPA
HHHHCCCCHHHCCCC
36.3328826663

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
128SPhosphorylationKinasePRKCBP05771-2
GPS
128SPhosphorylationKinasePRKCDP09215
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCRM_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KCRM_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCRM_RAT

loading...

Related Literatures of Post-Translational Modification

TOP