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Protein

Creatine kinase M-type

Gene

CKM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

ATP + creatine = ADP + phosphocreatine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei191ATPPROSITE-ProRule annotation1
Binding sitei236ATPPROSITE-ProRule annotation1
Binding sitei292ATPPROSITE-ProRule annotation1
Binding sitei335ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 132ATPPROSITE-ProRule annotation5
Nucleotide bindingi320 – 325ATPPROSITE-ProRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-71288 Creatine metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase M-type (EC:2.7.3.2)
Alternative name(s):
Creatine kinase M chain
Creatine phosphokinase M-type
Short name:
CPK-M
M-CK
Gene namesi
Name:CKM
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Organism-specific databases

VGNCiVGNC:27385 CKM

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Protein family/group databases

Allergomei11907 Bos d CK

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002119731 – 381Creatine kinase M-typeAdd BLAST381

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei164PhosphoserineBy similarity1
Modified residuei166PhosphothreonineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei180PhosphothreonineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei313PhosphothreonineBy similarity1
Modified residuei322PhosphothreonineBy similarity1
Modified residuei372PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9XSC6
PeptideAtlasiQ9XSC6
PRIDEiQ9XSC6

Expressioni

Gene expression databases

BgeeiENSBTAG00000013921

Interactioni

Subunit structurei

Dimer of identical or non-identical chains, which can be either B (brain type) or M (muscle type). With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018492

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 11Combined sources6
Helixi16 – 19Combined sources4
Helixi29 – 33Combined sources5
Helixi36 – 42Combined sources7
Helixi53 – 62Combined sources10
Helixi81 – 84Combined sources4
Helixi86 – 96Combined sources11
Turni97 – 99Combined sources3
Helixi112 – 114Combined sources3
Turni123 – 125Combined sources3
Beta strandi126 – 135Combined sources10
Turni143 – 145Combined sources3
Helixi148 – 162Combined sources15
Helixi167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Helixi176 – 178Combined sources3
Helixi181 – 190Combined sources10
Helixi200 – 203Combined sources4
Turni204 – 214Combined sources11
Beta strandi216 – 220Combined sources5
Beta strandi225 – 244Combined sources20
Helixi246 – 266Combined sources21
Turni275 – 277Combined sources3
Helixi284 – 286Combined sources3
Beta strandi292 – 298Combined sources7
Turni300 – 303Combined sources4
Helixi308 – 315Combined sources8
Beta strandi317 – 320Combined sources4
Beta strandi332 – 338Combined sources7
Beta strandi342 – 344Combined sources3
Helixi346 – 369Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G0WX-ray2.30A7-359[»]
ProteinModelPortaliQ9XSC6
SMRiQ9XSC6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XSC6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 98Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd BLAST88
Domaini125 – 367Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd BLAST243

Sequence similaritiesi

Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3581 Eukaryota
COG3869 LUCA
GeneTreeiENSGT00550000074561
HOGENOMiHOG000232165
HOVERGENiHBG001339
InParanoidiQ9XSC6
KOiK00933
OMAiGNTHNNF
OrthoDBiEOG091G0HZ0
TreeFamiTF314214

Family and domain databases

Gene3Di1.10.135.101 hit
InterProiView protein in InterPro
IPR000749 ATP-guanido_PTrfase
IPR022415 ATP-guanido_PTrfase_AS
IPR022414 ATP-guanido_PTrfase_cat
IPR022413 ATP-guanido_PTrfase_N
IPR036802 ATP-guanido_PTrfase_N_sf
IPR014746 Gln_synth/guanido_kin_cat_dom
PANTHERiPTHR11547 PTHR11547, 1 hit
PfamiView protein in Pfam
PF00217 ATP-gua_Ptrans, 1 hit
PF02807 ATP-gua_PtransN, 1 hit
SUPFAMiSSF48034 SSF48034, 1 hit
SSF55931 SSF55931, 1 hit
PROSITEiView protein in PROSITE
PS00112 PHOSPHAGEN_KINASE, 1 hit
PS51510 PHOSPHAGEN_KINASE_C, 1 hit
PS51509 PHOSPHAGEN_KINASE_N, 1 hit

Sequencei

Sequence statusi: Complete.

Q9XSC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFGNTHNKH KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF
110 120 130 140 150
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY ALPPHCSRGE
160 170 180 190 200
RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF
260 270 280 290 300
RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
310 320 330 340 350
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV
360 370 380
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
Length:381
Mass (Da):42,989
Last modified:June 27, 2006 - v2
Checksum:iC97EBBFB00BCF2FC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti376M → L in AAD30974 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti377I → M1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120106 mRNA Translation: AAD30974.1
BT020785 mRNA Translation: AAX08802.1
BT021173 mRNA Translation: AAX31355.1
BC102907 mRNA Translation: AAI02908.1
RefSeqiNP_777198.2, NM_174773.4
UniGeneiBt.3651

Genome annotation databases

EnsembliENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921
GeneIDi286822
KEGGibta:286822

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKCRM_BOVIN
AccessioniPrimary (citable) accession number: Q9XSC6
Secondary accession number(s): Q5E9Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 27, 2006
Last modified: March 28, 2018
This is version 126 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome