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P06732

- KCRM_HUMAN

UniProt

P06732 - KCRM_HUMAN

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Protein

Creatine kinase M-type

Gene
CKM, CKMM
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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.

Catalytic activityi

ATP + creatine = ADP + phosphocreatine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911ATP By similarity
Binding sitei236 – 2361ATP By similarity
Binding sitei292 – 2921ATP By similarity
Binding sitei335 – 3351ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1325ATP By similarity
Nucleotide bindingi320 – 3256ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. creatine kinase activity Source: ProtInc

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. creatine metabolic process Source: Reactome
  3. phosphocreatine biosynthetic process Source: Ensembl
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02640-MONOMER.
ReactomeiREACT_813. Creatine metabolism.
SABIO-RKP06732.

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase M-type (EC:2.7.3.2)
Alternative name(s):
Creatine kinase M chain
M-CK
Cleaved into the following chain:
Gene namesi
Name:CKM
Synonyms:CKMM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1994. CKM.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26532.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Creatine kinase M-typePRO_0000211975Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 381380Creatine kinase M-type, N-terminally processedPRO_0000421788Add
BLAST

Proteomic databases

MaxQBiP06732.
PaxDbiP06732.
PeptideAtlasiP06732.
PRIDEiP06732.

2D gel databases

UCD-2DPAGEP06732.

PTM databases

PhosphoSiteiP06732.

Expressioni

Gene expression databases

BgeeiP06732.
CleanExiHS_CKM.
GenevestigatoriP06732.

Organism-specific databases

HPAiHPA047859.

Interactioni

Subunit structurei

Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain.

Protein-protein interaction databases

BioGridi107578. 9 interactions.
IntActiP06732. 2 interactions.
STRINGi9606.ENSP00000221476.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 194
Helixi29 – 335
Helixi36 – 427
Helixi53 – 6210
Beta strandi67 – 693
Helixi80 – 845
Helixi86 – 938
Turni94 – 963
Beta strandi97 – 993
Turni123 – 1253
Beta strandi126 – 1327
Turni143 – 1453
Helixi148 – 16417
Helixi167 – 1693
Beta strandi171 – 1766
Turni181 – 1833
Helixi184 – 1896
Turni200 – 2067
Turni209 – 2146
Beta strandi216 – 2205
Beta strandi223 – 24422
Helixi246 – 26621
Turni275 – 2773
Helixi284 – 2863
Beta strandi292 – 2987
Turni300 – 3045
Helixi308 – 3147
Beta strandi333 – 3386
Beta strandi342 – 3443
Helixi346 – 36823

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I0EX-ray3.50A/B/C/D1-381[»]
ProteinModelPortaliP06732.
SMRiP06732. Positions 8-381.

Miscellaneous databases

EvolutionaryTraceiP06732.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9888Phosphagen kinase N-terminalAdd
BLAST
Domaini125 – 367243Phosphagen kinase C-terminalAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3869.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP06732.
KOiK00933.
OMAiGNTHNNF.
OrthoDBiEOG7XM2XW.
PhylomeDBiP06732.
TreeFamiTF314214.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamiPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMiSSF48034. SSF48034. 1 hit.
PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06732-1 [UniParc]FASTAAdd to Basket

« Hide

MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG    50
FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY 100
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE 150
RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP 200
LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF 250
RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA 300
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV 350
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K 381
Length:381
Mass (Da):43,101
Last modified:November 1, 1990 - v2
Checksum:i418FEAD0C2E138C8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831E → G.1 Publication
Corresponds to variant rs11559024 [ dbSNP | Ensembl ].
VAR_018680
Natural varianti127 – 1271L → V.1 Publication
Corresponds to variant rs17875653 [ dbSNP | Ensembl ].
VAR_018681
Natural varianti166 – 1661T → M.
Corresponds to variant rs17357122 [ dbSNP | Ensembl ].
VAR_049675
Natural varianti243 – 2431G → A.1 Publication
Corresponds to variant rs17875625 [ dbSNP | Ensembl ].
VAR_018682

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471T → I in AAA52025. 1 Publication
Sequence conflicti130 – 1301R → P in AAA52025. 1 Publication
Sequence conflicti193 – 1931L → Q in AAA52025. 1 Publication
Sequence conflicti210 – 2101D → H in AAA52025. 1 Publication
Sequence conflicti215 – 2151R → P in AAA52025. 1 Publication
Sequence conflicti225 – 2251F → L in AAP35439. 1 Publication
Sequence conflicti225 – 2251F → L in AAH07462. 1 Publication
Sequence conflicti324 – 3241G → A in AAA52025. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14780 mRNA. Translation: AAA52025.1.
M21494
, M21488, M21489, M21490, M21491, M21492, M21493 Genomic DNA. Translation: AAA96609.1.
BT006793 mRNA. Translation: AAP35439.1.
AY585238 Genomic DNA. Translation: AAS79321.1.
AC005781 Genomic DNA. Translation: AAC62841.1.
BC007462 mRNA. Translation: AAH07462.1.
M16440 mRNA. Translation: AAA52026.1. Sequence problems.
CCDSiCCDS12659.1.
PIRiA31793. KIHUCM.
RefSeqiNP_001815.2. NM_001824.4.
UniGeneiHs.334347.

Genome annotation databases

EnsembliENST00000221476; ENSP00000221476; ENSG00000104879.
GeneIDi1158.
KEGGihsa:1158.
UCSCiuc002pbd.4. human.

Polymorphism databases

DMDMi125305.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Creatine kinase entry

SeattleSNPs
Wikipedia

CKM entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14780 mRNA. Translation: AAA52025.1 .
M21494
, M21488 , M21489 , M21490 , M21491 , M21492 , M21493 Genomic DNA. Translation: AAA96609.1 .
BT006793 mRNA. Translation: AAP35439.1 .
AY585238 Genomic DNA. Translation: AAS79321.1 .
AC005781 Genomic DNA. Translation: AAC62841.1 .
BC007462 mRNA. Translation: AAH07462.1 .
M16440 mRNA. Translation: AAA52026.1 . Sequence problems.
CCDSi CCDS12659.1.
PIRi A31793. KIHUCM.
RefSeqi NP_001815.2. NM_001824.4.
UniGenei Hs.334347.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I0E X-ray 3.50 A/B/C/D 1-381 [» ]
ProteinModelPortali P06732.
SMRi P06732. Positions 8-381.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107578. 9 interactions.
IntActi P06732. 2 interactions.
STRINGi 9606.ENSP00000221476.

Chemistry

BindingDBi P06732.
ChEMBLi CHEMBL2656.
DrugBanki DB00148. Creatine.

PTM databases

PhosphoSitei P06732.

Polymorphism databases

DMDMi 125305.

2D gel databases

UCD-2DPAGE P06732.

Proteomic databases

MaxQBi P06732.
PaxDbi P06732.
PeptideAtlasi P06732.
PRIDEi P06732.

Protocols and materials databases

DNASUi 1158.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000221476 ; ENSP00000221476 ; ENSG00000104879 .
GeneIDi 1158.
KEGGi hsa:1158.
UCSCi uc002pbd.4. human.

Organism-specific databases

CTDi 1158.
GeneCardsi GC19M045809.
HGNCi HGNC:1994. CKM.
HPAi HPA047859.
MIMi 123310. gene.
neXtProti NX_P06732.
PharmGKBi PA26532.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3869.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi P06732.
KOi K00933.
OMAi GNTHNNF.
OrthoDBi EOG7XM2XW.
PhylomeDBi P06732.
TreeFami TF314214.

Enzyme and pathway databases

BioCyci MetaCyc:HS02640-MONOMER.
Reactomei REACT_813. Creatine metabolism.
SABIO-RK P06732.

Miscellaneous databases

ChiTaRSi CKM. human.
EvolutionaryTracei P06732.
GeneWikii CKM_(gene).
GenomeRNAii 1158.
NextBioi 4804.
PROi P06732.
SOURCEi Search...

Gene expression databases

Bgeei P06732.
CleanExi HS_CKM.
Genevestigatori P06732.

Family and domain databases

Gene3Di 1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProi IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view ]
Pfami PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view ]
SUPFAMi SSF48034. SSF48034. 1 hit.
PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence analysis of a full-length cDNA for human M creatine kinase."
    Perryman M.B., Kerner S.A., Bohlmeyer T.J., Roberts R.
    Biochem. Biophys. Res. Commun. 140:981-989(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene."
    Trask R.V., Strauss A.W., Billadello J.J.
    J. Biol. Chem. 263:17142-17149(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. SeattleSNPs variation discovery resource
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-83; VAL-127 AND ALA-243.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  7. "Muscle creatine kinase isoenzyme expression in adult human brain."
    Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D., Goodman C., Puleo P.R., Perryman M.B.
    J. Biol. Chem. 265:6403-6409(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-30.
    Tissue: Brain.
  8. "cDNA cloning and mapping of the human creatine kinase M gene to 19q13."
    Nigro J.M., Schweinfest C.W., Rajkovic A., Pavlovic J., Jamal S., Dottin R.P., Hart J.T., Kamarck M.E., Rae P.M.M., Carty M.D., Martin-Deleon P.
    Am. J. Hum. Genet. 40:115-125(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-327.
  9. "Crystallization and preliminary X-ray analysis of human muscle creatine kinase."
    Tang L., Zhou H.M., Lin Z.J.
    Acta Crystallogr. D 55:669-670(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

Entry informationi

Entry nameiKCRM_HUMAN
AccessioniPrimary (citable) accession number: P06732
Secondary accession number(s): Q96QL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: September 3, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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