Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06732

- KCRM_HUMAN

UniProt

P06732 - KCRM_HUMAN

Protein

Creatine kinase M-type

Gene

CKM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Nov 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei191 – 1911ATPPROSITE-ProRule annotation
    Binding sitei236 – 2361ATPPROSITE-ProRule annotation
    Binding sitei292 – 2921ATPPROSITE-ProRule annotation
    Binding sitei335 – 3351ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi128 – 1325ATPPROSITE-ProRule annotation
    Nucleotide bindingi320 – 3256ATPPROSITE-ProRule annotation

    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

    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

    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; alternateBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06732.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase N-terminal domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti47 – 471T → I in AAA52025. (PubMed:3778496)Curated
    Sequence conflicti130 – 1301R → P in AAA52025. (PubMed:3778496)Curated
    Sequence conflicti193 – 1931L → Q in AAA52025. (PubMed:3778496)Curated
    Sequence conflicti210 – 2101D → H in AAA52025. (PubMed:3778496)Curated
    Sequence conflicti215 – 2151R → P in AAA52025. (PubMed:3778496)Curated
    Sequence conflicti225 – 2251F → L in AAP35439. 1 PublicationCurated
    Sequence conflicti225 – 2251F → L in AAH07462. (PubMed:15489334)Curated
    Sequence conflicti324 – 3241G → A in AAA52025. (PubMed:3778496)Curated

    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 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

    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: October 1, 2014
    This is version 150 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