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P12532

- KCRU_HUMAN

UniProt

P12532 - KCRU_HUMAN

Protein

Creatine kinase U-type, mitochondrial

Gene

CKMT1A

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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 sitei224 – 2241ATPPROSITE-ProRule annotation
    Binding sitei269 – 2691ATPPROSITE-ProRule annotation
    Binding sitei325 – 3251ATPPROSITE-ProRule annotation
    Binding sitei368 – 3681ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi161 – 1655ATPPROSITE-ProRule annotation
    Nucleotide bindingi353 – 3586ATPPROSITE-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. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09820-MONOMER.
    ReactomeiREACT_813. Creatine metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase U-type, mitochondrial (EC:2.7.3.2)
    Alternative name(s):
    Acidic-type mitochondrial creatine kinase
    Short name:
    Mia-CK
    Ubiquitous mitochondrial creatine kinase
    Short name:
    U-MtCK
    Gene namesi
    Name:CKMT1A
    Synonyms:CKMT
    AND
    Name:CKMT1B
    Synonyms:CKMT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:31736. CKMT1A.
    HGNC:1995. CKMT1B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: Reactome
    3. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672108.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionAdd
    BLAST
    Chaini40 – 417378Creatine kinase U-type, mitochondrialPRO_0000016590Add
    BLAST

    Proteomic databases

    MaxQBiP12532.
    PaxDbiP12532.
    PeptideAtlasiP12532.
    PRIDEiP12532.

    2D gel databases

    UCD-2DPAGEP12532.

    PTM databases

    PhosphoSiteiP12532.

    Expressioni

    Gene expression databases

    BgeeiP12532.
    CleanExiHS_CKMT1A.
    HS_CKMT1B.
    GenevestigatoriP12532.

    Organism-specific databases

    HPAiHPA043491.

    Interactioni

    Subunit structurei

    Exists as an octamer composed of four MTCK homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi107579. 10 interactions.
    139227. 6 interactions.
    IntActiP12532. 4 interactions.
    MINTiMINT-3304503.
    STRINGi9606.ENSP00000300283.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi49 – 524
    Helixi62 – 665
    Helixi69 – 757
    Helixi86 – 9510
    Beta strandi100 – 1023
    Helixi114 – 1174
    Helixi119 – 12911
    Turni130 – 1323
    Turni135 – 1373
    Helixi146 – 1483
    Turni156 – 1583
    Beta strandi159 – 16810
    Turni176 – 1783
    Helixi181 – 19515
    Helixi200 – 2023
    Beta strandi204 – 2085
    Helixi209 – 2113
    Helixi214 – 2229
    Helixi233 – 2364
    Turni237 – 24711
    Beta strandi249 – 2535
    Beta strandi258 – 27720
    Helixi279 – 29820
    Turni299 – 3013
    Turni308 – 3103
    Helixi317 – 3193
    Beta strandi325 – 3317
    Helixi333 – 3375
    Helixi341 – 3488
    Beta strandi350 – 3534
    Turni359 – 3613
    Beta strandi364 – 3729
    Beta strandi375 – 3773
    Helixi379 – 40022
    Turni401 – 4033

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QK1X-ray2.70A/B/C/D/E/F/G/H39-417[»]
    ProteinModelPortaliP12532.
    SMRiP12532. Positions 39-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12532.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 13187Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini158 – 400243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 6425Cardiolipin-bindingBy similarityAdd
    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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG3869.
    HOGENOMiHOG000232165.
    HOVERGENiHBG001339.
    InParanoidiP12532.
    KOiK00933.
    OMAiERHNGYN.
    PhylomeDBiP12532.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12532-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPVRAA SERRRLYPPS    50
    AEYPDLRKHN NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP 100
    FIKTVGMVAG DEETYEVFAD LFDPVIQERH NGYDPRTMKH TTDLDASKIR 150
    SGYFDERYVL SSRVRTGRSI RGLSLPPACT RAERREVERV VVDALSGLKG 200
    DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM ARDWPDARGI 250
    WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER 300
    GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL 350
    QKRGTGGVDT AATGGVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL 400
    ERGQDIRIPT PVIHTKH 417
    Length:417
    Mass (Da):47,037
    Last modified:October 1, 1989 - v1
    Checksum:i274DAC2E9A8AD882
    GO
    Isoform 2 (identifier: P12532-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-50: S → SQTWPTGQLPGNCTRSRRLCPPSMVTGYPLPS

    Show »
    Length:448
    Mass (Da):50,421
    Checksum:i460CD2E9E9D6A0E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761P → L in BAG58600. (PubMed:14702039)Curated
    Sequence conflicti401 – 4011E → G in BAD97085. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 501S → SQTWPTGQLPGNCTRSRRLC PPSMVTGYPLPS in isoform 2. 1 PublicationVSP_038045

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04469 Genomic DNA. Translation: AAA98744.1.
    BT006628 mRNA. Translation: AAP35274.1.
    AK295776 mRNA. Translation: BAG58600.1.
    AK223365 mRNA. Translation: BAD97085.1.
    AK316124 mRNA. Translation: BAH14495.1.
    AK316319 mRNA. Translation: BAH14690.1.
    BC001926 mRNA. Translation: AAH01926.1.
    BC006467 mRNA. Translation: AAH06467.1.
    BC108652 mRNA. Translation: AAI08653.1.
    BC121001 mRNA. Translation: AAI21002.1.
    BC121002 mRNA. Translation: AAI21003.1.
    CCDSiCCDS10097.1. [P12532-1]
    CCDS32217.1. [P12532-1]
    PIRiA31431. A30789.
    RefSeqiNP_001015001.1. NM_001015001.1. [P12532-1]
    NP_066270.1. NM_020990.3. [P12532-1]
    UniGeneiHs.654988.
    Hs.741420.

    Genome annotation databases

    EnsembliENST00000300283; ENSP00000300283; ENSG00000237289. [P12532-1]
    ENST00000413453; ENSP00000406577; ENSG00000223572. [P12532-1]
    ENST00000434505; ENSP00000413165; ENSG00000223572. [P12532-1]
    ENST00000441322; ENSP00000413255; ENSG00000237289. [P12532-1]
    GeneIDi1159.
    548596.
    KEGGihsa:1159.
    hsa:548596.
    UCSCiuc001zsc.3. human. [P12532-1]
    uc010uds.2. human. [P12532-2]

    Polymorphism databases

    DMDMi125315.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04469 Genomic DNA. Translation: AAA98744.1 .
    BT006628 mRNA. Translation: AAP35274.1 .
    AK295776 mRNA. Translation: BAG58600.1 .
    AK223365 mRNA. Translation: BAD97085.1 .
    AK316124 mRNA. Translation: BAH14495.1 .
    AK316319 mRNA. Translation: BAH14690.1 .
    BC001926 mRNA. Translation: AAH01926.1 .
    BC006467 mRNA. Translation: AAH06467.1 .
    BC108652 mRNA. Translation: AAI08653.1 .
    BC121001 mRNA. Translation: AAI21002.1 .
    BC121002 mRNA. Translation: AAI21003.1 .
    CCDSi CCDS10097.1. [P12532-1 ]
    CCDS32217.1. [P12532-1 ]
    PIRi A31431. A30789.
    RefSeqi NP_001015001.1. NM_001015001.1. [P12532-1 ]
    NP_066270.1. NM_020990.3. [P12532-1 ]
    UniGenei Hs.654988.
    Hs.741420.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QK1 X-ray 2.70 A/B/C/D/E/F/G/H 39-417 [» ]
    ProteinModelPortali P12532.
    SMRi P12532. Positions 39-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107579. 10 interactions.
    139227. 6 interactions.
    IntActi P12532. 4 interactions.
    MINTi MINT-3304503.
    STRINGi 9606.ENSP00000300283.

    Chemistry

    DrugBanki DB00148. Creatine.

    PTM databases

    PhosphoSitei P12532.

    Polymorphism databases

    DMDMi 125315.

    2D gel databases

    UCD-2DPAGE P12532.

    Proteomic databases

    MaxQBi P12532.
    PaxDbi P12532.
    PeptideAtlasi P12532.
    PRIDEi P12532.

    Protocols and materials databases

    DNASUi 1159.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300283 ; ENSP00000300283 ; ENSG00000237289 . [P12532-1 ]
    ENST00000413453 ; ENSP00000406577 ; ENSG00000223572 . [P12532-1 ]
    ENST00000434505 ; ENSP00000413165 ; ENSG00000223572 . [P12532-1 ]
    ENST00000441322 ; ENSP00000413255 ; ENSG00000237289 . [P12532-1 ]
    GeneIDi 1159.
    548596.
    KEGGi hsa:1159.
    hsa:548596.
    UCSCi uc001zsc.3. human. [P12532-1 ]
    uc010uds.2. human. [P12532-2 ]

    Organism-specific databases

    CTDi 1159.
    548596.
    GeneCardsi GC15P043885.
    GC15P043985.
    HGNCi HGNC:31736. CKMT1A.
    HGNC:1995. CKMT1B.
    HPAi HPA043491.
    MIMi 123290. gene.
    613415. gene.
    neXtProti NX_P12532.
    PharmGKBi PA142672108.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3869.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi P12532.
    KOi K00933.
    OMAi ERHNGYN.
    PhylomeDBi P12532.
    TreeFami TF314214.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09820-MONOMER.
    Reactomei REACT_813. Creatine metabolism.

    Miscellaneous databases

    ChiTaRSi CKMT1B. human.
    EvolutionaryTracei P12532.
    GeneWikii CKMT1B.
    NextBioi 4808.
    PROi P12532.
    SOURCEi Search...

    Gene expression databases

    Bgeei P12532.
    CleanExi HS_CKMT1A.
    HS_CKMT1B.
    Genevestigatori P12532.

    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 characterization of the gene and cDNA encoding human mitochondrial creatine kinase."
      Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D., Strauss A.W.
      J. Biol. Chem. 264:2890-2897(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon and Hippocampus.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    5. "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] (ISOFORM 1).
      Tissue: Lung and PNS.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Crystal structure of human ubiquitous mitochondrial creatine kinase."
      Eder M., Fritz-Wolf K., Kabsch W., Wallimann T., Schlattner U.
      Proteins 39:216-225(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-417, SUBUNIT.

    Entry informationi

    Entry nameiKCRU_HUMAN
    AccessioniPrimary (citable) accession number: P12532
    Secondary accession number(s): B4DIT8
    , B7ZA09, Q0VAM3, Q32NF6, Q53FC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 159 of the entry and version 1 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

    Miscellaneous

    Mitochondrial creatine kinase binds cardiolipin.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3