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P12277

- KCRB_HUMAN

UniProt

P12277 - KCRB_HUMAN

Protein

Creatine kinase B-type

Gene

CKB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (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 sitei72 – 721Substrate; via amide nitrogen
    Binding sitei130 – 1301ATP
    Binding sitei132 – 1321ATP
    Binding sitei191 – 1911ATP
    Binding sitei232 – 2321Substrate
    Binding sitei236 – 2361ATP
    Binding sitei285 – 2851Substrate
    Binding sitei292 – 2921ATP
    Binding sitei320 – 3201ATP
    Binding sitei335 – 3351ATPPROSITE-ProRule annotation

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular chloride ion homeostasis Source: Ensembl
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. creatine metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. substantia nigra development Source: UniProt

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09344-MONOMER.
    ReactomeiREACT_813. Creatine metabolism.
    SABIO-RKP12277.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase B-type (EC:2.7.3.2)
    Alternative name(s):
    B-CK
    Creatine kinase B chain
    Gene namesi
    Name:CKB
    Synonyms:CKBB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:1991. CKB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi283 – 2831C → S or Y: Complete loss of activity. 1 Publication
    Mutagenesisi292 – 2921R → H, L or Q: Complete loss of activity. 1 Publication
    Mutagenesisi292 – 2921R → K: 42% of wild-type activity. 1 Publication
    Mutagenesisi340 – 3401D → E: No change in activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA26528.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 381380Creatine kinase B-typePRO_0000211966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41Phosphoserine1 Publication
    Modified residuei35 – 351Phosphothreonine1 Publication
    Modified residuei125 – 1251PhosphotyrosineBy similarity
    Modified residuei199 – 1991Phosphoserine1 Publication
    Modified residuei269 – 2691Nitrated tyrosineBy similarity

    Keywords - PTMi

    Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP12277.
    PaxDbiP12277.
    PeptideAtlasiP12277.
    PRIDEiP12277.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00022977.
    P12277.
    UCD-2DPAGEP12277.

    PTM databases

    PhosphoSiteiP12277.

    Expressioni

    Gene expression databases

    ArrayExpressiP12277.
    BgeeiP12277.
    CleanExiHS_CKB.
    GenevestigatoriP12277.

    Organism-specific databases

    HPAiCAB047313.
    HPA001254.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q034633EBI-357706,EBI-9081620From a different organism.
    ASB9Q96DX53EBI-357706,EBI-745641

    Protein-protein interaction databases

    BioGridi107572. 51 interactions.
    IntActiP12277. 25 interactions.
    MINTiMINT-1484821.
    STRINGi9606.ENSP00000299198.

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 115
    Helixi16 – 194
    Helixi29 – 335
    Helixi36 – 427
    Helixi53 – 6210
    Beta strandi67 – 693
    Helixi81 – 844
    Helixi86 – 9611
    Helixi112 – 1143
    Turni123 – 1253
    Beta strandi126 – 13510
    Turni143 – 1453
    Helixi148 – 16215
    Helixi167 – 1693
    Beta strandi171 – 1766
    Helixi181 – 1899
    Helixi200 – 2034
    Turni204 – 21411
    Beta strandi216 – 2205
    Beta strandi223 – 24422
    Helixi246 – 26621
    Turni275 – 2773
    Helixi284 – 2863
    Beta strandi292 – 2987
    Helixi300 – 3034
    Helixi308 – 3147
    Beta strandi317 – 3215
    Helixi325 – 3306
    Beta strandi333 – 3386
    Beta strandi342 – 3443
    Helixi346 – 36823
    Helixi374 – 3763

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3B6RX-ray2.00A/B1-381[»]
    3DRBX-ray2.00A/B1-381[»]
    3DREX-ray2.20A/B1-381[»]
    ProteinModelPortaliP12277.
    SMRiP12277. Positions 6-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12277.

    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.
    InParanoidiP12277.
    KOiK00933.
    OMAiQCLSDVR.
    OrthoDBiEOG7XM2XW.
    PhylomeDBiP12277.
    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.

    P12277-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG    50
    FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY 100
    KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE 150
    RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP 200
    LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF 250
    TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 300
    NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV 350
    QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K 381
    Length:381
    Mass (Da):42,644
    Last modified:October 1, 1989 - v1
    Checksum:i637AA67A86AE3059
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 422EL → DV in AAA76851. (PubMed:3034271)Curated
    Sequence conflicti78 – 781D → G in AAA76850. (PubMed:2883200)Curated
    Sequence conflicti78 – 781D → G in AAA52024. (PubMed:2828370)Curated
    Sequence conflicti98 – 992GG → RR in AAA76851. (PubMed:3034271)Curated
    Sequence conflicti105 – 1062EH → DD in AAA76851. (PubMed:3034271)Curated
    Sequence conflicti130 – 1301R → G in AAA76850. (PubMed:2883200)Curated
    Sequence conflicti132 – 1321R → A in AAA76851. (PubMed:3034271)Curated
    Sequence conflicti144 – 1441P → Q in CAG47064. 1 PublicationCurated
    Sequence conflicti203 – 2031L → S in AAC31758. (PubMed:3692484)Curated
    Sequence conflicti215 – 2162RG → AR in AAA76851. (PubMed:3034271)Curated
    Sequence conflicti296 – 2961H → D in AAA76851. (PubMed:3034271)Curated
    Sequence conflicti358 – 3581K → R in BAG35211. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti177 – 1771K → R.1 Publication
    Corresponds to variant rs36002620 [ dbSNP | Ensembl ].
    VAR_025838
    Natural varianti309 – 3091S → L.1 Publication
    Corresponds to variant rs35156510 [ dbSNP | Ensembl ].
    VAR_025839
    Natural varianti360 – 3601L → F.
    Corresponds to variant rs12505 [ dbSNP | Ensembl ].
    VAR_049674

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16451 mRNA. Translation: AAA76851.1.
    M21243
    , M21237, M21238, M21239, M21240, M21241, M21242 Genomic DNA. Translation: AAC31758.1.
    L47647 mRNA. Translation: AAA76852.1.
    M16364 mRNA. Translation: AAA76850.1.
    X15334 Genomic DNA. Translation: CAA33389.1.
    AK290101 mRNA. Translation: BAF82790.1.
    AK312282 mRNA. Translation: BAG35211.1.
    CR542268 mRNA. Translation: CAG47064.1.
    DQ333313 Genomic DNA. Translation: ABC67465.1.
    CH471061 Genomic DNA. Translation: EAW81822.1.
    BC001190 mRNA. Translation: AAH01190.1.
    BC004914 mRNA. Translation: AAH04914.1.
    BC008323 mRNA. Translation: AAH08323.1.
    BC010002 mRNA. Translation: AAH10002.1.
    BC019259 mRNA. Translation: AAH19259.1.
    BC019281 mRNA. Translation: AAH19281.1.
    M22356, M22355 Genomic DNA. Translation: AAA52024.1.
    CCDSiCCDS9981.1.
    PIRiS15935. KIHUCB.
    RefSeqiNP_001814.2. NM_001823.4.
    UniGeneiHs.173724.

    Genome annotation databases

    EnsembliENST00000348956; ENSP00000299198; ENSG00000166165.
    GeneIDi1152.
    KEGGihsa:1152.
    UCSCiuc001ynf.2. human.

    Polymorphism databases

    DMDMi125294.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Creatine kinase entry

    Wikipedia

    CKB entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16451 mRNA. Translation: AAA76851.1 .
    M21243
    , M21237 , M21238 , M21239 , M21240 , M21241 , M21242 Genomic DNA. Translation: AAC31758.1 .
    L47647 mRNA. Translation: AAA76852.1 .
    M16364 mRNA. Translation: AAA76850.1 .
    X15334 Genomic DNA. Translation: CAA33389.1 .
    AK290101 mRNA. Translation: BAF82790.1 .
    AK312282 mRNA. Translation: BAG35211.1 .
    CR542268 mRNA. Translation: CAG47064.1 .
    DQ333313 Genomic DNA. Translation: ABC67465.1 .
    CH471061 Genomic DNA. Translation: EAW81822.1 .
    BC001190 mRNA. Translation: AAH01190.1 .
    BC004914 mRNA. Translation: AAH04914.1 .
    BC008323 mRNA. Translation: AAH08323.1 .
    BC010002 mRNA. Translation: AAH10002.1 .
    BC019259 mRNA. Translation: AAH19259.1 .
    BC019281 mRNA. Translation: AAH19281.1 .
    M22356 , M22355 Genomic DNA. Translation: AAA52024.1 .
    CCDSi CCDS9981.1.
    PIRi S15935. KIHUCB.
    RefSeqi NP_001814.2. NM_001823.4.
    UniGenei Hs.173724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3B6R X-ray 2.00 A/B 1-381 [» ]
    3DRB X-ray 2.00 A/B 1-381 [» ]
    3DRE X-ray 2.20 A/B 1-381 [» ]
    ProteinModelPortali P12277.
    SMRi P12277. Positions 6-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107572. 51 interactions.
    IntActi P12277. 25 interactions.
    MINTi MINT-1484821.
    STRINGi 9606.ENSP00000299198.

    Chemistry

    ChEMBLi CHEMBL6049.
    DrugBanki DB00148. Creatine.

    PTM databases

    PhosphoSitei P12277.

    Polymorphism databases

    DMDMi 125294.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00022977.
    P12277.
    UCD-2DPAGE P12277.

    Proteomic databases

    MaxQBi P12277.
    PaxDbi P12277.
    PeptideAtlasi P12277.
    PRIDEi P12277.

    Protocols and materials databases

    DNASUi 1152.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348956 ; ENSP00000299198 ; ENSG00000166165 .
    GeneIDi 1152.
    KEGGi hsa:1152.
    UCSCi uc001ynf.2. human.

    Organism-specific databases

    CTDi 1152.
    GeneCardsi GC14M103986.
    HGNCi HGNC:1991. CKB.
    HPAi CAB047313.
    HPA001254.
    MIMi 123280. gene.
    neXtProti NX_P12277.
    PharmGKBi PA26528.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3869.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi P12277.
    KOi K00933.
    OMAi QCLSDVR.
    OrthoDBi EOG7XM2XW.
    PhylomeDBi P12277.
    TreeFami TF314214.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09344-MONOMER.
    Reactomei REACT_813. Creatine metabolism.
    SABIO-RK P12277.

    Miscellaneous databases

    ChiTaRSi CKB. human.
    EvolutionaryTracei P12277.
    GeneWikii CKB_(gene).
    GenomeRNAii 1152.
    NextBioi 4784.
    PROi P12277.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12277.
    Bgeei P12277.
    CleanExi HS_CKB.
    Genevestigatori P12277.

    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. "Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number."
      Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B.
      Biochem. Biophys. Res. Commun. 144:1116-1127(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure and expression of the human creatine kinase B gene."
      Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I., Wieringa B.
      Genomics 1:126-137(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci."
      Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A.
      J. Clin. Invest. 79:1412-1420(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Complete nucleotide sequence of the human creatine kinase B gene."
      Mariman E.C.M., Schepens J.T.G., Wieringa B.
      Nucleic Acids Res. 17:6385-6385(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Brain.
    5. "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].
      Tissue: Cerebellum and Subthalamic nucleus.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. NIEHS SNPs program
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-177 AND LEU-309.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Brain, Eye and Lung.
    10. "Isolation of a functional human gene for brain creatine kinase."
      Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P.
      J. Biol. Chem. 263:2442-2446(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
    11. "Protein analysis of human maculae in relation to age-related maculopathy."
      Kliffen M., de Jong P.T.V.M., Luider T.M.
      Lab. Invest. 73:267-272(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22.
      Tissue: Eye.
    12. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 33-43; 157-172; 224-236; 253-265; 308-314 AND 342-366, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    13. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 157-172; 224-236; 253-265; 320-341 AND 359-381, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    14. "Determination of the catalytic site of creatine kinase by site-directed mutagenesis."
      Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S.
      Biochim. Biophys. Acta 1206:97-104(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-283; ARG-292 AND ASP-340.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex."
      Bong S.M., Moon J.H., Nam K.H., Lee K.S., Chi Y.M., Hwang K.Y.
      FEBS Lett. 582:3959-3965(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CREATINE, ATP-BINDING SITES, SUBSTRATE-BINDING SITES.

    Entry informationi

    Entry nameiKCRB_HUMAN
    AccessioniPrimary (citable) accession number: P12277
    Secondary accession number(s): A8K236
    , B2R5R4, Q2LE07, Q6FG40, Q9UC66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 157 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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