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Q04447

- KCRB_MOUSE

UniProt

Q04447 - KCRB_MOUSE

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Protein

Creatine kinase B-type

Gene

Ckb

Organism
Mus musculus (Mouse)
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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301ATPPROSITE-ProRule annotation
Binding sitei132 – 1321ATPPROSITE-ProRule annotation
Binding sitei191 – 1911ATPPROSITE-ProRule annotation
Binding sitei232 – 2321SubstrateBy similarity
Binding sitei236 – 2361ATPPROSITE-ProRule annotation
Binding sitei285 – 2851SubstrateBy similarity
Binding sitei292 – 2921ATPPROSITE-ProRule annotation
Binding sitei320 – 3201ATPPROSITE-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: UniProtKB-EC

GO - Biological processi

  1. cellular chloride ion homeostasis Source: Ensembl
  2. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:88407. Ckb.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 381380Creatine kinase B-typePRO_0000211967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei35 – 351PhosphothreonineBy similarity
Modified residuei125 – 1251Phosphotyrosine1 Publication
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei269 – 2691Nitrated tyrosine1 Publication

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ04447.
PaxDbiQ04447.
PRIDEiQ04447.

2D gel databases

REPRODUCTION-2DPAGEQ04447.
UCD-2DPAGEQ04447.

PTM databases

PhosphoSiteiQ04447.

Expressioni

Gene expression databases

BgeeiQ04447.
CleanExiMM_CKB.
GenevestigatoriQ04447.

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

BioGridi198725. 2 interactions.
IntActiQ04447. 8 interactions.
MINTiMINT-4099724.

Structurei

3D structure databases

ProteinModelPortaliQ04447.
SMRiQ04447. Positions 6-381.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00550000074561.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiQ04447.
KOiK00933.
OMAiQCLSDVR.
OrthoDBiEOG7XM2XW.
PhylomeDBiQ04447.
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.

Q04447-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG
60 70 80 90 100
FTLDDAIQTG VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEERHGGY
110 120 130 140 150
QPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE
160 170 180 190 200
RRAIEKLAVE ALSSLDGDLS GRYYALKSMT EAEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
310 320 330 340 350
HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV
360 370 380
QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
Length:381
Mass (Da):42,713
Last modified:October 1, 1993 - v1
Checksum:iD901C5653054A490
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431P → H in BAE28690. (PubMed:16141072)Curated
Sequence conflicti217 – 2171I → M in BAE39162. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74149 Genomic DNA. Translation: AAA37462.1.
L09069 Genomic DNA. Translation: AAA37455.1.
AK002467 mRNA. Translation: BAB22121.1.
AK014299 mRNA. Translation: BAB29254.1.
AK148885 mRNA. Translation: BAE28690.1.
AK152388 mRNA. Translation: BAE31176.1.
AK153484 mRNA. Translation: BAE32032.1.
AK166980 mRNA. Translation: BAE39162.1.
AK161990 mRNA. Translation: BAE36669.1.
AK167034 mRNA. Translation: BAE39205.1.
BC015271 mRNA. Translation: AAH15271.1.
BC106109 mRNA. Translation: AAI06110.2.
X04591 mRNA. Translation: CAA28259.1.
CCDSiCCDS26183.1.
PIRiA42078.
RefSeqiNP_067248.1. NM_021273.4.
UniGeneiMm.16831.

Genome annotation databases

EnsembliENSMUST00000001304; ENSMUSP00000001304; ENSMUSG00000001270.
GeneIDi12709.
KEGGimmu:12709.
UCSCiuc007pdn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74149 Genomic DNA. Translation: AAA37462.1 .
L09069 Genomic DNA. Translation: AAA37455.1 .
AK002467 mRNA. Translation: BAB22121.1 .
AK014299 mRNA. Translation: BAB29254.1 .
AK148885 mRNA. Translation: BAE28690.1 .
AK152388 mRNA. Translation: BAE31176.1 .
AK153484 mRNA. Translation: BAE32032.1 .
AK166980 mRNA. Translation: BAE39162.1 .
AK161990 mRNA. Translation: BAE36669.1 .
AK167034 mRNA. Translation: BAE39205.1 .
BC015271 mRNA. Translation: AAH15271.1 .
BC106109 mRNA. Translation: AAI06110.2 .
X04591 mRNA. Translation: CAA28259.1 .
CCDSi CCDS26183.1.
PIRi A42078.
RefSeqi NP_067248.1. NM_021273.4.
UniGenei Mm.16831.

3D structure databases

ProteinModelPortali Q04447.
SMRi Q04447. Positions 6-381.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198725. 2 interactions.
IntActi Q04447. 8 interactions.
MINTi MINT-4099724.

PTM databases

PhosphoSitei Q04447.

2D gel databases

REPRODUCTION-2DPAGE Q04447.
UCD-2DPAGE Q04447.

Proteomic databases

MaxQBi Q04447.
PaxDbi Q04447.
PRIDEi Q04447.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001304 ; ENSMUSP00000001304 ; ENSMUSG00000001270 .
GeneIDi 12709.
KEGGi mmu:12709.
UCSCi uc007pdn.2. mouse.

Organism-specific databases

CTDi 1152.
MGIi MGI:88407. Ckb.

Phylogenomic databases

eggNOGi COG3869.
GeneTreei ENSGT00550000074561.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi Q04447.
KOi K00933.
OMAi QCLSDVR.
OrthoDBi EOG7XM2XW.
PhylomeDBi Q04447.
TreeFami TF314214.

Miscellaneous databases

NextBioi 281980.
PROi Q04447.
SOURCEi Search...

Gene expression databases

Bgeei Q04447.
CleanExi MM_CKB.
Genevestigatori Q04447.

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. "Genetic variability of the murine creatine kinase B gene locus and related pseudogenes in different inbred strains of mice."
    van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G., Hendriks W., Wieringa B.
    Genomics 12:340-349(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Pentecost B.T.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic head, Kidney, Sympathetic ganglion and Wolffian duct.
  4. "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].
    Strain: FVB/N.
    Tissue: Colon.
  5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 12-43; 87-96; 108-130; 139-148; 157-172; 178-209; 224-236; 253-265; 268-292 AND 320-381, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  6. "The 3' non-coding region of the mouse brain B creatine kinase mRNA: a sequence with exceptional homology among species."
    Papenbrock T., Wille W.
    Nucleic Acids Res. 14:8690-8690(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  7. "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol."
    Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.
    Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKCRB_MOUSE
AccessioniPrimary (citable) accession number: Q04447
Secondary accession number(s): Q3KQP4
, Q3TKI3, Q3U5P5, Q3UF71, Q9CXK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3