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P12277

- KCRB_HUMAN

UniProt

P12277 - KCRB_HUMAN

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Protein

Creatine kinase B-type

Gene

CKB

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.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

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
Complete GO annotation...

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: UniProtKB
  3. mitochondrion Source: Ensembl
Complete GO annotation...

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

BgeeiP12277.
CleanExiHS_CKB.
ExpressionAtlasiP12277. baseline and differential.
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. 53 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 – 115Combined sources
Helixi16 – 194Combined sources
Helixi29 – 335Combined sources
Helixi36 – 427Combined sources
Helixi53 – 6210Combined sources
Beta strandi67 – 693Combined sources
Helixi81 – 844Combined sources
Helixi86 – 9611Combined sources
Helixi112 – 1143Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 13510Combined sources
Turni143 – 1453Combined sources
Helixi148 – 16215Combined sources
Helixi167 – 1693Combined sources
Beta strandi171 – 1766Combined sources
Helixi181 – 1899Combined sources
Helixi200 – 2034Combined sources
Turni204 – 21411Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi223 – 24422Combined sources
Helixi246 – 26621Combined sources
Turni275 – 2773Combined sources
Helixi284 – 2863Combined sources
Beta strandi292 – 2987Combined sources
Helixi300 – 3034Combined sources
Helixi308 – 3147Combined sources
Beta strandi317 – 3215Combined sources
Helixi325 – 3306Combined sources
Beta strandi333 – 3386Combined sources
Beta strandi342 – 3443Combined sources
Helixi346 – 36823Combined sources
Helixi374 – 3763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY
110 120 130 140 150
KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE
160 170 180 190 200
RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
310 320 330 340 350
NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV
360 370 380
QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 53 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

Bgeei P12277.
CleanExi HS_CKB.
ExpressionAtlasi P12277. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 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

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