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Protein

Creatine kinase B-type

Gene

CKB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

ATP + creatine = ADP + phosphocreatine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei130ATPPROSITE-ProRule annotation1
Binding sitei132ATPPROSITE-ProRule annotation1
Binding sitei191ATPPROSITE-ProRule annotation1
Binding sitei232SubstrateBy similarity1
Binding sitei236ATPPROSITE-ProRule annotation1
Binding sitei285SubstrateBy similarity1
Binding sitei292ATPPROSITE-ProRule annotation1
Binding sitei320ATPPROSITE-ProRule annotation1
Binding sitei335ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 132ATPPROSITE-ProRule annotation5
Nucleotide bindingi320 – 325ATPPROSITE-ProRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-71288. Creatine metabolism.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 21

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002447322 – 381Creatine kinase B-typeAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphoserineBy similarity1
Modified residuei35PhosphothreonineBy similarity1
Modified residuei125PhosphotyrosineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei269Nitrated tyrosineBy similarity1
Modified residuei322PhosphothreonineBy similarity1

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

PaxDbiQ5EA61.
PeptideAtlasiQ5EA61.
PRIDEiQ5EA61.

Expressioni

Gene expression databases

BgeeiENSBTAG00000035998.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000047181.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 13Combined sources3
Helixi16 – 19Combined sources4
Helixi29 – 33Combined sources5
Helixi36 – 42Combined sources7
Helixi53 – 62Combined sources10
Helixi81 – 84Combined sources4
Helixi86 – 96Combined sources11
Turni97 – 99Combined sources3
Helixi112 – 114Combined sources3
Turni123 – 125Combined sources3
Beta strandi126 – 135Combined sources10
Turni143 – 145Combined sources3
Helixi148 – 163Combined sources16
Helixi167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Turni176 – 178Combined sources3
Helixi181 – 189Combined sources9
Helixi200 – 203Combined sources4
Turni204 – 214Combined sources11
Beta strandi216 – 220Combined sources5
Beta strandi223 – 244Combined sources22
Helixi246 – 266Combined sources21
Turni275 – 277Combined sources3
Helixi284 – 286Combined sources3
Beta strandi292 – 298Combined sources7
Helixi300 – 303Combined sources4
Helixi308 – 314Combined sources7
Beta strandi317 – 320Combined sources4
Beta strandi333 – 338Combined sources6
Beta strandi342 – 344Combined sources3
Helixi346 – 368Combined sources23
Helixi374 – 376Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q2RX-ray1.65A/B1-381[»]
ProteinModelPortaliQ5EA61.
SMRiQ5EA61.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 98Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd BLAST88
Domaini125 – 367Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd BLAST243

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

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
GeneTreeiENSGT00550000074561.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiQ5EA61.
KOiK00933.
OMAiRGHEFMW.
OrthoDBiEOG091G0HZ0.
TreeFamiTF314214.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 1 hit.
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.

Q5EA61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFSNSHNTL KLRFPAEDEF PDLSGHNNHM AKVLTPELYA ELRAKSTPSG
60 70 80 90 100
FTVDDVIQTG VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY
110 120 130 140 150
KPTDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE
160 170 180 190 200
RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
310 320 330 340 350
HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV
360 370 380
QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
Length:381
Mass (Da):42,719
Last modified:March 15, 2005 - v1
Checksum:iECBA70EF44052A22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020708 mRNA. Translation: AAX08725.1.
BC102333 mRNA. Translation: AAI02334.1.
RefSeqiNP_001015613.1. NM_001015613.1.
UniGeneiBt.88935.

Genome annotation databases

EnsembliENSBTAT00000050490; ENSBTAP00000047181; ENSBTAG00000035998.
GeneIDi516210.
KEGGibta:516210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020708 mRNA. Translation: AAX08725.1.
BC102333 mRNA. Translation: AAI02334.1.
RefSeqiNP_001015613.1. NM_001015613.1.
UniGeneiBt.88935.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q2RX-ray1.65A/B1-381[»]
ProteinModelPortaliQ5EA61.
SMRiQ5EA61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000047181.

Proteomic databases

PaxDbiQ5EA61.
PeptideAtlasiQ5EA61.
PRIDEiQ5EA61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000050490; ENSBTAP00000047181; ENSBTAG00000035998.
GeneIDi516210.
KEGGibta:516210.

Organism-specific databases

CTDi1152.

Phylogenomic databases

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
GeneTreeiENSGT00550000074561.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiQ5EA61.
KOiK00933.
OMAiRGHEFMW.
OrthoDBiEOG091G0HZ0.
TreeFamiTF314214.

Enzyme and pathway databases

ReactomeiR-BTA-71288. Creatine metabolism.

Gene expression databases

BgeeiENSBTAG00000035998.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiKCRB_BOVIN
AccessioniPrimary (citable) accession number: Q5EA61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 15, 2005
Last modified: November 2, 2016
This is version 92 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.