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P12532

- KCRU_HUMAN

UniProt

P12532 - KCRU_HUMAN

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Protein

Creatine kinase U-type, mitochondrial

Gene
CKMT1A, CKMT
CKMT1B, CKMT
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 annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei224 – 2241ATPPROSITE-ProRule annotations
Binding sitei269 – 2691ATPPROSITE-ProRule annotations
Binding sitei325 – 3251ATPPROSITE-ProRule annotations
Binding sitei368 – 3681ATPPROSITE-ProRule annotations

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi161 – 1655ATPPROSITE-ProRule annotations
Nucleotide bindingi353 – 3586ATPPROSITE-ProRule annotations

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
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS09820-MONOMER.
ReactomeiREACT_813. Creatine metabolism.

Names & Taxonomyi

Organism-specific databases

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
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.

Miscellaneous databases

EvolutionaryTraceiP12532.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6425Cardiolipin-bindingAdd
BLAST

Sequence similaritiesi

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

Alternative sequence

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

Sequence conflict

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

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

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