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Protein

Carnosine N-methyltransferase

Gene

CARNMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).1 Publication

Catalytic activityi

S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine.1 Publication

Kineticsi

kcat is 0.09 min(-1) for carnosine. kcat is 3.57 min(-1) for S-adenosyl-L-methionine.1 Publication

  1. KM=4.959 mM for carnosine1 Publication
  2. KM=0.053 mM for S-adenosyl-L-methionine1 Publication
  1. Vmax=1.77 nmol/min/mg enzyme with carnosine as substrate1 Publication

pH dependencei

Optimum pH is 7.0-7.5.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

GO - Molecular functioni

  • carnosine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • carnosine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Carnosine N-methyltransferase1 PublicationImported (EC:2.1.1.221 Publication)
Gene namesi
Name:CARNMT1Imported
Synonyms:C9orf41Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:23435. CARNMT1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134929393.

Polymorphism and mutation databases

BioMutaiC9orf41.
DMDMi68565210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Carnosine N-methyltransferasePRO_0000089685Add
BLAST

Proteomic databases

EPDiQ8N4J0.
MaxQBiQ8N4J0.
PaxDbiQ8N4J0.
PRIDEiQ8N4J0.

PTM databases

iPTMnetiQ8N4J0.
PhosphoSiteiQ8N4J0.

Expressioni

Tissue specificityi

Expressed at higher level in kidney. Expressed at lower level in brain and skeletal musclea.1 Publication

Gene expression databases

BgeeiQ8N4J0.
CleanExiHS_C9orf41.
ExpressionAtlasiQ8N4J0. baseline and differential.
GenevisibleiQ8N4J0. HS.

Organism-specific databases

HPAiHPA026756.

Interactioni

Protein-protein interaction databases

BioGridi126504. 41 interactions.
STRINGi9606.ENSP00000366030.

Structurei

3D structure databases

ProteinModelPortaliQ8N4J0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2798. Eukaryota.
ENOG410Z0B7. LUCA.
GeneTreeiENSGT00390000005323.
HOGENOMiHOG000204444.
HOVERGENiHBG055166.
InParanoidiQ8N4J0.
KOiK19787.
OMAiAYNCVAT.
PhylomeDBiQ8N4J0.
TreeFamiTF313564.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR012901. N2227.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF07942. N2227. 1 hit.
[Graphical view]
SMARTiSM01296. N2227. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8N4J0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRRRRPPPP TSRLPEGCGG GGGGSEEVEV QFSAGRWGSA AAVSAAAAAA
60 70 80 90 100
TRSTEEEEER LEREHFWKII NAFRYYGTSM HERVNRTERQ FRSLPANQQK
110 120 130 140 150
LLPQFLLHLD KIRKCIDHNQ EILLTIVNDC IHMFENKEYG EDGNGKIMPA
160 170 180 190 200
STFDMDKLKS TLKQFVRDWS ETGKAERDAC YQPIIKEILK NFPKERWDPS
210 220 230 240 250
KVNILVPGAG LGRLAWEIAM LGYACQGNEW SFFMLFSSNF VLNRCSEINK
260 270 280 290 300
YKLYPWIHQF SNNRRSADQI RPIFFPDVDP HSLPPGSNFS MTAGDFQEIY
310 320 330 340 350
SECNTWDCIA TCFFIDTAHN VIDYIDTIWK ILKPGGIWIN LGPLLYHFEN
360 370 380 390 400
LANELSIELS YEDIKNVVLQ YGFKVEVEKE SVLSTYTVND LSMMKYYYEC

VLFVVRKPQ
Length:409
Mass (Da):47,186
Last modified:October 1, 2002 - v1
Checksum:i458584B41E1794EF
GO

Sequence cautioni

The sequence BAC05369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti333 – 3331K → R in CAD97992 (PubMed:17974005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL158825 Genomic DNA. Translation: CAI12577.1.
BC034033 mRNA. Translation: AAH34033.1.
BX538061 mRNA. Translation: CAD97992.1.
AK098661 mRNA. Translation: BAC05369.1. Different initiation.
CCDSiCCDS6649.1.
RefSeqiNP_001307426.1. NM_001320497.1.
NP_689633.1. NM_152420.2.
UniGeneiHs.567688.

Genome annotation databases

EnsembliENST00000376834; ENSP00000366030; ENSG00000156017.
GeneIDi138199.
KEGGihsa:138199.
UCSCiuc004ajq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL158825 Genomic DNA. Translation: CAI12577.1.
BC034033 mRNA. Translation: AAH34033.1.
BX538061 mRNA. Translation: CAD97992.1.
AK098661 mRNA. Translation: BAC05369.1. Different initiation.
CCDSiCCDS6649.1.
RefSeqiNP_001307426.1. NM_001320497.1.
NP_689633.1. NM_152420.2.
UniGeneiHs.567688.

3D structure databases

ProteinModelPortaliQ8N4J0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126504. 41 interactions.
STRINGi9606.ENSP00000366030.

PTM databases

iPTMnetiQ8N4J0.
PhosphoSiteiQ8N4J0.

Polymorphism and mutation databases

BioMutaiC9orf41.
DMDMi68565210.

Proteomic databases

EPDiQ8N4J0.
MaxQBiQ8N4J0.
PaxDbiQ8N4J0.
PRIDEiQ8N4J0.

Protocols and materials databases

DNASUi138199.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376834; ENSP00000366030; ENSG00000156017.
GeneIDi138199.
KEGGihsa:138199.
UCSCiuc004ajq.4. human.

Organism-specific databases

CTDi138199.
GeneCardsiC9orf41.
H-InvDBHIX0201379.
HGNCiHGNC:23435. CARNMT1.
HPAiHPA026756.
MIMi616552. gene.
neXtProtiNX_Q8N4J0.
PharmGKBiPA134929393.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2798. Eukaryota.
ENOG410Z0B7. LUCA.
GeneTreeiENSGT00390000005323.
HOGENOMiHOG000204444.
HOVERGENiHBG055166.
InParanoidiQ8N4J0.
KOiK19787.
OMAiAYNCVAT.
PhylomeDBiQ8N4J0.
TreeFamiTF313564.

Miscellaneous databases

GenomeRNAii138199.
NextBioi83758.
PROiQ8N4J0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N4J0.
CleanExiHS_C9orf41.
ExpressionAtlasiQ8N4J0. baseline and differential.
GenevisibleiQ8N4J0. HS.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR012901. N2227.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF07942. N2227. 1 hit.
[Graphical view]
SMARTiSM01296. N2227. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-409.
    Tissue: Uterine endothelium.
  4. "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] OF 129-409.
    Tissue: Testis.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "UPF0586 protein C9orf41 homolog is anserine-producing methyltransferase."
    Drozak J., Piecuch M., Poleszak O., Kozlowski P., Chrobok L., Baelde H.J., de Heer E.
    J. Biol. Chem. 290:17190-17205(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCARME_HUMAN
AccessioniPrimary (citable) accession number: Q8N4J0
Secondary accession number(s): Q7Z383, Q8N7C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 98 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.