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Protein

Methionine adenosyltransferase 2 subunit beta

Gene

Mat2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S-adenosylmethionine inhibition.

Pathwayi: S-adenosyl-L-methionine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase isoform type-2 (Mat2a), Methionine adenosyltransferase 2 subunit beta (Mat2b), S-adenosylmethionine synthase isoform type-1 (Mat1a), S-adenosylmethionine synthase (Mat2a), S-adenosylmethionine synthase (Mat2a)
This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

One-carbon metabolism

Enzyme and pathway databases

ReactomeiR-MMU-156581. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine adenosyltransferase 2 subunit beta
Alternative name(s):
Methionine adenosyltransferase II beta
Short name:
MAT II beta
Gene namesi
Name:Mat2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1913667. Mat2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 334333Methionine adenosyltransferase 2 subunit betaPRO_0000287521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99LB6.
MaxQBiQ99LB6.
PaxDbiQ99LB6.
PeptideAtlasiQ99LB6.
PRIDEiQ99LB6.

2D gel databases

REPRODUCTION-2DPAGEIPI00649402.
Q99LB6.

PTM databases

iPTMnetiQ99LB6.
PhosphoSiteiQ99LB6.

Expressioni

Gene expression databases

BgeeiQ99LB6.
CleanExiMM_MAT2B.
ExpressionAtlasiQ99LB6. baseline and differential.
GenevisibleiQ99LB6. MM.

Interactioni

Subunit structurei

Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi224352. 1 interaction.
IntActiQ99LB6. 3 interactions.
MINTiMINT-1869783.
STRINGi10090.ENSMUSP00000048222.

Structurei

3D structure databases

ProteinModelPortaliQ99LB6.
SMRiQ99LB6. Positions 26-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IQ9F. Eukaryota.
COG1091. LUCA.
GeneTreeiENSGT00390000006721.
HOGENOMiHOG000227713.
HOVERGENiHBG105851.
InParanoidiQ99LB6.
KOiK00789.
OMAiFTKYEIC.
OrthoDBiEOG74FF26.
PhylomeDBiQ99LB6.
TreeFamiTF332849.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
IPR029903. RmlD-like-bd.
[Graphical view]
PANTHERiPTHR10491. PTHR10491. 1 hit.
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

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. AlignAdd to basket

Isoform 1 (identifier: Q99LB6-1) [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

        10         20         30         40         50
MVGREKELSI HFVPGCCQLV EEEVNIPSRR VLITGATGLL GRAVYKEFQQ
60 70 80 90 100
SNWHTVGCGF RRARPKFEQV NLLDSEAVHH LIHDFQPHVI VHCAAERRPD
110 120 130 140 150
VVESQPDAAS QLNVGASGNL AKEAAAIGAF LIYISSDYVF DGTNPPYTEE
160 170 180 190 200
DIPSPLNLYG KTKLDGEKAV LENNLGAAVL RIPVLYGEVE KLEESAVTVM
210 220 230 240 250
FDKVQFSNKS ANMDHWQQRF PTHVKDVASV CRQLAEKRML DPSIKGTFHW
260 270 280 290 300
SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVIGAQRP KNAQLDCSKL
310 320 330
ETLGIGQRTP FRTGIKESLW PFLIDKRWRQ TVFH
Length:334
Mass (Da):37,393
Last modified:June 1, 2001 - v1
Checksum:i0B209731D713BD02
GO
Isoform 2 (identifier: Q99LB6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MVGREKELSIHFVPGCCQLVE → MPEMPEAMEQ

Show »
Length:323
Mass (Da):36,210
Checksum:i95CAF37E602D6949
GO

Sequence cautioni

The sequence BAC29963.1 differs from that shown.Intron retention.Curated
The sequence CAI25424.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971R → G in BAD06938 (PubMed:16022199).Curated
Sequence conflicti140 – 1401F → L in BAD06938 (PubMed:16022199).Curated
Sequence conflicti170 – 1701V → A in BAD06938 (PubMed:16022199).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MVGRE…CQLVE → MPEMPEAMEQ in isoform 2. 1 PublicationVSP_025541Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070267 mRNA. Translation: BAD06938.1.
AK038303 mRNA. Translation: BAC29963.1. Sequence problems.
AK075947 mRNA. Translation: BAC36076.1.
AK162087 mRNA. Translation: BAE36716.1.
AL646055 Genomic DNA. Translation: CAI25424.1. Sequence problems.
AL646055 Genomic DNA. Translation: CAI25422.1.
AL646055 Genomic DNA. Translation: CAI25423.1.
BC003457 mRNA. Translation: AAH03457.1.
CCDSiCCDS24547.1. [Q99LB6-1]
CCDS56767.1. [Q99LB6-2]
RefSeqiNP_001186203.1. NM_001199274.1. [Q99LB6-2]
NP_598778.1. NM_134017.2. [Q99LB6-1]
UniGeneiMm.293771.

Genome annotation databases

EnsembliENSMUST00000040167; ENSMUSP00000048222; ENSMUSG00000042032. [Q99LB6-1]
ENSMUST00000101347; ENSMUSP00000098901; ENSMUSG00000042032. [Q99LB6-2]
GeneIDi108645.
KEGGimmu:108645.
UCSCiuc007ilp.2. mouse. [Q99LB6-1]
uc007ilq.2. mouse. [Q99LB6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070267 mRNA. Translation: BAD06938.1.
AK038303 mRNA. Translation: BAC29963.1. Sequence problems.
AK075947 mRNA. Translation: BAC36076.1.
AK162087 mRNA. Translation: BAE36716.1.
AL646055 Genomic DNA. Translation: CAI25424.1. Sequence problems.
AL646055 Genomic DNA. Translation: CAI25422.1.
AL646055 Genomic DNA. Translation: CAI25423.1.
BC003457 mRNA. Translation: AAH03457.1.
CCDSiCCDS24547.1. [Q99LB6-1]
CCDS56767.1. [Q99LB6-2]
RefSeqiNP_001186203.1. NM_001199274.1. [Q99LB6-2]
NP_598778.1. NM_134017.2. [Q99LB6-1]
UniGeneiMm.293771.

3D structure databases

ProteinModelPortaliQ99LB6.
SMRiQ99LB6. Positions 26-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224352. 1 interaction.
IntActiQ99LB6. 3 interactions.
MINTiMINT-1869783.
STRINGi10090.ENSMUSP00000048222.

PTM databases

iPTMnetiQ99LB6.
PhosphoSiteiQ99LB6.

2D gel databases

REPRODUCTION-2DPAGEIPI00649402.
Q99LB6.

Proteomic databases

EPDiQ99LB6.
MaxQBiQ99LB6.
PaxDbiQ99LB6.
PeptideAtlasiQ99LB6.
PRIDEiQ99LB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040167; ENSMUSP00000048222; ENSMUSG00000042032. [Q99LB6-1]
ENSMUST00000101347; ENSMUSP00000098901; ENSMUSG00000042032. [Q99LB6-2]
GeneIDi108645.
KEGGimmu:108645.
UCSCiuc007ilp.2. mouse. [Q99LB6-1]
uc007ilq.2. mouse. [Q99LB6-2]

Organism-specific databases

CTDi27430.
MGIiMGI:1913667. Mat2b.

Phylogenomic databases

eggNOGiENOG410IQ9F. Eukaryota.
COG1091. LUCA.
GeneTreeiENSGT00390000006721.
HOGENOMiHOG000227713.
HOVERGENiHBG105851.
InParanoidiQ99LB6.
KOiK00789.
OMAiFTKYEIC.
OrthoDBiEOG74FF26.
PhylomeDBiQ99LB6.
TreeFamiTF332849.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
ReactomeiR-MMU-156581. Methylation.

Miscellaneous databases

PROiQ99LB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LB6.
CleanExiMM_MAT2B.
ExpressionAtlasiQ99LB6. baseline and differential.
GenevisibleiQ99LB6. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
IPR029903. RmlD-like-bd.
[Graphical view]
PANTHERiPTHR10491. PTHR10491. 1 hit.
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Effect of fasting on methionine adenosyltransferase expression and the methionine cycle in the mouse liver."
    Sakata S.F., Okumura S., Matsuda K., Horikawa Y., Maeda M., Kawasaki K., Chou J.Y., Tamaki N.
    J. Nutr. Sci. Vitaminol. 51:118-123(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ddY.
    Tissue: Kidney.
  2. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-86 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Egg.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMAT2B_MOUSE
AccessioniPrimary (citable) accession number: Q99LB6
Secondary accession number(s): Q5NC89
, Q76LX2, Q8BVX6, Q8BYT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 103 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.