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Q9NZL9 (MAT2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine adenosyltransferase 2 subunit beta
Alternative name(s):
Methionine adenosyltransferase II beta
Short name=MAT II beta
Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase
Gene names
Name:MAT2B
Synonyms:TGR
ORF Names:MSTP045, Nbla02999, UNQ2435/PRO4995
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.

Subunit structure

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

Tissue specificity

Widely expressed. Ref.1 Ref.11

Miscellaneous

Its expression in hepatoma cell lines may lead to increase DNA synthesis and thereby participate in cell proliferation.

Sequence similarities

Belongs to the dTDP-4-dehydrorhamnose reductase family. MAT2B subfamily.

Sequence caution

The sequence AAG39296.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processS-adenosylmethionine biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

extracellular polysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

methylation

Traceable author statement. Source: Reactome

one-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of catalytic activity

Inferred from direct assay Ref.1. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

intracellular

Inferred by curator Ref.1. Source: UniProtKB

methionine adenosyltransferase complex

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: LIFEdb

   Molecular_functiondTDP-4-dehydrorhamnose reductase activity

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from physical interaction Ref.1. Source: UniProtKB

methionine adenosyltransferase regulator activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZL9-1)

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.
Isoform 2 (identifier: Q9NZL9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MVGREKELSIHFVPGSCRLVE → MPEMPEDMEQ
Isoform 3 (identifier: Q9NZL9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     241-259: DPSIKGTFHWSGNEQMTKY → VRRIPESCLSEGPLCLFHA
     260-334: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9NZL9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MVGREKELSIHFVPGSCRLVE → MPEMPEDMEQ
     279-295: Missing.
Isoform 5 (identifier: Q9NZL9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MVGREKELSIHFVPGSCRLV → MPEMPEDMEQ
     87-93: PHVIVHC → VLLTALS
     94-334: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 334333Methionine adenosyltransferase 2 subunit beta
PRO_0000287520

Natural variations

Alternative sequence1 – 2121MVGRE…CRLVE → MPEMPEDMEQ in isoform 2 and isoform 4.
VSP_025534
Alternative sequence1 – 2020MVGRE…SCRLV → MPEMPEDMEQ in isoform 5.
VSP_025535
Alternative sequence87 – 937PHVIVHC → VLLTALS in isoform 5.
VSP_025536
Alternative sequence94 – 334241Missing in isoform 5.
VSP_025537
Alternative sequence241 – 25919DPSIK…QMTKY → VRRIPESCLSEGPLCLFHA in isoform 3.
VSP_025538
Alternative sequence260 – 33475Missing in isoform 3.
VSP_025539
Alternative sequence279 – 29517Missing in isoform 4.
VSP_025540
Natural variant2931A → T. Ref.9
Corresponds to variant rs17849948 [ dbSNP | Ensembl ].
VAR_032318

Experimental info

Sequence conflict1501E → G in AAH93030. Ref.9
Sequence conflict3021T → I in AAH66645. Ref.9

Secondary structure

........................................................... 334
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6AAA5381BAF3F65F

FASTA33437,552
        10         20         30         40         50         60 
MVGREKELSI HFVPGSCRLV EEEVNIPNRR VLVTGATGLL GRAVHKEFQQ NNWHAVGCGF 

        70         80         90        100        110        120 
RRARPKFEQV NLLDSNAVHH IIHDFQPHVI VHCAAERRPD VVENQPDAAS QLNVDASGNL 

       130        140        150        160        170        180 
AKEAAAVGAF LIYISSDYVF DGTNPPYREE DIPAPLNLYG KTKLDGEKAV LENNLGAAVL 

       190        200        210        220        230        240 
RIPILYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML 

       250        260        270        280        290        300 
DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCSKL 

       310        320        330 
ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH 

« Hide

Isoform 2 [UniParc].

Checksum: 4B2197246063E711
Show »

FASTA32336,401
Isoform 3 [UniParc].

Checksum: 7F4682A780B15E47
Show »

FASTA25928,954
Isoform 4 [UniParc].

Checksum: ECF509E5B6BE02EF
Show »

FASTA30634,583
Isoform 5 [UniParc].

Checksum: F471368C041DE99A
Show »

FASTA839,488

References

« Hide 'large scale' references
[1]"Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II)."
LeGros H.L., Halim A.-B., Geller A.M., Kotb M.
J. Biol. Chem. 275:2359-2366(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-20 AND 240-257, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.
[2]"Occurrence of a novel metabolic pathway converting dTDP-D-glucose in human cells."
Sturla L., Zanardi D., Bisso A., Damonte G., Fasano M., De Flora A., Tonetti M.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Alternative splicing of the MAT2B gene."
Yang H., Magilnick N., Lu S.C.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Neuroblastoma.
[6]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]"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. expand/collapse author list , 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 1).
Tissue: Amygdala.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 1 AND 2), VARIANT THR-293.
Tissue: Pancreas, Placenta and Skin.
[10]Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. expand/collapse author list , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-334.
Tissue: Heart.
[11]"Regulation of the human MAT2B gene encoding the regulatory beta subunit of methionine adenosyltransferase, MAT II."
LeGros L., Halim A.-B., Chamberlin M.E., Geller A., Kotb M.
J. Biol. Chem. 276:24918-24924(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Methionine adenosyltransferase II beta subunit gene expression provides a proliferative advantage in human hepatoma."
Martinez-Chantar M.L., Garcia-Trevijano E.R., Latasa M.U., Martin-Duce A., Fortes P., Caballeria J., Avila M.A., Mato J.M.
Gastroenterology 124:940-948(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPRESSION IN HEPATOMA.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182814 mRNA. Translation: AAF28477.1.
AJ243721 mRNA. Translation: CAB56837.1.
DQ395260 mRNA. Translation: ABD59011.1.
DQ413183 mRNA. Translation: ABD85290.1.
AL136664 mRNA. Translation: CAB66599.1.
AB073390 mRNA. Translation: BAE45720.1.
AY358695 mRNA. Translation: AAQ89058.1.
AK312365 mRNA. Translation: BAG35283.1.
CH471062 Genomic DNA. Translation: EAW61517.1.
BC005218 mRNA. Translation: AAH05218.1.
BC066645 mRNA. Translation: AAH66645.1.
BC093030 mRNA. Translation: AAH93030.1.
AF113225 mRNA. Translation: AAG39296.1. Different initiation.
RefSeqNP_037415.1. NM_013283.4.
NP_877725.1. NM_182796.2.
UniGeneHs.54642.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YDXX-ray2.80A/B/C/D/E28-334[»]
2YDYX-ray2.25A28-334[»]
ProteinModelPortalQ9NZL9.
SMRQ9NZL9. Positions 28-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118166. 30 interactions.
MINTMINT-2819994.

Chemistry

DrugBankDB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

PTM databases

PhosphoSiteQ9NZL9.

Polymorphism databases

DMDM74719662.

2D gel databases

REPRODUCTION-2DPAGEIPI00002324.

Proteomic databases

PaxDbQ9NZL9.
PRIDEQ9NZL9.

Protocols and materials databases

DNASU27430.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280969; ENSP00000280969; ENSG00000038274. [Q9NZL9-2]
ENST00000321757; ENSP00000325425; ENSG00000038274. [Q9NZL9-1]
ENST00000518095; ENSP00000428046; ENSG00000038274. [Q9NZL9-3]
GeneID27430.
KEGGhsa:27430.
UCSCuc003lzj.4. human. [Q9NZL9-2]
uc003lzk.4. human. [Q9NZL9-1]
uc003lzl.2. human. [Q9NZL9-3]

Organism-specific databases

CTD27430.
GeneCardsGC05P162930.
HGNCHGNC:6905. MAT2B.
HPAHPA037721.
HPA037722.
MIM605527. gene.
neXtProtNX_Q9NZL9.
PharmGKBPA30648.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1091.
HOVERGENHBG105851.
InParanoidQ9NZL9.
KOK00789.
OMAYDCHLST.
OrthoDBEOG74FF26.
PhylomeDBQ9NZL9.
TreeFamTF332849.

Enzyme and pathway databases

BRENDA2.5.1.6. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00315; UER00080.

Gene expression databases

ArrayExpressQ9NZL9.
BgeeQ9NZL9.
GenevestigatorQ9NZL9.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAT2B. human.
EvolutionaryTraceQ9NZL9.
GenomeRNAi27430.
NextBio50469.
PROQ9NZL9.
SOURCESearch...

Entry information

Entry nameMAT2B_HUMAN
AccessionPrimary (citable) accession number: Q9NZL9
Secondary accession number(s): B2R5Y6 expand/collapse secondary AC list , Q1WAI7, Q27J92, Q3LIE8, Q567T7, Q6NYC7, Q9BS89, Q9H3E1, Q9UJ54
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM