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Protein

Methionine adenosyltransferase 2 subunit beta

Gene

MAT2B

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

Functioni

Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine (PubMed:10644686, PubMed:23189196, PubMed:25075345). Can bind NADP (in vitro) (PubMed:23189196, PubMed:23425511).4 Publications

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.3 Publications
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine adenosyltransferase 2 subunit beta (MAT2B), S-adenosylmethionine synthase isoform type-1 (MAT1A), S-adenosylmethionine synthase, S-adenosylmethionine synthase, S-adenosylmethionine synthase isoform type-2 (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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei93NADP; via carbonyl oxygenCombined sources1
Binding sitei97NADPCombined sources1
Binding sitei159NADPCombined sources1
Binding sitei185NADP; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi37 – 40NADPCombined sources4
Nucleotide bindingi60 – 62NADPCombined sources3
Nucleotide bindingi71 – 72NADPCombined sources2

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • methionine adenosyltransferase regulator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciZFISH:HS00531-MONOMER.
BRENDAi2.5.1.6. 2681.
ReactomeiR-HSA-156581. Methylation.
R-HSA-5689880. Ub-specific processing proteases.
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
Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase
Gene namesi
Name:MAT2B
Synonyms:TGR
ORF Names:MSTP045, Nbla02999, UNQ2435/PRO4995
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6905. MAT2B.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intracellular Source: UniProtKB
  • methionine adenosyltransferase complex Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi27430.
OpenTargetsiENSG00000038274.
PharmGKBiPA30648.

Chemistry databases

DrugBankiDB00134. L-Methionine.

Polymorphism and mutation databases

DMDMi74719662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002875202 – 334Methionine adenosyltransferase 2 subunit betaAdd BLAST333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei309PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NZL9.
MaxQBiQ9NZL9.
PaxDbiQ9NZL9.
PeptideAtlasiQ9NZL9.
PRIDEiQ9NZL9.

2D gel databases

REPRODUCTION-2DPAGEIPI00002324.

PTM databases

iPTMnetiQ9NZL9.
PhosphoSitePlusiQ9NZL9.
SwissPalmiQ9NZL9.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiENSG00000038274.
ExpressionAtlasiQ9NZL9. baseline and differential.
GenevisibleiQ9NZL9. HS.

Organism-specific databases

HPAiHPA037721.
HPA037722.

Interactioni

Subunit structurei

Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain (PubMed:10644686, PubMed:23189196). Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain (PubMed:25075345). NADP binding increases the affinity for MAT2A (PubMed:23189196).1 Publication2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA3Q8IYQ93EBI-10317491,EBI-742146
KPNA4O006293EBI-10317491,EBI-396343
MAT2AP311533EBI-10317491,EBI-1050743
TRIM27P143733EBI-10317491,EBI-719493

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118166. 39 interactors.
IntActiQ9NZL9. 6 interactors.
MINTiMINT-2819994.
STRINGi9606.ENSP00000325425.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 34Combined sources5
Turni35 – 37Combined sources3
Helixi39 – 49Combined sources11
Turni50 – 52Combined sources3
Beta strandi54 – 58Combined sources5
Turni60 – 62Combined sources3
Turni64 – 66Combined sources3
Beta strandi67 – 69Combined sources3
Helixi79 – 85Combined sources7
Beta strandi88 – 92Combined sources5
Helixi99 – 104Combined sources6
Helixi106 – 113Combined sources8
Helixi115 – 126Combined sources12
Beta strandi130 – 136Combined sources7
Helixi137 – 139Combined sources3
Beta strandi142 – 144Combined sources3
Helixi158 – 173Combined sources16
Beta strandi178 – 182Combined sources5
Beta strandi184 – 186Combined sources3
Helixi192 – 194Combined sources3
Helixi198 – 200Combined sources3
Helixi201 – 205Combined sources5
Beta strandi207 – 209Combined sources3
Beta strandi211 – 214Combined sources4
Beta strandi216 – 219Combined sources4
Helixi224 – 239Combined sources16
Beta strandi246 – 249Combined sources4
Helixi258 – 268Combined sources11
Beta strandi276 – 279Combined sources4
Beta strandi285 – 287Combined sources3
Helixi298 – 302Combined sources5
Helixi311 – 319Combined sources9
Helixi320 – 322Combined sources3
Helixi324 – 327Combined sources4
Turni330 – 333Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YDXX-ray2.80A/B/C/D/E28-334[»]
2YDYX-ray2.25A28-334[»]
4KTTX-ray2.59E/F22-334[»]
4KTVX-ray3.30E/F22-334[»]
4NDNX-ray2.34E/F22-334[»]
ProteinModelPortaliQ9NZL9.
SMRiQ9NZL9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZL9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni319 – 334Required for interaction with MAT2A1 PublicationAdd BLAST16

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IQ9F. Eukaryota.
COG1091. LUCA.
GeneTreeiENSGT00390000006721.
HOVERGENiHBG105851.
InParanoidiQ9NZL9.
KOiK00789.
OMAiYKMDHYA.
OrthoDBiEOG091G0AS1.
PhylomeDBiQ9NZL9.
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 (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZL9-1) [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 HFVPGSCRLV EEEVNIPNRR VLVTGATGLL GRAVHKEFQQ
60 70 80 90 100
NNWHAVGCGF RRARPKFEQV NLLDSNAVHH IIHDFQPHVI VHCAAERRPD
110 120 130 140 150
VVENQPDAAS QLNVDASGNL AKEAAAVGAF LIYISSDYVF DGTNPPYREE
160 170 180 190 200
DIPAPLNLYG KTKLDGEKAV LENNLGAAVL RIPILYGEVE KLEESAVTVM
210 220 230 240 250
FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML DPSIKGTFHW
260 270 280 290 300
SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCSKL
310 320 330
ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH
Length:334
Mass (Da):37,552
Last modified:October 1, 2000 - v1
Checksum:i6AAA5381BAF3F65F
GO
Isoform 2 (identifier: Q9NZL9-2) [UniParc]FASTAAdd to basket

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

Show »
Length:323
Mass (Da):36,401
Checksum:i4B2197246063E711
GO
Isoform 3 (identifier: Q9NZL9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     241-259: DPSIKGTFHWSGNEQMTKY → VRRIPESCLSEGPLCLFHA
     260-334: Missing.

Note: No experimental confirmation available.
Show »
Length:259
Mass (Da):28,954
Checksum:i7F4682A780B15E47
GO
Isoform 4 (identifier: Q9NZL9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MVGREKELSIHFVPGSCRLVE → MPEMPEDMEQ
     279-295: Missing.

Show »
Length:306
Mass (Da):34,583
Checksum:iECF509E5B6BE02EF
GO
Isoform 5 (identifier: Q9NZL9-5) [UniParc]FASTAAdd to basket

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

Show »
Length:83
Mass (Da):9,488
Checksum:iF471368C041DE99A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti150E → G in AAH93030 (PubMed:15489334).Curated1
Sequence conflicti302T → I in AAH66645 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032318293A → T.1 PublicationCorresponds to variant rs17849948dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0255341 – 21MVGRE…CRLVE → MPEMPEDMEQ in isoform 2 and isoform 4. 4 PublicationsAdd BLAST21
Alternative sequenceiVSP_0255351 – 20MVGRE…SCRLV → MPEMPEDMEQ in isoform 5. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_02553687 – 93PHVIVHC → VLLTALS in isoform 5. 1 Publication7
Alternative sequenceiVSP_02553794 – 334Missing in isoform 5. 1 PublicationAdd BLAST241
Alternative sequenceiVSP_025538241 – 259DPSIK…QMTKY → VRRIPESCLSEGPLCLFHA in isoform 3. 1 PublicationAdd BLAST19
Alternative sequenceiVSP_025539260 – 334Missing in isoform 3. 1 PublicationAdd BLAST75
Alternative sequenceiVSP_025540279 – 295Missing in isoform 4. 1 PublicationAdd BLAST17

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4364.1. [Q9NZL9-2]
CCDS4365.1. [Q9NZL9-1]
RefSeqiNP_037415.1. NM_013283.4. [Q9NZL9-1]
NP_877725.1. NM_182796.2. [Q9NZL9-2]
UniGeneiHs.54642.

Genome annotation databases

EnsembliENST00000280969; ENSP00000280969; ENSG00000038274. [Q9NZL9-2]
ENST00000321757; ENSP00000325425; ENSG00000038274. [Q9NZL9-1]
ENST00000518095; ENSP00000428046; ENSG00000038274. [Q9NZL9-3]
GeneIDi27430.
KEGGihsa:27430.
UCSCiuc003lzj.5. human. [Q9NZL9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4364.1. [Q9NZL9-2]
CCDS4365.1. [Q9NZL9-1]
RefSeqiNP_037415.1. NM_013283.4. [Q9NZL9-1]
NP_877725.1. NM_182796.2. [Q9NZL9-2]
UniGeneiHs.54642.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YDXX-ray2.80A/B/C/D/E28-334[»]
2YDYX-ray2.25A28-334[»]
4KTTX-ray2.59E/F22-334[»]
4KTVX-ray3.30E/F22-334[»]
4NDNX-ray2.34E/F22-334[»]
ProteinModelPortaliQ9NZL9.
SMRiQ9NZL9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118166. 39 interactors.
IntActiQ9NZL9. 6 interactors.
MINTiMINT-2819994.
STRINGi9606.ENSP00000325425.

Chemistry databases

DrugBankiDB00134. L-Methionine.

PTM databases

iPTMnetiQ9NZL9.
PhosphoSitePlusiQ9NZL9.
SwissPalmiQ9NZL9.

Polymorphism and mutation databases

DMDMi74719662.

2D gel databases

REPRODUCTION-2DPAGEIPI00002324.

Proteomic databases

EPDiQ9NZL9.
MaxQBiQ9NZL9.
PaxDbiQ9NZL9.
PeptideAtlasiQ9NZL9.
PRIDEiQ9NZL9.

Protocols and materials databases

DNASUi27430.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280969; ENSP00000280969; ENSG00000038274. [Q9NZL9-2]
ENST00000321757; ENSP00000325425; ENSG00000038274. [Q9NZL9-1]
ENST00000518095; ENSP00000428046; ENSG00000038274. [Q9NZL9-3]
GeneIDi27430.
KEGGihsa:27430.
UCSCiuc003lzj.5. human. [Q9NZL9-1]

Organism-specific databases

CTDi27430.
DisGeNETi27430.
GeneCardsiMAT2B.
HGNCiHGNC:6905. MAT2B.
HPAiHPA037721.
HPA037722.
MIMi605527. gene.
neXtProtiNX_Q9NZL9.
OpenTargetsiENSG00000038274.
PharmGKBiPA30648.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQ9F. Eukaryota.
COG1091. LUCA.
GeneTreeiENSGT00390000006721.
HOVERGENiHBG105851.
InParanoidiQ9NZL9.
KOiK00789.
OMAiYKMDHYA.
OrthoDBiEOG091G0AS1.
PhylomeDBiQ9NZL9.
TreeFamiTF332849.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciZFISH:HS00531-MONOMER.
BRENDAi2.5.1.6. 2681.
ReactomeiR-HSA-156581. Methylation.
R-HSA-5689880. Ub-specific processing proteases.

Miscellaneous databases

ChiTaRSiMAT2B. human.
EvolutionaryTraceiQ9NZL9.
GenomeRNAii27430.
PROiQ9NZL9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000038274.
ExpressionAtlasiQ9NZL9. baseline and differential.
GenevisibleiQ9NZL9. HS.

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...

Entry informationi

Entry nameiMAT2B_HUMAN
AccessioniPrimary (citable) accession number: Q9NZL9
Secondary accession number(s): B2R5Y6
, Q1WAI7, Q27J92, Q3LIE8, Q567T7, Q6NYC7, Q9BS89, Q9H3E1, Q9UJ54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 135 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

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.