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Q9NZL9

- MAT2B_HUMAN

UniProt

Q9NZL9 - MAT2B_HUMAN

Protein

Methionine adenosyltransferase 2 subunit beta

Gene

MAT2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. dTDP-4-dehydrorhamnose reductase activity Source: InterPro
    2. enzyme binding Source: UniProtKB
    3. methionine adenosyltransferase regulator activity Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. extracellular polysaccharide biosynthetic process Source: InterPro
    3. methylation Source: Reactome
    4. one-carbon metabolic process Source: UniProtKB-KW
    5. regulation of catalytic activity Source: GOC
    6. S-adenosylmethionine biosynthetic process Source: UniProtKB
    7. small molecule metabolic process Source: Reactome
    8. sulfur amino acid metabolic process Source: Reactome
    9. xenobiotic metabolic process Source: Reactome

    Keywords - Biological processi

    One-carbon metabolism

    Enzyme and pathway databases

    BRENDAi2.5.1.6. 2681.
    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_6946. 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
    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
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6905. MAT2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. intracellular Source: UniProtKB
    3. methionine adenosyltransferase complex Source: UniProtKB
    4. mitochondrion Source: Ensembl
    5. nucleus Source: LIFEdb

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30648.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 334333Methionine adenosyltransferase 2 subunit betaPRO_0000287520Add
    BLAST

    Proteomic databases

    MaxQBiQ9NZL9.
    PaxDbiQ9NZL9.
    PRIDEiQ9NZL9.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00002324.

    PTM databases

    PhosphoSiteiQ9NZL9.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ9NZL9.
    BgeeiQ9NZL9.
    GenevestigatoriQ9NZL9.

    Organism-specific databases

    HPAiHPA037721.
    HPA037722.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi118166. 30 interactions.
    MINTiMINT-2819994.

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 345
    Turni35 – 373
    Helixi39 – 4911
    Turni50 – 523
    Beta strandi54 – 585
    Turni64 – 663
    Beta strandi67 – 693
    Helixi79 – 857
    Beta strandi88 – 925
    Helixi99 – 1046
    Helixi106 – 1138
    Helixi115 – 12612
    Beta strandi130 – 1367
    Helixi137 – 1393
    Beta strandi142 – 1443
    Helixi158 – 17316
    Beta strandi178 – 1825
    Beta strandi184 – 1863
    Helixi192 – 1943
    Helixi198 – 2003
    Helixi201 – 2055
    Beta strandi211 – 2144
    Beta strandi216 – 2194
    Helixi224 – 23916
    Beta strandi246 – 2494
    Helixi258 – 26811
    Beta strandi276 – 2794
    Beta strandi285 – 2873
    Helixi298 – 3025
    Helixi311 – 3199
    Helixi320 – 3223
    Turni330 – 3334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YDXX-ray2.80A/B/C/D/E28-334[»]
    2YDYX-ray2.25A28-334[»]
    ProteinModelPortaliQ9NZL9.
    SMRiQ9NZL9. Positions 28-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZL9.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1091.
    HOVERGENiHBG105851.
    InParanoidiQ9NZL9.
    KOiK00789.
    OMAiFTKYEIC.
    OrthoDBiEOG74FF26.
    PhylomeDBiQ9NZL9.
    TreeFamiTF332849.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005913. dTDP_dehydrorham_reduct.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF04321. RmlD_sub_bind. 1 hit.
    [Graphical view]

    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. Align

    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

    MVGREKELSI HFVPGSCRLV EEEVNIPNRR VLVTGATGLL GRAVHKEFQQ    50
    NNWHAVGCGF RRARPKFEQV NLLDSNAVHH IIHDFQPHVI VHCAAERRPD 100
    VVENQPDAAS QLNVDASGNL AKEAAAVGAF LIYISSDYVF DGTNPPYREE 150
    DIPAPLNLYG KTKLDGEKAV LENNLGAAVL RIPILYGEVE KLEESAVTVM 200
    FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML DPSIKGTFHW 250
    SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCSKL 300
    ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH 334
    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 AAG39296.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501E → G in AAH93030. (PubMed:15489334)Curated
    Sequence conflicti302 – 3021T → I in AAH66645. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti293 – 2931A → T.1 Publication
    Corresponds to variant rs17849948 [ dbSNP | Ensembl ].
    VAR_032318

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2121MVGRE…CRLVE → MPEMPEDMEQ in isoform 2 and isoform 4. 4 PublicationsVSP_025534Add
    BLAST
    Alternative sequencei1 – 2020MVGRE…SCRLV → MPEMPEDMEQ in isoform 5. 1 PublicationVSP_025535Add
    BLAST
    Alternative sequencei87 – 937PHVIVHC → VLLTALS in isoform 5. 1 PublicationVSP_025536
    Alternative sequencei94 – 334241Missing in isoform 5. 1 PublicationVSP_025537Add
    BLAST
    Alternative sequencei241 – 25919DPSIK…QMTKY → VRRIPESCLSEGPLCLFHA in isoform 3. 1 PublicationVSP_025538Add
    BLAST
    Alternative sequencei260 – 33475Missing in isoform 3. 1 PublicationVSP_025539Add
    BLAST
    Alternative sequencei279 – 29517Missing in isoform 4. 1 PublicationVSP_025540Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.4. human. [Q9NZL9-2]
    uc003lzk.4. human. [Q9NZL9-1]
    uc003lzl.2. human. [Q9NZL9-3]

    Polymorphism databases

    DMDMi74719662.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS4364.1. [Q9NZL9-2 ]
    CCDS4365.1. [Q9NZL9-1 ]
    RefSeqi NP_037415.1. NM_013283.4. [Q9NZL9-1 ]
    NP_877725.1. NM_182796.2. [Q9NZL9-2 ]
    UniGenei Hs.54642.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YDX X-ray 2.80 A/B/C/D/E 28-334 [» ]
    2YDY X-ray 2.25 A 28-334 [» ]
    ProteinModelPortali Q9NZL9.
    SMRi Q9NZL9. Positions 28-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118166. 30 interactions.
    MINTi MINT-2819994.

    Chemistry

    DrugBanki DB00134. L-Methionine.
    DB00118. S-Adenosylmethionine.

    PTM databases

    PhosphoSitei Q9NZL9.

    Polymorphism databases

    DMDMi 74719662.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00002324.

    Proteomic databases

    MaxQBi Q9NZL9.
    PaxDbi Q9NZL9.
    PRIDEi Q9NZL9.

    Protocols and materials databases

    DNASUi 27430.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280969 ; ENSP00000280969 ; ENSG00000038274 . [Q9NZL9-2 ]
    ENST00000321757 ; ENSP00000325425 ; ENSG00000038274 . [Q9NZL9-1 ]
    ENST00000518095 ; ENSP00000428046 ; ENSG00000038274 . [Q9NZL9-3 ]
    GeneIDi 27430.
    KEGGi hsa:27430.
    UCSCi uc003lzj.4. human. [Q9NZL9-2 ]
    uc003lzk.4. human. [Q9NZL9-1 ]
    uc003lzl.2. human. [Q9NZL9-3 ]

    Organism-specific databases

    CTDi 27430.
    GeneCardsi GC05P162930.
    HGNCi HGNC:6905. MAT2B.
    HPAi HPA037721.
    HPA037722.
    MIMi 605527. gene.
    neXtProti NX_Q9NZL9.
    PharmGKBi PA30648.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1091.
    HOVERGENi HBG105851.
    InParanoidi Q9NZL9.
    KOi K00789.
    OMAi FTKYEIC.
    OrthoDBi EOG74FF26.
    PhylomeDBi Q9NZL9.
    TreeFami TF332849.

    Enzyme and pathway databases

    UniPathwayi UPA00315 ; UER00080 .
    BRENDAi 2.5.1.6. 2681.
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.

    Miscellaneous databases

    ChiTaRSi MAT2B. human.
    EvolutionaryTracei Q9NZL9.
    GenomeRNAii 27430.
    NextBioi 50469.
    PROi Q9NZL9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZL9.
    Bgeei Q9NZL9.
    Genevestigatori Q9NZL9.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR005913. dTDP_dehydrorham_reduct.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF04321. RmlD_sub_bind. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.
      , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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: October 1, 2014
    This is version 112 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

    External Data

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