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Q9NZL9

- MAT2B_HUMAN

UniProt

Q9NZL9 - MAT2B_HUMAN

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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

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
Complete GO annotation...

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. extracellular vesicular exosome Source: UniProtKB
  3. intracellular Source: UniProtKB
  4. methionine adenosyltransferase complex Source: UniProtKB
  5. mitochondrion Source: Ensembl
  6. nucleus Source: LIFEdb
Complete GO annotation...

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

BgeeiQ9NZL9.
ExpressionAtlasiQ9NZL9. baseline and differential.
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. 32 interactions.
MINTiMINT-2819994.

Structurei

Secondary structure

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

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[»]
4KTTX-ray2.59E/F22-334[»]
4KTVX-ray3.30E/F22-334[»]
4NDNX-ray2.34E/F22-334[»]
ProteinModelPortaliQ9NZL9.
SMRiQ9NZL9. Positions 28-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZL9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1091.
GeneTreeiENSGT00390000006721.
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]
PANTHERiPTHR10491. PTHR10491. 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. 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

        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 AAG39296.1 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 [» ]
4KTT X-ray 2.59 E/F 22-334 [» ]
4KTV X-ray 3.30 E/F 22-334 [» ]
4NDN X-ray 2.34 E/F 22-334 [» ]
ProteinModelPortali Q9NZL9.
SMRi Q9NZL9. Positions 28-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118166. 32 interactions.
MINTi MINT-2819994.

Chemistry

DrugBanki DB00134. L-Methionine.

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.
GeneTreei ENSGT00390000006721.
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

Bgeei Q9NZL9.
ExpressionAtlasi Q9NZL9. baseline and differential.
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 ]
PANTHERi PTHR10491. PTHR10491. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 113 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

Dasty 3