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Q2TBA3

- MALT1_MOUSE

UniProt

Q2TBA3 - MALT1_MOUSE

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Protein

Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog

Gene

Malt1

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

Functioni

Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei423 – 4231Sequence Analysis
Active sitei472 – 4721Sequence Analysis

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro
  2. kinase activator activity Source: Ensembl
  3. protease binding Source: BHF-UCL
  4. signal transducer activity Source: Ensembl
  5. ubiquitin-protein transferase activity Source: Ensembl

GO - Biological processi

  1. activation of NF-kappaB-inducing kinase activity Source: Ensembl
  2. B-1 B cell differentiation Source: MGI
  3. B cell activation Source: MGI
  4. innate immune response Source: UniProtKB
  5. nuclear export Source: Ensembl
  6. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  7. positive regulation of interleukin-2 production Source: Ensembl
  8. positive regulation of NF-kappaB transcription factor activity Source: MGI
  9. positive regulation of T cell activation Source: MGI
  10. positive regulation of T cell cytokine production Source: Ensembl
  11. protein oligomerization Source: Ensembl
  12. regulation of apoptotic process Source: MGI
  13. regulation of T cell receptor signaling pathway Source: MGI
  14. response to fungus Source: MGI
  15. response to molecule of bacterial origin Source: UniProtKB
  16. T cell proliferation Source: MGI
  17. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_199121. Activation of NF-kappaB in B cells.
REACT_205561. FCERI mediated NF-kB activation.
REACT_225145. Downstream TCR signaling.

Protein family/group databases

MEROPSiC14.026.

Names & Taxonomyi

Protein namesi
Recommended name:
Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homolog (EC:3.4.22.-)
Alternative name(s):
Paracaspase
Gene namesi
Name:Malt1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:2445027. Malt1.

Subcellular locationi

Cytoplasmperinuclear region By similarity. Nucleus By similarity
Note: Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10 (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleolus Source: Ensembl
  3. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 832831Mucosa-associated lymphoid tissue lymphoma translocation protein 1 homologPRO_0000272961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei141 – 1411PhosphoserineBy similarity
Disulfide bondi154 ↔ 196PROSITE-ProRule annotation
Disulfide bondi257 ↔ 299PROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ2TBA3.
PaxDbiQ2TBA3.
PRIDEiQ2TBA3.

PTM databases

PhosphoSiteiQ2TBA3.

Expressioni

Gene expression databases

BgeeiQ2TBA3.
GenevestigatoriQ2TBA3.

Interactioni

Subunit structurei

Binds through its Ig-like domains to BCL10. Forms oligomers which bind to TRAF6 (By similarity).By similarity

Protein-protein interaction databases

BioGridi232195. 6 interactions.
DIPiDIP-60308N.

Structurei

Secondary structure

1
832
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi351 – 3577Combined sources
Beta strandi362 – 3643Combined sources
Helixi369 – 38315Combined sources
Beta strandi387 – 3937Combined sources
Helixi396 – 40712Combined sources
Beta strandi415 – 42713Combined sources
Beta strandi430 – 4345Combined sources
Turni444 – 4463Combined sources
Beta strandi447 – 4493Combined sources
Helixi450 – 4589Combined sources
Turni459 – 4613Combined sources
Beta strandi463 – 4719Combined sources
Beta strandi494 – 5007Combined sources
Beta strandi507 – 5093Combined sources
Beta strandi512 – 5143Combined sources
Helixi518 – 5236Combined sources
Turni524 – 5285Combined sources
Helixi533 – 54513Combined sources
Turni548 – 5536Combined sources
Beta strandi557 – 5604Combined sources
Helixi579 – 58911Combined sources
Beta strandi598 – 6014Combined sources
Beta strandi607 – 61610Combined sources
Beta strandi619 – 62810Combined sources
Beta strandi633 – 6419Combined sources
Helixi645 – 6473Combined sources
Helixi651 – 6533Combined sources
Beta strandi654 – 6585Combined sources
Helixi659 – 6624Combined sources
Turni668 – 6703Combined sources
Beta strandi675 – 6806Combined sources
Helixi683 – 6853Combined sources
Beta strandi690 – 70011Combined sources
Beta strandi707 – 71711Combined sources
Helixi719 – 7235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V4LX-ray3.15A338-729[»]
ProteinModelPortaliQ2TBA3.
SMRiQ2TBA3. Positions 48-130, 134-729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 13288DeathSequence AnalysisAdd
BLAST
Domaini131 – 20777Ig-like C2-type 1Sequence AnalysisAdd
BLAST
Domaini218 – 31497Ig-like C2-type 2Sequence AnalysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni356 – 570215Caspase-likeSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi377 – 3848Nuclear export signalBy similarity

Sequence similaritiesi

Belongs to the peptidase C14B family.Curated
Contains 1 death domain.Sequence Analysis
Contains 2 Ig-like C2-type (immunoglobulin-like) domains.Sequence Analysis

Keywords - Domaini

Immunoglobulin domain, Repeat

Phylogenomic databases

eggNOGiCOG4249.
GeneTreeiENSGT00390000018044.
HOGENOMiHOG000113471.
HOVERGENiHBG052402.
InParanoidiQ2TBA3.
KOiK07369.
OMAiMNKEIPN.
OrthoDBiEOG7673BH.
PhylomeDBiQ2TBA3.
TreeFamiTF319744.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
2.60.40.10. 2 hits.
3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR011029. DEATH-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
[Graphical view]
PfamiPF00656. Peptidase_C14. 1 hit.
[Graphical view]
SMARTiSM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50208. CASPASE_P20. 1 hit.
PS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q2TBA3-1) [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
MSLWGQPLQA SPPLAVRQPP TASSGPSTSP PAGATLNRLP EPLLRRLSES
60 70 80 90 100
LDRAPEGRGW RQLAELAGSR GRLRLSGLDL EQCSLKVLEP EGSPSLCLLK
110 120 130 140 150
LMGEKGCTVT ELSDFLQALE HTEVLPLLNP PGLKITVNPE SKAVLAGQFV
160 170 180 190 200
KLCCRATGHP FVQYQWFKMN KEIPYGNSSE LVFNTVHVKD AGFYVCRVNN
210 220 230 240 250
SSTFEFSQWS QLDVCDVAEV TDSFQGSMDG ISESRLQICV EPRSQRLVPG
260 270 280 290 300
SMLLLQCVAI GSPMPHYQWF KDESPLTHET KKHYTVPYVD IEHEGTYWCH
310 320 330 340 350
VYNDRDSQDS KKAEVTIGRT DEAVECTEDE LNNLGHPDNK EQTGQPLAKD
360 370 380 390 400
KVALLIGNMS YWEHPKLKAP LVDVYELTNL LRQLDFKVVS LLDLTEYEMC
410 420 430 440 450
NAVDEFLLLL DKGVYGLLYY AGHGYENFGN SFMVPVDAPN PYRSENCLCV
460 470 480 490 500
QNILKLMQEK ETGLNVFLLD MCRKRNDYDD TIPILDALKV TANIVFGYAT
510 520 530 540 550
CQGAEAFEIQ HSGLANGIFM KFLKDRLLED KKITVLLDEV AEDMGKCHLT
560 570 580 590 600
KGRQALEIRS SLSEKRALTD PVQGAPCSAE ALVRNLQWAK AHELPESMCL
610 620 630 640 650
KFQCGVHIQL GFAAEFSNVM IIYTSIVHKP PEIIMCDAYV TDFPLDLDID
660 670 680 690 700
PKHANKGTPE ETGSYLVSKD LPKHCLYTRL SSLQKLKEHL IFTVCLSYQY
710 720 730 740 750
SGLEDTVEEK QEVNVGKPLI AKLDMHRGLG RKTCFQACRM PDEPYHSSTS
760 770 780 790 800
TSAGAGHFHS SQDSFHDVYH SHLGNADSGM PPDRCHCSRT PHTFISNYPP
810 820 830
HHYCQFGRSN VPVETTDEMP FSFSDRLMIS EN
Length:832
Mass (Da):93,216
Last modified:January 23, 2007 - v2
Checksum:i891D59585A360D68
GO
Isoform 22 Publications (identifier: Q2TBA3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     318-328: Missing.

Show »
Length:821
Mass (Da):92,025
Checksum:iF1B9027E3EC5B6E6
GO
Isoform 31 Publication (identifier: Q2TBA3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-543: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:289
Mass (Da):32,428
Checksum:i78378D64D756224F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 2651P → S in AAI10489. (PubMed:15489334)Curated
Sequence conflicti576 – 5761P → H in AAI10488. (PubMed:15489334)Curated
Sequence conflicti793 – 7931T → A in AAH46536. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 543543Missing in isoform 3. 1 PublicationVSP_052278Add
BLAST
Alternative sequencei318 – 32811Missing in isoform 2. 2 PublicationsVSP_052279Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041919 mRNA. Translation: BAC31096.1.
AK049821 mRNA. Translation: BAC33935.1.
AK085071 mRNA. Translation: BAC39355.1.
BC046536 mRNA. Translation: AAH46536.1.
BC110487 mRNA. Translation: AAI10488.1.
BC110488 mRNA. Translation: AAI10489.1.
CCDSiCCDS29306.1. [Q2TBA3-2]
RefSeqiNP_766421.1. NM_172833.2. [Q2TBA3-2]
XP_006526000.1. XM_006525937.1. [Q2TBA3-1]
UniGeneiMm.132613.

Genome annotation databases

EnsembliENSMUST00000049248; ENSMUSP00000048376; ENSMUSG00000032688. [Q2TBA3-2]
GeneIDi240354.
KEGGimmu:240354.
UCSCiuc008fez.1. mouse. [Q2TBA3-2]
uc008ffa.1. mouse. [Q2TBA3-1]
uc008ffb.1. mouse. [Q2TBA3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041919 mRNA. Translation: BAC31096.1 .
AK049821 mRNA. Translation: BAC33935.1 .
AK085071 mRNA. Translation: BAC39355.1 .
BC046536 mRNA. Translation: AAH46536.1 .
BC110487 mRNA. Translation: AAI10488.1 .
BC110488 mRNA. Translation: AAI10489.1 .
CCDSi CCDS29306.1. [Q2TBA3-2 ]
RefSeqi NP_766421.1. NM_172833.2. [Q2TBA3-2 ]
XP_006526000.1. XM_006525937.1. [Q2TBA3-1 ]
UniGenei Mm.132613.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V4L X-ray 3.15 A 338-729 [» ]
ProteinModelPortali Q2TBA3.
SMRi Q2TBA3. Positions 48-130, 134-729.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 232195. 6 interactions.
DIPi DIP-60308N.

Protein family/group databases

MEROPSi C14.026.

PTM databases

PhosphoSitei Q2TBA3.

Proteomic databases

MaxQBi Q2TBA3.
PaxDbi Q2TBA3.
PRIDEi Q2TBA3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049248 ; ENSMUSP00000048376 ; ENSMUSG00000032688 . [Q2TBA3-2 ]
GeneIDi 240354.
KEGGi mmu:240354.
UCSCi uc008fez.1. mouse. [Q2TBA3-2 ]
uc008ffa.1. mouse. [Q2TBA3-1 ]
uc008ffb.1. mouse. [Q2TBA3-3 ]

Organism-specific databases

CTDi 10892.
MGIi MGI:2445027. Malt1.

Phylogenomic databases

eggNOGi COG4249.
GeneTreei ENSGT00390000018044.
HOGENOMi HOG000113471.
HOVERGENi HBG052402.
InParanoidi Q2TBA3.
KOi K07369.
OMAi MNKEIPN.
OrthoDBi EOG7673BH.
PhylomeDBi Q2TBA3.
TreeFami TF319744.

Enzyme and pathway databases

Reactomei REACT_199121. Activation of NF-kappaB in B cells.
REACT_205561. FCERI mediated NF-kB activation.
REACT_225145. Downstream TCR signaling.

Miscellaneous databases

NextBioi 384566.
PROi Q2TBA3.
SOURCEi Search...

Gene expression databases

Bgeei Q2TBA3.
Genevestigatori Q2TBA3.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
2.60.40.10. 2 hits.
3.40.50.1460. 1 hit.
InterProi IPR029030. Caspase-like_dom.
IPR011029. DEATH-like_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
[Graphical view ]
Pfami PF00656. Peptidase_C14. 1 hit.
[Graphical view ]
SMARTi SM00408. IGc2. 2 hits.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi PS50208. CASPASE_P20. 1 hit.
PS50835. IG_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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).
    Strain: C57BL/6JImported.
    Tissue: HippocampusImported, LungImported and ThymusImported.
  2. "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; 2 AND 3).
    Strain: Czech IIImported.
    Tissue: Mammary glandImported.

Entry informationi

Entry nameiMALT1_MOUSE
AccessioniPrimary (citable) accession number: Q2TBA3
Secondary accession number(s): Q2TBA2
, Q811E3, Q8BFT0, Q8C7N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3