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A2BE28

- LAS1L_MOUSE

UniProt

A2BE28 - LAS1L_MOUSE

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Protein

Ribosomal biogenesis protein LAS1L

Gene
Las1l
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the biogenesis of the 60S ribosomal subunit. Required for maturation of the 28S rRNA By similarity. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.1 Publication

GO - Biological processi

  1. rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal biogenesis protein LAS1L
Alternative name(s):
Protein LAS1 homolog
Gene namesi
Name:Las1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1923380. Las1l.

Subcellular locationi

Nucleusnucleolus By similarity. Nucleusnucleoplasm. Cytoplasm
Note: Localizes mainly to the granular component, the region implicated in the later steps of rRNA processing and subunit assembly and export By similarity. Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. MLL1 complex Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 776776Ribosomal biogenesis protein LAS1LPRO_0000390998Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei509 – 5091Phosphoserine By similarity
Modified residuei658 – 6581Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA2BE28.
PaxDbiA2BE28.
PRIDEiA2BE28.

Expressioni

Gene expression databases

ArrayExpressiA2BE28.
BgeeiA2BE28.
GenevestigatoriA2BE28.

Interactioni

Subunit structurei

Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 By similarity. Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148.1 Publication

Protein-protein interaction databases

BioGridi217980. 3 interactions.

Family & Domainsi

Sequence similaritiesi

Belongs to the LAS1 family.

Phylogenomic databases

eggNOGiNOG323169.
GeneTreeiENSGT00390000014785.
HOGENOMiHOG000232090.
HOVERGENiHBG080556.
InParanoidiQ6KAR5.
KOiK16912.
OMAiPFSQFWQ.
OrthoDBiEOG7G7KPC.
TreeFamiTF314042.

Family and domain databases

InterProiIPR007174. Las1.
[Graphical view]
PANTHERiPTHR15002. PTHR15002. 1 hit.
PfamiPF04031. Las1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: A2BE28-1) [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

MDRVWRAWDG QSFKENQPES PSARGIVVSW LSRAEWEQVT VYLFCDDHKL    50
QQYALNRITV WRSRLGNELP LAVASTADLV RCKLIDAAGT LGTDELRLLY 100
GMALVRFVNL ISERKTKCSN LPLKYLAQEV NIPDWIVELR HNLTHKKMPH 150
INECRRGCYF VLNWLQKTYW SRQLEGSLKE TWELDEDQLD AEDPEEEERE 200
IIADDVLEEI PEPQDDDKDE ELAVEDDANT KGNEEVASHP EPSSRHKELY 250
EKARELLVSY EEEQFKVLEK HRHLLQAIKV WNNLSPRVQC ILEELKSISW 300
ENRDAVLDAF LDDGFLIPTF EQLAALQIEY EDGQTEVQKG EVTEPNSHKN 350
IDLNEVLVPK PFSQFWQPLL RGLHSQTFTQ ALLERMFSEL STVGSTGIRP 400
TYILRWTVEL IVANTKTGRN ARRFSASQWE ARKSWRLFNC SATLDWPQVI 450
ESCLGSPCWA SPQLLQVVFK AMGQVLPDEE QEKLLRVCSI YTQNGENGLA 500
KAIEGSSSSS TGKAPYTLDT LHEDLQPPGT NCESEESIQQ KEQGNLKDVK 550
QEEKKENEEE EKEEEEMEEE EEEEEEEKEE EEEEQEQEEH QEEEQEEEEE 600
EENQKVFQDQ MEADVEESDD VEEEEEVDDE EEDEDDDYDD DEEEDRMEVG 650
AFSLAQGSSV FENTRTTSRK REALQGSAWQ VSSEDVRWGT FPLGRLPGQT 700
EDPAELMLDN YDTMYLLDQP VIEHRLEPQK SKSSTLSLCC GGSNTNSSSS 750
SSSGNMEGLL WNQGQMHGLK AGLQLF 776
Length:776
Mass (Da):89,414
Last modified:February 20, 2007 - v1
Checksum:i6855167CD37D57EC
GO
Isoform 2 (identifier: A2BE28-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     332-349: DGQTEVQKGEVTEPNSHK → E

Show »
Length:759
Mass (Da):87,578
Checksum:i93701CFEE32B2326
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei332 – 34918DGQTE…PNSHK → E in isoform 2. VSP_038670Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX005184 Genomic DNA. Translation: CAM25407.1.
BX005184 Genomic DNA. Translation: CAM25408.1.
BC141155 mRNA. Translation: AAI41156.1.
AK052578 mRNA. Translation: BAC35047.1.
AK131142 mRNA. Translation: BAD21392.1.
CCDSiCCDS30287.1. [A2BE28-2]
RefSeqiNP_690035.2. NM_152822.3. [A2BE28-2]
XP_006528397.1. XM_006528334.1. [A2BE28-1]
UniGeneiMm.274318.

Genome annotation databases

EnsembliENSMUST00000079987; ENSMUSP00000078901; ENSMUSG00000057421. [A2BE28-2]
ENSMUST00000113864; ENSMUSP00000109495; ENSMUSG00000057421. [A2BE28-1]
GeneIDi76130.
KEGGimmu:76130.
UCSCiuc009tud.1. mouse. [A2BE28-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX005184 Genomic DNA. Translation: CAM25407.1 .
BX005184 Genomic DNA. Translation: CAM25408.1 .
BC141155 mRNA. Translation: AAI41156.1 .
AK052578 mRNA. Translation: BAC35047.1 .
AK131142 mRNA. Translation: BAD21392.1 .
CCDSi CCDS30287.1. [A2BE28-2 ]
RefSeqi NP_690035.2. NM_152822.3. [A2BE28-2 ]
XP_006528397.1. XM_006528334.1. [A2BE28-1 ]
UniGenei Mm.274318.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 217980. 3 interactions.

Proteomic databases

MaxQBi A2BE28.
PaxDbi A2BE28.
PRIDEi A2BE28.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079987 ; ENSMUSP00000078901 ; ENSMUSG00000057421 . [A2BE28-2 ]
ENSMUST00000113864 ; ENSMUSP00000109495 ; ENSMUSG00000057421 . [A2BE28-1 ]
GeneIDi 76130.
KEGGi mmu:76130.
UCSCi uc009tud.1. mouse. [A2BE28-2 ]

Organism-specific databases

CTDi 81887.
MGIi MGI:1923380. Las1l.

Phylogenomic databases

eggNOGi NOG323169.
GeneTreei ENSGT00390000014785.
HOGENOMi HOG000232090.
HOVERGENi HBG080556.
InParanoidi Q6KAR5.
KOi K16912.
OMAi PFSQFWQ.
OrthoDBi EOG7G7KPC.
TreeFami TF314042.

Miscellaneous databases

NextBioi 344645.
PROi A2BE28.
SOURCEi Search...

Gene expression databases

ArrayExpressi A2BE28.
Bgeei A2BE28.
Genevestigatori A2BE28.

Family and domain databases

InterProi IPR007174. Las1.
[Graphical view ]
PANTHERi PTHR15002. PTHR15002. 1 hit.
Pfami PF04031. Las1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORM 1).
    Tissue: Brain.
  3. "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] OF 253-575 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Stomach.
  4. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 541-776.
    Tissue: Spleen.
  5. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC COMPLEX WITH CHTOP AND ZNF148, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLAS1L_MOUSE
AccessioniPrimary (citable) accession number: A2BE28
Secondary accession number(s): A2BE30, Q6KAR5, Q8C742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi