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Protein

Ribosomal biogenesis protein LAS1L

Gene

LAS1L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. 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.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

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
ORF Names:MSTP060
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:25726. LAS1L.

Subcellular locationi

Nucleusnucleolus 2 Publications. Nucleusnucleoplasm By similarity. Cytoplasm By similarity
Note: Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). Localizes mainly to the granular component, the region implicated in the later steps of rRNA processing and subunit assembly and export.By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. membrane Source: UniProtKB
  3. microtubule organizing center Source: HPA
  4. MLL1 complex Source: UniProtKB
  5. nucleolus Source: UniProtKB-SubCell
  6. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti404521. Spinal muscular atrophy with respiratory distress type 2.
PharmGKBiPA128394732.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 734734Ribosomal biogenesis protein LAS1LPRO_0000211559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei523 – 5231Phosphoserine2 Publications
Modified residuei560 – 5601Phosphoserine2 Publications
Modified residuei617 – 6171Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y4W2.
PaxDbiQ9Y4W2.
PRIDEiQ9Y4W2.

2D gel databases

SWISS-2DPAGEQ9Y4W2.

PTM databases

PhosphoSiteiQ9Y4W2.

Expressioni

Gene expression databases

BgeeiQ9Y4W2.
CleanExiHS_LAS1L.
ExpressionAtlasiQ9Y4W2. baseline and differential.
GenevestigatoriQ9Y4W2.

Organism-specific databases

HPAiHPA044431.

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, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PNKPQ96T601EBI-1051591,EBI-1045072

Protein-protein interaction databases

BioGridi123620. 25 interactions.
IntActiQ9Y4W2. 10 interactions.
MINTiMINT-4728360.
STRINGi9606.ENSP00000363944.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4W2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LAS1 family.Curated

Phylogenomic databases

eggNOGiNOG323169.
GeneTreeiENSGT00390000014785.
HOGENOMiHOG000232090.
HOVERGENiHBG080556.
InParanoidiQ9Y4W2.
KOiK16912.
OMAiPFSQFWQ.
OrthoDBiEOG7G7KPC.
PhylomeDBiQ9Y4W2.
TreeFamiTF314042.

Family and domain databases

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

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4W2-1) [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
MSWESGAGPG LGSQGMDLVW SAWYGKCVKG KGSLPLSAHG IVVAWLSRAE
60 70 80 90 100
WDQVTVYLFC DDHKLQRYAL NRITVWRSRS GNELPLAVAS TADLIRCKLL
110 120 130 140 150
DVTGGLGTDE LRLLYGMALV RFVNLISERK TKFAKVPLKC LAQEVNIPDW
160 170 180 190 200
IVDLRHELTH KKMPHINDCR RGCYFVLDWL QKTYWCRQLE NSLRETWELE
210 220 230 240 250
EFREGIEEED QEEDKNIVVD DITEQKPEPQ DDGKSTESDV KADGDSKGSE
260 270 280 290 300
EVDSHCKKAL SHKELYERAR ELLVSYEEEQ FTVLEKFRYL PKAIKAWNNP
310 320 330 340 350
SPRVECVLAE LKGVTCENRE AVLDAFLDDG FLVPTFEQLA ALQIEYEDGQ
360 370 380 390 400
TEVQRGEGTD PKSHKNVDLN DVLVPKPFSQ FWQPLLRGLH SQNFTQALLE
410 420 430 440 450
RMLSELPALG ISGIRPTYIL RWTVELIVAN TKTGRNARRF SAGQWEARRG
460 470 480 490 500
WRLFNCSASL DWPRMVESCL GSPCWASPQL LRIIFKAMGQ GLPDEEQEKL
510 520 530 540 550
LRICSIYTQS GENSLVQEGS EASPIGKSPY TLDSLYWSVK PASSSFGSEA
560 570 580 590 600
KAQQQEEQGS VNDVKEEEKE EKEVLPDQVE EEEENDDQEE EEEDEDDEDD
610 620 630 640 650
EEEDRMEVGP FSTGQESPTA ENARLLAQKR GALQGSAWQV SSEDVRWDTF
660 670 680 690 700
PLGRMPGQTE DPAELMLENY DTMYLLDQPV LEQRLEPSTC KTDTLGLSCG
710 720 730
VGSGNCSNSS SSNFEGLLWS QGQLHGLKTG LQLF
Length:734
Mass (Da):83,065
Last modified:August 30, 2005 - v2
Checksum:iA35CC38F95C39F7D
GO
Isoform 2 (identifier: Q9Y4W2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-365: DGQTEVQRGEGTDPKSHK → E

Show »
Length:717
Mass (Da):81,243
Checksum:i651B7F0FFB3FD07F
GO
Isoform 3 (identifier: Q9Y4W2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-120: Missing.
     348-365: DGQTEVQRGEGTDPKSHK → E

Note: Gene prediction based on EST data. No experimental confirmation available.

Show »
Length:675
Mass (Da):76,845
Checksum:iEC904EABA17F0028
GO
Isoform 4 (identifier: Q9Y4W2-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     283-291: VLEKFRYLP → GGCAGCFSG
     292-734: Missing.

Show »
Length:291
Mass (Da):33,108
Checksum:i500B863F92E96866
GO

Sequence cautioni

The sequence BAB84913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036587

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 12042Missing in isoform 3. CuratedVSP_015178Add
BLAST
Alternative sequencei283 – 2919VLEKFRYLP → GGCAGCFSG in isoform 4. 1 PublicationVSP_015179
Alternative sequencei292 – 734443Missing in isoform 4. 1 PublicationVSP_015180Add
BLAST
Alternative sequencei348 – 36518DGQTE…PKSHK → E in isoform 2 and isoform 3. 1 PublicationVSP_015181Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116730 mRNA. Translation: AAO15306.1.
AK074087 mRNA. Translation: BAB84913.1. Different initiation.
AK022587 mRNA. Translation: BAB14114.1.
AL050306 Genomic DNA. Translation: CAB51351.1.
AL050306 Genomic DNA. Translation: CAI42835.1.
AL050306 Genomic DNA. Translation: CAI42836.1.
BC014545 mRNA. Translation: AAH14545.1.
BC018610 mRNA. Translation: AAH18610.1.
BC019302 mRNA. Translation: AAH19302.1.
DQ323624 mRNA. Translation: ABD39127.1.
CCDSiCCDS14381.1. [Q9Y4W2-1]
CCDS55433.1. [Q9Y4W2-3]
CCDS55434.1. [Q9Y4W2-2]
RefSeqiNP_001164120.1. NM_001170649.1. [Q9Y4W2-2]
NP_001164121.1. NM_001170650.1. [Q9Y4W2-3]
NP_112483.1. NM_031206.4. [Q9Y4W2-1]
UniGeneiHs.522675.

Genome annotation databases

EnsembliENST00000374804; ENSP00000363937; ENSG00000001497. [Q9Y4W2-3]
ENST00000374807; ENSP00000363940; ENSG00000001497. [Q9Y4W2-2]
ENST00000374811; ENSP00000363944; ENSG00000001497. [Q9Y4W2-1]
ENST00000484069; ENSP00000473471; ENSG00000001497. [Q9Y4W2-4]
GeneIDi81887.
KEGGihsa:81887.
UCSCiuc004dwa.2. human. [Q9Y4W2-1]
uc004dwc.2. human. [Q9Y4W2-2]
uc004dwd.2. human. [Q9Y4W2-3]

Polymorphism databases

DMDMi73920837.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF116730 mRNA. Translation: AAO15306.1.
AK074087 mRNA. Translation: BAB84913.1. Different initiation.
AK022587 mRNA. Translation: BAB14114.1.
AL050306 Genomic DNA. Translation: CAB51351.1.
AL050306 Genomic DNA. Translation: CAI42835.1.
AL050306 Genomic DNA. Translation: CAI42836.1.
BC014545 mRNA. Translation: AAH14545.1.
BC018610 mRNA. Translation: AAH18610.1.
BC019302 mRNA. Translation: AAH19302.1.
DQ323624 mRNA. Translation: ABD39127.1.
CCDSiCCDS14381.1. [Q9Y4W2-1]
CCDS55433.1. [Q9Y4W2-3]
CCDS55434.1. [Q9Y4W2-2]
RefSeqiNP_001164120.1. NM_001170649.1. [Q9Y4W2-2]
NP_001164121.1. NM_001170650.1. [Q9Y4W2-3]
NP_112483.1. NM_031206.4. [Q9Y4W2-1]
UniGeneiHs.522675.

3D structure databases

ProteinModelPortaliQ9Y4W2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123620. 25 interactions.
IntActiQ9Y4W2. 10 interactions.
MINTiMINT-4728360.
STRINGi9606.ENSP00000363944.

PTM databases

PhosphoSiteiQ9Y4W2.

Polymorphism databases

DMDMi73920837.

2D gel databases

SWISS-2DPAGEQ9Y4W2.

Proteomic databases

MaxQBiQ9Y4W2.
PaxDbiQ9Y4W2.
PRIDEiQ9Y4W2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374804; ENSP00000363937; ENSG00000001497. [Q9Y4W2-3]
ENST00000374807; ENSP00000363940; ENSG00000001497. [Q9Y4W2-2]
ENST00000374811; ENSP00000363944; ENSG00000001497. [Q9Y4W2-1]
ENST00000484069; ENSP00000473471; ENSG00000001497. [Q9Y4W2-4]
GeneIDi81887.
KEGGihsa:81887.
UCSCiuc004dwa.2. human. [Q9Y4W2-1]
uc004dwc.2. human. [Q9Y4W2-2]
uc004dwd.2. human. [Q9Y4W2-3]

Organism-specific databases

CTDi81887.
GeneCardsiGC0XM064649.
HGNCiHGNC:25726. LAS1L.
HPAiHPA044431.
neXtProtiNX_Q9Y4W2.
Orphaneti404521. Spinal muscular atrophy with respiratory distress type 2.
PharmGKBiPA128394732.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG323169.
GeneTreeiENSGT00390000014785.
HOGENOMiHOG000232090.
HOVERGENiHBG080556.
InParanoidiQ9Y4W2.
KOiK16912.
OMAiPFSQFWQ.
OrthoDBiEOG7G7KPC.
PhylomeDBiQ9Y4W2.
TreeFamiTF314042.

Miscellaneous databases

ChiTaRSiLAS1L. human.
GeneWikiiLAS1L.
GenomeRNAii81887.
NextBioi72228.
PROiQ9Y4W2.

Gene expression databases

BgeeiQ9Y4W2.
CleanExiHS_LAS1L.
ExpressionAtlasiQ9Y4W2. baseline and differential.
GenevestigatoriQ9Y4W2.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  2. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
    Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Spleen.
  3. "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: Teratocarcinoma.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Bone marrow, Lung and Placenta.
  6. "Functional persistence of exonized mammalian-wide interspersed repeat elements (MIRs)."
    Krull M., Petrusma M., Makalowski W., Brosius J., Schmitz J.
    Genome Res. 17:1139-1145(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 345-377.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Las1L is a nucleolar protein required for cell proliferation and ribosome biogenesis."
    Castle C.D., Cassimere E.K., Lee J., Denicourt C.
    Mol. Cell. Biol. 30:4404-4414(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-617, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-170.

Entry informationi

Entry nameiLAS1L_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4W2
Secondary accession number(s): A9X410
, Q5JXQ0, Q8TEN5, Q9H9V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: February 4, 2015
This is version 118 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.