Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y4W2 (LAS1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal biogenesis protein LAS1L
Alternative name(s):
Protein LAS1 homolog
Gene names
Name:LAS1L
ORF Names:MSTP060
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length734 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.17

Subunit structure

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. Ref.8 Ref.17

Subcellular location

Nucleusnucleolus. 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. Ref.7 Ref.13

Sequence similarities

Belongs to the LAS1 family.

Sequence caution

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

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

microtubule organizing center

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PNKPQ96T601EBI-1051591,EBI-1045072

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4W2-1)

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.
Isoform 2 (identifier: Q9Y4W2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     348-365: DGQTEVQRGEGTDPKSHK → E
Isoform 3 (identifier: Q9Y4W2-3)

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.
Isoform 4 (identifier: Q9Y4W2-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 734734Ribosomal biogenesis protein LAS1L
PRO_0000211559

Amino acid modifications

Modified residue5231Phosphoserine Ref.9 Ref.10
Modified residue5601Phosphoserine Ref.14 Ref.16
Modified residue6171Phosphoserine Ref.12 Ref.14 Ref.16

Natural variations

Alternative sequence79 – 12042Missing in isoform 3.
VSP_015178
Alternative sequence283 – 2919VLEKFRYLP → GGCAGCFSG in isoform 4.
VSP_015179
Alternative sequence292 – 734443Missing in isoform 4.
VSP_015180
Alternative sequence348 – 36518DGQTE…PKSHK → E in isoform 2 and isoform 3.
VSP_015181
Natural variant1701R → C in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036587

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: A35CC38F95C39F7D

FASTA73483,065
        10         20         30         40         50         60 
MSWESGAGPG LGSQGMDLVW SAWYGKCVKG KGSLPLSAHG IVVAWLSRAE WDQVTVYLFC 

        70         80         90        100        110        120 
DDHKLQRYAL NRITVWRSRS GNELPLAVAS TADLIRCKLL DVTGGLGTDE LRLLYGMALV 

       130        140        150        160        170        180 
RFVNLISERK TKFAKVPLKC LAQEVNIPDW IVDLRHELTH KKMPHINDCR RGCYFVLDWL 

       190        200        210        220        230        240 
QKTYWCRQLE NSLRETWELE EFREGIEEED QEEDKNIVVD DITEQKPEPQ DDGKSTESDV 

       250        260        270        280        290        300 
KADGDSKGSE EVDSHCKKAL SHKELYERAR ELLVSYEEEQ FTVLEKFRYL PKAIKAWNNP 

       310        320        330        340        350        360 
SPRVECVLAE LKGVTCENRE AVLDAFLDDG FLVPTFEQLA ALQIEYEDGQ TEVQRGEGTD 

       370        380        390        400        410        420 
PKSHKNVDLN DVLVPKPFSQ FWQPLLRGLH SQNFTQALLE RMLSELPALG ISGIRPTYIL 

       430        440        450        460        470        480 
RWTVELIVAN TKTGRNARRF SAGQWEARRG WRLFNCSASL DWPRMVESCL GSPCWASPQL 

       490        500        510        520        530        540 
LRIIFKAMGQ GLPDEEQEKL LRICSIYTQS GENSLVQEGS EASPIGKSPY TLDSLYWSVK 

       550        560        570        580        590        600 
PASSSFGSEA KAQQQEEQGS VNDVKEEEKE EKEVLPDQVE EEEENDDQEE EEEDEDDEDD 

       610        620        630        640        650        660 
EEEDRMEVGP FSTGQESPTA ENARLLAQKR GALQGSAWQV SSEDVRWDTF PLGRMPGQTE 

       670        680        690        700        710        720 
DPAELMLENY DTMYLLDQPV LEQRLEPSTC KTDTLGLSCG VGSGNCSNSS SSNFEGLLWS 

       730 
QGQLHGLKTG LQLF 

« Hide

Isoform 2 [UniParc].

Checksum: 651B7F0FFB3FD07F
Show »

FASTA71781,243
Isoform 3 [UniParc].

Checksum: EC904EABA17F0028
Show »

FASTA67576,845
Isoform 4 [UniParc].

Checksum: 500B863F92E96866
Show »

FASTA29133,108

References

« Hide 'large scale' references
[1]Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y., Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-170.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001164120.1. NM_001170649.1.
NP_001164121.1. NM_001170650.1.
NP_112483.1. NM_031206.4.
UniGeneHs.522675.

3D structure databases

ProteinModelPortalQ9Y4W2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123620. 20 interactions.
IntActQ9Y4W2. 9 interactions.
MINTMINT-4728360.
STRING9606.ENSP00000363944.

PTM databases

PhosphoSiteQ9Y4W2.

Polymorphism databases

DMDM73920837.

2D gel databases

SWISS-2DPAGEQ9Y4W2.

Proteomic databases

PaxDbQ9Y4W2.
PRIDEQ9Y4W2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312391; ENSP00000308649; ENSG00000001497. [Q9Y4W2-4]
ENST00000374804; ENSP00000363937; ENSG00000001497. [Q9Y4W2-3]
ENST00000374807; ENSP00000363940; ENSG00000001497. [Q9Y4W2-2]
ENST00000374811; ENSP00000363944; ENSG00000001497. [Q9Y4W2-1]
ENST00000484069; ENSP00000473471; ENSG00000001497. [Q9Y4W2-4]
GeneID81887.
KEGGhsa:81887.
UCSCuc004dwa.2. human. [Q9Y4W2-1]
uc004dwc.2. human. [Q9Y4W2-2]
uc004dwd.2. human. [Q9Y4W2-3]

Organism-specific databases

CTD81887.
GeneCardsGC0XM064649.
HGNCHGNC:25726. LAS1L.
HPAHPA044431.
neXtProtNX_Q9Y4W2.
PharmGKBPA128394732.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323169.
HOGENOMHOG000232090.
HOVERGENHBG080556.
InParanoidQ9Y4W2.
KOK16912.
OMAFWQPLLR.
OrthoDBEOG7G7KPC.
PhylomeDBQ9Y4W2.
TreeFamTF314042.

Gene expression databases

ArrayExpressQ9Y4W2.
BgeeQ9Y4W2.
CleanExHS_LAS1L.
GenevestigatorQ9Y4W2.

Family and domain databases

InterProIPR007174. Las1.
[Graphical view]
PANTHERPTHR15002. PTHR15002. 1 hit.
PfamPF04031. Las1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAS1L. human.
GeneWikiLAS1L.
GenomeRNAi81887.
NextBio72228.
PROQ9Y4W2.

Entry information

Entry nameLAS1L_HUMAN
AccessionPrimary (citable) accession number: Q9Y4W2
Secondary accession number(s): A9X410 expand/collapse secondary AC list , Q5JXQ0, Q8TEN5, Q9H9V5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM