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Q8WVC0 (LEO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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:
RNA polymerase-associated protein LEO1
Alternative name(s):
Replicative senescence down-regulated leo1-like protein
Gene names
Name:LEO1
Synonyms:RDL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling. Ref.1 Ref.4 Ref.11 Ref.12 Ref.14

Subunit structure

Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with TCEA1, SUPT5H and CTNNB1. Ref.4 Ref.5 Ref.12 Ref.14

Subcellular location

Nucleus Ref.1.

Tissue specificity

Highly expressed in skeletal muscle and heart. Weakly expressed in placenta and liver. Ref.1

Sequence similarities

Belongs to the LEO1 family.

Sequence caution

The sequence BAB71006.1 differs from that shown. Reason: Frameshift at position 473.

Isoform 2: The sequence BAB71006.1 differs from that shown. Reason: Frameshift at position 471.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

endodermal cell fate commitment

Inferred from sequence or structural similarity. Source: UniProtKB

histone H2B ubiquitination

Inferred from direct assay PubMed 16307923. Source: UniProtKB

histone monoubiquitination

Inferred from direct assay PubMed 16307923. Source: UniProtKB

mRNA polyadenylation

Inferred from mutant phenotype PubMed 21329879. Source: UniProtKB

negative regulation of myeloid cell differentiation

Inferred from direct assay PubMed 20541477. Source: UniProtKB

positive regulation of mRNA 3'-end processing

Inferred from mutant phenotype PubMed 21329879. Source: UniProtKB

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: UniProtKB

stem cell maintenance

Inferred from direct assay Ref.11. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCdc73/Paf1 complex

Inferred from direct assay PubMed 16307923PubMed 18987311Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WVC0-1)

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: Q8WVC0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     387-446: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 666665RNA polymerase-associated protein LEO1
PRO_0000247819

Regions

Compositional bias3 – 329327Asp-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.15 Ref.17 Ref.18
Modified residue101Phosphoserine Ref.6 Ref.15
Modified residue141Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue1511Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue1541Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue1621Phosphoserine Ref.15 Ref.17
Modified residue1711Phosphoserine Ref.15 Ref.17
Modified residue1791Phosphoserine Ref.15 Ref.17
Modified residue1881Phosphothreonine Ref.6 Ref.15 Ref.17
Modified residue1971Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue2051Phosphoserine Ref.6
Modified residue2121Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue2201Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue2291Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue2381Phosphoserine Ref.6 Ref.15 Ref.17
Modified residue2771Phosphoserine By similarity
Modified residue2791Phosphoserine Ref.7 Ref.15 Ref.17
Modified residue2941Phosphoserine Ref.8 Ref.17
Modified residue2961Phosphoserine Ref.8
Modified residue3001Phosphoserine Ref.15 Ref.17
Modified residue6071Phosphoserine Ref.8 Ref.17
Modified residue6081Phosphoserine Ref.8 Ref.17
Modified residue6101Phosphoserine Ref.8 Ref.17
Modified residue6141Phosphoserine Ref.8
Modified residue6291Phosphothreonine Ref.8 Ref.13
Modified residue6301Phosphoserine Ref.7 Ref.8 Ref.13 Ref.15 Ref.17
Modified residue6581Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.17

Natural variations

Alternative sequence387 – 44660Missing in isoform 2.
VSP_020051

Secondary structure

................. 666
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2002. Version 1.
Checksum: EB405BE0EDA7E0B0

FASTA66675,404
        10         20         30         40         50         60 
MADMEDLFGS DADSEAERKD SDSGSDSDSD QENAASGSNA SGSESDQDER GDSGQPSNKE 

        70         80         90        100        110        120 
LFGDDSEDEG ASHHSGSDNH SERSDNRSEA SERSDHEDND PSDVDQHSGS EAPNDDEDEG 

       130        140        150        160        170        180 
HRSDGGSHHS EAEGSEKAHS DDEKWGREDK SDQSDDEKIQ NSDDEERAQG SDEDKLQNSD 

       190        200        210        220        230        240 
DDEKMQNTDD EERPQLSDDE RQQLSEEEKA NSDDERPVAS DNDDEKQNSD DEEQPQLSDE 

       250        260        270        280        290        300 
EKMQNSDDER PQASDEEHRH SDDEEEQDHK SESARGSDSE DEVLRMKRKN AIASDSEADS 

       310        320        330        340        350        360 
DTEVPKDNSG TMDLFGGADD ISSGSDGEDK PPTPGQPVDE NGLPQDQQEE EPIPETRIEV 

       370        380        390        400        410        420 
EIPKVNTDLG NDLYFVKLPN FLSVEPRPFD PQYYEDEFED EEMLDEEGRT RLKLKVENTI 

       430        440        450        460        470        480 
RWRIRRDEEG NEIKESNARI VKWSDGSMSL HLGNEVFDVY KAPLQGDHNH LFIRQGTGLQ 

       490        500        510        520        530        540 
GQAVFKTKLT FRPHSTDSAT HRKMTLSLAD RCSKTQKIRI LPMAGRDPEC QRTEMIKKEE 

       550        560        570        580        590        600 
ERLRASIRRE SQQRRMREKQ HQRGLSASYL EPDRYDEEEE GEESISLAAI KNRYKGGIRE 

       610        620        630        640        650        660 
ERARIYSSDS DEGSEEDKAQ RLLKAKKLTS DEEGEPSGKR KAEDDDKANK KHKKYVISDE 


EEEDDD 

« Hide

Isoform 2 [UniParc].

Checksum: AF31C9793F9545D5
Show »

FASTA60668,004

References

« Hide 'large scale' references
[1]"Expression of the Leo1-like domain of replicative senescence down-regulated Leo1-like (RDL) protein promotes senescence of 2BS fibroblasts."
Zhao L., Tong T., Zhang Z.
FASEB J. 19:521-532(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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 2).
Tissue: Kidney.
[3]"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: Colon.
[4]"The parafibromin tumor suppressor protein is part of a human Paf1 complex."
Rozenblatt-Rosen O., Hughes C.M., Nannepaga S.J., Shanmugam K.S., Copeland T.D., Guszczynski T., Resau J.H., Meyerson M.
Mol. Cell. Biol. 25:612-620(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF PAF1 COMPLEX, FUNCTION, INTERACTION WITH CDC73.
[5]"Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct association with beta-catenin/Armadillo."
Mosimann C., Hausmann G., Basler K.
Cell 125:327-341(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNB1.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-151; SER-154; THR-188; SER-197; SER-205; SER-212; SER-220; SER-229; SER-238 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-279; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-296; SER-607; SER-608; SER-610; SER-614; THR-629; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"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].
[11]"A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1 complex for embryonic stem cell identity."
Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T. expand/collapse author list , Caldarelli A., Poser I., Theis M., Buchholz F.
Cell Stem Cell 4:403-415(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation."
Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., Hisatake K., Handa H.
Genes Dev. 23:2765-2777(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH SUPT5H.
[13]"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 THR-629; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS."
Kim J., Guermah M., Roeder R.G.
Cell 140:491-503(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH TCEA1.
[15]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-151; SER-154; SER-162; SER-171; SER-179; THR-188; SER-197; SER-212; SER-220; SER-229; SER-238; SER-279; SER-300; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-151; SER-154; SER-162; SER-171; SER-179; THR-188; SER-197; SER-212; SER-220; SER-229; SER-238; SER-279; SER-294; SER-300; SER-607; SER-608; SER-610; SER-630 AND SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY302186 mRNA. Translation: AAP68819.1.
AK055762 mRNA. Translation: BAB71006.1. Frameshift.
BC018147 mRNA. Translation: AAH18147.1.
RefSeqNP_001273359.1. NM_001286430.1.
NP_620147.1. NM_138792.3.
UniGeneHs.567662.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M6TX-ray2.50A367-462[»]
ProteinModelPortalQ8WVC0.
SMRQ8WVC0. Positions 370-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125817. 30 interactions.
DIPDIP-37885N.
IntActQ8WVC0. 25 interactions.
STRING9606.ENSP00000299601.

PTM databases

PhosphoSiteQ8WVC0.

Polymorphism databases

DMDM74751545.

Proteomic databases

PaxDbQ8WVC0.
PeptideAtlasQ8WVC0.
PRIDEQ8WVC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299601; ENSP00000299601; ENSG00000166477. [Q8WVC0-1]
ENST00000315141; ENSP00000314610; ENSG00000166477. [Q8WVC0-2]
GeneID123169.
KEGGhsa:123169.
UCSCuc002abo.3. human. [Q8WVC0-1]
uc010bfd.3. human. [Q8WVC0-2]

Organism-specific databases

CTD123169.
GeneCardsGC15M052230.
HGNCHGNC:30401. LEO1.
HPAHPA040741.
HPA040941.
MIM610507. gene.
neXtProtNX_Q8WVC0.
PharmGKBPA142671558.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG130430.
HOGENOMHOG000253934.
HOVERGENHBG081913.
InParanoidQ8WVC0.
KOK15177.
OMAHEDNEPS.
OrthoDBEOG7W41BG.
PhylomeDBQ8WVC0.
TreeFamTF321961.

Gene expression databases

BgeeQ8WVC0.
CleanExHS_LEO1.
GenevestigatorQ8WVC0.

Family and domain databases

InterProIPR007149. Leo1.
[Graphical view]
PfamPF04004. Leo1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLEO1. human.
GeneWikiLEO1.
GenomeRNAi123169.
NextBio81081.
PROQ8WVC0.
SOURCESearch...

Entry information

Entry nameLEO1_HUMAN
AccessionPrimary (citable) accession number: Q8WVC0
Secondary accession number(s): Q96N99
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 99 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM