Q8WVC0 (LEO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase-associated protein LEO1

Alternative name(s):
Replicative senescence down-regulated leo1-like protein

Gene names

Name:	LEO1
Synonyms:	RDL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	666 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 MLL1; it promotes leukemogenesis though association with MLL-rearranged oncoproteins, such as MLL-MLLT3/AF9 and MLL-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.10 Ref.11 Ref.13
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.11 Ref.13
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 process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor 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.13. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.13. Source: UniProtKB stem cell maintenance Inferred from direct assay Ref.10. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cdc73/Paf1 complex Inferred from direct assay PubMed 16307923PubMed 18987311Ref.13. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC73	Q6P1J9	11	EBI-932432,EBI-930143
CTNNB1	P35222	2	EBI-932432,EBI-491549
PAF1	Q8N7H5	17	EBI-932432,EBI-2607770
TCEA1	P23193	4	EBI-932432,EBI-2608271

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.14
	Chain	2 – 666	665	RNA polymerase-associated protein LEO1		PRO_0000247819
Regions
	Compositional bias	3 – 329	327	Asp-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.14 Ref.16
	Modified residue	10	1	Phosphoserine Ref.6 Ref.14
	Modified residue	14	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	151	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	154	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	162	1	Phosphoserine Ref.14 Ref.16
	Modified residue	171	1	Phosphoserine Ref.14 Ref.16
	Modified residue	179	1	Phosphoserine Ref.14 Ref.16
	Modified residue	188	1	Phosphothreonine Ref.6 Ref.14 Ref.16
	Modified residue	197	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	205	1	Phosphoserine Ref.6
	Modified residue	212	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	220	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	229	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	238	1	Phosphoserine Ref.6 Ref.14 Ref.16
	Modified residue	246	1	Phosphoserine By similarity
	Modified residue	254	1	Phosphoserine By similarity
	Modified residue	277	1	Phosphoserine By similarity
	Modified residue	279	1	Phosphoserine Ref.7 Ref.14 Ref.16
	Modified residue	294	1	Phosphoserine Ref.8 Ref.16
	Modified residue	296	1	Phosphoserine Ref.8
	Modified residue	300	1	Phosphoserine Ref.14 Ref.16
	Modified residue	607	1	Phosphoserine Ref.8 Ref.16
	Modified residue	608	1	Phosphoserine Ref.8 Ref.16
	Modified residue	610	1	Phosphoserine Ref.8 Ref.16
	Modified residue	614	1	Phosphoserine Ref.8
	Modified residue	629	1	Phosphothreonine Ref.8 Ref.12
	Modified residue	630	1	Phosphoserine Ref.7 Ref.8 Ref.12 Ref.14 Ref.16
	Modified residue	658	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14 Ref.16
Natural variations
	Alternative sequence	387 – 446	60	Missing in isoform 2.		VSP_020051

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: EB405BE0EDA7E0B0	FASTA	666	75,404
	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
	Isoform 2 [UniParc]. Checksum: AF31C9793F9545D5	FASTA	606	68,004
	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 FLSVEPSMSL HLGNEVFDVY KAPLQGDHNH LFIRQGTGLQ 430 440 450 460 470 480 GQAVFKTKLT FRPHSTDSAT HRKMTLSLAD RCSKTQKIRI LPMAGRDPEC QRTEMIKKEE 490 500 510 520 530 540 ERLRASIRRE SQQRRMREKQ HQRGLSASYL EPDRYDEEEE GEESISLAAI KNRYKGGIRE 550 560 570 580 590 600 ERARIYSSDS DEGSEEDKAQ RLLKAKKLTS DEEGEPSGKR KAEDDDKANK KHKKYVISDE EEEDDD

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[10]	"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. , Caldarelli A., Poser I., Theis M., Buchholz F. Cell Stem Cell 4:403-415(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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.
[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 THR-629; SER-630 AND SER-658, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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.
[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: 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. 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: 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, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY302186 mRNA. Translation: AAP68819.1. AK055762 mRNA. Translation: BAB71006.1. Frameshift. BC018147 mRNA. Translation: AAH18147.1.
IPI	IPI00103090. IPI00154162.
RefSeq	NP_620147.1. NM_138792.2.
UniGene	Hs.567662.
3D structure databases
ProteinModelPortal	Q8WVC0.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-37885N.
IntAct	Q8WVC0. 25 interactions.
STRING	9606.ENSP00000299601.
PTM databases
PhosphoSite	Q8WVC0.
Polymorphism databases
DMDM	74751545.
Proteomic databases
PaxDb	Q8WVC0.
PeptideAtlas	Q8WVC0.
PRIDE	Q8WVC0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000299601; ENSP00000299601; ENSG00000166477. ENST00000315141; ENSP00000314610; ENSG00000166477.
GeneID	123169.
KEGG	hsa:123169.
UCSC	uc002abo.3. human. uc010bfd.3. human.
Organism-specific databases
CTD	123169.
GeneCards	GC15M052230.
HGNC	HGNC:30401. LEO1.
HPA	HPA040741. HPA040941.
MIM	610507. gene.
neXtProt	NX_Q8WVC0.
PharmGKB	PA142671558.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG130430.
HOGENOM	HOG000253934.
HOVERGEN	HBG081913.
InParanoid	Q8WVC0.
KO	K15177.
OMA	NNGTMDL.
OrthoDB	EOG4HQDJC.
PhylomeDB	Q8WVC0.
Gene expression databases
ArrayExpress	Q8WVC0.
Bgee	Q8WVC0.
CleanEx	HS_LEO1.
Genevestigator	Q8WVC0.
GermOnline	ENSG00000166477. Homo sapiens.
Family and domain databases
InterPro	IPR007149. Leo1. [Graphical view]
Pfam	PF04004. Leo1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LEO1. human.
GenomeRNAi	123169.
NextBio	81081.
SOURCE	Search...

Entry information

Entry name

LEO1_HUMAN

Accession

Primary (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 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.