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Q8WVC0

- LEO1_HUMAN

UniProt

Q8WVC0 - LEO1_HUMAN

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Protein

RNA polymerase-associated protein LEO1

Gene

LEO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Biological processi

  1. endodermal cell fate commitment Source: UniProtKB
  2. histone H2B ubiquitination Source: UniProtKB
  3. histone monoubiquitination Source: UniProtKB
  4. mRNA polyadenylation Source: UniProtKB
  5. negative regulation of myeloid cell differentiation Source: UniProtKB
  6. positive regulation of mRNA 3'-end processing Source: UniProtKB
  7. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. stem cell maintenance Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB-KW
  11. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_200753. formation of the beta-catenin:TCF transactivating complex.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase-associated protein LEO1
Alternative name(s):
Replicative senescence down-regulated leo1-like protein
Gene namesi
Name:LEO1
Synonyms:RDL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:30401. LEO1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. Cdc73/Paf1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671558.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 666665RNA polymerase-associated protein LEO1PRO_0000247819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei10 – 101Phosphoserine2 Publications
Modified residuei14 – 141Phosphoserine3 Publications
Modified residuei151 – 1511Phosphoserine3 Publications
Modified residuei154 – 1541Phosphoserine3 Publications
Modified residuei162 – 1621Phosphoserine2 Publications
Modified residuei171 – 1711Phosphoserine2 Publications
Modified residuei179 – 1791Phosphoserine2 Publications
Modified residuei188 – 1881Phosphothreonine3 Publications
Modified residuei197 – 1971Phosphoserine3 Publications
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei212 – 2121Phosphoserine3 Publications
Modified residuei220 – 2201Phosphoserine3 Publications
Modified residuei229 – 2291Phosphoserine3 Publications
Modified residuei238 – 2381Phosphoserine3 Publications
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei279 – 2791Phosphoserine3 Publications
Modified residuei294 – 2941Phosphoserine2 Publications
Modified residuei296 – 2961Phosphoserine1 Publication
Modified residuei300 – 3001Phosphoserine2 Publications
Modified residuei607 – 6071Phosphoserine2 Publications
Modified residuei608 – 6081Phosphoserine2 Publications
Modified residuei610 – 6101Phosphoserine2 Publications
Modified residuei614 – 6141Phosphoserine1 Publication
Modified residuei629 – 6291Phosphothreonine2 Publications
Modified residuei630 – 6301Phosphoserine5 Publications
Modified residuei658 – 6581Phosphoserine7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WVC0.
PaxDbiQ8WVC0.
PeptideAtlasiQ8WVC0.
PRIDEiQ8WVC0.

PTM databases

PhosphoSiteiQ8WVC0.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8WVC0.
CleanExiHS_LEO1.
GenevestigatoriQ8WVC0.

Organism-specific databases

HPAiHPA040741.
HPA040941.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC73Q6P1J911EBI-932432,EBI-930143
CTNNB1P352222EBI-932432,EBI-491549
PAF1Q8N7H517EBI-932432,EBI-2607770
TCEA1P231934EBI-932432,EBI-2608271

Protein-protein interaction databases

BioGridi125817. 32 interactions.
DIPiDIP-37885N.
IntActiQ8WVC0. 25 interactions.
STRINGi9606.ENSP00000299601.

Structurei

Secondary structure

1
666
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi372 – 3776
Helixi391 – 3933
Helixi409 – 4168
Beta strandi418 – 4203
Beta strandi422 – 4265
Beta strandi432 – 44312
Beta strandi448 – 4525
Beta strandi455 – 4595

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M6TX-ray2.50A370-462[»]
ProteinModelPortaliQ8WVC0.
SMRiQ8WVC0. Positions 370-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 329327Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the LEO1 family.Curated

Phylogenomic databases

eggNOGiNOG130430.
GeneTreeiENSGT00550000074952.
HOGENOMiHOG000253934.
HOVERGENiHBG081913.
InParanoidiQ8WVC0.
KOiK15177.
OMAiEERPQMS.
OrthoDBiEOG7W41BG.
PhylomeDBiQ8WVC0.
TreeFamiTF321961.

Family and domain databases

InterProiIPR007149. Leo1.
[Graphical view]
PfamiPF04004. Leo1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WVC0-1) [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
MADMEDLFGS DADSEAERKD SDSGSDSDSD QENAASGSNA SGSESDQDER
60 70 80 90 100
GDSGQPSNKE LFGDDSEDEG ASHHSGSDNH SERSDNRSEA SERSDHEDND
110 120 130 140 150
PSDVDQHSGS EAPNDDEDEG HRSDGGSHHS EAEGSEKAHS DDEKWGREDK
160 170 180 190 200
SDQSDDEKIQ NSDDEERAQG SDEDKLQNSD DDEKMQNTDD EERPQLSDDE
210 220 230 240 250
RQQLSEEEKA NSDDERPVAS DNDDEKQNSD DEEQPQLSDE EKMQNSDDER
260 270 280 290 300
PQASDEEHRH SDDEEEQDHK SESARGSDSE DEVLRMKRKN AIASDSEADS
310 320 330 340 350
DTEVPKDNSG TMDLFGGADD ISSGSDGEDK PPTPGQPVDE NGLPQDQQEE
360 370 380 390 400
EPIPETRIEV EIPKVNTDLG NDLYFVKLPN FLSVEPRPFD PQYYEDEFED
410 420 430 440 450
EEMLDEEGRT RLKLKVENTI RWRIRRDEEG NEIKESNARI VKWSDGSMSL
460 470 480 490 500
HLGNEVFDVY KAPLQGDHNH LFIRQGTGLQ GQAVFKTKLT FRPHSTDSAT
510 520 530 540 550
HRKMTLSLAD RCSKTQKIRI LPMAGRDPEC QRTEMIKKEE ERLRASIRRE
560 570 580 590 600
SQQRRMREKQ HQRGLSASYL EPDRYDEEEE GEESISLAAI KNRYKGGIRE
610 620 630 640 650
ERARIYSSDS DEGSEEDKAQ RLLKAKKLTS DEEGEPSGKR KAEDDDKANK
660
KHKKYVISDE EEEDDD
Length:666
Mass (Da):75,404
Last modified:March 1, 2002 - v1
Checksum:iEB405BE0EDA7E0B0
GO
Isoform 2 (identifier: Q8WVC0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     387-446: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:606
Mass (Da):68,004
Checksum:iAF31C9793F9545D5
GO

Sequence cautioni

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei387 – 44660Missing in isoform 2. 1 PublicationVSP_020051Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY302186 mRNA. Translation: AAP68819.1.
AK055762 mRNA. Translation: BAB71006.1. Frameshift.
BC018147 mRNA. Translation: AAH18147.1.
CCDSiCCDS10146.1. [Q8WVC0-1]
CCDS66767.1. [Q8WVC0-2]
RefSeqiNP_001273359.1. NM_001286430.1. [Q8WVC0-2]
NP_620147.1. NM_138792.3. [Q8WVC0-1]
UniGeneiHs.567662.

Genome annotation databases

EnsembliENST00000299601; ENSP00000299601; ENSG00000166477. [Q8WVC0-1]
ENST00000315141; ENSP00000314610; ENSG00000166477. [Q8WVC0-2]
GeneIDi123169.
KEGGihsa:123169.
UCSCiuc002abo.3. human. [Q8WVC0-1]
uc010bfd.3. human. [Q8WVC0-2]

Polymorphism databases

DMDMi74751545.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY302186 mRNA. Translation: AAP68819.1 .
AK055762 mRNA. Translation: BAB71006.1 . Frameshift.
BC018147 mRNA. Translation: AAH18147.1 .
CCDSi CCDS10146.1. [Q8WVC0-1 ]
CCDS66767.1. [Q8WVC0-2 ]
RefSeqi NP_001273359.1. NM_001286430.1. [Q8WVC0-2 ]
NP_620147.1. NM_138792.3. [Q8WVC0-1 ]
UniGenei Hs.567662.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4M6T X-ray 2.50 A 370-462 [» ]
ProteinModelPortali Q8WVC0.
SMRi Q8WVC0. Positions 370-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125817. 32 interactions.
DIPi DIP-37885N.
IntActi Q8WVC0. 25 interactions.
STRINGi 9606.ENSP00000299601.

PTM databases

PhosphoSitei Q8WVC0.

Polymorphism databases

DMDMi 74751545.

Proteomic databases

MaxQBi Q8WVC0.
PaxDbi Q8WVC0.
PeptideAtlasi Q8WVC0.
PRIDEi Q8WVC0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299601 ; ENSP00000299601 ; ENSG00000166477 . [Q8WVC0-1 ]
ENST00000315141 ; ENSP00000314610 ; ENSG00000166477 . [Q8WVC0-2 ]
GeneIDi 123169.
KEGGi hsa:123169.
UCSCi uc002abo.3. human. [Q8WVC0-1 ]
uc010bfd.3. human. [Q8WVC0-2 ]

Organism-specific databases

CTDi 123169.
GeneCardsi GC15M052230.
HGNCi HGNC:30401. LEO1.
HPAi HPA040741.
HPA040941.
MIMi 610507. gene.
neXtProti NX_Q8WVC0.
PharmGKBi PA142671558.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG130430.
GeneTreei ENSGT00550000074952.
HOGENOMi HOG000253934.
HOVERGENi HBG081913.
InParanoidi Q8WVC0.
KOi K15177.
OMAi EERPQMS.
OrthoDBi EOG7W41BG.
PhylomeDBi Q8WVC0.
TreeFami TF321961.

Enzyme and pathway databases

Reactomei REACT_200753. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

ChiTaRSi LEO1. human.
GeneWikii LEO1.
GenomeRNAii 123169.
NextBioi 81081.
PROi Q8WVC0.
SOURCEi Search...

Gene expression databases

Bgeei Q8WVC0.
CleanExi HS_LEO1.
Genevestigatori Q8WVC0.

Family and domain databases

InterProi IPR007149. Leo1.
[Graphical view ]
Pfami PF04004. Leo1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLEO1_HUMAN
AccessioniPrimary (citable) accession number: Q8WVC0
Secondary accession number(s): Q96N99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 105 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3