Full text data of WDR61
WDR61
[Confidence: low (only semi-automatic identification from reviews)]
WD repeat-containing protein 61 (Meiotic recombination REC14 protein homolog; SKI8 homolog; Ski8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
WD repeat-containing protein 61 (Meiotic recombination REC14 protein homolog; SKI8 homolog; Ski8)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9GZS3
ID WDR61_HUMAN Reviewed; 305 AA.
AC Q9GZS3; D3DW84; Q6IA22; Q7Z4X4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=WD repeat-containing protein 61;
DE AltName: Full=Meiotic recombination REC14 protein homolog;
DE AltName: Full=SKI8 homolog;
DE Short=Ski8;
GN Name=WDR61;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shannon M., Thelen M.P.;
RT "Mammalian homologs of meiotic recombination proteins SpRec14 and
RT ScRec103.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tu Q., Yu L., Hu P.R., Fu Q., Cui Y.Y., Xin Y.R., Xu Z.G., Zhang X.N.,
RA Gong R.M., Wang X.K., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to S.mansoni
RT G protein beta subunit-like mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PAF1 COMPLEX,
RP AND IDENTIFICATION IN THE SKI COMPLEX.
RX PubMed=16024656; DOI=10.1101/gad.1292105;
RA Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H.,
RA Batra S.K., Tempst P., Reinberg D.;
RT "The human PAF complex coordinates transcription with events
RT downstream of RNA synthesis.";
RL Genes Dev. 19:1668-1673(2005).
RN [8]
RP FUNCTION.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
RA Tempst P., Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and
RT their roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=19952111; DOI=10.1101/gad.1834709;
RA Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T.,
RA Nakamura M., Hisatake K., Handa H.;
RT "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative
RT roles in RNA polymerase II elongation.";
RL Genes Dev. 23:2765-2777(2009).
RN [11]
RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
RP AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
RA Kim J., Guermah M., Roeder R.G.;
RT "The human PAF1 complex acts in chromatin transcription elongation
RT both independently and cooperatively with SII/TFIIS.";
RL Cell 140:491-503(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
RA Xu C., Min J.;
RT "Structure and function of WD40 domain proteins.";
RL Protein Cell 2:202-214(2011).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is
CC implicated in regulation of development and maintenance of
CC embryonic stem cell pluripotency. PAF1C associates with RNA
CC polymerase II through interaction with POLR2A CTD non-
CC phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
CC is involved in transcriptional elongation, acting both
CC indepentently and synergistically with TCEA1 and in cooperation
CC with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of
CC KMT2A/MLL1; it promotes leukemogenesis through association with
CC KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9
CC and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone
CC modifications such as ubiquitination of histone H2B and
CC methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the
CC RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme
CC UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C
CC is involved in mRNA 3' end formation probably through association
CC with cleavage and poly(A) factors. In case of infection by
CC influenza A strain H3N2, PAF1C associates with viral NS1 protein,
CC thereby regulating gene transcription. Required for mono- and
CC trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on
CC histone H3 'Lys-79' (H3K4me3). Required for Hox gene
CC transcription. Component of the SKI complex which is thought to be
CC involved in exosome-mediated RNA decay and associates with
CC transcriptionally active genes in a manner dependent on PAF1C.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
CC PAF1, LEO1, CTR9, RTF1 and WDR61. Component of the SKI complex
CC which consists of WDR61, SKIV2L and TTC37.
CC -!- INTERACTION:
CC Q6PD62:CTR9; NbExp=9; IntAct=EBI-358545, EBI-1019583;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (Probable).
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF309553; AAG31639.1; -; mRNA.
DR EMBL; AF100786; AAP97225.1; -; mRNA.
DR EMBL; AF127799; AAP97249.1; -; mRNA.
DR EMBL; AK024754; BAB14986.1; -; mRNA.
DR EMBL; CR457333; CAG33614.1; -; mRNA.
DR EMBL; CH471136; EAW99174.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99175.1; -; Genomic_DNA.
DR EMBL; BC010080; AAH10080.1; -; mRNA.
DR RefSeq; NP_079510.1; NM_025234.1.
DR RefSeq; XP_005254754.1; XM_005254697.1.
DR RefSeq; XP_005254755.1; XM_005254698.1.
DR UniGene; Hs.513055; -.
DR PDB; 3OW8; X-ray; 2.30 A; A/B/C/D=2-305.
DR PDBsum; 3OW8; -.
DR ProteinModelPortal; Q9GZS3; -.
DR SMR; Q9GZS3; 5-304.
DR DIP; DIP-36672N; -.
DR IntAct; Q9GZS3; 23.
DR MINT; MINT-1376321; -.
DR STRING; 9606.ENSP00000267973; -.
DR PhosphoSite; Q9GZS3; -.
DR DMDM; 74761365; -.
DR PaxDb; Q9GZS3; -.
DR PeptideAtlas; Q9GZS3; -.
DR PRIDE; Q9GZS3; -.
DR DNASU; 80349; -.
DR Ensembl; ENST00000267973; ENSP00000267973; ENSG00000140395.
DR Ensembl; ENST00000558311; ENSP00000453801; ENSG00000140395.
DR GeneID; 80349; -.
DR KEGG; hsa:80349; -.
DR UCSC; uc002bdn.3; human.
DR CTD; 80349; -.
DR GeneCards; GC15M078575; -.
DR HGNC; HGNC:30300; WDR61.
DR HPA; HPA039932; -.
DR HPA; HPA040065; -.
DR MIM; 609540; gene.
DR neXtProt; NX_Q9GZS3; -.
DR PharmGKB; PA142670595; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000036765; -.
DR HOVERGEN; HBG059813; -.
DR InParanoid; Q9GZS3; -.
DR KO; K12602; -.
DR OMA; IATGSHH; -.
DR PhylomeDB; Q9GZS3; -.
DR SignaLink; Q9GZS3; -.
DR ChiTaRS; WDR61; human.
DR EvolutionaryTrace; Q9GZS3; -.
DR GenomeRNAi; 80349; -.
DR NextBio; 70956; -.
DR PRO; PR:Q9GZS3; -.
DR ArrayExpress; Q9GZS3; -.
DR Bgee; Q9GZS3; -.
DR CleanEx; HS_WDR61; -.
DR Genevestigator; Q9GZS3; -.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0055087; C:Ski complex; IDA:UniProtKB.
DR GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW WD repeat; Wnt signaling pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 305 WD repeat-containing protein 61.
FT /FTId=PRO_0000245851.
FT REPEAT 14 57 WD 1.
FT REPEAT 62 101 WD 2.
FT REPEAT 104 143 WD 3.
FT REPEAT 146 187 WD 4.
FT REPEAT 188 227 WD 5.
FT REPEAT 230 269 WD 6.
FT REPEAT 272 305 WD 7.
FT MOD_RES 2 2 N-acetylthreonine.
FT CONFLICT 91 91 W -> R (in Ref. 2; AAP97249).
FT CONFLICT 176 176 D -> A (in Ref. 2; AAP97249).
FT CONFLICT 229 229 S -> G (in Ref. 4; CAG33614).
FT CONFLICT 255 255 S -> N (in Ref. 4; CAG33614).
FT CONFLICT 259 259 W -> R (in Ref. 2; AAP97249).
FT STRAND 6 11
FT STRAND 14 17
FT STRAND 19 24
FT STRAND 34 39
FT STRAND 44 50
FT STRAND 53 60
FT STRAND 67 72
FT STRAND 74 83
FT STRAND 86 92
FT TURN 93 96
FT STRAND 97 103
FT STRAND 112 114
FT STRAND 118 124
FT STRAND 128 134
FT TURN 135 137
FT STRAND 139 145
FT STRAND 147 149
FT STRAND 151 156
FT STRAND 160 167
FT STRAND 172 176
FT TURN 177 179
FT STRAND 182 186
FT STRAND 195 198
FT STRAND 204 208
FT STRAND 214 218
FT TURN 219 221
FT STRAND 224 228
FT STRAND 235 240
FT STRAND 244 251
FT STRAND 256 260
FT TURN 261 264
FT STRAND 265 270
FT STRAND 277 282
FT STRAND 286 293
FT STRAND 298 302
SQ SEQUENCE 305 AA; 33581 MW; A26C4BBD4F8ADB80 CRC64;
MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL
EGHQLGVVSV DISHTLPIAA SSSLDAHIRL WDLENGKQIK SIDAGPVDAW TLAFSPDSQY
LATGTHVGKV NIFGVESGKK EYSLDTRGKF ILSIAYSPDG KYLASGAIDG IINIFDIATG
KLLHTLEGHA MPIRSLTFSP DSQLLVTASD DGYIKIYDVQ HANLAGTLSG HASWVLNVAF
CPDDTHFVSS SSDKSVKVWD VGTRTCVHTF FDHQDQVWGV KYNGNGSKIV SVGDDQEIHI
YDCPI
//
ID WDR61_HUMAN Reviewed; 305 AA.
AC Q9GZS3; D3DW84; Q6IA22; Q7Z4X4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=WD repeat-containing protein 61;
DE AltName: Full=Meiotic recombination REC14 protein homolog;
DE AltName: Full=SKI8 homolog;
DE Short=Ski8;
GN Name=WDR61;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shannon M., Thelen M.P.;
RT "Mammalian homologs of meiotic recombination proteins SpRec14 and
RT ScRec103.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tu Q., Yu L., Hu P.R., Fu Q., Cui Y.Y., Xin Y.R., Xu Z.G., Zhang X.N.,
RA Gong R.M., Wang X.K., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to S.mansoni
RT G protein beta subunit-like mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PAF1 COMPLEX,
RP AND IDENTIFICATION IN THE SKI COMPLEX.
RX PubMed=16024656; DOI=10.1101/gad.1292105;
RA Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H.,
RA Batra S.K., Tempst P., Reinberg D.;
RT "The human PAF complex coordinates transcription with events
RT downstream of RNA synthesis.";
RL Genes Dev. 19:1668-1673(2005).
RN [8]
RP FUNCTION.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
RA Tempst P., Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and
RT their roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=19952111; DOI=10.1101/gad.1834709;
RA Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T.,
RA Nakamura M., Hisatake K., Handa H.;
RT "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative
RT roles in RNA polymerase II elongation.";
RL Genes Dev. 23:2765-2777(2009).
RN [11]
RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
RP AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
RA Kim J., Guermah M., Roeder R.G.;
RT "The human PAF1 complex acts in chromatin transcription elongation
RT both independently and cooperatively with SII/TFIIS.";
RL Cell 140:491-503(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
RA Xu C., Min J.;
RT "Structure and function of WD40 domain proteins.";
RL Protein Cell 2:202-214(2011).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is
CC implicated in regulation of development and maintenance of
CC embryonic stem cell pluripotency. PAF1C associates with RNA
CC polymerase II through interaction with POLR2A CTD non-
CC phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
CC is involved in transcriptional elongation, acting both
CC indepentently and synergistically with TCEA1 and in cooperation
CC with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of
CC KMT2A/MLL1; it promotes leukemogenesis through association with
CC KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9
CC and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone
CC modifications such as ubiquitination of histone H2B and
CC methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the
CC RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme
CC UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C
CC is involved in mRNA 3' end formation probably through association
CC with cleavage and poly(A) factors. In case of infection by
CC influenza A strain H3N2, PAF1C associates with viral NS1 protein,
CC thereby regulating gene transcription. Required for mono- and
CC trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on
CC histone H3 'Lys-79' (H3K4me3). Required for Hox gene
CC transcription. Component of the SKI complex which is thought to be
CC involved in exosome-mediated RNA decay and associates with
CC transcriptionally active genes in a manner dependent on PAF1C.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
CC PAF1, LEO1, CTR9, RTF1 and WDR61. Component of the SKI complex
CC which consists of WDR61, SKIV2L and TTC37.
CC -!- INTERACTION:
CC Q6PD62:CTR9; NbExp=9; IntAct=EBI-358545, EBI-1019583;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (Probable).
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF309553; AAG31639.1; -; mRNA.
DR EMBL; AF100786; AAP97225.1; -; mRNA.
DR EMBL; AF127799; AAP97249.1; -; mRNA.
DR EMBL; AK024754; BAB14986.1; -; mRNA.
DR EMBL; CR457333; CAG33614.1; -; mRNA.
DR EMBL; CH471136; EAW99174.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99175.1; -; Genomic_DNA.
DR EMBL; BC010080; AAH10080.1; -; mRNA.
DR RefSeq; NP_079510.1; NM_025234.1.
DR RefSeq; XP_005254754.1; XM_005254697.1.
DR RefSeq; XP_005254755.1; XM_005254698.1.
DR UniGene; Hs.513055; -.
DR PDB; 3OW8; X-ray; 2.30 A; A/B/C/D=2-305.
DR PDBsum; 3OW8; -.
DR ProteinModelPortal; Q9GZS3; -.
DR SMR; Q9GZS3; 5-304.
DR DIP; DIP-36672N; -.
DR IntAct; Q9GZS3; 23.
DR MINT; MINT-1376321; -.
DR STRING; 9606.ENSP00000267973; -.
DR PhosphoSite; Q9GZS3; -.
DR DMDM; 74761365; -.
DR PaxDb; Q9GZS3; -.
DR PeptideAtlas; Q9GZS3; -.
DR PRIDE; Q9GZS3; -.
DR DNASU; 80349; -.
DR Ensembl; ENST00000267973; ENSP00000267973; ENSG00000140395.
DR Ensembl; ENST00000558311; ENSP00000453801; ENSG00000140395.
DR GeneID; 80349; -.
DR KEGG; hsa:80349; -.
DR UCSC; uc002bdn.3; human.
DR CTD; 80349; -.
DR GeneCards; GC15M078575; -.
DR HGNC; HGNC:30300; WDR61.
DR HPA; HPA039932; -.
DR HPA; HPA040065; -.
DR MIM; 609540; gene.
DR neXtProt; NX_Q9GZS3; -.
DR PharmGKB; PA142670595; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000036765; -.
DR HOVERGEN; HBG059813; -.
DR InParanoid; Q9GZS3; -.
DR KO; K12602; -.
DR OMA; IATGSHH; -.
DR PhylomeDB; Q9GZS3; -.
DR SignaLink; Q9GZS3; -.
DR ChiTaRS; WDR61; human.
DR EvolutionaryTrace; Q9GZS3; -.
DR GenomeRNAi; 80349; -.
DR NextBio; 70956; -.
DR PRO; PR:Q9GZS3; -.
DR ArrayExpress; Q9GZS3; -.
DR Bgee; Q9GZS3; -.
DR CleanEx; HS_WDR61; -.
DR Genevestigator; Q9GZS3; -.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0055087; C:Ski complex; IDA:UniProtKB.
DR GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW WD repeat; Wnt signaling pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 305 WD repeat-containing protein 61.
FT /FTId=PRO_0000245851.
FT REPEAT 14 57 WD 1.
FT REPEAT 62 101 WD 2.
FT REPEAT 104 143 WD 3.
FT REPEAT 146 187 WD 4.
FT REPEAT 188 227 WD 5.
FT REPEAT 230 269 WD 6.
FT REPEAT 272 305 WD 7.
FT MOD_RES 2 2 N-acetylthreonine.
FT CONFLICT 91 91 W -> R (in Ref. 2; AAP97249).
FT CONFLICT 176 176 D -> A (in Ref. 2; AAP97249).
FT CONFLICT 229 229 S -> G (in Ref. 4; CAG33614).
FT CONFLICT 255 255 S -> N (in Ref. 4; CAG33614).
FT CONFLICT 259 259 W -> R (in Ref. 2; AAP97249).
FT STRAND 6 11
FT STRAND 14 17
FT STRAND 19 24
FT STRAND 34 39
FT STRAND 44 50
FT STRAND 53 60
FT STRAND 67 72
FT STRAND 74 83
FT STRAND 86 92
FT TURN 93 96
FT STRAND 97 103
FT STRAND 112 114
FT STRAND 118 124
FT STRAND 128 134
FT TURN 135 137
FT STRAND 139 145
FT STRAND 147 149
FT STRAND 151 156
FT STRAND 160 167
FT STRAND 172 176
FT TURN 177 179
FT STRAND 182 186
FT STRAND 195 198
FT STRAND 204 208
FT STRAND 214 218
FT TURN 219 221
FT STRAND 224 228
FT STRAND 235 240
FT STRAND 244 251
FT STRAND 256 260
FT TURN 261 264
FT STRAND 265 270
FT STRAND 277 282
FT STRAND 286 293
FT STRAND 298 302
SQ SEQUENCE 305 AA; 33581 MW; A26C4BBD4F8ADB80 CRC64;
MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL
EGHQLGVVSV DISHTLPIAA SSSLDAHIRL WDLENGKQIK SIDAGPVDAW TLAFSPDSQY
LATGTHVGKV NIFGVESGKK EYSLDTRGKF ILSIAYSPDG KYLASGAIDG IINIFDIATG
KLLHTLEGHA MPIRSLTFSP DSQLLVTASD DGYIKIYDVQ HANLAGTLSG HASWVLNVAF
CPDDTHFVSS SSDKSVKVWD VGTRTCVHTF FDHQDQVWGV KYNGNGSKIV SVGDDQEIHI
YDCPI
//
MIM
609540
*RECORD*
*FIELD* NO
609540
*FIELD* TI
*609540 WD REPEAT-CONTAINING PROTEIN 61; WDR61
;;SKI8, YEAST, HOMOLOG OF; SKI8
*FIELD* TX
read more
DESCRIPTION
WDR61 is a subunit of the human PAF and SKI complexes, which function in
transcriptional regulation and are involved in events downstream of RNA
synthesis, such as RNA surveillance (Zhu et al., 2005).
CLONING
Zhu et al. (2005) purified WDR61 from a 600-kD PAF complex and from a
400-kD SKI complex in HeLa cell nuclear extracts.
GENE FUNCTION
Zhu et al. (2005) determined that the human PAF and SKI complexes
interact. SKI8 RNA interference showed that SKI8 was required for
PAF-dependent mono- and trimethylation of histone H3 (see 602810) at
lys4 (H3-K4) and dimethylation of H3-K79, but not dimethylation of
H3-K36.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the WDR61
gene to chromosome 15 (TMAP RH26799).
*FIELD* RF
1. Zhu, B.; Mandal, S. S.; Pham, A.-D.; Zheng, Y.; Erdjument-Bromage,
H.; Batra, S. K.; Tempst, P.; Reinberg, D.: The human PAF complex
coordinates transcription with events downstream of RNA synthesis. Genes
Dev. 19: 1668-1673, 2005.
*FIELD* CD
Patricia A. Hartz: 8/22/2005
*FIELD* ED
mgross: 02/05/2013
mgross: 8/22/2005
*RECORD*
*FIELD* NO
609540
*FIELD* TI
*609540 WD REPEAT-CONTAINING PROTEIN 61; WDR61
;;SKI8, YEAST, HOMOLOG OF; SKI8
*FIELD* TX
read more
DESCRIPTION
WDR61 is a subunit of the human PAF and SKI complexes, which function in
transcriptional regulation and are involved in events downstream of RNA
synthesis, such as RNA surveillance (Zhu et al., 2005).
CLONING
Zhu et al. (2005) purified WDR61 from a 600-kD PAF complex and from a
400-kD SKI complex in HeLa cell nuclear extracts.
GENE FUNCTION
Zhu et al. (2005) determined that the human PAF and SKI complexes
interact. SKI8 RNA interference showed that SKI8 was required for
PAF-dependent mono- and trimethylation of histone H3 (see 602810) at
lys4 (H3-K4) and dimethylation of H3-K79, but not dimethylation of
H3-K36.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the WDR61
gene to chromosome 15 (TMAP RH26799).
*FIELD* RF
1. Zhu, B.; Mandal, S. S.; Pham, A.-D.; Zheng, Y.; Erdjument-Bromage,
H.; Batra, S. K.; Tempst, P.; Reinberg, D.: The human PAF complex
coordinates transcription with events downstream of RNA synthesis. Genes
Dev. 19: 1668-1673, 2005.
*FIELD* CD
Patricia A. Hartz: 8/22/2005
*FIELD* ED
mgross: 02/05/2013
mgross: 8/22/2005