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Protein

WD repeat-containing protein 61

Gene

WDR61

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Component of the SKI complex which is thought to be involved in exosome-mediated RNA decay and associates with transcriptionally active genes in a manner dependent on PAF1C.4 Publications

GO - Biological processi

  • histone H3-K4 trimethylation Source: UniProtKB
  • negative regulation of myeloid cell differentiation Source: UniProtKB
  • positive regulation of histone H3-K4 methylation Source: UniProtKB
  • positive regulation of histone H3-K79 methylation Source: UniProtKB
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

SignaLinkiQ9GZS3.

Names & Taxonomyi

Protein namesi
Recommended name:
WD repeat-containing protein 61
Alternative name(s):
Meiotic recombination REC14 protein homolog
SKI8 homolog
Short name:
Ski8
Cleaved into the following chain:
Gene namesi
Name:WDR61
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30300. WDR61.

Subcellular locationi

GO - Cellular componenti

  • Cdc73/Paf1 complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • Ski complex Source: UniProtKB
  • transcriptionally active chromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670595.

Polymorphism and mutation databases

BioMutaiWDR61.
DMDMi74761365.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305WD repeat-containing protein 61PRO_0000245851Add
BLAST
Initiator methionineiRemoved; alternateCombined sources
Chaini2 – 305304WD repeat-containing protein 61, N-terminally processedPRO_0000425748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei2 – 21N-acetylthreonine; in WD repeat-containing protein 61, N-terminally processedCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9GZS3.
MaxQBiQ9GZS3.
PaxDbiQ9GZS3.
PeptideAtlasiQ9GZS3.
PRIDEiQ9GZS3.

PTM databases

iPTMnetiQ9GZS3.
PhosphoSiteiQ9GZS3.

Expressioni

Gene expression databases

BgeeiQ9GZS3.
CleanExiHS_WDR61.
ExpressionAtlasiQ9GZS3. baseline and differential.
GenevisibleiQ9GZS3. HS.

Organism-specific databases

HPAiHPA039932.
HPA040065.

Interactioni

Subunit structurei

Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Component of the SKI complex which consists of WDR61, SKIV2L and TTC37.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTR9Q6PD6210EBI-358545,EBI-1019583

Protein-protein interaction databases

BioGridi123255. 46 interactions.
DIPiDIP-36672N.
IntActiQ9GZS3. 27 interactions.
MINTiMINT-1376321.
STRINGi9606.ENSP00000267973.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Beta strandi14 – 174Combined sources
Beta strandi19 – 246Combined sources
Turni28 – 303Combined sources
Beta strandi34 – 396Combined sources
Beta strandi44 – 507Combined sources
Beta strandi53 – 608Combined sources
Beta strandi67 – 726Combined sources
Beta strandi74 – 8310Combined sources
Beta strandi86 – 927Combined sources
Turni93 – 964Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi128 – 1347Combined sources
Turni135 – 1373Combined sources
Beta strandi139 – 1457Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi160 – 1678Combined sources
Beta strandi172 – 1765Combined sources
Turni177 – 1793Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi214 – 2185Combined sources
Turni219 – 2213Combined sources
Beta strandi224 – 2285Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi244 – 2518Combined sources
Beta strandi256 – 2605Combined sources
Turni261 – 2644Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi286 – 2938Combined sources
Beta strandi298 – 3025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OW8X-ray2.30A/B/C/D2-305[»]
ProteinModelPortaliQ9GZS3.
SMRiQ9GZS3. Positions 5-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GZS3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati14 – 5744WD 1Add
BLAST
Repeati62 – 10140WD 2Add
BLAST
Repeati104 – 14340WD 3Add
BLAST
Repeati146 – 18742WD 4Add
BLAST
Repeati188 – 22740WD 5Add
BLAST
Repeati230 – 26940WD 6Add
BLAST
Repeati272 – 30534WD 7Add
BLAST

Sequence similaritiesi

Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG4155. Eukaryota.
ENOG410XP1Z. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000036765.
HOVERGENiHBG059813.
InParanoidiQ9GZS3.
KOiK12602.
OMAiWKWSDER.
PhylomeDBiQ9GZS3.
TreeFamiTF324549.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9GZS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR
60 70 80 90 100
DERLDLQWSL EGHQLGVVSV DISHTLPIAA SSSLDAHIRL WDLENGKQIK
110 120 130 140 150
SIDAGPVDAW TLAFSPDSQY LATGTHVGKV NIFGVESGKK EYSLDTRGKF
160 170 180 190 200
ILSIAYSPDG KYLASGAIDG IINIFDIATG KLLHTLEGHA MPIRSLTFSP
210 220 230 240 250
DSQLLVTASD DGYIKIYDVQ HANLAGTLSG HASWVLNVAF CPDDTHFVSS
260 270 280 290 300
SSDKSVKVWD VGTRTCVHTF FDHQDQVWGV KYNGNGSKIV SVGDDQEIHI

YDCPI
Length:305
Mass (Da):33,581
Last modified:March 1, 2001 - v1
Checksum:iA26C4BBD4F8ADB80
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911W → R in AAP97249 (Ref. 2) Curated
Sequence conflicti176 – 1761D → A in AAP97249 (Ref. 2) Curated
Sequence conflicti229 – 2291S → G in CAG33614 (Ref. 4) Curated
Sequence conflicti255 – 2551S → N in CAG33614 (Ref. 4) Curated
Sequence conflicti259 – 2591W → R in AAP97249 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309553 mRNA. Translation: AAG31639.1.
AF100786 mRNA. Translation: AAP97225.1.
AF127799 mRNA. Translation: AAP97249.1.
AK024754 mRNA. Translation: BAB14986.1.
CR457333 mRNA. Translation: CAG33614.1.
CH471136 Genomic DNA. Translation: EAW99174.1.
CH471136 Genomic DNA. Translation: EAW99175.1.
BC010080 mRNA. Translation: AAH10080.1.
CCDSiCCDS10300.1.
RefSeqiNP_001290176.1. NM_001303247.1.
NP_001290177.1. NM_001303248.1.
NP_079510.1. NM_025234.2.
XP_011520396.1. XM_011522094.1.
UniGeneiHs.513055.

Genome annotation databases

EnsembliENST00000267973; ENSP00000267973; ENSG00000140395.
ENST00000558311; ENSP00000453801; ENSG00000140395.
GeneIDi80349.
KEGGihsa:80349.
UCSCiuc002bdn.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309553 mRNA. Translation: AAG31639.1.
AF100786 mRNA. Translation: AAP97225.1.
AF127799 mRNA. Translation: AAP97249.1.
AK024754 mRNA. Translation: BAB14986.1.
CR457333 mRNA. Translation: CAG33614.1.
CH471136 Genomic DNA. Translation: EAW99174.1.
CH471136 Genomic DNA. Translation: EAW99175.1.
BC010080 mRNA. Translation: AAH10080.1.
CCDSiCCDS10300.1.
RefSeqiNP_001290176.1. NM_001303247.1.
NP_001290177.1. NM_001303248.1.
NP_079510.1. NM_025234.2.
XP_011520396.1. XM_011522094.1.
UniGeneiHs.513055.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OW8X-ray2.30A/B/C/D2-305[»]
ProteinModelPortaliQ9GZS3.
SMRiQ9GZS3. Positions 5-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123255. 46 interactions.
DIPiDIP-36672N.
IntActiQ9GZS3. 27 interactions.
MINTiMINT-1376321.
STRINGi9606.ENSP00000267973.

PTM databases

iPTMnetiQ9GZS3.
PhosphoSiteiQ9GZS3.

Polymorphism and mutation databases

BioMutaiWDR61.
DMDMi74761365.

Proteomic databases

EPDiQ9GZS3.
MaxQBiQ9GZS3.
PaxDbiQ9GZS3.
PeptideAtlasiQ9GZS3.
PRIDEiQ9GZS3.

Protocols and materials databases

DNASUi80349.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267973; ENSP00000267973; ENSG00000140395.
ENST00000558311; ENSP00000453801; ENSG00000140395.
GeneIDi80349.
KEGGihsa:80349.
UCSCiuc002bdn.4. human.

Organism-specific databases

CTDi80349.
GeneCardsiWDR61.
HGNCiHGNC:30300. WDR61.
HPAiHPA039932.
HPA040065.
MIMi609540. gene.
neXtProtiNX_Q9GZS3.
PharmGKBiPA142670595.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4155. Eukaryota.
ENOG410XP1Z. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000036765.
HOVERGENiHBG059813.
InParanoidiQ9GZS3.
KOiK12602.
OMAiWKWSDER.
PhylomeDBiQ9GZS3.
TreeFamiTF324549.

Enzyme and pathway databases

SignaLinkiQ9GZS3.

Miscellaneous databases

ChiTaRSiWDR61. human.
EvolutionaryTraceiQ9GZS3.
GenomeRNAii80349.
PROiQ9GZS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZS3.
CleanExiHS_WDR61.
ExpressionAtlasiQ9GZS3. baseline and differential.
GenevisibleiQ9GZS3. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian homologs of meiotic recombination proteins SpRec14 and ScRec103."
    Shannon M., Thelen M.P.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and sequencing of a novel human cDNA homologous to S.mansoni G protein beta subunit-like mRNA."
    Tu Q., Yu L., Hu P.R., Fu Q., Cui Y.Y., Xin Y.R., Xu Z.G., Zhang X.N., Gong R.M., Wang X.K., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , 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].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Uterus.
  7. "The human PAF complex coordinates transcription with events downstream of RNA synthesis."
    Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D.
    Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PAF1 COMPLEX, IDENTIFICATION IN THE SKI COMPLEX.
  8. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
    Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Structure and function of WD40 domain proteins."
    Xu C., Min J.
    Protein Cell 2:202-214(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiWDR61_HUMAN
AccessioniPrimary (citable) accession number: Q9GZS3
Secondary accession number(s): D3DW84, Q6IA22, Q7Z4X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.