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Q9GZL7 (WDR12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosome biogenesis protein WDR12
Alternative name(s):
WD repeat-containing protein 12
Gene names
Name:WDR12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. Ref.5 Ref.7

Subunit structure

Component of the PeBoW complex, composed of BOP1, PES1 and WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and WDR12. The PeBoW complex also associates with the 66S pre-ribosome. Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm Ref.4 Ref.5.

Induction

By MYC. Ref.5

Sequence similarities

Belongs to the WD repeat WDR12/YTM1 family.

Contains 7 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BOP1Q141373EBI-2490660,EBI-1050828

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 423422Ribosome biogenesis protein WDR12 HAMAP-Rule MF_03029
PRO_0000051358

Regions

Repeat99 – 13739WD 1 HAMAP-Rule MF_03029
Repeat138 – 18043WD 2 HAMAP-Rule MF_03029
Repeat187 – 22640WD 3 HAMAP-Rule MF_03029
Repeat255 – 29339WD 4 HAMAP-Rule MF_03029
Repeat295 – 33440WD 5 HAMAP-Rule MF_03029
Repeat340 – 38041WD 6 HAMAP-Rule MF_03029
Repeat384 – 42239WD 7 HAMAP-Rule MF_03029
Region98 – 423326Sufficient for nucleolar localization HAMAP-Rule MF_03029

Amino acid modifications

Modified residue21N-acetylalanine Ref.9

Natural variations

Natural variant721M → V.
VAR_012863
Natural variant751I → V. Ref.2
Corresponds to variant rs35212307 [ dbSNP | Ensembl ].
VAR_054888
Natural variant891Y → C.
VAR_012864
Natural variant2861E → G.
VAR_012865

Experimental info

Sequence conflict3331L → M in AAF60355. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9GZL7 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 6D088C640AC981D8

FASTA42347,708
        10         20         30         40         50         60 
MAQLQTRFYT DNKKYAVDDV PFSIPAASEI ADLSNIINKL LKDKNEFHKH VEFDFLIKGQ 

        70         80         90        100        110        120 
FLRMPLDKHM EMENISSEEV VEIEYVEKYT APQPEQCMFH DDWISSIKGA EEWILTGSYD 

       130        140        150        160        170        180 
KTSRIWSLEG KSIMTIVGHT DVVKDVAWVK KDSLSCLLLS ASMDQTILLW EWNVERNKVK 

       190        200        210        220        230        240 
ALHCCRGHAG SVDSIAVDGS GTKFCSGSWD KMLKIWSTVP TDEEDEMEES TNRPRKKQKT 

       250        260        270        280        290        300 
EQLGLTRTPI VTLSGHMEAV SSVLWSDAEE ICSASWDHTI RVWDVESGSL KSTLTGNKVF 

       310        320        330        340        350        360 
NCISYSPLCK RLASGSTDRH IRLWDPRTKD GSLVSLSLTS HTGWVTSVKW SPTHEQQLIS 

       370        380        390        400        410        420 
GSLDNIVKLW DTRSCKAPLY DLAAHEDKVL SVDWTDTGLL LSGGADNKLY SYRYSPTTSH 


VGA 

« Hide

References

« Hide 'large scale' references
[1]"Human homolog of Saccharomyces cervisiae YTM1."
Matsumoto S.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-75.
[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].
Tissue: Skin.
[4]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation."
Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.
J. Cell Biol. 170:367-378(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BOP1 AND PES1, SUBCELLULAR LOCATION, INDUCTION.
[6]"Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell proliferation via incorporation into the PeBoW-complex."
Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Eick D.
Nucleic Acids Res. 34:3030-3043(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PES1 AND WDR12.
[7]"Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit."
Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.
Mol. Cell. Biol. 27:3682-3694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BOP1 AND PES1.
[8]"The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing."
Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T., Gruber-Eber A., Kremmer E., Eick D.
Nucleic Acids Res. 35:789-800(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BOP1 AND PES1.
[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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF242546 mRNA. Translation: AAF60355.1.
AK001743 mRNA. Translation: BAA91875.1.
AK022781 mRNA. Translation: BAB14242.1.
AK022782 mRNA. Translation: BAB14243.1.
AK056092 mRNA. Translation: BAG51621.1.
BC008082 mRNA. Translation: AAH08082.1.
CCDSCCDS2356.1.
RefSeqNP_060726.3. NM_018256.3.
UniGeneHs.73291.

3D structure databases

ProteinModelPortalQ9GZL7.
SMRQ9GZL7. Positions 114-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120877. 36 interactions.
IntActQ9GZL7. 2 interactions.
MINTMINT-3065035.
STRING9606.ENSP00000261015.

PTM databases

PhosphoSiteQ9GZL7.

Polymorphism databases

DMDM20140802.

2D gel databases

SWISS-2DPAGEQ9GZL7.

Proteomic databases

MaxQBQ9GZL7.
PaxDbQ9GZL7.
PeptideAtlasQ9GZL7.
PRIDEQ9GZL7.

Protocols and materials databases

DNASU55759.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261015; ENSP00000261015; ENSG00000138442.
GeneID55759.
KEGGhsa:55759.
UCSCuc002uzl.3. human.

Organism-specific databases

CTD55759.
GeneCardsGC02M203709.
HGNCHGNC:14098. WDR12.
HPAHPA036389.
neXtProtNX_Q9GZL7.
PharmGKBPA37841.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000264464.
HOVERGENHBG054155.
InParanoidQ9GZL7.
KOK14863.
OMAATEEWIL.
OrthoDBEOG7Q2N5C.
PhylomeDBQ9GZL7.
TreeFamTF313023.

Enzyme and pathway databases

SignaLinkQ9GZL7.

Gene expression databases

ArrayExpressQ9GZL7.
BgeeQ9GZL7.
CleanExHS_WDR12.
GenevestigatorQ9GZL7.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
HAMAPMF_03029. WDR12.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR012972. NLE.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR028599. WDR12/Ytm1.
[Graphical view]
PfamPF08154. NLE. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiWDR12.
GenomeRNAi55759.
NextBio60775.
PROQ9GZL7.

Entry information

Entry nameWDR12_HUMAN
AccessionPrimary (citable) accession number: Q9GZL7
Secondary accession number(s): B3KPA9 expand/collapse secondary AC list , Q96HU0, Q9NV80, Q9NYI8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM