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Protein

Pescadillo homolog

Gene

PES1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesisUniRule annotationSAAS annotation, rRNA processingUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Pescadillo homologUniRule annotation
Gene namesi
Name:PES1UniRule annotationImported
ORF Names:hCG_2010949Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  • Nucleusnucleolus UniRule annotation
  • Nucleusnucleoplasm UniRule annotation
  • Chromosome UniRule annotation

  • Note: Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli.UniRule annotation
  • Nucleusnucleoplasm SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

ChromosomeUniRule annotation, NucleusUniRule annotationSAAS annotation

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33190.

PTM / Processingi

Post-translational modificationi

Sumoylated.UniRule annotation

Keywords - PTMi

Ubl conjugationUniRule annotation

Interactioni

Subunit structurei

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. Interacts with IRS1 and UBTF. May interact with MAP1B.UniRule annotation

Protein-protein interaction databases

STRINGi9606.ENSP00000346725.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 41594BRCTInterPro annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili518 – 54528Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the pescadillo family.UniRule annotationSAAS annotation
Contains 1 BRCT domain.UniRule annotation

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

eggNOGiKOG2481. Eukaryota.
COG5163. LUCA.
HOVERGENiHBG023409.
OMAiQYISRDY.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
HAMAPiMF_03028. Pescadillo.
InterProiIPR001357. BRCT_dom.
IPR010613. PES.
[Graphical view]
PfamiPF16589. BRCT_2. 1 hit.
PF06732. Pescadillo_N. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2RDF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH
60 70 80 90 100
KKKVNKGSTA ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE
110 120 130 140 150
WNTVERLKDN KPNYKLDHII KERYPTFIDA LRDLDDALSM CFLFSTFPRT
160 170 180 190 200
GKCHVQTIQL CRRLTVEFMH YIIAARALRK VFLSIKGIYY QAEVLGQPIV
210 220 230 240 250
WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ LLNLHYPPKL
260 270 280 290 300
EGQAQAEAKA GEGTYALDSE SCMEKLAALS ASLARVVVPA TEEEAEVDEF
310 320 330 340 350
PTDGEMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF
360 370 380 390 400
GGEVSWDKSL CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD
410 420 430 440 450
SVNARLLLPV AEYFSGVQLP PHLSPFVTEK EGDYVPPEKL KLLALQRGED
460 470 480 490 500
PGNLNESEEE EEEDDNNEGD GDEEGENEEE EEDAEAGSEK EEEARLAALE
510 520 530 540 550
EQRMEGKKPR VMAGTLKLED KQRLAQEEES EAKRLAIMMM KKREKYLYQK
560 570 580
IMFGKRRKIR EANKLAEKRK AHDEAVRSEK KAKKARPE
Length:588
Mass (Da):68,003
Last modified:July 1, 2008 - v1
Checksum:iCB6201D6E34D82B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei588 – 5881Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK315518 mRNA. Translation: BAG37899.1.
AB451380 mRNA. Translation: BAG70194.1.
CH471095 Genomic DNA. Translation: EAW59904.1.
RefSeqiNP_055118.1. NM_014303.3.
UniGeneiHs.517543.

Genome annotation databases

GeneIDi23481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK315518 mRNA. Translation: BAG37899.1.
AB451380 mRNA. Translation: BAG70194.1.
CH471095 Genomic DNA. Translation: EAW59904.1.
RefSeqiNP_055118.1. NM_014303.3.
UniGeneiHs.517543.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000346725.

Protocols and materials databases

DNASUi23481.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23481.

Organism-specific databases

CTDi23481.
PharmGKBiPA33190.

Phylogenomic databases

eggNOGiKOG2481. Eukaryota.
COG5163. LUCA.
HOVERGENiHBG023409.
OMAiQYISRDY.

Miscellaneous databases

ChiTaRSiPES1. human.
GenomeRNAii23481.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
HAMAPiMF_03028. Pescadillo.
InterProiIPR001357. BRCT_dom.
IPR010613. PES.
[Graphical view]
PfamiPF16589. BRCT_2. 1 hit.
PF06732. Pescadillo_N. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. "NEDO functional analysis of protein and research application project."
    Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: TongueImported.
  4. "Human Protein Factory: an infrastructure to convert the human transcriptome into the in vitro-expressed human proteome of versatile utility."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J.-I., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K.-I., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J.-I., Watanabe S., Nomura N.
    Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiB2RDF2_HUMAN
AccessioniPrimary (citable) accession number: B2RDF2
Secondary accession number(s): A6NNS1
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: July 6, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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.