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Protein

Putative tRNA pseudouridine synthase Pus10

Gene

PUS10

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

Functioni

Pseudouridylate synthases catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. PUS10 catalyzes the formation of the universal psi55 in the GC loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell death via activation of procaspase 8 and BID cleavage. Required for the progression of the apoptotic signal through intrinsic mitochondrial cell death.Curated2 Publications

Catalytic activityi

tRNA uridine = tRNA pseudouridine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei344 – 3441NucleophileSequence analysis
Binding sitei414 – 4141SubstrateSequence analysis
Binding sitei485 – 4851SubstrateSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Putative tRNA pseudouridine synthase Pus10 (EC:5.4.99.-)
Alternative name(s):
Coiled-coil domain-containing protein 139
tRNA pseudouridine 55 synthase
Short name:
Psi55 synthase
tRNA pseudouridylate synthase
tRNA-uridine isomerase
Gene namesi
Name:PUS10
Synonyms:CCDC139, DOBI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:26505. PUS10.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400393.

Polymorphism and mutation databases

BioMutaiPUS10.
DMDMi121942830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Putative tRNA pseudouridine synthase Pus10PRO_0000299022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources

Post-translational modificationi

Proteolytically cleaved during TRAIL-induced cell death. Cleaved, in vitro, either by caspase-3 or caspase-8.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3MIT2.
MaxQBiQ3MIT2.
PaxDbiQ3MIT2.
PeptideAtlasiQ3MIT2.
PRIDEiQ3MIT2.

PTM databases

iPTMnetiQ3MIT2.
PhosphoSiteiQ3MIT2.

Expressioni

Gene expression databases

BgeeiQ3MIT2.
CleanExiHS_PUS10.
ExpressionAtlasiQ3MIT2. baseline and differential.
GenevisibleiQ3MIT2. HS.

Organism-specific databases

HPAiHPA044736.
HPA049582.

Interactioni

Protein-protein interaction databases

BioGridi127335. 1 interaction.
STRINGi9606.ENSP00000326003.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi9 – 1810Combined sources
Helixi22 – 287Combined sources
Helixi35 – 384Combined sources
Helixi41 – 5212Combined sources
Turni110 – 1178Combined sources
Helixi118 – 1203Combined sources
Helixi122 – 13413Combined sources
Beta strandi142 – 1476Combined sources
Helixi152 – 16918Combined sources
Helixi176 – 1783Combined sources
Helixi182 – 19817Combined sources
Beta strandi207 – 2159Combined sources
Helixi217 – 2204Combined sources
Helixi221 – 2277Combined sources
Helixi246 – 25510Combined sources
Helixi258 – 2647Combined sources
Beta strandi277 – 2859Combined sources
Beta strandi288 – 2969Combined sources
Beta strandi307 – 3159Combined sources
Helixi318 – 3236Combined sources
Helixi326 – 3305Combined sources
Beta strandi333 – 3419Combined sources
Beta strandi348 – 36215Combined sources
Helixi370 – 38112Combined sources
Beta strandi385 – 39511Combined sources
Helixi398 – 40912Combined sources
Beta strandi412 – 42211Combined sources
Helixi426 – 4294Combined sources
Helixi430 – 4345Combined sources
Beta strandi437 – 4437Combined sources
Helixi446 – 4483Combined sources
Turni449 – 4513Combined sources
Beta strandi456 – 47015Combined sources
Beta strandi473 – 4808Combined sources
Helixi486 – 4916Combined sources
Turni493 – 4964Combined sources
Beta strandi497 – 4993Combined sources
Helixi501 – 5055Combined sources
Beta strandi509 – 51911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V9KX-ray2.00A1-529[»]
ProteinModelPortaliQ3MIT2.
SMRiQ3MIT2. Positions 1-528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3MIT2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni304 – 31714RNA binding forefinger loopSequence analysisAdd
BLAST
Regioni442 – 45716RNA binding thumb loopSequence analysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili42 – 8948Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2364. Eukaryota.
COG1258. LUCA.
GeneTreeiENSGT00390000007529.
HOGENOMiHOG000030855.
HOVERGENiHBG056180.
InParanoidiQ3MIT2.
KOiK07583.
OMAiIKKVCQK.
OrthoDBiEOG7H4DV4.
PhylomeDBiQ3MIT2.
TreeFamiTF106109.

Family and domain databases

InterProiIPR020103. PsdUridine_synth_cat_dom.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3MIT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPLTEENKH VAQLLLNTGT CPRCIFRFCG VDFHAPYKLP YKELLNELQK
60 70 80 90 100
FLETEKDELI LEVMNPPPKK IRLQELEDSI DNLSQNGEGR ISVSHVGSTA
110 120 130 140 150
SKNSNLNVCN VCLGILQEFC EKDFIKKVCQ KVEASGFEFT SLVFSVSFPP
160 170 180 190 200
QLSVREHAAW LLVKQEMGKQ SLSLGRDDIV QLKEAYKWIT HPLFSEELGV
210 220 230 240 250
PIDGKSLFEV SVVFAHPETV EDCHFLAAIC PDCFKPAKNK QSVFTRMAVM
260 270 280 290 300
KALNKIKEED FLKQFPCPPN SPKAVCAVLE IECAHGAVFV AGRYNKYSRN
310 320 330 340 350
LPQTPWIIDG ERKLESSVEE LISDHLLAVF KAESFNFSSS GREDVDVRTL
360 370 380 390 400
GNGRPFAIEL VNPHRVHFTS QEIKELQQKI NNSSNKIQVR DLQLVTREAI
410 420 430 440 450
GHMKEGEEEK TKTYSALIWT NKAIQKKDIE FLNDIKDLKI DQKTPLRVLH
460 470 480 490 500
RRPLAVRARV IHFMETQYVD EHHFRLHLKT QAGTYIKEFV HGDFGRTKPN
510 520
IGSLMNVTAD ILELDVESVD VDWPPALDD
Length:529
Mass (Da):60,244
Last modified:October 25, 2005 - v1
Checksum:i44E7BD6ED9C9864E
GO

Sequence cautioni

The sequence CAI46123.1 differs from that shown.Partially unspliced pre-RNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081F → L in BAB71300 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti484 – 4841T → I in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035617

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056874 mRNA. Translation: BAB71300.1.
AL832208 Transcribed RNA. Translation: CAI46123.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAX00024.1.
BC101680 mRNA. Translation: AAI01681.1.
BC101706 mRNA. Translation: AAI01707.1.
CCDSiCCDS1865.1.
RefSeqiNP_001309052.1. NM_001322123.1.
NP_001309053.1. NM_001322124.1.
NP_653310.2. NM_144709.3.
XP_011530870.1. XM_011532568.1.
XP_011530872.1. XM_011532570.1.
XP_011530873.1. XM_011532571.1.
XP_011530874.1. XM_011532572.1.
XP_011530875.1. XM_011532573.1.
XP_011530876.1. XM_011532574.1.
XP_011530877.1. XM_011532575.1.
XP_011530878.1. XM_011532576.1.
XP_011530879.1. XM_011532577.1.
UniGeneiHs.368348.

Genome annotation databases

EnsembliENST00000316752; ENSP00000326003; ENSG00000162927.
ENST00000407787; ENSP00000386074; ENSG00000162927.
GeneIDi150962.
KEGGihsa:150962.
UCSCiuc002sao.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK056874 mRNA. Translation: BAB71300.1.
AL832208 Transcribed RNA. Translation: CAI46123.1. Sequence problems.
CH471053 Genomic DNA. Translation: EAX00024.1.
BC101680 mRNA. Translation: AAI01681.1.
BC101706 mRNA. Translation: AAI01707.1.
CCDSiCCDS1865.1.
RefSeqiNP_001309052.1. NM_001322123.1.
NP_001309053.1. NM_001322124.1.
NP_653310.2. NM_144709.3.
XP_011530870.1. XM_011532568.1.
XP_011530872.1. XM_011532570.1.
XP_011530873.1. XM_011532571.1.
XP_011530874.1. XM_011532572.1.
XP_011530875.1. XM_011532573.1.
XP_011530876.1. XM_011532574.1.
XP_011530877.1. XM_011532575.1.
XP_011530878.1. XM_011532576.1.
XP_011530879.1. XM_011532577.1.
UniGeneiHs.368348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V9KX-ray2.00A1-529[»]
ProteinModelPortaliQ3MIT2.
SMRiQ3MIT2. Positions 1-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127335. 1 interaction.
STRINGi9606.ENSP00000326003.

PTM databases

iPTMnetiQ3MIT2.
PhosphoSiteiQ3MIT2.

Polymorphism and mutation databases

BioMutaiPUS10.
DMDMi121942830.

Proteomic databases

EPDiQ3MIT2.
MaxQBiQ3MIT2.
PaxDbiQ3MIT2.
PeptideAtlasiQ3MIT2.
PRIDEiQ3MIT2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316752; ENSP00000326003; ENSG00000162927.
ENST00000407787; ENSP00000386074; ENSG00000162927.
GeneIDi150962.
KEGGihsa:150962.
UCSCiuc002sao.4. human.

Organism-specific databases

CTDi150962.
GeneCardsiPUS10.
HGNCiHGNC:26505. PUS10.
HPAiHPA044736.
HPA049582.
MIMi612787. gene.
neXtProtiNX_Q3MIT2.
PharmGKBiPA162400393.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2364. Eukaryota.
COG1258. LUCA.
GeneTreeiENSGT00390000007529.
HOGENOMiHOG000030855.
HOVERGENiHBG056180.
InParanoidiQ3MIT2.
KOiK07583.
OMAiIKKVCQK.
OrthoDBiEOG7H4DV4.
PhylomeDBiQ3MIT2.
TreeFamiTF106109.

Miscellaneous databases

ChiTaRSiPUS10. human.
EvolutionaryTraceiQ3MIT2.
GenomeRNAii150962.
PROiQ3MIT2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3MIT2.
CleanExiHS_PUS10.
ExpressionAtlasiQ3MIT2. baseline and differential.
GenevisibleiQ3MIT2. HS.

Family and domain databases

InterProiIPR020103. PsdUridine_synth_cat_dom.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Prostate.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain.
  5. "Identification of modulators of TRAIL-induced apoptosis via RNAi-based phenotypic screening."
    Aza-Blanc P., Cooper C.L., Wagner K., Batalov S., Deveraux Q.L., Cooke M.P.
    Mol. Cell 12:627-637(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. "DOBI is cleaved by caspases during TRAIL-induced apoptotic cell death."
    Park S.Y., Shin J.N., Woo H.N., Piya S., Moon A.R., Seo Y.W., Seol D.W., Kim T.H.
    BMB Rep. 42:511-515(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE, FUNCTION.
  8. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  9. "Crystal structure of human Pus10, a novel pseudouridine synthase."
    McCleverty C.J., Hornsby M., Spraggon G., Kreusch A.
    J. Mol. Biol. 373:1243-1254(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-484.

Entry informationi

Entry nameiPUS10_HUMAN
AccessioniPrimary (citable) accession number: Q3MIT2
Secondary accession number(s): Q5JPJ5, Q96MI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 25, 2005
Last modified: July 6, 2016
This is version 93 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.