Q3MIT2 (PUS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PUS10
Synonyms:	CCDC139, DOBI

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.7
Catalytic activity	tRNA uridine = tRNA pseudouridine.
Post-translational modification	Proteolytically cleaved during TRAIL-induced cell death. Cleaved, in vitro, either by caspase-3 or caspase-8. Ref.7
Sequence similarities	Belongs to the pseudouridine synthase Pus10 family.
Sequence caution	The sequence CAI46123.1 differs from that shown. Reason: Partially unspliced pre-RNA.

Ontologies

Keywords
Biological process	tRNA processing
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pseudouridine synthesis Inferred from electronic annotation. Source: InterPro tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro pseudouridine synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 529

529

Putative tRNA pseudouridine synthase Pus10

PRO_0000299022

Regions

Region

304 – 317

14

RNA binding forefinger loop Potential

Region

442 – 457

16

RNA binding thumb loop Potential

Coiled coil

42 – 89

48

Potential

Sites

Active site

344

1

Nucleophile Potential

Binding site

414

1

Substrate Potential

Binding site

485

1

Substrate Potential

Amino acid modifications

Modified residue

79

1

Phosphoserine Ref.6

Modified residue

84

1

Phosphoserine Ref.6

Natural variations

Natural variant

484

1

T → I in a colorectal cancer sample; somatic mutation. Ref.9

VAR_035617

Experimental info

Sequence conflict

208

1

F → L in BAB71300. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

529

Helix Strand Turn

Details...

Helix

6 – 8

3

Helix

9 – 18

10

Helix

22 – 28

7

Helix

35 – 38

4

Helix

41 – 52

12

Turn

110 – 117

8

Helix

118 – 120

3

Helix

122 – 134

13

Beta strand

142 – 147

6

Helix

152 – 169

18

Helix

176 – 178

3

Helix

182 – 198

17

Beta strand

207 – 215

9

Helix

217 – 220

4

Helix

221 – 227

7

Helix

246 – 255

10

Helix

258 – 264

7

Beta strand

277 – 285

9

Beta strand

288 – 296

9

Beta strand

307 – 315

9

Helix

318 – 323

6

Helix

326 – 330

5

Beta strand

333 – 341

9

Beta strand

348 – 362

15

Helix

370 – 381

12

Beta strand

385 – 395

11

Helix

398 – 409

12

Beta strand

412 – 422

11

Helix

426 – 429

4

Helix

430 – 434

5

Beta strand

437 – 443

7

Helix

446 – 448

3

Turn

449 – 451

3

Beta strand

456 – 470

15

Beta strand

473 – 480

8

Helix

486 – 491

6

Turn

493 – 496

4

Beta strand

497 – 499

3

Helix

501 – 505

5

Beta strand

509 – 519

11

Sequences

	Sequence		Length	Mass (Da)
	Q3MIT2 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: 44E7BD6ED9C9864E	FASTA	529	60,244
	10 20 30 40 50 60 MFPLTEENKH VAQLLLNTGT CPRCIFRFCG VDFHAPYKLP YKELLNELQK FLETEKDELI 70 80 90 100 110 120 LEVMNPPPKK IRLQELEDSI DNLSQNGEGR ISVSHVGSTA SKNSNLNVCN VCLGILQEFC 130 140 150 160 170 180 EKDFIKKVCQ KVEASGFEFT SLVFSVSFPP QLSVREHAAW LLVKQEMGKQ SLSLGRDDIV 190 200 210 220 230 240 QLKEAYKWIT HPLFSEELGV PIDGKSLFEV SVVFAHPETV EDCHFLAAIC PDCFKPAKNK 250 260 270 280 290 300 QSVFTRMAVM KALNKIKEED FLKQFPCPPN SPKAVCAVLE IECAHGAVFV AGRYNKYSRN 310 320 330 340 350 360 LPQTPWIIDG ERKLESSVEE LISDHLLAVF KAESFNFSSS GREDVDVRTL GNGRPFAIEL 370 380 390 400 410 420 VNPHRVHFTS QEIKELQQKI NNSSNKIQVR DLQLVTREAI GHMKEGEEEK TKTYSALIWT 430 440 450 460 470 480 NKAIQKKDIE FLNDIKDLKI DQKTPLRVLH RRPLAVRARV IHFMETQYVD EHHFRLHLKT 490 500 510 520 QAGTYIKEFV HGDFGRTKPN IGSLMNVTAD ILELDVESVD VDWPPALDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-84, MASS SPECTROMETRY. 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]	"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).
[9]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-484.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00065521.

RefSeq

NP_653310.2. NM_144709.2.

UniGene

Hs.368348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V9K	X-ray	2.00	A	1-529	[»]

ProteinModelPortal

Q3MIT2.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000326003.

PTM databases

PhosphoSite

Q3MIT2.

Polymorphism databases

DMDM

121942830.

Proteomic databases

PaxDb

Q3MIT2.

PRIDE

Q3MIT2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316752; ENSP00000326003; ENSG00000162927.
ENST00000407787; ENSP00000386074; ENSG00000162927.

GeneID

150962.

KEGG

hsa:150962.

UCSC

uc002sao.3. human.

Organism-specific databases

CTD

150962.

GeneCards

GC02M061167.

HGNC

HGNC:26505. PUS10.

HPA

HPA044736.
HPA049582.

MIM

612787. gene.

neXtProt

NX_Q3MIT2.

PharmGKB

PA162400393.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1258.

HOGENOM

HOG000030855.

HOVERGEN

HBG056180.

InParanoid

Q3MIT2.

KO

K07583.

OMA

VFTRMAV.

OrthoDB

EOG4CNQQR.

PhylomeDB

Q3MIT2.

Enzyme and pathway databases

BRENDA

5.4.99.12. 2681.

Gene expression databases

ArrayExpress

Q3MIT2.

Bgee

Q3MIT2.

CleanEx

HS_PUS10.

Genevestigator

Q3MIT2.

Family and domain databases

InterPro

IPR020103. PsdUridine_synth_cat_dom.
[Graphical view]

SUPFAM

SSF55120. PsdUridine_synth_cat_dom. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q3MIT2.

GenomeRNAi

150962.

NextBio

86567.

SOURCE

Search...

Entry information

Entry name

PUS10_HUMAN

Accession

Primary (citable) accession number: Q3MIT2
Secondary accession number(s): Q5JPJ5, Q96MI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.