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Protein

Pseudouridylate synthase 7 homolog

Gene

PUS7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

tRNA uridine = tRNA pseudouridine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei294 – 2941NucleophileBy similarity

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • pseudouridine synthase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

tRNA processing

Enzyme and pathway databases

ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Pseudouridylate synthase 7 homolog (EC:5.4.99.-)
Gene namesi
Name:PUS7
Synonyms:KIAA1897
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:26033. PUS7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485587.

Polymorphism and mutation databases

BioMutaiPUS7.
DMDMi37090412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Pseudouridylate synthase 7 homologPRO_0000152558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei610 – 6101PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96PZ0.
MaxQBiQ96PZ0.
PaxDbiQ96PZ0.
PeptideAtlasiQ96PZ0.
PRIDEiQ96PZ0.

PTM databases

iPTMnetiQ96PZ0.
PhosphoSiteiQ96PZ0.

Expressioni

Gene expression databases

BgeeiQ96PZ0.
CleanExiHS_PUS7.
ExpressionAtlasiQ96PZ0. baseline and differential.
GenevisibleiQ96PZ0. HS.

Organism-specific databases

HPAiHPA024116.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120011. 42 interactions.
IntActiQ96PZ0. 1 interaction.
STRINGi9606.ENSP00000348722.

Structurei

3D structure databases

ProteinModelPortaliQ96PZ0.
SMRiQ96PZ0. Positions 251-646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini370 – 580211TRUDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the pseudouridine synthase TruD family.Curated
Contains 1 TRUD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2339. Eukaryota.
COG0585. LUCA.
GeneTreeiENSGT00530000063554.
HOGENOMiHOG000203484.
HOVERGENiHBG056990.
InParanoidiQ96PZ0.
KOiK06176.
OMAiNFSYKNH.
OrthoDBiEOG7D2FD1.
PhylomeDBiQ96PZ0.
TreeFamiTF314278.

Family and domain databases

InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR001656. PsdUridine_synth_TruD.
IPR020119. PsdUridine_synth_TruD_CS.
IPR011760. PsdUridine_synth_TruD_insert.
[Graphical view]
PANTHERiPTHR13326. PTHR13326. 2 hits.
PfamiPF01142. TruD. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 4 hits.
TIGRFAMsiTIGR00094. tRNA_TruD_broad. 1 hit.
PROSITEiPS50984. TRUD. 1 hit.
PS01268. UPF0024. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96PZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMTEMTGVS LKRGALVVED NDSGVPVEET KKQKLSECSL TKGQDGLQND
60 70 80 90 100
FLSISEDVPR PPDTVSTGKG GKNSEAQLED EEEEEEDGLS EECEEEESES
110 120 130 140 150
FADMMKHGLT EADVGITKFV SSHQGFSGIL KERYSDFVVH EIGKDGRISH
160 170 180 190 200
LNDLSIPVDE EDPSEDIFTV LTAEEKQRLE ELQLFKNKET SVAIEVIEDT
210 220 230 240 250
KEKRTIIHQA IKSLFPGLET KTEDREGKKY IVAYHAAGKK ALANPRKHSW
260 270 280 290 300
PKSRGSYCHF VLYKENKDTM DAINVLSKYL RVKPNIFSYM GTKDKRAITV
310 320 330 340 350
QEIAVLKITA QRLAHLNKCL MNFKLGNFSY QKNPLKLGEL QGNHFTVVLR
360 370 380 390 400
NITGTDDQVQ QAMNSLKEIG FINYYGMQRF GTTAVPTYQV GRAILQNSWT
410 420 430 440 450
EVMDLILKPR SGAEKGYLVK CREEWAKTKD PTAALRKLPV KRCVEGQLLR
460 470 480 490 500
GLSKYGMKNI VSAFGIIPRN NRLMYIHSYQ SYVWNNMVSK RIEDYGLKPV
510 520 530 540 550
PGDLVLKGAT ATYIEEDDVN NYSIHDVVMP LPGFDVIYPK HKIQEAYREM
560 570 580 590 600
LTADNLDIDN MRHKIRDYSL SGAYRKIIIR PQNVSWEVVA YDDPKIPLFN
610 620 630 640 650
TDVDNLEGKT PPVFASEGKY RALKMDFSLP PSTYATMAIR EVLKMDTSIK
660
NQTQLNTTWL R
Length:661
Mass (Da):75,035
Last modified:September 26, 2003 - v2
Checksum:i6F6A05A9B57B1560
GO

Sequence cautioni

The sequence BAA91203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441N → KVRTAAD (PubMed:11572484).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC073138 Genomic DNA. Translation: AAS07447.1.
AC074013 Genomic DNA. No translation available.
BC005209 mRNA. Translation: AAH05209.3.
BC011396 mRNA. Translation: AAH11396.2.
AB067484 mRNA. Translation: BAB67790.1.
AK000492 mRNA. Translation: BAA91203.1. Different initiation.
CCDSiCCDS34725.1.
RefSeqiNP_001305092.1. NM_001318163.1.
NP_001305093.1. NM_001318164.1.
NP_061915.2. NM_019042.4.
UniGeneiHs.520619.

Genome annotation databases

EnsembliENST00000356362; ENSP00000348722; ENSG00000091127.
ENST00000469408; ENSP00000417402; ENSG00000091127.
GeneIDi54517.
KEGGihsa:54517.
UCSCiuc003vcx.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC073138 Genomic DNA. Translation: AAS07447.1.
AC074013 Genomic DNA. No translation available.
BC005209 mRNA. Translation: AAH05209.3.
BC011396 mRNA. Translation: AAH11396.2.
AB067484 mRNA. Translation: BAB67790.1.
AK000492 mRNA. Translation: BAA91203.1. Different initiation.
CCDSiCCDS34725.1.
RefSeqiNP_001305092.1. NM_001318163.1.
NP_001305093.1. NM_001318164.1.
NP_061915.2. NM_019042.4.
UniGeneiHs.520619.

3D structure databases

ProteinModelPortaliQ96PZ0.
SMRiQ96PZ0. Positions 251-646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120011. 42 interactions.
IntActiQ96PZ0. 1 interaction.
STRINGi9606.ENSP00000348722.

PTM databases

iPTMnetiQ96PZ0.
PhosphoSiteiQ96PZ0.

Polymorphism and mutation databases

BioMutaiPUS7.
DMDMi37090412.

Proteomic databases

EPDiQ96PZ0.
MaxQBiQ96PZ0.
PaxDbiQ96PZ0.
PeptideAtlasiQ96PZ0.
PRIDEiQ96PZ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356362; ENSP00000348722; ENSG00000091127.
ENST00000469408; ENSP00000417402; ENSG00000091127.
GeneIDi54517.
KEGGihsa:54517.
UCSCiuc003vcx.5. human.

Organism-specific databases

CTDi54517.
GeneCardsiPUS7.
HGNCiHGNC:26033. PUS7.
HPAiHPA024116.
MIMi616261. gene.
neXtProtiNX_Q96PZ0.
PharmGKBiPA143485587.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2339. Eukaryota.
COG0585. LUCA.
GeneTreeiENSGT00530000063554.
HOGENOMiHOG000203484.
HOVERGENiHBG056990.
InParanoidiQ96PZ0.
KOiK06176.
OMAiNFSYKNH.
OrthoDBiEOG7D2FD1.
PhylomeDBiQ96PZ0.
TreeFamiTF314278.

Enzyme and pathway databases

ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

GenomeRNAii54517.
PROiQ96PZ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ96PZ0.
CleanExiHS_PUS7.
ExpressionAtlasiQ96PZ0. baseline and differential.
GenevisibleiQ96PZ0. HS.

Family and domain databases

InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR001656. PsdUridine_synth_TruD.
IPR020119. PsdUridine_synth_TruD_CS.
IPR011760. PsdUridine_synth_TruD_insert.
[Graphical view]
PANTHERiPTHR13326. PTHR13326. 2 hits.
PfamiPF01142. TruD. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 4 hits.
TIGRFAMsiTIGR00094. tRNA_TruD_broad. 1 hit.
PROSITEiPS50984. TRUD. 1 hit.
PS01268. UPF0024. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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: Eye and Urinary bladder.
  3. "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
    Nagase T., Kikuno R., Ohara O.
    DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-661.
    Tissue: Brain.
  4. "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] OF 420-661.
  5. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-10; SER-127 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.

Entry informationi

Entry nameiPUS7_HUMAN
AccessioniPrimary (citable) accession number: Q96PZ0
Secondary accession number(s): Q75MG4, Q9NX19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: July 6, 2016
This is version 122 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. 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.