Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Regulator of nonsense transcripts 1

Gene

UPF1

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

Functioni

RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD. Essential for embryonic viability.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei486ATP1
Binding sitei676ATP1
Binding sitei713ATP1
Binding sitei844ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 272UPF1-typeAdd BLAST152
Nucleotide bindingi506 – 510ATP5

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: UniProtKB
  • chromatin binding Source: HGNC
  • helicase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • telomeric DNA binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • 3'-UTR-mediated mRNA destabilization Source: UniProtKB
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to lipopolysaccharide Source: UniProtKB
  • DNA repair Source: HGNC
  • DNA replication Source: HGNC
  • dosage compensation by inactivation of X chromosome Source: Ensembl
  • histone mRNA catabolic process Source: UniProtKB
  • mRNA export from nucleus Source: HGNC
  • nuclear-transcribed mRNA catabolic process Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: UniProtKB
  • regulation of translational termination Source: UniProtKB
  • telomere maintenance Source: BHF-UCL
  • telomere maintenance via semi-conservative replication Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Nonsense-mediated mRNA decay

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000005007-MONOMER.
ReactomeiR-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiQ92900.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of nonsense transcripts 1 (EC:3.6.4.-)
Alternative name(s):
ATP-dependent helicase RENT1
Nonsense mRNA reducing factor 1
Short name:
NORF1
Up-frameshift suppressor 1 homolog
Short name:
hUpf1
Gene namesi
Name:UPF1
Synonyms:KIAA0221, RENT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9962. UPF1.

Subcellular locationi

  • Cytoplasm
  • CytoplasmP-body
  • Nucleus

  • Note: Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm.

GO - Cellular componenti

  • chromatin Source: HGNC
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • exon-exon junction complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • supraspliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi126C → S: Abolishes ability to interact with UPF2/RENT2 and copurifies with greater amounts of SMG1, SMG8 and SMG9. 2 Publications1
Mutagenesisi506 – 508GTG → RTE: Prevents dephosphorylation and targets the protein to the P-body. 1 Publication3
Mutagenesisi509K → A: Inhibits histone mRNA degradation, ATPase activity and ATP binding. 3 Publications1
Mutagenesisi610 – 611KR → AA: Impairs RNA binding. 2
Mutagenesisi615R → A: Impairs RNA binding. 1 Publication1
Mutagenesisi647 – 648DE → AA: Loss of ATPase activity and helicase activity. 2 Publications2
Mutagenesisi647 – 648DE → AA: Loss of ATPase activity and helicase activity. Inhibits ZC3H12A-mediated IL6 mRNA degradation. 3 Publications2
Mutagenesisi676Q → A: Impairs ATPase activity, no effect on ATP binding. 1 Publication1
Mutagenesisi714R → A: Impairs ATPase activity and ATP binding. 1 Publication1
Mutagenesisi843R → A: Inhibits histone mRNA degradation. 2 Publications1
Mutagenesisi843R → C: Abolishes NMD. 2 Publications1
Mutagenesisi876R → A: Impairs ATPase activity and ATP binding. 1 Publication1
Mutagenesisi1084S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1089, A-1107 and A-1127. 1 Publication1
Mutagenesisi1089S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1107 and A-1127. 2 Publications1
Mutagenesisi1089S → A: Still phosphorylated but with less efficiency. 2 Publications1
Mutagenesisi1107S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1089 and A-1127. 2 Publications1
Mutagenesisi1107S → A: Impairs phosphorylation. 2 Publications1
Mutagenesisi1108Q → N: Impairs phosphorylation. 1 Publication1
Mutagenesisi1127S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1089 and A-1107. 1 Publication1

Organism-specific databases

DisGeNETi5976.
OpenTargetsiENSG00000005007.
PharmGKBiPA34328.

Polymorphism and mutation databases

BioMutaiUPF1.
DMDMi17380291.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000807161 – 1129Regulator of nonsense transcripts 1Add BLAST1129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineCombined sources1
Modified residuei31PhosphoserineCombined sources1
Modified residuei565PhosphoserineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei1019Omega-N-methylarginineCombined sources1
Modified residuei1089Phosphoserine2 Publications1
Modified residuei1107PhosphoserineCombined sources2 Publications1
Modified residuei1110PhosphoserineCombined sources1
Modified residuei1127PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by SMG1; required for formation of mRNA surveillance complexes.5 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ92900.
MaxQBiQ92900.
PaxDbiQ92900.
PeptideAtlasiQ92900.
PRIDEiQ92900.

PTM databases

iPTMnetiQ92900.
PhosphoSitePlusiQ92900.
SwissPalmiQ92900.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000005007.
CleanExiHS_UPF1.
ExpressionAtlasiQ92900. baseline and differential.
GenevisibleiQ92900. HS.

Organism-specific databases

HPAiHPA019587.
HPA020857.

Interactioni

Subunit structurei

Found in a post-splicing messenger ribonucleoprotein (mRNP) complex (PubMed:21419344). Associates with the exon junction complex (EJC) (PubMed:11546874, PubMed:16452507). Associates with the SGM1C complex; is phosphorylated by the complex kinase component SGM1 (PubMed:19417104). Interacts with UPF2 (PubMed:11163187, PubMed:11073994, PubMed:11113196, PubMed:19556969). Interacts with UPF3A and UPF3B (PubMed:11163187). Interacts with EST1A (PubMed:12554878). Interacts with SLBP (PubMed:16086026). Interacts (when hyperphosphorylated) with PNRC2 (PubMed:19150429). Interacts with AGO1 and AGO2 (PubMed:17932509). Interacts with GSPT2 (PubMed:18447585). Interacts with isoform 1 and isoform 5 of ADAR/ADAR1 (PubMed:18362360). Interacts with SMG7 (PubMed:15721257). Interacts with ZC3H12A; this interaction occurs in a mRNA translationally active- and termination-dependent manner and is essential for ZC3H12A-mediated degradation of target mRNAs (PubMed:26000482).16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACDQ96AP03EBI-373471,EBI-717666
DCP1AQ9NPI613EBI-373471,EBI-374238
DCP2Q8IU603EBI-373471,EBI-521577
EIF3AQ141525EBI-373492,EBI-366617
GSPT1P151702EBI-373471,EBI-948993
GSPT2Q8IYD13EBI-373471,EBI-3869637
L1RE1Q9UN816EBI-373471,EBI-722458
PNRC2Q9NPJ49EBI-373471,EBI-726549
SKI7Q084912EBI-373471,EBI-1389From a different organism.
SMG5Q9UPR32EBI-373492,EBI-3400861
SMG6Q86US82EBI-373492,EBI-3232100
SMG7Q925403EBI-373471,EBI-719830
STAU1O957935EBI-373471,EBI-358174
TERTO147463EBI-373471,EBI-1772203
UPF2Q9HAU525EBI-373471,EBI-372073
UPF3AQ9H1J14EBI-373471,EBI-521530
UPF3BQ9BZI78EBI-373471,EBI-372780

Protein-protein interaction databases

BioGridi111908. 158 interactors.
DIPiDIP-29875N.
IntActiQ92900. 107 interactors.
MINTiMINT-5005507.
STRINGi9606.ENSP00000262803.

Structurei

Secondary structure

11129
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni124 – 126Combined sources3
Helixi131 – 133Combined sources3
Beta strandi134 – 137Combined sources4
Turni138 – 141Combined sources4
Beta strandi142 – 146Combined sources5
Beta strandi151 – 153Combined sources3
Helixi155 – 163Combined sources9
Beta strandi168 – 170Combined sources3
Beta strandi174 – 176Combined sources3
Turni184 – 186Combined sources3
Turni191 – 193Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi200 – 202Combined sources3
Beta strandi204 – 209Combined sources6
Turni210 – 213Combined sources4
Turni216 – 218Combined sources3
Turni220 – 222Combined sources3
Helixi226 – 228Combined sources3
Beta strandi230 – 233Combined sources4
Beta strandi235 – 238Combined sources4
Turni240 – 242Combined sources3
Helixi248 – 253Combined sources6
Helixi259 – 269Combined sources11
Helixi299 – 321Combined sources23
Beta strandi326 – 329Combined sources4
Beta strandi332 – 335Combined sources4
Turni337 – 339Combined sources3
Beta strandi341 – 345Combined sources5
Helixi364 – 366Combined sources3
Beta strandi372 – 377Combined sources6
Beta strandi379 – 382Combined sources4
Beta strandi385 – 393Combined sources9
Beta strandi396 – 398Combined sources3
Beta strandi402 – 407Combined sources6
Beta strandi410 – 412Combined sources3
Beta strandi418 – 425Combined sources8
Helixi429 – 443Combined sources15
Helixi450 – 456Combined sources7
Helixi484 – 493Combined sources10
Beta strandi497 – 502Combined sources6
Helixi509 – 522Combined sources14
Beta strandi523 – 525Combined sources3
Beta strandi528 – 534Combined sources7
Helixi535 – 547Combined sources13
Beta strandi552 – 554Combined sources3
Helixi558 – 560Combined sources3
Helixi568 – 570Combined sources3
Helixi572 – 577Combined sources6
Helixi582 – 591Combined sources10
Turni593 – 595Combined sources3
Helixi600 – 620Combined sources21
Beta strandi622 – 627Combined sources6
Helixi630 – 632Combined sources3
Helixi634 – 636Combined sources3
Beta strandi642 – 646Combined sources5
Helixi649 – 651Combined sources3
Helixi654 – 661Combined sources8
Turni662 – 664Combined sources3
Beta strandi665 – 672Combined sources8
Helixi684 – 688Combined sources5
Turni689 – 692Combined sources4
Helixi695 – 702Combined sources8
Helixi717 – 727Combined sources11
Beta strandi733 – 736Combined sources4
Helixi739 – 741Combined sources3
Beta strandi751 – 754Combined sources4
Beta strandi757 – 761Combined sources5
Beta strandi766 – 768Combined sources3
Beta strandi770 – 773Combined sources4
Beta strandi775 – 777Combined sources3
Helixi778 – 794Combined sources17
Helixi798 – 800Combined sources3
Beta strandi801 – 806Combined sources6
Helixi808 – 819Combined sources12
Helixi826 – 830Combined sources5
Beta strandi832 – 836Combined sources5
Turni837 – 842Combined sources6
Beta strandi845 – 851Combined sources7
Beta strandi857 – 859Combined sources3
Helixi862 – 865Combined sources4
Helixi867 – 874Combined sources8
Beta strandi875 – 885Combined sources11
Helixi887 – 890Combined sources4
Helixi894 – 905Combined sources12
Beta strandi909 – 912Combined sources4
Helixi914 – 916Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GJKX-ray2.60A295-925[»]
2GK6X-ray2.40A/B295-925[»]
2GK7X-ray2.80A295-925[»]
2IYKX-ray2.95A/B115-272[»]
2WJVX-ray2.85A/B115-925[»]
2WJYX-ray2.50A115-925[»]
2XZOX-ray2.40A295-925[»]
2XZPX-ray2.72A295-925[»]
ProteinModelPortaliQ92900.
SMRiQ92900.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92900.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 415Sufficient for interaction with RENT2Add BLAST415

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1089 – 1090[ST]-Q motif 12
Motifi1107 – 1108[ST]-Q motif 22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi47 – 80Ala/Gly/Pro-richAdd BLAST34
Compositional biasi1042 – 1129Gln/Ser-richAdd BLAST88

Domaini

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated
Contains 1 UPF1-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 272UPF1-typeAdd BLAST152

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1802. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00800000124068.
HOGENOMiHOG000205990.
HOVERGENiHBG061556.
InParanoidiQ92900.
KOiK14326.
OMAiHDSIGYI.
OrthoDBiEOG091G01B6.
PhylomeDBiQ92900.
TreeFamiTF300554.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR006935. Helicase/UvrB_N.
IPR027417. P-loop_NTPase.
IPR018999. RNA-helicase_UPF1_UPF2-interct.
[Graphical view]
PfamiPF04851. ResIII. 1 hit.
PF09416. UPF1_Zn_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92900-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSVEAYGPSS QTLTFLDTEE AELLGADTQG SEFEFTDFTL PSQTQTPPGG
60 70 80 90 100
PGGPGGGGAG GPGGAGAGAA AGQLDAQVGP EGILQNGAVD DSVAKTSQLL
110 120 130 140 150
AELNFEEDEE DTYYTKDLPI HACSYCGIHD PACVVYCNTS KKWFCNGRGN
160 170 180 190 200
TSGSHIVNHL VRAKCKEVTL HKDGPLGETV LECYNCGCRN VFLLGFIPAK
210 220 230 240 250
ADSVVVLLCR QPCASQSSLK DINWDSSQWQ PLIQDRCFLS WLVKIPSEQE
260 270 280 290 300
QLRARQITAQ QINKLEELWK ENPSATLEDL EKPGVDEEPQ HVLLRYEDAY
310 320 330 340 350
QYQNIFGPLV KLEADYDKKL KESQTQDNIT VRWDLGLNKK RIAYFTLPKT
360 370 380 390 400
DSGNEDLVII WLRDMRLMQG DEICLRYKGD LAPLWKGIGH VIKVPDNYGD
410 420 430 440 450
EIAIELRSSV GAPVEVTHNF QVDFVWKSTS FDRMQSALKT FAVDETSVSG
460 470 480 490 500
YIYHKLLGHE VEDVIIKCQL PKRFTAQGLP DLNHSQVYAV KTVLQRPLSL
510 520 530 540 550
IQGPPGTGKT VTSATIVYHL ARQGNGPVLV CAPSNIAVDQ LTEKIHQTGL
560 570 580 590 600
KVVRLCAKSR EAIDSPVSFL ALHNQIRNMD SMPELQKLQQ LKDETGELSS
610 620 630 640 650
ADEKRYRALK RTAERELLMN ADVICCTCVG AGDPRLAKMQ FRSILIDEST
660 670 680 690 700
QATEPECMVP VVLGAKQLIL VGDHCQLGPV VMCKKAAKAG LSQSLFERLV
710 720 730 740 750
VLGIRPIRLQ VQYRMHPALS AFPSNIFYEG SLQNGVTAAD RVKKGFDFQW
760 770 780 790 800
PQPDKPMFFY VTQGQEEIAS SGTSYLNRTE AANVEKITTK LLKAGAKPDQ
810 820 830 840 850
IGIITPYEGQ RSYLVQYMQF SGSLHTKLYQ EVEIASVDAF QGREKDFIIL
860 870 880 890 900
SCVRANEHQG IGFLNDPRRL NVALTRARYG VIIVGNPKAL SKQPLWNHLL
910 920 930 940 950
NYYKEQKVLV EGPLNNLRES LMQFSKPRKL VNTINPGARF MTTAMYDARE
960 970 980 990 1000
AIIPGSVYDR SSQGRPSSMY FQTHDQIGMI SAGPSHVAAM NIPIPFNLVM
1010 1020 1030 1040 1050
PPMPPPGYFG QANGPAAGRG TPKGKTGRGG RQKNRFGLPG PSQTNLPNSQ
1060 1070 1080 1090 1100
ASQDVASQPF SQGALTQGYI SMSQPSQMSQ PGLSQPELSQ DSYLGDEFKS
1110 1120
QIDVALSQDS TYQGERAYQH GGVTGLSQY
Length:1,129
Mass (Da):124,345
Last modified:October 18, 2001 - v2
Checksum:i6CCA6FE42B15BA28
GO
Isoform 2 (identifier: Q92900-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     353-363: Missing.

Show »
Length:1,118
Mass (Da):123,036
Checksum:iA485D3ED52C39D06
GO

Sequence cautioni

The sequence BAA19664 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61G → S in AAC51140 (PubMed:9064659).Curated1
Sequence conflicti466I → T in AAC51140 (PubMed:9064659).Curated1
Sequence conflicti478G → A in AAC50771 (PubMed:8855285).Curated1
Sequence conflicti524G → D in AAC50771 (PubMed:8855285).Curated1
Sequence conflicti557A → P in AAC50771 (PubMed:8855285).Curated1
Sequence conflicti901 – 902NY → IF in AAC50771 (PubMed:8855285).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05620769A → S.1 PublicationCorresponds to variant rs17339451dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003393353 – 363Missing in isoform 2. 4 PublicationsAdd BLAST11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65533 mRNA. Translation: AAC50771.1.
U59323 mRNA. Translation: AAC51140.1.
D86988 mRNA. Translation: BAA19664.2. Different initiation.
AF074016 mRNA. Translation: AAC26788.1.
AC003972 Genomic DNA. Translation: AAB94785.1.
BC039817 mRNA. Translation: AAH39817.1.
CCDSiCCDS12386.1. [Q92900-2]
CCDS74315.1. [Q92900-1]
RefSeqiNP_001284478.1. NM_001297549.1. [Q92900-1]
NP_002902.2. NM_002911.3. [Q92900-2]
UniGeneiHs.515266.

Genome annotation databases

EnsembliENST00000262803; ENSP00000262803; ENSG00000005007. [Q92900-2]
ENST00000599848; ENSP00000470142; ENSG00000005007. [Q92900-1]
GeneIDi5976.
KEGGihsa:5976.
UCSCiuc002nkf.4. human. [Q92900-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65533 mRNA. Translation: AAC50771.1.
U59323 mRNA. Translation: AAC51140.1.
D86988 mRNA. Translation: BAA19664.2. Different initiation.
AF074016 mRNA. Translation: AAC26788.1.
AC003972 Genomic DNA. Translation: AAB94785.1.
BC039817 mRNA. Translation: AAH39817.1.
CCDSiCCDS12386.1. [Q92900-2]
CCDS74315.1. [Q92900-1]
RefSeqiNP_001284478.1. NM_001297549.1. [Q92900-1]
NP_002902.2. NM_002911.3. [Q92900-2]
UniGeneiHs.515266.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GJKX-ray2.60A295-925[»]
2GK6X-ray2.40A/B295-925[»]
2GK7X-ray2.80A295-925[»]
2IYKX-ray2.95A/B115-272[»]
2WJVX-ray2.85A/B115-925[»]
2WJYX-ray2.50A115-925[»]
2XZOX-ray2.40A295-925[»]
2XZPX-ray2.72A295-925[»]
ProteinModelPortaliQ92900.
SMRiQ92900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111908. 158 interactors.
DIPiDIP-29875N.
IntActiQ92900. 107 interactors.
MINTiMINT-5005507.
STRINGi9606.ENSP00000262803.

PTM databases

iPTMnetiQ92900.
PhosphoSitePlusiQ92900.
SwissPalmiQ92900.

Polymorphism and mutation databases

BioMutaiUPF1.
DMDMi17380291.

Proteomic databases

EPDiQ92900.
MaxQBiQ92900.
PaxDbiQ92900.
PeptideAtlasiQ92900.
PRIDEiQ92900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262803; ENSP00000262803; ENSG00000005007. [Q92900-2]
ENST00000599848; ENSP00000470142; ENSG00000005007. [Q92900-1]
GeneIDi5976.
KEGGihsa:5976.
UCSCiuc002nkf.4. human. [Q92900-1]

Organism-specific databases

CTDi5976.
DisGeNETi5976.
GeneCardsiUPF1.
HGNCiHGNC:9962. UPF1.
HPAiHPA019587.
HPA020857.
MIMi601430. gene.
neXtProtiNX_Q92900.
OpenTargetsiENSG00000005007.
PharmGKBiPA34328.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1802. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00800000124068.
HOGENOMiHOG000205990.
HOVERGENiHBG061556.
InParanoidiQ92900.
KOiK14326.
OMAiHDSIGYI.
OrthoDBiEOG091G01B6.
PhylomeDBiQ92900.
TreeFamiTF300554.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000005007-MONOMER.
ReactomeiR-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiQ92900.

Miscellaneous databases

ChiTaRSiUPF1. human.
EvolutionaryTraceiQ92900.
GeneWikiiUPF1.
GenomeRNAii5976.
PROiQ92900.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000005007.
CleanExiHS_UPF1.
ExpressionAtlasiQ92900. baseline and differential.
GenevisibleiQ92900. HS.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR006935. Helicase/UvrB_N.
IPR027417. P-loop_NTPase.
IPR018999. RNA-helicase_UPF1_UPF2-interct.
[Graphical view]
PfamiPF04851. ResIII. 1 hit.
PF09416. UPF1_Zn_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRENT1_HUMAN
AccessioniPrimary (citable) accession number: Q92900
Secondary accession number(s): O00239
, O43343, Q86Z25, Q92842
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: November 30, 2016
This is version 173 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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.