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Q9UHX1

- PUF60_HUMAN

UniProt

Q9UHX1 - PUF60_HUMAN

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Protein

Poly(U)-binding-splicing factor PUF60

Gene

PUF60

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

Functioni

DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA.6 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. mRNA processing Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. RNA splicing Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(U)-binding-splicing factor PUF60
Alternative name(s):
60 kDa poly(U)-binding-splicing factor
FUSE-binding protein-interacting repressor
Short name:
FBP-interacting repressor
Ro-binding protein 1
Short name:
RoBP1
Siah-binding protein 1
Short name:
Siah-BP1
Gene namesi
Name:PUF60
Synonyms:FIR, ROBPI, SIAHBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:17042. PUF60.

Subcellular locationi

Nucleus 2 Publications
Note: Colocalizes partially with TROVE2.

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
  2. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Verheij syndrome (VRJS) [MIM:615583]: A syndrome characterized by growth retardation, delayed psychomotor development, dysmorphic facial features, and skeletal, mainly vertebral, abnormalities. Additional variable features may include coloboma, renal defects, and cardiac defects.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti169 – 1691H → Y in VRJS; loss of function mutation; results in altered dosage of dfferent PUF60 protein forms and abnormal splicing profile of several target genes. 1 Publication
VAR_070939

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615583. phenotype.
PharmGKBiPA162400364.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Poly(U)-binding-splicing factor PUF60PRO_0000299519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphothreonine2 Publications
Modified residuei112 – 1121Phosphoserine1 Publication
Modified residuei251 – 2511N6-acetyllysine1 Publication
Modified residuei314 – 3141Phosphothreonine1 Publication
Modified residuei454 – 4541N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UHX1.
PaxDbiQ9UHX1.
PRIDEiQ9UHX1.

PTM databases

PhosphoSiteiQ9UHX1.

Expressioni

Tissue specificityi

Isoform 2 is expressed in colonic epithelium and colorectal epithelium cancer (at protein level). Isoform 6 is expressed in colorectal epithelial cancer but below detection level in colonic epithelium. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiQ9UHX1.
CleanExiHS_PUF60.
ExpressionAtlasiQ9UHX1. baseline and differential.
GenevestigatoriQ9UHX1.

Organism-specific databases

HPAiHPA045733.

Interactioni

Subunit structurei

Homodimer. Associates with the spliceosome. Found in a complex with TROVE2 and Y5 RNA. Found in a complex with FUBP1 and far upstream element (FUSE) DNA segment. Interacts directly with ERCC3. Interacts with CDK7, GTF2H1 and SFRS11. Does not interact with ERCC3 in xeroderma pigmentosum complementation group B (XPB) cells.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1053259,EBI-1053259
CACNA1AO005552EBI-1053259,EBI-766279
PCBP1Q153652EBI-1053259,EBI-946095
PPP1R16AQ96I342EBI-1053259,EBI-710402
SAP30BPQ9UHR56EBI-1053259,EBI-751683

Protein-protein interaction databases

BioGridi116502. 90 interactions.
DIPiDIP-34636N.
IntActiQ9UHX1. 30 interactions.
MINTiMINT-1374433.
STRINGi9606.ENSP00000322016.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi118 – 12811Combined sources
Beta strandi130 – 1345Combined sources
Helixi142 – 1498Combined sources
Helixi150 – 1523Combined sources
Beta strandi155 – 1606Combined sources
Turni164 – 1663Combined sources
Beta strandi171 – 1799Combined sources
Helixi180 – 19011Combined sources
Beta strandi194 – 1996Combined sources
Beta strandi201 – 2033Combined sources
Helixi206 – 2083Combined sources
Helixi209 – 2113Combined sources
Helixi212 – 22211Combined sources
Helixi223 – 2253Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi235 – 2373Combined sources
Helixi239 – 2468Combined sources
Beta strandi252 – 2598Combined sources
Turni261 – 2633Combined sources
Beta strandi266 – 27611Combined sources
Helixi277 – 28711Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi306 – 3094Combined sources
Helixi445 – 4484Combined sources
Turni449 – 4524Combined sources
Helixi453 – 4597Combined sources
Beta strandi463 – 4686Combined sources
Helixi472 – 4743Combined sources
Helixi479 – 4879Combined sources
Turni488 – 4903Combined sources
Beta strandi493 – 50614Combined sources
Beta strandi510 – 52112Combined sources
Helixi522 – 53211Combined sources
Beta strandi543 – 5475Combined sources
Helixi549 – 5535Combined sources
Beta strandi557 – 5593Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNYNMR-A454-559[»]
2KXFNMR-A119-314[»]
2KXHNMR-A119-314[»]
2QFJX-ray2.10A/B118-316[»]
3DXBX-ray2.20A/B/C/D/E/F/G/H460-499[»]
3UE2X-ray1.23A443-559[»]
3US5X-ray1.38A443-559[»]
3UWTX-ray2.50A118-316[»]
ProteinModelPortaliQ9UHX1.
SMRiQ9UHX1. Positions 118-313, 443-559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHX1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 20779RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini226 – 30479RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini462 – 54988RRM 3; atypicalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 516516Inhibits homodimerizationAdd
BLAST
Regioni77 – 559483Inhibits transcriptional repression, interaction with ERCC3 and apoptosis inductionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi321 – 34323Ala-richAdd
BLAST

Domaini

The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.

Sequence similaritiesi

Belongs to the RRM half pint family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000119252.
HOVERGENiHBG055622.
InParanoidiQ9UHX1.
KOiK12838.
OMAiAFVEYDV.
PhylomeDBiQ9UHX1.
TreeFamiTF313987.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006532. PolyU-bd.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
SM00361. RRM_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01645. half-pint. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UHX1) [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
MATATIALQV NGQQGGGSEP AAAAAVVAAG DKWKPPQGTD SIKMENGQST
60 70 80 90 100
AAKLGLPPLT PEQQEALQKA KKYAMEQSIK SVLVKQTIAH QQQQLTNLQM
110 120 130 140 150
AAVTMGFGDP LSPLQSMAAQ RQRALAIMCR VYVGSIYYEL GEDTIRQAFA
160 170 180 190 200
PFGPIKSIDM SWDSVTMKHK GFAFVEYEVP EAAQLALEQM NSVMLGGRNI
210 220 230 240 250
KVGRPSNIGQ AQPIIDQLAE EARAFNRIYV ASVHQDLSDD DIKSVFEAFG
260 270 280 290 300
KIKSCTLARD PTTGKHKGYG FIEYEKAQSS QDAVSSMNLF DLGGQYLRVG
310 320 330 340 350
KAVTPPMPLL TPATPGGLPP AAAVAAAAAT AKITAQEAVA GAAVLGTLGT
360 370 380 390 400
PGLVSPALTL AQPLGTLPQA VMAAQAPGVI TGVTPARPPI PVTIPSVGVV
410 420 430 440 450
NPILASPPTL GLLEPKKEKE EEELFPESER PEMLSEQEHM SISGSSARHM
460 470 480 490 500
VMQKLLRKQE STVMVLRNMV DPKDIDDDLE GEVTEECGKF GAVNRVIIYQ
510 520 530 540 550
EKQGEEEDAE IIVKIFVEFS IASETHKAIQ ALNGRWFAGR KVVAEVYDQE

RFDNSDLSA
Length:559
Mass (Da):59,875
Last modified:May 1, 2000 - v1
Checksum:i619F3C30D1C5951C
GO
Isoform 2 (identifier: Q9UHX1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-117: Missing.

Show »
Length:542
Mass (Da):58,171
Checksum:i2C67EBE529A0922E
GO
Isoform 3 (identifier: Q9UHX1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.

Show »
Length:516
Mass (Da):55,729
Checksum:iF52D8C619E874B55
GO
Isoform 4 (identifier: Q9UHX1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
     101-117: Missing.

Show »
Length:499
Mass (Da):54,025
Checksum:i77881512A09C3EFD
GO
Isoform 5 (identifier: Q9UHX1-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-37: Missing.

Show »
Length:530
Mass (Da):57,103
Checksum:i850251A390ECD30C
GO
Isoform 6 (identifier: Q9UHX1-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-37: Missing.
     101-117: Missing.

Show »
Length:513
Mass (Da):55,399
Checksum:i2A5BA6848E391E3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31T → R in AAB41656. 1 PublicationCurated
Sequence conflicti123 – 1231R → G in AAB41656. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti169 – 1691H → Y in VRJS; loss of function mutation; results in altered dosage of dfferent PUF60 protein forms and abnormal splicing profile of several target genes. 1 Publication
VAR_070939

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343Missing in isoform 3 and isoform 4. 1 PublicationVSP_027717Add
BLAST
Alternative sequencei9 – 3729Missing in isoform 5 and isoform 6. CuratedVSP_027718Add
BLAST
Alternative sequencei101 – 11717Missing in isoform 2, isoform 4 and isoform 6. 3 PublicationsVSP_027719Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF217197 mRNA. Translation: AAF27522.2.
AF114818 mRNA. Translation: AAF23589.1.
AK292373 mRNA. Translation: BAF85062.1.
CR457143 mRNA. Translation: CAG33424.1.
CH471162 Genomic DNA. Translation: EAW82187.1.
CH471162 Genomic DNA. Translation: EAW82189.1.
BC008875 mRNA. Translation: AAH08875.1.
BC009734 mRNA. Translation: AAH09734.1.
BC011265 mRNA. Translation: AAH11265.1.
BC011979 mRNA. Translation: AAH11979.1.
U51586 mRNA. Translation: AAB41656.1.
AF190744 mRNA. Translation: AAF05605.1.
CCDSiCCDS47933.1. [Q9UHX1-2]
CCDS47934.1. [Q9UHX1-1]
CCDS47935.1. [Q9UHX1-3]
CCDS59514.1. [Q9UHX1-4]
CCDS59515.1. [Q9UHX1-6]
CCDS59516.1. [Q9UHX1-5]
RefSeqiNP_001129505.1. NM_001136033.2. [Q9UHX1-3]
NP_001258025.1. NM_001271096.1.
NP_001258026.1. NM_001271097.1. [Q9UHX1-6]
NP_001258027.1. NM_001271098.1.
NP_001258028.1. NM_001271099.1. [Q9UHX1-5]
NP_001258029.1. NM_001271100.1. [Q9UHX1-4]
NP_055096.2. NM_014281.4. [Q9UHX1-2]
NP_510965.1. NM_078480.2. [Q9UHX1-1]
UniGeneiHs.521924.

Genome annotation databases

EnsembliENST00000313352; ENSP00000322016; ENSG00000179950. [Q9UHX1-4]
ENST00000349157; ENSP00000322036; ENSG00000179950. [Q9UHX1-2]
ENST00000453551; ENSP00000402953; ENSG00000179950. [Q9UHX1-3]
ENST00000456095; ENSP00000395417; ENSG00000179950. [Q9UHX1-5]
ENST00000526683; ENSP00000434359; ENSG00000179950. [Q9UHX1-1]
ENST00000527197; ENSP00000431960; ENSG00000179950. [Q9UHX1-6]
GeneIDi22827.
KEGGihsa:22827.
UCSCiuc003yzq.4. human. [Q9UHX1-1]
uc003yzr.4. human. [Q9UHX1-4]
uc003yzt.4. human. [Q9UHX1-2]
uc031tcp.1. human. [Q9UHX1-5]
uc031tcq.1. human. [Q9UHX1-6]

Polymorphism databases

DMDMi74761960.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF217197 mRNA. Translation: AAF27522.2 .
AF114818 mRNA. Translation: AAF23589.1 .
AK292373 mRNA. Translation: BAF85062.1 .
CR457143 mRNA. Translation: CAG33424.1 .
CH471162 Genomic DNA. Translation: EAW82187.1 .
CH471162 Genomic DNA. Translation: EAW82189.1 .
BC008875 mRNA. Translation: AAH08875.1 .
BC009734 mRNA. Translation: AAH09734.1 .
BC011265 mRNA. Translation: AAH11265.1 .
BC011979 mRNA. Translation: AAH11979.1 .
U51586 mRNA. Translation: AAB41656.1 .
AF190744 mRNA. Translation: AAF05605.1 .
CCDSi CCDS47933.1. [Q9UHX1-2 ]
CCDS47934.1. [Q9UHX1-1 ]
CCDS47935.1. [Q9UHX1-3 ]
CCDS59514.1. [Q9UHX1-4 ]
CCDS59515.1. [Q9UHX1-6 ]
CCDS59516.1. [Q9UHX1-5 ]
RefSeqi NP_001129505.1. NM_001136033.2. [Q9UHX1-3 ]
NP_001258025.1. NM_001271096.1.
NP_001258026.1. NM_001271097.1. [Q9UHX1-6 ]
NP_001258027.1. NM_001271098.1.
NP_001258028.1. NM_001271099.1. [Q9UHX1-5 ]
NP_001258029.1. NM_001271100.1. [Q9UHX1-4 ]
NP_055096.2. NM_014281.4. [Q9UHX1-2 ]
NP_510965.1. NM_078480.2. [Q9UHX1-1 ]
UniGenei Hs.521924.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DNY NMR - A 454-559 [» ]
2KXF NMR - A 119-314 [» ]
2KXH NMR - A 119-314 [» ]
2QFJ X-ray 2.10 A/B 118-316 [» ]
3DXB X-ray 2.20 A/B/C/D/E/F/G/H 460-499 [» ]
3UE2 X-ray 1.23 A 443-559 [» ]
3US5 X-ray 1.38 A 443-559 [» ]
3UWT X-ray 2.50 A 118-316 [» ]
ProteinModelPortali Q9UHX1.
SMRi Q9UHX1. Positions 118-313, 443-559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116502. 90 interactions.
DIPi DIP-34636N.
IntActi Q9UHX1. 30 interactions.
MINTi MINT-1374433.
STRINGi 9606.ENSP00000322016.

PTM databases

PhosphoSitei Q9UHX1.

Polymorphism databases

DMDMi 74761960.

Proteomic databases

MaxQBi Q9UHX1.
PaxDbi Q9UHX1.
PRIDEi Q9UHX1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313352 ; ENSP00000322016 ; ENSG00000179950 . [Q9UHX1-4 ]
ENST00000349157 ; ENSP00000322036 ; ENSG00000179950 . [Q9UHX1-2 ]
ENST00000453551 ; ENSP00000402953 ; ENSG00000179950 . [Q9UHX1-3 ]
ENST00000456095 ; ENSP00000395417 ; ENSG00000179950 . [Q9UHX1-5 ]
ENST00000526683 ; ENSP00000434359 ; ENSG00000179950 . [Q9UHX1-1 ]
ENST00000527197 ; ENSP00000431960 ; ENSG00000179950 . [Q9UHX1-6 ]
GeneIDi 22827.
KEGGi hsa:22827.
UCSCi uc003yzq.4. human. [Q9UHX1-1 ]
uc003yzr.4. human. [Q9UHX1-4 ]
uc003yzt.4. human. [Q9UHX1-2 ]
uc031tcp.1. human. [Q9UHX1-5 ]
uc031tcq.1. human. [Q9UHX1-6 ]

Organism-specific databases

CTDi 22827.
GeneCardsi GC08M144898.
HGNCi HGNC:17042. PUF60.
HPAi HPA045733.
MIMi 604819. gene.
615583. phenotype.
neXtProti NX_Q9UHX1.
PharmGKBi PA162400364.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00760000119252.
HOVERGENi HBG055622.
InParanoidi Q9UHX1.
KOi K12838.
OMAi AFVEYDV.
PhylomeDBi Q9UHX1.
TreeFami TF313987.

Miscellaneous databases

EvolutionaryTracei Q9UHX1.
GeneWikii PUF60.
GenomeRNAii 22827.
NextBioi 43236.
PROi Q9UHX1.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHX1.
CleanExi HS_PUF60.
ExpressionAtlasi Q9UHX1. baseline and differential.
Genevestigatori Q9UHX1.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR006532. PolyU-bd.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view ]
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
SM00361. RRM_1. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01645. half-pint. 1 hit.
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The FBP interacting repressor targets TFIIH to inhibit activated transcription."
    Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
    Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN A COMPLEX WITH FUBP1 AND FUSE DNA, INTERACTION WITH CDK7; ERCC3; FUBP1 AND GTF2H1.
  2. "Interaction cloning and characterization of RoBPI, a novel protein binding to human Ro ribonucleoproteins."
    Bouffard P., Barbar E., Briere F., Boire G.
    RNA 6:66-78(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 5), IDENTIFICATION IN A COMPLEX WITH TROVE2 AND Y5 RNA, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 2; 3 AND 4).
    Tissue: Brain, Lung, Muscle and Ovary.
  7. "Interaction of sina and siah ring finger proteins with proteins involved in RNA metabolism, detected using the yeast two hybrid system."
    Hu Y., Holloway A.J., Bowtell D.D.L.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-559 (ISOFORM 2).
  8. "PUF60: a novel U2AF65-related splicing activity."
    Page-McCaw P.S., Amonlirdviman K., Sharp P.A.
    RNA 5:1548-1560(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-559 (ISOFORM 1), PROTEIN SEQUENCE OF 32-43; 53-69; 72-80; 156-167; 169-185; 227-243; 267-296; 301-313; 332-342; 419-437 AND 527-559, FUNCTION, SUBUNIT, RNA-BINDING, INTERACTION WITH SFRS11.
  9. "Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum."
    Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D., Wang X.W., Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D.
    Cell 104:353-363(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERCC3.
  10. "An essential role of alternative splicing of c-myc suppressor FUSE-binding protein-interacting repressor in carcinogenesis."
    Matsushita K., Tomonaga T., Shimada H., Shioya A., Higashi M., Matsubara H., Harigaya K., Nomura F., Libutti D., Levens D., Ochiai T.
    Cancer Res. 66:1409-1417(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 6), TISSUE SPECIFICITY.
  11. "The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse of c-myc expression."
    Liu J., Kouzine F., Nie Z., Chung H.-J., Elisha-Feil Z., Weber A., Zhao K., Levens D.
    EMBO J. 25:2119-2130(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Control of pre-mRNA splicing by the general splicing factors PUF60 and U2AF."
    Hastings M.L., Allemand E., Duelli D.M., Myers M.P., Krainer A.R.
    PLoS ONE 2:E538-E538(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING, SUBCELLULAR LOCATION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-251 AND LYS-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60; SER-112 AND THR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Solution structure of the third RNA binding domain of FBP-interacting repressor, SIAHBP1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 454-559.
  20. Cited for: VARIANT VRJS TYR-169, CHARACTERIZATION OF VARIANT VRJS TYR-169.

Entry informationi

Entry nameiPUF60_HUMAN
AccessioniPrimary (citable) accession number: Q9UHX1
Secondary accession number(s): A8K8K8
, Q969E7, Q96D94, Q96H63, Q99628, Q9NZA0, Q9UJY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 127 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

Miscellaneous

Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

External Data

Dasty 3