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Q9UHX1 (PUF60_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PUF60
Synonyms:FIR, ROBPI, SIAHBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Subunit structure

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. Ref.1 Ref.2 Ref.8 Ref.9 Ref.13

Subcellular location

Nucleus. Note: Colocalizes partially with TROVE2. Ref.2 Ref.13

Tissue specificity

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. Ref.2 Ref.10

Domain

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Miscellaneous

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

Sequence similarities

Belongs to the RRM half pint family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processApoptosis
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainRepeat
   LigandDNA-binding
RNA-binding
   Molecular functionRepressor
Ribonucleoprotein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 21516116PubMed 22365833. Source: IntAct

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16169070PubMed 16189514PubMed 16713569PubMed 18255255PubMed 21078624PubMed 21516116PubMed 22365833. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UHX1-1)

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.
Isoform 2 (identifier: Q9UHX1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     101-117: Missing.
Isoform 3 (identifier: Q9UHX1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
Isoform 4 (identifier: Q9UHX1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: Missing.
     101-117: Missing.
Isoform 5 (identifier: Q9UHX1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     9-37: Missing.
Isoform 6 (identifier: Q9UHX1-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Poly(U)-binding-splicing factor PUF60
PRO_0000299519

Regions

Domain129 – 20779RRM 1
Domain226 – 30479RRM 2
Domain462 – 54988RRM 3; atypical
Region1 – 516516Inhibits homodimerization
Region77 – 559483Inhibits transcriptional repression, interaction with ERCC3 and apoptosis induction
Compositional bias321 – 34323Ala-rich

Amino acid modifications

Modified residue601Phosphothreonine Ref.12 Ref.17
Modified residue1121Phosphoserine Ref.17
Modified residue2511N6-acetyllysine Ref.16
Modified residue3141Phosphothreonine Ref.17
Modified residue4541N6-acetyllysine Ref.16

Natural variations

Alternative sequence1 – 4343Missing in isoform 3 and isoform 4.
VSP_027717
Alternative sequence9 – 3729Missing in isoform 5 and isoform 6.
VSP_027718
Alternative sequence101 – 11717Missing in isoform 2, isoform 4 and isoform 6.
VSP_027719
Natural variant1691H → Y in VRJS; loss of function mutation; results in altered dosage of dfferent PUF60 protein forms and abnormal splicing profile of several target genes. Ref.20
VAR_070939

Experimental info

Sequence conflict31T → R in AAB41656. Ref.7
Sequence conflict1231R → G in AAB41656. Ref.7

Secondary structure

................................................................ 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 619F3C30D1C5951C

FASTA55959,875
        10         20         30         40         50         60 
MATATIALQV NGQQGGGSEP AAAAAVVAAG DKWKPPQGTD SIKMENGQST AAKLGLPPLT 

        70         80         90        100        110        120 
PEQQEALQKA KKYAMEQSIK SVLVKQTIAH QQQQLTNLQM AAVTMGFGDP LSPLQSMAAQ 

       130        140        150        160        170        180 
RQRALAIMCR VYVGSIYYEL GEDTIRQAFA PFGPIKSIDM SWDSVTMKHK GFAFVEYEVP 

       190        200        210        220        230        240 
EAAQLALEQM NSVMLGGRNI KVGRPSNIGQ AQPIIDQLAE EARAFNRIYV ASVHQDLSDD 

       250        260        270        280        290        300 
DIKSVFEAFG KIKSCTLARD PTTGKHKGYG FIEYEKAQSS QDAVSSMNLF DLGGQYLRVG 

       310        320        330        340        350        360 
KAVTPPMPLL TPATPGGLPP AAAVAAAAAT AKITAQEAVA GAAVLGTLGT PGLVSPALTL 

       370        380        390        400        410        420 
AQPLGTLPQA VMAAQAPGVI TGVTPARPPI PVTIPSVGVV NPILASPPTL GLLEPKKEKE 

       430        440        450        460        470        480 
EEELFPESER PEMLSEQEHM SISGSSARHM VMQKLLRKQE STVMVLRNMV DPKDIDDDLE 

       490        500        510        520        530        540 
GEVTEECGKF GAVNRVIIYQ EKQGEEEDAE IIVKIFVEFS IASETHKAIQ ALNGRWFAGR 

       550 
KVVAEVYDQE RFDNSDLSA 

« Hide

Isoform 2 [UniParc].

Checksum: 2C67EBE529A0922E
Show »

FASTA54258,171
Isoform 3 [UniParc].

Checksum: F52D8C619E874B55
Show »

FASTA51655,729
Isoform 4 [UniParc].

Checksum: 77881512A09C3EFD
Show »

FASTA49954,025
Isoform 5 [UniParc].

Checksum: 850251A390ECD30C
Show »

FASTA53057,103
Isoform 6 [UniParc].

Checksum: 2A5BA6848E391E3A
Show »

FASTA51355,399

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"SCRIB and PUF60 are primary drivers of the multisystemic phenotypes of the 8q24.3 copy-number variant."
Dauber A., Golzio C., Guenot C., Jodelka F.M., Kibaek M., Kjaergaard S., Leheup B., Martinet D., Nowaczyk M.J., Rosenfeld J.A., Zeesman S., Zunich J., Beckmann J.S., Hirschhorn J.N., Hastings M.L., Jacquemont S., Katsanis N.
Am. J. Hum. Genet. 93:798-811(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VRJS TYR-169, CHARACTERIZATION OF VARIANT VRJS TYR-169.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47933.1. [Q9UHX1-2]
CCDS47934.1. [Q9UHX1-1]
CCDS47935.1. [Q9UHX1-3]
CCDS59514.1. [Q9UHX1-4]
CCDS59515.1. [Q9UHX1-6]
CCDS59516.1. [Q9UHX1-5]
RefSeqNP_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]
UniGeneHs.521924.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9UHX1.
SMRQ9UHX1. Positions 118-313, 443-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116502. 88 interactions.
DIPDIP-34636N.
IntActQ9UHX1. 29 interactions.
MINTMINT-1374433.
STRING9606.ENSP00000322016.

PTM databases

PhosphoSiteQ9UHX1.

Polymorphism databases

DMDM74761960.

Proteomic databases

MaxQBQ9UHX1.
PaxDbQ9UHX1.
PRIDEQ9UHX1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313352; 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]
ENST00000563311; ENSP00000454452; ENSG00000260485. [Q9UHX1-1]
ENST00000563654; ENSP00000454436; ENSG00000260485. [Q9UHX1-3]
ENST00000566765; ENSP00000455879; ENSG00000260485. [Q9UHX1-5]
ENST00000567937; ENSP00000456640; ENSG00000260485. [Q9UHX1-6]
ENST00000568960; ENSP00000454822; ENSG00000260485. [Q9UHX1-4]
ENST00000569567; ENSP00000456170; ENSG00000260485. [Q9UHX1-2]
GeneID22827.
KEGGhsa:22827.
UCSCuc003yzq.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

CTD22827.
GeneCardsGC08M144898.
HGNCHGNC:17042. PUF60.
HPAHPA045733.
MIM604819. gene.
615583. phenotype.
neXtProtNX_Q9UHX1.
PharmGKBPA162400364.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOVERGENHBG055622.
InParanoidQ9UHX1.
KOK12838.
OMAAFVEYDV.
PhylomeDBQ9UHX1.
TreeFamTF313987.

Gene expression databases

ArrayExpressQ9UHX1.
BgeeQ9UHX1.
CleanExHS_PUF60.
GenevestigatorQ9UHX1.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR006532. PolyU-bd.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
SM00361. RRM_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01645. half-pint. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UHX1.
GeneWikiPUF60.
GenomeRNAi22827.
NextBio43236.
PROQ9UHX1.
SOURCESearch...

Entry information

Entry namePUF60_HUMAN
AccessionPrimary (citable) accession number: Q9UHX1
Secondary accession number(s): A8K8K8 expand/collapse secondary AC list , Q969E7, Q96D94, Q96H63, Q99628, Q9NZA0, Q9UJY7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM